---
_id: '8419'
abstract:
- lang: eng
  text: "In this survey, we provide a concise introduction to convex billiards and
    describe some recent results, obtained by the authors and collaborators, on the
    classification of integrable billiards, namely the so-called Birkhoff conjecture.\r\n\r\nThis
    article is part of the theme issue ‘Finite dimensional integrable systems: new
    trends and methods’."
article_number: '20170419'
article_processing_charge: No
article_type: original
author:
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: Alfonso
  full_name: Sorrentino, Alfonso
  last_name: Sorrentino
citation:
  ama: 'Kaloshin V, Sorrentino A. On the integrability of Birkhoff billiards. <i>Philosophical
    Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences</i>.
    2018;376(2131). doi:<a href="https://doi.org/10.1098/rsta.2017.0419">10.1098/rsta.2017.0419</a>'
  apa: 'Kaloshin, V., &#38; Sorrentino, A. (2018). On the integrability of Birkhoff
    billiards. <i>Philosophical Transactions of the Royal Society A: Mathematical,
    Physical and Engineering Sciences</i>. The Royal Society. <a href="https://doi.org/10.1098/rsta.2017.0419">https://doi.org/10.1098/rsta.2017.0419</a>'
  chicago: 'Kaloshin, Vadim, and Alfonso Sorrentino. “On the Integrability of Birkhoff
    Billiards.” <i>Philosophical Transactions of the Royal Society A: Mathematical,
    Physical and Engineering Sciences</i>. The Royal Society, 2018. <a href="https://doi.org/10.1098/rsta.2017.0419">https://doi.org/10.1098/rsta.2017.0419</a>.'
  ieee: 'V. Kaloshin and A. Sorrentino, “On the integrability of Birkhoff billiards,”
    <i>Philosophical Transactions of the Royal Society A: Mathematical, Physical and
    Engineering Sciences</i>, vol. 376, no. 2131. The Royal Society, 2018.'
  ista: 'Kaloshin V, Sorrentino A. 2018. On the integrability of Birkhoff billiards.
    Philosophical Transactions of the Royal Society A: Mathematical, Physical and
    Engineering Sciences. 376(2131), 20170419.'
  mla: 'Kaloshin, Vadim, and Alfonso Sorrentino. “On the Integrability of Birkhoff
    Billiards.” <i>Philosophical Transactions of the Royal Society A: Mathematical,
    Physical and Engineering Sciences</i>, vol. 376, no. 2131, 20170419, The Royal
    Society, 2018, doi:<a href="https://doi.org/10.1098/rsta.2017.0419">10.1098/rsta.2017.0419</a>.'
  short: 'V. Kaloshin, A. Sorrentino, Philosophical Transactions of the Royal Society
    A: Mathematical, Physical and Engineering Sciences 376 (2018).'
date_created: 2020-09-17T10:42:01Z
date_published: 2018-10-28T00:00:00Z
date_updated: 2021-01-12T08:19:09Z
day: '28'
doi: 10.1098/rsta.2017.0419
extern: '1'
intvolume: '       376'
issue: '2131'
keyword:
- General Engineering
- General Physics and Astronomy
- General Mathematics
language:
- iso: eng
month: '10'
oa_version: None
publication: 'Philosophical Transactions of the Royal Society A: Mathematical, Physical
  and Engineering Sciences'
publication_identifier:
  issn:
  - 1364-503X
  - 1471-2962
publication_status: published
publisher: The Royal Society
quality_controlled: '1'
status: public
title: On the integrability of Birkhoff billiards
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 376
year: '2018'
...
---
_id: '8420'
abstract:
- lang: eng
  text: We show that in the space of all convex billiard boundaries, the set of boundaries
    with rational caustics is dense. More precisely, the set of billiard boundaries
    with caustics of rotation number 1/q is polynomially sense in the smooth case,
    and exponentially dense in the analytic case.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: Ke
  full_name: Zhang, Ke
  last_name: Zhang
citation:
  ama: Kaloshin V, Zhang K. Density of convex billiards with rational caustics. <i>Nonlinearity</i>.
    2018;31(11):5214-5234. doi:<a href="https://doi.org/10.1088/1361-6544/aadc12">10.1088/1361-6544/aadc12</a>
  apa: Kaloshin, V., &#38; Zhang, K. (2018). Density of convex billiards with rational
    caustics. <i>Nonlinearity</i>. IOP Publishing. <a href="https://doi.org/10.1088/1361-6544/aadc12">https://doi.org/10.1088/1361-6544/aadc12</a>
  chicago: Kaloshin, Vadim, and Ke Zhang. “Density of Convex Billiards with Rational
    Caustics.” <i>Nonlinearity</i>. IOP Publishing, 2018. <a href="https://doi.org/10.1088/1361-6544/aadc12">https://doi.org/10.1088/1361-6544/aadc12</a>.
  ieee: V. Kaloshin and K. Zhang, “Density of convex billiards with rational caustics,”
    <i>Nonlinearity</i>, vol. 31, no. 11. IOP Publishing, pp. 5214–5234, 2018.
  ista: Kaloshin V, Zhang K. 2018. Density of convex billiards with rational caustics.
    Nonlinearity. 31(11), 5214–5234.
  mla: Kaloshin, Vadim, and Ke Zhang. “Density of Convex Billiards with Rational Caustics.”
    <i>Nonlinearity</i>, vol. 31, no. 11, IOP Publishing, 2018, pp. 5214–34, doi:<a
    href="https://doi.org/10.1088/1361-6544/aadc12">10.1088/1361-6544/aadc12</a>.
  short: V. Kaloshin, K. Zhang, Nonlinearity 31 (2018) 5214–5234.
date_created: 2020-09-17T10:42:09Z
date_published: 2018-10-15T00:00:00Z
date_updated: 2021-01-12T08:19:10Z
day: '15'
doi: 10.1088/1361-6544/aadc12
extern: '1'
external_id:
  arxiv:
  - '1706.07968'
intvolume: '        31'
issue: '11'
keyword:
- Mathematical Physics
- General Physics and Astronomy
- Applied Mathematics
- Statistical and Nonlinear Physics
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1706.07968
month: '10'
oa: 1
oa_version: Preprint
page: 5214-5234
publication: Nonlinearity
publication_identifier:
  issn:
  - 0951-7715
  - 1361-6544
publication_status: published
publisher: IOP Publishing
quality_controlled: '1'
status: public
title: Density of convex billiards with rational caustics
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 31
year: '2018'
...
---
_id: '8421'
abstract:
- lang: eng
  text: 'The classical Birkhoff conjecture claims that the boundary of a strictly
    convex integrable billiard table is necessarily an ellipse (or a circle as a special
    case). In this article we prove a complete local version of this conjecture: a
    small integrable perturbation of an ellipse must be an ellipse. This extends and
    completes the result in Avila-De Simoi-Kaloshin, where nearly circular domains
    were considered. One of the crucial ideas in the proof is to extend action-angle
    coordinates for elliptic billiards into complex domains (with respect to the angle),
    and to thoroughly analyze the nature of their complex singularities. As an application,
    we are able to prove some spectral rigidity results for elliptic domains.'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: Alfonso
  full_name: Sorrentino, Alfonso
  last_name: Sorrentino
citation:
  ama: Kaloshin V, Sorrentino A. On the local Birkhoff conjecture for convex billiards.
    <i>Annals of Mathematics</i>. 2018;188(1):315-380. doi:<a href="https://doi.org/10.4007/annals.2018.188.1.6">10.4007/annals.2018.188.1.6</a>
  apa: Kaloshin, V., &#38; Sorrentino, A. (2018). On the local Birkhoff conjecture
    for convex billiards. <i>Annals of Mathematics</i>. Annals of Mathematics, Princeton
    U. <a href="https://doi.org/10.4007/annals.2018.188.1.6">https://doi.org/10.4007/annals.2018.188.1.6</a>
  chicago: Kaloshin, Vadim, and Alfonso Sorrentino. “On the Local Birkhoff Conjecture
    for Convex Billiards.” <i>Annals of Mathematics</i>. Annals of Mathematics, Princeton
    U, 2018. <a href="https://doi.org/10.4007/annals.2018.188.1.6">https://doi.org/10.4007/annals.2018.188.1.6</a>.
  ieee: V. Kaloshin and A. Sorrentino, “On the local Birkhoff conjecture for convex
    billiards,” <i>Annals of Mathematics</i>, vol. 188, no. 1. Annals of Mathematics,
    Princeton U, pp. 315–380, 2018.
  ista: Kaloshin V, Sorrentino A. 2018. On the local Birkhoff conjecture for convex
    billiards. Annals of Mathematics. 188(1), 315–380.
  mla: Kaloshin, Vadim, and Alfonso Sorrentino. “On the Local Birkhoff Conjecture
    for Convex Billiards.” <i>Annals of Mathematics</i>, vol. 188, no. 1, Annals of
    Mathematics, Princeton U, 2018, pp. 315–80, doi:<a href="https://doi.org/10.4007/annals.2018.188.1.6">10.4007/annals.2018.188.1.6</a>.
  short: V. Kaloshin, A. Sorrentino, Annals of Mathematics 188 (2018) 315–380.
date_created: 2020-09-17T10:42:22Z
date_published: 2018-07-01T00:00:00Z
date_updated: 2021-01-12T08:19:10Z
day: '01'
doi: 10.4007/annals.2018.188.1.6
extern: '1'
external_id:
  arxiv:
  - '1612.09194'
intvolume: '       188'
issue: '1'
keyword:
- Statistics
- Probability and Uncertainty
- Statistics and Probability
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1612.09194
month: '07'
oa: 1
oa_version: Preprint
page: 315-380
publication: Annals of Mathematics
publication_identifier:
  issn:
  - 0003-486X
publication_status: published
publisher: Annals of Mathematics, Princeton U
quality_controlled: '1'
status: public
title: On the local Birkhoff conjecture for convex billiards
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 188
year: '2018'
...
---
_id: '8422'
abstract:
- lang: eng
  text: 'The Birkhoff conjecture says that the boundary of a strictly convex integrable
    billiard table is necessarily an ellipse. In this article, we consider a stronger
    notion of integrability, namely integrability close to the boundary, and prove
    a local version of this conjecture: a small perturbation of an ellipse of small
    eccentricity which preserves integrability near the boundary, is itself an ellipse.
    This extends the result in Avila et al. (Ann Math 184:527–558, ADK16), where integrability
    was assumed on a larger set. In particular, it shows that (local) integrability
    near the boundary implies global integrability. One of the crucial ideas in the
    proof consists in analyzing Taylor expansion of the corresponding action-angle
    coordinates with respect to the eccentricity parameter, deriving and studying
    higher order conditions for the preservation of integrable rational caustics.'
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Guan
  full_name: Huang, Guan
  last_name: Huang
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
- first_name: Alfonso
  full_name: Sorrentino, Alfonso
  last_name: Sorrentino
citation:
  ama: Huang G, Kaloshin V, Sorrentino A. Nearly circular domains which are integrable
    close to the boundary are ellipses. <i>Geometric and Functional Analysis</i>.
    2018;28(2):334-392. doi:<a href="https://doi.org/10.1007/s00039-018-0440-4">10.1007/s00039-018-0440-4</a>
  apa: Huang, G., Kaloshin, V., &#38; Sorrentino, A. (2018). Nearly circular domains
    which are integrable close to the boundary are ellipses. <i>Geometric and Functional
    Analysis</i>. Springer Nature. <a href="https://doi.org/10.1007/s00039-018-0440-4">https://doi.org/10.1007/s00039-018-0440-4</a>
  chicago: Huang, Guan, Vadim Kaloshin, and Alfonso Sorrentino. “Nearly Circular Domains
    Which Are Integrable Close to the Boundary Are Ellipses.” <i>Geometric and Functional
    Analysis</i>. Springer Nature, 2018. <a href="https://doi.org/10.1007/s00039-018-0440-4">https://doi.org/10.1007/s00039-018-0440-4</a>.
  ieee: G. Huang, V. Kaloshin, and A. Sorrentino, “Nearly circular domains which are
    integrable close to the boundary are ellipses,” <i>Geometric and Functional Analysis</i>,
    vol. 28, no. 2. Springer Nature, pp. 334–392, 2018.
  ista: Huang G, Kaloshin V, Sorrentino A. 2018. Nearly circular domains which are
    integrable close to the boundary are ellipses. Geometric and Functional Analysis.
    28(2), 334–392.
  mla: Huang, Guan, et al. “Nearly Circular Domains Which Are Integrable Close to
    the Boundary Are Ellipses.” <i>Geometric and Functional Analysis</i>, vol. 28,
    no. 2, Springer Nature, 2018, pp. 334–92, doi:<a href="https://doi.org/10.1007/s00039-018-0440-4">10.1007/s00039-018-0440-4</a>.
  short: G. Huang, V. Kaloshin, A. Sorrentino, Geometric and Functional Analysis 28
    (2018) 334–392.
date_created: 2020-09-17T10:42:30Z
date_published: 2018-03-18T00:00:00Z
date_updated: 2021-01-12T08:19:11Z
day: '18'
doi: 10.1007/s00039-018-0440-4
extern: '1'
external_id:
  arxiv:
  - '1705.10601'
intvolume: '        28'
issue: '2'
keyword:
- Geometry and Topology
- Analysis
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1705.10601
month: '03'
oa: 1
oa_version: Preprint
page: 334-392
publication: Geometric and Functional Analysis
publication_identifier:
  issn:
  - 1016-443X
  - 1420-8970
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Nearly circular domains which are integrable close to the boundary are ellipses
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 28
year: '2018'
...
---
_id: '8426'
abstract:
- lang: eng
  text: For any strictly convex planar domain Ω ⊂ R2 with a C∞ boundary one can associate
    an infinite sequence of spectral invariants introduced by Marvizi–Merlose [5].
    These invariants can generically be determined using the spectrum of the Dirichlet
    problem of the Laplace operator. A natural question asks if this collection is
    sufficient to determine Ω up to isometry. In this paper we give a counterexample,
    namely, we present two nonisometric domains Ω and Ω¯ with the same collection
    of Marvizi–Melrose invariants. Moreover, each domain has countably many periodic
    orbits {Sn}n≥1 (resp. {S¯n}n⩾1) of period going to infinity such that Sn and S¯n
    have the same period and perimeter for each n.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Lev
  full_name: Buhovsky, Lev
  last_name: Buhovsky
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
citation:
  ama: Buhovsky L, Kaloshin V. Nonisometric domains with the same Marvizi-Melrose
    invariants. <i>Regular and Chaotic Dynamics</i>. 2018;23:54-59. doi:<a href="https://doi.org/10.1134/s1560354718010057">10.1134/s1560354718010057</a>
  apa: Buhovsky, L., &#38; Kaloshin, V. (2018). Nonisometric domains with the same
    Marvizi-Melrose invariants. <i>Regular and Chaotic Dynamics</i>. Springer Nature.
    <a href="https://doi.org/10.1134/s1560354718010057">https://doi.org/10.1134/s1560354718010057</a>
  chicago: Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same
    Marvizi-Melrose Invariants.” <i>Regular and Chaotic Dynamics</i>. Springer Nature,
    2018. <a href="https://doi.org/10.1134/s1560354718010057">https://doi.org/10.1134/s1560354718010057</a>.
  ieee: L. Buhovsky and V. Kaloshin, “Nonisometric domains with the same Marvizi-Melrose
    invariants,” <i>Regular and Chaotic Dynamics</i>, vol. 23. Springer Nature, pp.
    54–59, 2018.
  ista: Buhovsky L, Kaloshin V. 2018. Nonisometric domains with the same Marvizi-Melrose
    invariants. Regular and Chaotic Dynamics. 23, 54–59.
  mla: Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same Marvizi-Melrose
    Invariants.” <i>Regular and Chaotic Dynamics</i>, vol. 23, Springer Nature, 2018,
    pp. 54–59, doi:<a href="https://doi.org/10.1134/s1560354718010057">10.1134/s1560354718010057</a>.
  short: L. Buhovsky, V. Kaloshin, Regular and Chaotic Dynamics 23 (2018) 54–59.
date_created: 2020-09-17T10:43:21Z
date_published: 2018-02-05T00:00:00Z
date_updated: 2021-01-12T08:19:11Z
day: '05'
doi: 10.1134/s1560354718010057
extern: '1'
external_id:
  arxiv:
  - '1801.00952'
intvolume: '        23'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1801.00952
month: '02'
oa: 1
oa_version: Preprint
page: 54-59
publication: Regular and Chaotic Dynamics
publication_identifier:
  issn:
  - 1560-3547
  - 1468-4845
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Nonisometric domains with the same Marvizi-Melrose invariants
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 23
year: '2018'
...
---
_id: '8436'
abstract:
- lang: eng
  text: The exchange of metabolites between the mitochondrial matrix and the cytosol
    depends on β-barrel channels in the outer membrane and α-helical carrier proteins
    in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones
    escort these proteins through the intermembrane space, but the structural and
    mechanistic details remain elusive. We have used an integrated structural biology
    approach to reveal the functional principle of TIM chaperones. Multiple clamp-like
    binding sites hold the mitochondrial membrane proteins in a translocation-competent
    elongated form, thus mimicking characteristics of co-translational membrane insertion.
    The bound preprotein undergoes conformational dynamics within the chaperone binding
    clefts, pointing to a multitude of dynamic local binding events. Mutations in
    these binding sites cause cell death or growth defects associated with impairment
    of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial
    “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins
    in a “nascent chain-like” conformation through a ribosome-free compartment.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
  full_name: Weinhäupl, Katharina
  last_name: Weinhäupl
- first_name: Caroline
  full_name: Lindau, Caroline
  last_name: Lindau
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Yong
  full_name: Wang, Yong
  last_name: Wang
- first_name: Conny
  full_name: Schütze, Conny
  last_name: Schütze
- first_name: Tobias
  full_name: Jores, Tobias
  last_name: Jores
- first_name: Laura
  full_name: Melchionda, Laura
  last_name: Melchionda
- first_name: Birgit
  full_name: Schönfisch, Birgit
  last_name: Schönfisch
- first_name: Hubert
  full_name: Kalbacher, Hubert
  last_name: Kalbacher
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- first_name: Doron
  full_name: Rapaport, Doron
  last_name: Rapaport
- first_name: Martha
  full_name: Brennich, Martha
  last_name: Brennich
- first_name: Kresten
  full_name: Lindorff-Larsen, Kresten
  last_name: Lindorff-Larsen
- first_name: Nils
  full_name: Wiedemann, Nils
  last_name: Wiedemann
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein
    chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. 2018;175(5):1365-1379.e25.
    doi:<a href="https://doi.org/10.1016/j.cell.2018.10.039">10.1016/j.cell.2018.10.039</a>
  apa: Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., …
    Schanda, P. (2018). Structural basis of membrane protein chaperoning through the
    mitochondrial intermembrane space. <i>Cell</i>. Elsevier. <a href="https://doi.org/10.1016/j.cell.2018.10.039">https://doi.org/10.1016/j.cell.2018.10.039</a>
  chicago: Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny
    Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane
    Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>.
    Elsevier, 2018. <a href="https://doi.org/10.1016/j.cell.2018.10.039">https://doi.org/10.1016/j.cell.2018.10.039</a>.
  ieee: K. Weinhäupl <i>et al.</i>, “Structural basis of membrane protein chaperoning
    through the mitochondrial intermembrane space,” <i>Cell</i>, vol. 175, no. 5.
    Elsevier, p. 1365–1379.e25, 2018.
  ista: Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L,
    Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K,
    Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning
    through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.
  mla: Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning
    through the Mitochondrial Intermembrane Space.” <i>Cell</i>, vol. 175, no. 5,
    Elsevier, 2018, p. 1365–1379.e25, doi:<a href="https://doi.org/10.1016/j.cell.2018.10.039">10.1016/j.cell.2018.10.039</a>.
  short: K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda,
    B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen,
    N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.
date_created: 2020-09-18T10:04:39Z
date_published: 2018-11-15T00:00:00Z
date_updated: 2021-01-12T08:19:15Z
day: '15'
doi: 10.1016/j.cell.2018.10.039
extern: '1'
intvolume: '       175'
issue: '5'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
month: '11'
oa_version: None
page: 1365-1379.e25
publication: Cell
publication_identifier:
  issn:
  - 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: Structural basis of membrane protein chaperoning through the mitochondrial
  intermembrane space
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 175
year: '2018'
...
---
_id: '8437'
abstract:
- lang: eng
  text: Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota,
    and archaea, facilitating the folding of proteins, preventing protein aggregation,
    and thus participating in maintaining protein homeostasis in the cell. During
    their functional cycle, they bind unfolded client proteins inside their double
    ring structure and promote protein folding by closing the ring chamber in an adenosine
    5′-triphosphate (ATP)–dependent manner. Although the static structures of fully
    open and closed forms of chaperonins were solved by x-ray crystallography or electron
    microscopy, elucidating the mechanisms of such ATP-driven molecular events requires
    studying the proteins at the structural level under working conditions. We introduce
    an approach that combines site-specific nuclear magnetic resonance observation
    of very large proteins, enabled by advanced isotope labeling methods, with an
    in situ ATP regeneration system. Using this method, we provide functional insight
    into the 1-MDa large hsp60 chaperonin while processing client proteins and reveal
    how nucleotide binding, hydrolysis, and release control switching between closed
    and open states. While the open conformation stabilizes the unfolded state of
    client proteins, the internalization of the client protein inside the chaperonin
    cavity speeds up its functional cycle. This approach opens new perspectives to
    study structures and mechanisms of various ATP-driven biological machineries in
    the heat of action.
article_number: eaau4196
article_processing_charge: No
article_type: original
author:
- first_name: Guillaume
  full_name: Mas, Guillaume
  last_name: Mas
- first_name: Jia-Ying
  full_name: Guan, Jia-Ying
  last_name: Guan
- first_name: Elodie
  full_name: Crublet, Elodie
  last_name: Crublet
- first_name: Elisa Colas
  full_name: Debled, Elisa Colas
  last_name: Debled
- first_name: Christine
  full_name: Moriscot, Christine
  last_name: Moriscot
- first_name: Pierre
  full_name: Gans, Pierre
  last_name: Gans
- first_name: Guy
  full_name: Schoehn, Guy
  last_name: Schoehn
- first_name: Pavel
  full_name: Macek, Pavel
  last_name: Macek
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Jerome
  full_name: Boisbouvier, Jerome
  last_name: Boisbouvier
citation:
  ama: Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin
    in action reveals how nucleotide binding regulates the functional cycle. <i>Science
    Advances</i>. 2018;4(9). doi:<a href="https://doi.org/10.1126/sciadv.aau4196">10.1126/sciadv.aau4196</a>
  apa: Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., …
    Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals
    how nucleotide binding regulates the functional cycle. <i>Science Advances</i>.
    American Association for the Advancement of Science. <a href="https://doi.org/10.1126/sciadv.aau4196">https://doi.org/10.1126/sciadv.aau4196</a>
  chicago: Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine
    Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier.
    “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding
    Regulates the Functional Cycle.” <i>Science Advances</i>. American Association
    for the Advancement of Science, 2018. <a href="https://doi.org/10.1126/sciadv.aau4196">https://doi.org/10.1126/sciadv.aau4196</a>.
  ieee: G. Mas <i>et al.</i>, “Structural investigation of a chaperonin in action
    reveals how nucleotide binding regulates the functional cycle,” <i>Science Advances</i>,
    vol. 4, no. 9. American Association for the Advancement of Science, 2018.
  ista: Mas G, Guan J-Y, Crublet E, Debled EC, Moriscot C, Gans P, Schoehn G, Macek
    P, Schanda P, Boisbouvier J. 2018. Structural investigation of a chaperonin in
    action reveals how nucleotide binding regulates the functional cycle. Science
    Advances. 4(9), eaau4196.
  mla: Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action
    Reveals How Nucleotide Binding Regulates the Functional Cycle.” <i>Science Advances</i>,
    vol. 4, no. 9, eaau4196, American Association for the Advancement of Science,
    2018, doi:<a href="https://doi.org/10.1126/sciadv.aau4196">10.1126/sciadv.aau4196</a>.
  short: G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn,
    P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).
date_created: 2020-09-18T10:04:51Z
date_published: 2018-09-19T00:00:00Z
date_updated: 2022-08-26T09:11:06Z
day: '19'
doi: 10.1126/sciadv.aau4196
extern: '1'
intvolume: '         4'
issue: '9'
language:
- iso: eng
month: '09'
oa_version: None
publication: Science Advances
publication_identifier:
  issn:
  - 2375-2548
publication_status: published
publisher: American Association for the Advancement of Science
quality_controlled: '1'
status: public
title: Structural investigation of a chaperonin in action reveals how nucleotide binding
  regulates the functional cycle
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 4
year: '2018'
...
---
_id: '8438'
article_processing_charge: No
article_type: letter_note
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: François
  full_name: Dehez, François
  last_name: Dehez
- first_name: Christophe
  full_name: Chipot, Christophe
  last_name: Chipot
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and
    interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural
    &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href="https://doi.org/10.1038/s41594-018-0127-4">10.1038/s41594-018-0127-4</a>
  apa: Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda,
    P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant.
    <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href="https://doi.org/10.1038/s41594-018-0127-4">https://doi.org/10.1038/s41594-018-0127-4</a>
  chicago: Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate
    Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally
    Relevant.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature,
    2018. <a href="https://doi.org/10.1038/s41594-018-0127-4">https://doi.org/10.1038/s41594-018-0127-4</a>.
  ieee: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics
    and interactions of AAC3 in DPC are not functionally relevant,” <i>Nature Structural
    &#38; Molecular Biology</i>, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.
  ista: Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics
    and interactions of AAC3 in DPC are not functionally relevant. Nature Structural
    &#38; Molecular Biology. 25(9), 745–747.
  mla: Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not
    Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>, vol.
    25, no. 9, Springer Nature, 2018, pp. 745–47, doi:<a href="https://doi.org/10.1038/s41594-018-0127-4">10.1038/s41594-018-0127-4</a>.
  short: V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature
    Structural &#38; Molecular Biology 25 (2018) 745–747.
date_created: 2020-09-18T10:04:59Z
date_published: 2018-09-03T00:00:00Z
date_updated: 2021-01-12T08:19:16Z
day: '03'
doi: 10.1038/s41594-018-0127-4
extern: '1'
intvolume: '        25'
issue: '9'
keyword:
- Molecular Biology
- Structural Biology
language:
- iso: eng
month: '09'
oa_version: None
page: 745-747
publication: Nature Structural & Molecular Biology
publication_identifier:
  issn:
  - 1545-9993
  - 1545-9985
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Dynamics and interactions of AAC3 in DPC are not functionally relevant
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 25
year: '2018'
...
---
_id: '8439'
abstract:
- lang: eng
  text: Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer
    of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly
    hampers their structural study in an environment similar to the bacterial surface.
    We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long
    O-antigen polysaccharides assembled in solution as vesicles or elongated micelles.
    Solid-state NMR with magic-angle spinning permitted the identification of NMR
    signals arising from regions with different flexibilities in the LPS, from the
    lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS
    enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa
    LPS, for which we could confirm that a specific oligosaccharide is involved in
    the antibiotic binding. The possibility to study LPS alone and bound to a ligand
    when it is assembled in membrane-like structures opens great prospects for the
    investigation of proteins and antibiotics that specifically target such an important
    molecule at the surface of Gram-negative bacteria.
article_processing_charge: No
article_type: original
author:
- first_name: Cedric
  full_name: Laguri, Cedric
  last_name: Laguri
- first_name: Alba
  full_name: Silipo, Alba
  last_name: Silipo
- first_name: Alessandra M.
  full_name: Martorana, Alessandra M.
  last_name: Martorana
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Roberta
  full_name: Marchetti, Roberta
  last_name: Marchetti
- first_name: Alessandra
  full_name: Polissi, Alessandra
  last_name: Polissi
- first_name: Antonio
  full_name: Molinaro, Antonio
  last_name: Molinaro
- first_name: Jean-Pierre
  full_name: Simorre, Jean-Pierre
  last_name: Simorre
citation:
  ama: Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact
    lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. 2018;13(8):2106-2113.
    doi:<a href="https://doi.org/10.1021/acschembio.8b00271">10.1021/acschembio.8b00271</a>
  apa: Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi,
    A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide
    endotoxin. <i>ACS Chemical Biology</i>. American Chemical Society. <a href="https://doi.org/10.1021/acschembio.8b00271">https://doi.org/10.1021/acschembio.8b00271</a>
  chicago: Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta
    Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid
    State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>.
    American Chemical Society, 2018. <a href="https://doi.org/10.1021/acschembio.8b00271">https://doi.org/10.1021/acschembio.8b00271</a>.
  ieee: C. Laguri <i>et al.</i>, “Solid state NMR studies of intact lipopolysaccharide
    endotoxin,” <i>ACS Chemical Biology</i>, vol. 13, no. 8. American Chemical Society,
    pp. 2106–2113, 2018.
  ista: Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro
    A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin.
    ACS Chemical Biology. 13(8), 2106–2113.
  mla: Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide
    Endotoxin.” <i>ACS Chemical Biology</i>, vol. 13, no. 8, American Chemical Society,
    2018, pp. 2106–13, doi:<a href="https://doi.org/10.1021/acschembio.8b00271">10.1021/acschembio.8b00271</a>.
  short: C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi,
    A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.
date_created: 2020-09-18T10:05:09Z
date_published: 2018-07-02T00:00:00Z
date_updated: 2021-01-12T08:19:16Z
day: '02'
doi: 10.1021/acschembio.8b00271
extern: '1'
intvolume: '        13'
issue: '8'
keyword:
- Molecular Medicine
- Biochemistry
- General Medicine
language:
- iso: eng
month: '07'
oa_version: None
page: 2106-2113
publication: ACS Chemical Biology
publication_identifier:
  issn:
  - 1554-8929
  - 1554-8937
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Solid state NMR studies of intact lipopolysaccharide endotoxin
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 13
year: '2018'
...
---
_id: '8440'
abstract:
- lang: eng
  text: Mycobacterium tuberculosis can remain dormant in the host, an ability that
    explains the failure of many current tuberculosis treatments. Recently, the natural
    products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill
    Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of
    the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein
    substrates, such as proteins containing phosphorylated arginine residues, to the
    ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit
    ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using
    NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding
    to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these
    dynamics are caused by conformational changes and do not result from unfolding
    or oligomerization of this domain. Cyclomarin binding to this domain specifically
    blocked these N-terminal dynamics. On the basis of these results, we propose a
    mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics,
    which modulates the chaperone enzymatic activity leading eventually to cell death.
article_processing_charge: No
article_type: original
author:
- first_name: Katharina
  full_name: Weinhäupl, Katharina
  last_name: Weinhäupl
- first_name: Martha
  full_name: Brennich, Martha
  last_name: Brennich
- first_name: Uli
  full_name: Kazmaier, Uli
  last_name: Kazmaier
- first_name: Joel
  full_name: Lelievre, Joel
  last_name: Lelievre
- first_name: Lluis
  full_name: Ballell, Lluis
  last_name: Ballell
- first_name: Alfred
  full_name: Goldberg, Alfred
  last_name: Goldberg
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Hugo
  full_name: Fraga, Hugo
  last_name: Fraga
citation:
  ama: Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks
    arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1
    from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393.
    doi:<a href="https://doi.org/10.1074/jbc.ra118.002251">10.1074/jbc.ra118.002251</a>
  apa: Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg,
    A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced
    millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
    <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38;
    Molecular Biology. <a href="https://doi.org/10.1074/jbc.ra118.002251">https://doi.org/10.1074/jbc.ra118.002251</a>
  chicago: Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis
    Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin
    Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain
    of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>.
    American Society for Biochemistry &#38; Molecular Biology, 2018. <a href="https://doi.org/10.1074/jbc.ra118.002251">https://doi.org/10.1074/jbc.ra118.002251</a>.
  ieee: K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced
    millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,”
    <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for
    Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018.
  ista: Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda
    P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced
    millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis.
    Journal of Biological Chemistry. 293(22), 8379–8393.
  mla: Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced
    Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.”
    <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for
    Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href="https://doi.org/10.1074/jbc.ra118.002251">10.1074/jbc.ra118.002251</a>.
  short: K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg,
    P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393.
date_created: 2020-09-18T10:05:18Z
date_published: 2018-06-01T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '01'
doi: 10.1074/jbc.ra118.002251
extern: '1'
intvolume: '       293'
issue: '22'
keyword:
- Cell Biology
- Biochemistry
- Molecular Biology
language:
- iso: eng
month: '06'
oa_version: None
page: 8379-8393
publication: Journal of Biological Chemistry
publication_identifier:
  issn:
  - 0021-9258
  - 1083-351X
publication_status: published
publisher: American Society for Biochemistry & Molecular Biology
quality_controlled: '1'
status: public
title: The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics
  in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 293
year: '2018'
...
---
_id: '8441'
abstract:
- lang: eng
  text: Solid-state near-rotary-resonance measurements of the spin–lattice relaxation
    rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular
    dynamics in the microsecond time scale. The small difference between the spin-lock
    (SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions,
    at the same time it brings up some methodological challenges. In this work, several
    issues affecting correct measurements and analysis of 15N R1ρ data are considered
    in detail. Among them are signal amplitude as a function of the difference between
    SL and MAS frequencies, “dead time” in the initial part of the relaxation decay
    caused by transient spin-dynamic oscillations, measurements under HORROR condition
    and proper treatment of the multi-exponential relaxation decays. The multiple
    15N R1ρ measurements at different SL fields and temperatures have been conducted
    in 1D mode (i.e. without site-specific resolution) for a set of four different
    microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin)
    to study the overall protein rocking in a crystal. While the amplitude of this
    motion varies very significantly, its correlation time for all four sample is
    practically the same, 30–50 μs. The amplitude of the rocking motion correlates
    with the packing density of a protein crystal. It has been suggested that the
    rocking motion is not diffusive but likely a jump-like dynamic process.
article_processing_charge: No
article_type: original
author:
- first_name: Alexey
  full_name: Krushelnitsky, Alexey
  last_name: Krushelnitsky
- first_name: Diego
  full_name: Gauto, Diego
  last_name: Gauto
- first_name: Diana C.
  full_name: Rodriguez Camargo, Diana C.
  last_name: Rodriguez Camargo
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Kay
  full_name: Saalwächter, Kay
  last_name: Saalwächter
citation:
  ama: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
    Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
    The model case of protein overall-rocking in crystals. <i>Journal of Biomolecular
    NMR</i>. 2018;71(1):53-67. doi:<a href="https://doi.org/10.1007/s10858-018-0191-4">10.1007/s10858-018-0191-4</a>'
  apa: 'Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., &#38;
    Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ
    15N MAS NMR experiments: The model case of protein overall-rocking in crystals.
    <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href="https://doi.org/10.1007/s10858-018-0191-4">https://doi.org/10.1007/s10858-018-0191-4</a>'
  chicago: 'Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda,
    and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ
    15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
    <i>Journal of Biomolecular NMR</i>. Springer Nature, 2018. <a href="https://doi.org/10.1007/s10858-018-0191-4">https://doi.org/10.1007/s10858-018-0191-4</a>.'
  ieee: 'A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter,
    “Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
    The model case of protein overall-rocking in crystals,” <i>Journal of Biomolecular
    NMR</i>, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.'
  ista: 'Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K.
    2018. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
    The model case of protein overall-rocking in crystals. Journal of Biomolecular
    NMR. 71(1), 53–67.'
  mla: 'Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance
    R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.”
    <i>Journal of Biomolecular NMR</i>, vol. 71, no. 1, Springer Nature, 2018, pp.
    53–67, doi:<a href="https://doi.org/10.1007/s10858-018-0191-4">10.1007/s10858-018-0191-4</a>.'
  short: A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter,
    Journal of Biomolecular NMR 71 (2018) 53–67.
date_created: 2020-09-18T10:05:28Z
date_published: 2018-05-30T00:00:00Z
date_updated: 2021-01-12T08:19:17Z
day: '30'
doi: 10.1007/s10858-018-0191-4
extern: '1'
intvolume: '        71'
issue: '1'
language:
- iso: eng
month: '05'
oa_version: Published Version
page: 53-67
publication: Journal of Biomolecular NMR
publication_identifier:
  issn:
  - 0925-2738
  - 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: 'Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments:
  The model case of protein overall-rocking in crystals'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 71
year: '2018'
...
---
_id: '8442'
abstract:
- lang: eng
  text: Membrane proteins perform a host of vital cellular functions. Deciphering
    the molecular mechanisms whereby they fulfill these functions requires detailed
    biophysical and structural investigations. Detergents have proven pivotal to extract
    the protein from its native surroundings. Yet, they provide a milieu that departs
    significantly from that of the biological membrane, to the extent that the structure,
    the dynamics, and the interactions of membrane proteins in detergents may considerably
    vary, as compared to the native environment. Understanding the impact of detergents
    on membrane proteins is, therefore, crucial to assess the biological relevance
    of results obtained in detergents. Here, we review the strengths and weaknesses
    of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR
    studies of membrane proteins. While this class of detergents is often successful
    for membrane protein solubilization, a growing list of examples points to destabilizing
    and denaturing properties, in particular for α-helical membrane proteins. Our
    comprehensive analysis stresses the importance of stringent controls when working
    with this class of detergents and when analyzing the structure and dynamics of
    membrane proteins in alkyl phosphocholine detergents.
article_processing_charge: No
article_type: original
author:
- first_name: Christophe
  full_name: Chipot, Christophe
  last_name: Chipot
- first_name: François
  full_name: Dehez, François
  last_name: Dehez
- first_name: Jason R.
  full_name: Schnell, Jason R.
  last_name: Schnell
- first_name: Nicole
  full_name: Zitzmann, Nicole
  last_name: Zitzmann
- first_name: Eva
  full_name: Pebay-Peyroula, Eva
  last_name: Pebay-Peyroula
- first_name: Laurent J.
  full_name: Catoire, Laurent J.
  last_name: Catoire
- first_name: Bruno
  full_name: Miroux, Bruno
  last_name: Miroux
- first_name: Edmund R. S.
  full_name: Kunji, Edmund R. S.
  last_name: Kunji
- first_name: Gianluigi
  full_name: Veglia, Gianluigi
  last_name: Veglia
- first_name: Timothy A.
  full_name: Cross, Timothy A.
  last_name: Cross
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein
    structure in alkyl phosphocholine detergents: A critical assessment of NMR and
    biophysical studies. <i>Chemical Reviews</i>. 2018;118(7):3559-3607. doi:<a href="https://doi.org/10.1021/acs.chemrev.7b00570">10.1021/acs.chemrev.7b00570</a>'
  apa: 'Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire,
    L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure
    in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
    studies. <i>Chemical Reviews</i>. American Chemical Society. <a href="https://doi.org/10.1021/acs.chemrev.7b00570">https://doi.org/10.1021/acs.chemrev.7b00570</a>'
  chicago: 'Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann,
    Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of
    Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical
    Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>. American
    Chemical Society, 2018. <a href="https://doi.org/10.1021/acs.chemrev.7b00570">https://doi.org/10.1021/acs.chemrev.7b00570</a>.'
  ieee: 'C. Chipot <i>et al.</i>, “Perturbations of native membrane protein structure
    in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical
    studies,” <i>Chemical Reviews</i>, vol. 118, no. 7. American Chemical Society,
    pp. 3559–3607, 2018.'
  ista: 'Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ,
    Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native
    membrane protein structure in alkyl phosphocholine detergents: A critical assessment
    of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.'
  mla: 'Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure
    in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical
    Studies.” <i>Chemical Reviews</i>, vol. 118, no. 7, American Chemical Society,
    2018, pp. 3559–607, doi:<a href="https://doi.org/10.1021/acs.chemrev.7b00570">10.1021/acs.chemrev.7b00570</a>.'
  short: C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire,
    B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118
    (2018) 3559–3607.
date_created: 2020-09-18T10:05:35Z
date_published: 2018-02-28T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '28'
doi: 10.1021/acs.chemrev.7b00570
extern: '1'
intvolume: '       118'
issue: '7'
keyword:
- General Chemistry
language:
- iso: eng
month: '02'
oa_version: None
page: 3559-3607
publication: Chemical Reviews
publication_identifier:
  issn:
  - 0009-2665
  - 1520-6890
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'Perturbations of native membrane protein structure in alkyl phosphocholine
  detergents: A critical assessment of NMR and biophysical studies'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 118
year: '2018'
...
---
_id: '8443'
abstract:
- lang: eng
  text: Characterizing the structure of membrane proteins (MPs) generally requires
    extraction from their native environment, most commonly with detergents. Yet,
    the physicochemical properties of detergent micelles and lipid bilayers differ
    markedly and could alter the structural organization of MPs, albeit without general
    rules. Dodecylphosphocholine (DPC) is the most widely used detergent for MP structure
    determination by NMR, but the physiological relevance of several prominent structures
    has been questioned, though indirectly, by other biophysical techniques, e.g.,
    functional/thermostability assay (TSA) and molecular dynamics (MD) simulations.
    Here, we resolve unambiguously this controversy by probing the functional relevance
    of three different mitochondrial carriers (MCs) in DPC at the atomic level, using
    an exhaustive set of solution-NMR experiments, complemented by functional/TSA
    and MD data. Our results provide atomic-level insight into the structure, substrate
    interaction and dynamics of the detergent–membrane protein complexes and demonstrates
    cogently that, while high-resolution NMR signals can be obtained for MCs in DPC,
    they systematically correspond to nonfunctional states.
article_processing_charge: No
article_type: original
author:
- first_name: Vilius
  full_name: Kurauskas, Vilius
  last_name: Kurauskas
- first_name: Audrey
  full_name: Hessel, Audrey
  last_name: Hessel
- first_name: Peixiang
  full_name: Ma, Peixiang
  last_name: Ma
- first_name: Paola
  full_name: Lunetti, Paola
  last_name: Lunetti
- first_name: Katharina
  full_name: Weinhäupl, Katharina
  last_name: Weinhäupl
- first_name: Lionel
  full_name: Imbert, Lionel
  last_name: Imbert
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
- first_name: Martin S.
  full_name: King, Martin S.
  last_name: King
- first_name: Rémy
  full_name: Sounier, Rémy
  last_name: Sounier
- first_name: Vincenza
  full_name: Dolce, Vincenza
  last_name: Dolce
- first_name: Edmund R. S.
  full_name: Kunji, Edmund R. S.
  last_name: Kunji
- first_name: Loredana
  full_name: Capobianco, Loredana
  last_name: Capobianco
- first_name: Christophe
  full_name: Chipot, Christophe
  last_name: Chipot
- first_name: François
  full_name: Dehez, François
  last_name: Dehez
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: 'Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins:
    Atomic-level views of mitochondrial carriers in dodecylphosphocholine. <i>The
    Journal of Physical Chemistry Letters</i>. 2018;9(5):933-938. doi:<a href="https://doi.org/10.1021/acs.jpclett.8b00269">10.1021/acs.jpclett.8b00269</a>'
  apa: 'Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L.,
    … Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views
    of mitochondrial carriers in dodecylphosphocholine. <i>The Journal of Physical
    Chemistry Letters</i>. American Chemical Society. <a href="https://doi.org/10.1021/acs.jpclett.8b00269">https://doi.org/10.1021/acs.jpclett.8b00269</a>'
  chicago: 'Kurauskas, Vilius, Audrey Hessel, Peixiang Ma, Paola Lunetti, Katharina
    Weinhäupl, Lionel Imbert, Bernhard Brutscher, et al. “How Detergent Impacts Membrane
    Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.”
    <i>The Journal of Physical Chemistry Letters</i>. American Chemical Society, 2018.
    <a href="https://doi.org/10.1021/acs.jpclett.8b00269">https://doi.org/10.1021/acs.jpclett.8b00269</a>.'
  ieee: 'V. Kurauskas <i>et al.</i>, “How detergent impacts membrane proteins: Atomic-level
    views of mitochondrial carriers in dodecylphosphocholine,” <i>The Journal of Physical
    Chemistry Letters</i>, vol. 9, no. 5. American Chemical Society, pp. 933–938,
    2018.'
  ista: 'Kurauskas V, Hessel A, Ma P, Lunetti P, Weinhäupl K, Imbert L, Brutscher
    B, King MS, Sounier R, Dolce V, Kunji ERS, Capobianco L, Chipot C, Dehez F, Bersch
    B, Schanda P. 2018. How detergent impacts membrane proteins: Atomic-level views
    of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry
    Letters. 9(5), 933–938.'
  mla: 'Kurauskas, Vilius, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level
    Views of Mitochondrial Carriers in Dodecylphosphocholine.” <i>The Journal of Physical
    Chemistry Letters</i>, vol. 9, no. 5, American Chemical Society, 2018, pp. 933–38,
    doi:<a href="https://doi.org/10.1021/acs.jpclett.8b00269">10.1021/acs.jpclett.8b00269</a>.'
  short: V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher,
    M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez,
    B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.
date_created: 2020-09-18T10:05:45Z
date_published: 2018-02-03T00:00:00Z
date_updated: 2021-01-12T08:19:18Z
day: '03'
doi: 10.1021/acs.jpclett.8b00269
extern: '1'
intvolume: '         9'
issue: '5'
keyword:
- General Materials Science
language:
- iso: eng
month: '02'
oa_version: None
page: 933-938
publication: The Journal of Physical Chemistry Letters
publication_identifier:
  issn:
  - 1948-7185
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: 'How detergent impacts membrane proteins: Atomic-level views of mitochondrial
  carriers in dodecylphosphocholine'
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 9
year: '2018'
...
---
_id: '85'
abstract:
- lang: eng
  text: Concurrent accesses to shared data structures must be synchronized to avoid
    data races. Coarse-grained synchronization, which locks the entire data structure,
    is easy to implement but does not scale. Fine-grained synchronization can scale
    well, but can be hard to reason about. Hand-over-hand locking, in which operations
    are pipelined as they traverse the data structure, combines fine-grained synchronization
    with ease of use. However, the traditional implementation suffers from inherent
    overheads. This paper introduces snapshot-based synchronization (SBS), a novel
    hand-over-hand locking mechanism. SBS decouples the synchronization state from
    the data, significantly improving cache utilization. Further, it relies on guarantees
    provided by pipelining to minimize synchronization that requires cross-thread
    communication. Snapshot-based synchronization thus scales much better than traditional
    hand-over-hand locking, while maintaining the same ease of use.
acknowledgement: Trevor Brown was supported in part by the ISF (grants 2005/17 & 1749/14)
  and by a NSERC post-doctoral fellowship.
alternative_title:
- LNCS
article_processing_charge: No
author:
- first_name: Eran
  full_name: Gilad, Eran
  last_name: Gilad
- first_name: Trevor A
  full_name: Brown, Trevor A
  id: 3569F0A0-F248-11E8-B48F-1D18A9856A87
  last_name: Brown
- first_name: Mark
  full_name: Oskin, Mark
  last_name: Oskin
- first_name: Yoav
  full_name: Etsion, Yoav
  last_name: Etsion
citation:
  ama: 'Gilad E, Brown TA, Oskin M, Etsion Y. Snapshot based synchronization: A fast
    replacement for Hand-over-Hand locking. In: Vol 11014. Springer; 2018:465-479.
    doi:<a href="https://doi.org/10.1007/978-3-319-96983-1_33">10.1007/978-3-319-96983-1_33</a>'
  apa: 'Gilad, E., Brown, T. A., Oskin, M., &#38; Etsion, Y. (2018). Snapshot based
    synchronization: A fast replacement for Hand-over-Hand locking (Vol. 11014, pp.
    465–479). Presented at the Euro-Par: European Conference on Parallel Processing,
    Turin, Italy: Springer. <a href="https://doi.org/10.1007/978-3-319-96983-1_33">https://doi.org/10.1007/978-3-319-96983-1_33</a>'
  chicago: 'Gilad, Eran, Trevor A Brown, Mark Oskin, and Yoav Etsion. “Snapshot Based
    Synchronization: A Fast Replacement for Hand-over-Hand Locking,” 11014:465–79.
    Springer, 2018. <a href="https://doi.org/10.1007/978-3-319-96983-1_33">https://doi.org/10.1007/978-3-319-96983-1_33</a>.'
  ieee: 'E. Gilad, T. A. Brown, M. Oskin, and Y. Etsion, “Snapshot based synchronization:
    A fast replacement for Hand-over-Hand locking,” presented at the Euro-Par: European
    Conference on Parallel Processing, Turin, Italy, 2018, vol. 11014, pp. 465–479.'
  ista: 'Gilad E, Brown TA, Oskin M, Etsion Y. 2018. Snapshot based synchronization:
    A fast replacement for Hand-over-Hand locking. Euro-Par: European Conference on
    Parallel Processing, LNCS, vol. 11014, 465–479.'
  mla: 'Gilad, Eran, et al. <i>Snapshot Based Synchronization: A Fast Replacement
    for Hand-over-Hand Locking</i>. Vol. 11014, Springer, 2018, pp. 465–79, doi:<a
    href="https://doi.org/10.1007/978-3-319-96983-1_33">10.1007/978-3-319-96983-1_33</a>.'
  short: E. Gilad, T.A. Brown, M. Oskin, Y. Etsion, in:, Springer, 2018, pp. 465–479.
conference:
  end_date: 2018-08-31
  location: Turin, Italy
  name: 'Euro-Par: European Conference on Parallel Processing'
  start_date: 2018-08-27
date_created: 2018-12-11T11:44:33Z
date_published: 2018-08-01T00:00:00Z
date_updated: 2023-09-18T09:32:36Z
day: '01'
ddc:
- '000'
department:
- _id: DaAl
doi: 10.1007/978-3-319-96983-1_33
external_id:
  isi:
  - '000851042300031'
file:
- access_level: open_access
  checksum: 13a3f250be8878405e791b53c19722ad
  content_type: application/pdf
  creator: dernst
  date_created: 2019-02-12T07:40:40Z
  date_updated: 2020-07-14T12:48:14Z
  file_id: '5954'
  file_name: 2018_Brown.pdf
  file_size: 665372
  relation: main_file
file_date_updated: 2020-07-14T12:48:14Z
has_accepted_license: '1'
intvolume: '     11014'
isi: 1
language:
- iso: eng
month: '08'
oa: 1
oa_version: Preprint
page: 465 - 479
project:
- _id: 26450934-B435-11E9-9278-68D0E5697425
  name: NSERC Postdoctoral fellowship
publication_identifier:
  issn:
  - '03029743'
publication_status: published
publisher: Springer
publist_id: '7969'
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'Snapshot based synchronization: A fast replacement for Hand-over-Hand locking'
type: conference
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 11014
year: '2018'
...
---
_id: '8547'
abstract:
- lang: eng
  text: The cerebral cortex contains multiple hierarchically organized areas with
    distinctive cytoarchitectonical patterns, but the cellular mechanisms underlying
    the emergence of this diversity remain unclear. Here, we have quantitatively investigated
    the neuronal output of individual progenitor cells in the ventricular zone of
    the developing mouse neocortex using a combination of methods that together circumvent
    the biases and limitations of individual approaches. We found that individual
    cortical progenitor cells show a high degree of stochasticity and generate pyramidal
    cell lineages that adopt a wide range of laminar configurations. Mathematical
    modelling these lineage data suggests that a small number of progenitor cell populations,
    each generating pyramidal cells following different stochastic developmental programs,
    suffice to generate the heterogenous complement of pyramidal cell lineages that
    collectively build the complex cytoarchitecture of the neocortex.
acknowledgement: We thank I. Andrew and S.E. Bae for excellent technical assistance,
  F. Gage for plasmids, and K. Nave (Nex-Cre) for mouse colonies. We thank members
  of the Marín and Rico laboratories for stimulating discussions and ideas. Our research
  on this topic is supported by grants from the European Research Council (ERC-2017-AdG
  787355 to O.M and ERC2016-CoG 725780 to S.H.) and Wellcome Trust (103714MA) to O.M.
  L.L. was the recipient of an EMBO long-term postdoctoral fellowship, R.B. received
  support from FWF Lise-Meitner program (M 2416) and F.K.W. was supported by an EMBO
  postdoctoral fellowship and is currently a Marie Skłodowska-Curie Fellow from the
  European Commission under the H2020 Programme.
article_processing_charge: No
author:
- first_name: Alfredo
  full_name: Llorca, Alfredo
  last_name: Llorca
- first_name: Gabriele
  full_name: Ciceri, Gabriele
  last_name: Ciceri
- first_name: Robert J
  full_name: Beattie, Robert J
  id: 2E26DF60-F248-11E8-B48F-1D18A9856A87
  last_name: Beattie
  orcid: 0000-0002-8483-8753
- first_name: Fong K.
  full_name: Wong, Fong K.
  last_name: Wong
- first_name: Giovanni
  full_name: Diana, Giovanni
  last_name: Diana
- first_name: Eleni
  full_name: Serafeimidou, Eleni
  last_name: Serafeimidou
- first_name: Marian
  full_name: Fernández-Otero, Marian
  last_name: Fernández-Otero
- first_name: Carmen
  full_name: Streicher, Carmen
  id: 36BCB99C-F248-11E8-B48F-1D18A9856A87
  last_name: Streicher
- first_name: Sebastian J.
  full_name: Arnold, Sebastian J.
  last_name: Arnold
- first_name: Martin
  full_name: Meyer, Martin
  last_name: Meyer
- first_name: Simon
  full_name: Hippenmeyer, Simon
  id: 37B36620-F248-11E8-B48F-1D18A9856A87
  last_name: Hippenmeyer
  orcid: 0000-0003-2279-1061
- first_name: Miguel
  full_name: Maravall, Miguel
  last_name: Maravall
- first_name: Oscar
  full_name: Marín, Oscar
  last_name: Marín
citation:
  ama: Llorca A, Ciceri G, Beattie RJ, et al. Heterogeneous progenitor cell behaviors
    underlie the assembly of neocortical cytoarchitecture. <i>bioRxiv</i>. doi:<a
    href="https://doi.org/10.1101/494088">10.1101/494088</a>
  apa: Llorca, A., Ciceri, G., Beattie, R. J., Wong, F. K., Diana, G., Serafeimidou,
    E., … Marín, O. (n.d.). Heterogeneous progenitor cell behaviors underlie the assembly
    of neocortical cytoarchitecture. <i>bioRxiv</i>. Cold Spring Harbor Laboratory.
    <a href="https://doi.org/10.1101/494088">https://doi.org/10.1101/494088</a>
  chicago: Llorca, Alfredo, Gabriele Ciceri, Robert J Beattie, Fong K. Wong, Giovanni
    Diana, Eleni Serafeimidou, Marian Fernández-Otero, et al. “Heterogeneous Progenitor
    Cell Behaviors Underlie the Assembly of Neocortical Cytoarchitecture.” <i>BioRxiv</i>.
    Cold Spring Harbor Laboratory, n.d. <a href="https://doi.org/10.1101/494088">https://doi.org/10.1101/494088</a>.
  ieee: A. Llorca <i>et al.</i>, “Heterogeneous progenitor cell behaviors underlie
    the assembly of neocortical cytoarchitecture,” <i>bioRxiv</i>. Cold Spring Harbor
    Laboratory.
  ista: Llorca A, Ciceri G, Beattie RJ, Wong FK, Diana G, Serafeimidou E, Fernández-Otero
    M, Streicher C, Arnold SJ, Meyer M, Hippenmeyer S, Maravall M, Marín O. Heterogeneous
    progenitor cell behaviors underlie the assembly of neocortical cytoarchitecture.
    bioRxiv, <a href="https://doi.org/10.1101/494088">10.1101/494088</a>.
  mla: Llorca, Alfredo, et al. “Heterogeneous Progenitor Cell Behaviors Underlie the
    Assembly of Neocortical Cytoarchitecture.” <i>BioRxiv</i>, Cold Spring Harbor
    Laboratory, doi:<a href="https://doi.org/10.1101/494088">10.1101/494088</a>.
  short: A. Llorca, G. Ciceri, R.J. Beattie, F.K. Wong, G. Diana, E. Serafeimidou,
    M. Fernández-Otero, C. Streicher, S.J. Arnold, M. Meyer, S. Hippenmeyer, M. Maravall,
    O. Marín, BioRxiv (n.d.).
date_created: 2020-09-21T12:01:50Z
date_published: 2018-12-13T00:00:00Z
date_updated: 2021-01-12T08:20:00Z
day: '13'
department:
- _id: SiHi
doi: 10.1101/494088
ec_funded: 1
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1101/494088
month: '12'
oa: 1
oa_version: Preprint
project:
- _id: 260018B0-B435-11E9-9278-68D0E5697425
  call_identifier: H2020
  grant_number: '725780'
  name: Principles of Neural Stem Cell Lineage Progression in Cerebral Cortex Development
- _id: 264E56E2-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: M02416
  name: Molecular Mechanisms Regulating Gliogenesis in the Cerebral Cortex
publication: bioRxiv
publication_status: submitted
publisher: Cold Spring Harbor Laboratory
status: public
title: Heterogeneous progenitor cell behaviors underlie the assembly of neocortical
  cytoarchitecture
type: preprint
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
year: '2018'
...
---
_id: '86'
abstract:
- lang: eng
  text: Responsiveness—the requirement that every request to a system be eventually
    handled—is one of the fundamental liveness properties of a reactive system. Average
    response time is a quantitative measure for the responsiveness requirement used
    commonly in performance evaluation. We show how average response time can be computed
    on state-transition graphs, on Markov chains, and on game graphs. In all three
    cases, we give polynomial-time algorithms.
acknowledgement: 'This research was supported in part by the Austrian Science Fund
  (FWF) under grants S11402-N23, S11407-N23 (RiSE/SHiNE) and Z211-N23 (Wittgenstein
  Award), ERC Start grant (279307: Graph Games), Vienna Science and Technology Fund
  (WWTF) through project ICT15-003 and by the National Science Centre (NCN), Poland
  under grant 2014/15/D/ST6/04543.'
alternative_title:
- LNCS
author:
- first_name: Krishnendu
  full_name: Chatterjee, Krishnendu
  id: 2E5DCA20-F248-11E8-B48F-1D18A9856A87
  last_name: Chatterjee
  orcid: 0000-0002-4561-241X
- first_name: Thomas A
  full_name: Henzinger, Thomas A
  id: 40876CD8-F248-11E8-B48F-1D18A9856A87
  last_name: Henzinger
  orcid: 0000−0002−2985−7724
- first_name: Jan
  full_name: Otop, Jan
  id: 2FC5DA74-F248-11E8-B48F-1D18A9856A87
  last_name: Otop
citation:
  ama: 'Chatterjee K, Henzinger TA, Otop J. Computing average response time. In: Lohstroh
    M, Derler P, Sirjani M, eds. <i>Principles of Modeling</i>. Vol 10760. Springer;
    2018:143-161. doi:<a href="https://doi.org/10.1007/978-3-319-95246-8_9">10.1007/978-3-319-95246-8_9</a>'
  apa: Chatterjee, K., Henzinger, T. A., &#38; Otop, J. (2018). Computing average
    response time. In M. Lohstroh, P. Derler, &#38; M. Sirjani (Eds.), <i>Principles
    of Modeling</i> (Vol. 10760, pp. 143–161). Springer. <a href="https://doi.org/10.1007/978-3-319-95246-8_9">https://doi.org/10.1007/978-3-319-95246-8_9</a>
  chicago: Chatterjee, Krishnendu, Thomas A Henzinger, and Jan Otop. “Computing Average
    Response Time.” In <i>Principles of Modeling</i>, edited by Marten Lohstroh, Patricia
    Derler, and Marjan Sirjani, 10760:143–61. Springer, 2018. <a href="https://doi.org/10.1007/978-3-319-95246-8_9">https://doi.org/10.1007/978-3-319-95246-8_9</a>.
  ieee: K. Chatterjee, T. A. Henzinger, and J. Otop, “Computing average response time,”
    in <i>Principles of Modeling</i>, vol. 10760, M. Lohstroh, P. Derler, and M. Sirjani,
    Eds. Springer, 2018, pp. 143–161.
  ista: 'Chatterjee K, Henzinger TA, Otop J. 2018.Computing average response time.
    In: Principles of Modeling. LNCS, vol. 10760, 143–161.'
  mla: Chatterjee, Krishnendu, et al. “Computing Average Response Time.” <i>Principles
    of Modeling</i>, edited by Marten Lohstroh et al., vol. 10760, Springer, 2018,
    pp. 143–61, doi:<a href="https://doi.org/10.1007/978-3-319-95246-8_9">10.1007/978-3-319-95246-8_9</a>.
  short: K. Chatterjee, T.A. Henzinger, J. Otop, in:, M. Lohstroh, P. Derler, M. Sirjani
    (Eds.), Principles of Modeling, Springer, 2018, pp. 143–161.
date_created: 2018-12-11T11:44:33Z
date_published: 2018-07-20T00:00:00Z
date_updated: 2021-01-12T08:20:14Z
day: '20'
ddc:
- '000'
department:
- _id: KrCh
- _id: ToHe
doi: 10.1007/978-3-319-95246-8_9
ec_funded: 1
editor:
- first_name: Marten
  full_name: Lohstroh, Marten
  last_name: Lohstroh
- first_name: Patricia
  full_name: Derler, Patricia
  last_name: Derler
- first_name: Marjan
  full_name: Sirjani, Marjan
  last_name: Sirjani
file:
- access_level: open_access
  checksum: 9995c6ce6957333baf616fc4f20be597
  content_type: application/pdf
  creator: dernst
  date_created: 2019-11-19T08:22:18Z
  date_updated: 2020-07-14T12:48:14Z
  file_id: '7053'
  file_name: 2018_PrinciplesModeling_Chatterjee.pdf
  file_size: 516307
  relation: main_file
file_date_updated: 2020-07-14T12:48:14Z
has_accepted_license: '1'
intvolume: '     10760'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Submitted Version
page: 143 - 161
project:
- _id: 25832EC2-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: S 11407_N23
  name: Rigorous Systems Engineering
- _id: 25863FF4-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: S11407
  name: Game Theory
- _id: 25F42A32-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: Z211
  name: The Wittgenstein Prize
- _id: 2581B60A-B435-11E9-9278-68D0E5697425
  call_identifier: FP7
  grant_number: '279307'
  name: 'Quantitative Graph Games: Theory and Applications'
- _id: 25892FC0-B435-11E9-9278-68D0E5697425
  grant_number: ICT15-003
  name: Efficient Algorithms for Computer Aided Verification
publication: Principles of Modeling
publication_status: published
publisher: Springer
publist_id: '7968'
quality_controlled: '1'
scopus_import: 1
status: public
title: Computing average response time
type: book_chapter
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 10760
year: '2018'
...
---
_id: '8618'
abstract:
- lang: eng
  text: The reversibly switchable fluorescent proteins (RSFPs) commonly used for RESOLFT
    nanoscopy have been developed from fluorescent proteins of the GFP superfamily.
    These proteins are bright, but exhibit several drawbacks such as relatively large
    size, oxygen-dependence, sensitivity to low pH, and limited switching speed. Therefore,
    RSFPs from other origins with improved properties need to be explored. Here, we
    report the development of two RSFPs based on the LOV domain of the photoreceptor
    protein YtvA from Bacillus subtilis. LOV domains obtain their fluorescence by
    association with the abundant cellular cofactor flavin mononucleotide (FMN). Under
    illumination with blue and ultraviolet light, they undergo a photocycle, making
    these proteins inherently photoswitchable. Our first improved variant, rsLOV1,
    can be used for RESOLFT imaging, whereas rsLOV2 proved useful for STED nanoscopy
    of living cells with a resolution of down to 50 nm. In addition to their smaller
    size compared to GFP-related proteins (17 kDa instead of 27 kDa) and their usability
    at low pH, rsLOV1 and rsLOV2 exhibit faster switching kinetics, switching on and
    off 3 times faster than rsEGFP2, the fastest-switching RSFP reported to date.
    Therefore, LOV-domain-based RSFPs have potential for applications where the switching
    speed of GFP-based proteins is limiting.
article_number: '2724'
article_processing_charge: No
article_type: original
author:
- first_name: Carola
  full_name: Gregor, Carola
  last_name: Gregor
- first_name: Sven C.
  full_name: Sidenstein, Sven C.
  last_name: Sidenstein
- first_name: Martin
  full_name: Andresen, Martin
  last_name: Andresen
- first_name: Steffen J.
  full_name: Sahl, Steffen J.
  last_name: Sahl
- first_name: Johann G
  full_name: Danzl, Johann G
  id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
  last_name: Danzl
  orcid: 0000-0001-8559-3973
- first_name: Stefan W.
  full_name: Hell, Stefan W.
  last_name: Hell
citation:
  ama: Gregor C, Sidenstein SC, Andresen M, Sahl SJ, Danzl JG, Hell SW. Novel reversibly
    switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from
    the bacterial photoreceptor YtvA. <i>Scientific Reports</i>. 2018;8. doi:<a href="https://doi.org/10.1038/s41598-018-19947-1">10.1038/s41598-018-19947-1</a>
  apa: Gregor, C., Sidenstein, S. C., Andresen, M., Sahl, S. J., Danzl, J. G., &#38;
    Hell, S. W. (2018). Novel reversibly switchable fluorescent proteins for RESOLFT
    and STED nanoscopy engineered from the bacterial photoreceptor YtvA. <i>Scientific
    Reports</i>. Springer Nature. <a href="https://doi.org/10.1038/s41598-018-19947-1">https://doi.org/10.1038/s41598-018-19947-1</a>
  chicago: Gregor, Carola, Sven C. Sidenstein, Martin Andresen, Steffen J. Sahl, Johann
    G Danzl, and Stefan W. Hell. “Novel Reversibly Switchable Fluorescent Proteins
    for RESOLFT and STED Nanoscopy Engineered from the Bacterial Photoreceptor YtvA.”
    <i>Scientific Reports</i>. Springer Nature, 2018. <a href="https://doi.org/10.1038/s41598-018-19947-1">https://doi.org/10.1038/s41598-018-19947-1</a>.
  ieee: C. Gregor, S. C. Sidenstein, M. Andresen, S. J. Sahl, J. G. Danzl, and S.
    W. Hell, “Novel reversibly switchable fluorescent proteins for RESOLFT and STED
    nanoscopy engineered from the bacterial photoreceptor YtvA,” <i>Scientific Reports</i>,
    vol. 8. Springer Nature, 2018.
  ista: Gregor C, Sidenstein SC, Andresen M, Sahl SJ, Danzl JG, Hell SW. 2018. Novel
    reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered
    from the bacterial photoreceptor YtvA. Scientific Reports. 8, 2724.
  mla: Gregor, Carola, et al. “Novel Reversibly Switchable Fluorescent Proteins for
    RESOLFT and STED Nanoscopy Engineered from the Bacterial Photoreceptor YtvA.”
    <i>Scientific Reports</i>, vol. 8, 2724, Springer Nature, 2018, doi:<a href="https://doi.org/10.1038/s41598-018-19947-1">10.1038/s41598-018-19947-1</a>.
  short: C. Gregor, S.C. Sidenstein, M. Andresen, S.J. Sahl, J.G. Danzl, S.W. Hell,
    Scientific Reports 8 (2018).
date_created: 2020-10-06T16:33:37Z
date_published: 2018-02-09T00:00:00Z
date_updated: 2023-09-19T15:04:49Z
day: '09'
ddc:
- '570'
department:
- _id: JoDa
doi: 10.1038/s41598-018-19947-1
external_id:
  isi:
  - '000424630400037'
  pmid:
  - '29426833'
file:
- access_level: open_access
  checksum: e642080fcbde9584c63544f587c74f03
  content_type: application/pdf
  creator: dernst
  date_created: 2020-10-06T16:35:16Z
  date_updated: 2020-10-06T16:35:16Z
  file_id: '8619'
  file_name: 2018_ScientificReports_Gregor.pdf
  file_size: 2818077
  relation: main_file
  success: 1
file_date_updated: 2020-10-06T16:35:16Z
has_accepted_license: '1'
intvolume: '         8'
isi: 1
keyword:
- Multidisciplinary
language:
- iso: eng
month: '02'
oa: 1
oa_version: Published Version
pmid: 1
publication: Scientific Reports
publication_identifier:
  issn:
  - 2045-2322
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy
  engineered from the bacterial photoreceptor YtvA
tmp:
  image: /images/cc_by.png
  legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
  name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
  short: CC BY (4.0)
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 8
year: '2018'
...
---
_id: '87'
abstract:
- lang: eng
  text: Using the geodesic distance on the n-dimensional sphere, we study the expected
    radius function of the Delaunay mosaic of a random set of points. Specifically,
    we consider the partition of the mosaic into intervals of the radius function
    and determine the expected number of intervals whose radii are less than or equal
    to a given threshold. We find that the expectations are essentially the same as
    for the Poisson–Delaunay mosaic in n-dimensional Euclidean space. Assuming the
    points are not contained in a hemisphere, the Delaunay mosaic is isomorphic to
    the boundary complex of the convex hull in Rn+1, so we also get the expected number
    of faces of a random inscribed polytope. As proved in Antonelli et al. [Adv. in
    Appl. Probab. 9–12 (1977–1980)], an orthant section of the n-sphere is isometric
    to the standard n-simplex equipped with the Fisher information metric. It follows
    that the latter space has similar stochastic properties as the n-dimensional Euclidean
    space. Our results are therefore relevant in information geometry and in population
    genetics.
article_processing_charge: No
article_type: original
arxiv: 1
author:
- first_name: Herbert
  full_name: Edelsbrunner, Herbert
  id: 3FB178DA-F248-11E8-B48F-1D18A9856A87
  last_name: Edelsbrunner
  orcid: 0000-0002-9823-6833
- first_name: Anton
  full_name: Nikitenko, Anton
  id: 3E4FF1BA-F248-11E8-B48F-1D18A9856A87
  last_name: Nikitenko
  orcid: 0000-0002-0659-3201
citation:
  ama: Edelsbrunner H, Nikitenko A. Random inscribed polytopes have similar radius
    functions as Poisson-Delaunay mosaics. <i>Annals of Applied Probability</i>. 2018;28(5):3215-3238.
    doi:<a href="https://doi.org/10.1214/18-AAP1389">10.1214/18-AAP1389</a>
  apa: Edelsbrunner, H., &#38; Nikitenko, A. (2018). Random inscribed polytopes have
    similar radius functions as Poisson-Delaunay mosaics. <i>Annals of Applied Probability</i>.
    Institute of Mathematical Statistics. <a href="https://doi.org/10.1214/18-AAP1389">https://doi.org/10.1214/18-AAP1389</a>
  chicago: Edelsbrunner, Herbert, and Anton Nikitenko. “Random Inscribed Polytopes
    Have Similar Radius Functions as Poisson-Delaunay Mosaics.” <i>Annals of Applied
    Probability</i>. Institute of Mathematical Statistics, 2018. <a href="https://doi.org/10.1214/18-AAP1389">https://doi.org/10.1214/18-AAP1389</a>.
  ieee: H. Edelsbrunner and A. Nikitenko, “Random inscribed polytopes have similar
    radius functions as Poisson-Delaunay mosaics,” <i>Annals of Applied Probability</i>,
    vol. 28, no. 5. Institute of Mathematical Statistics, pp. 3215–3238, 2018.
  ista: Edelsbrunner H, Nikitenko A. 2018. Random inscribed polytopes have similar
    radius functions as Poisson-Delaunay mosaics. Annals of Applied Probability. 28(5),
    3215–3238.
  mla: Edelsbrunner, Herbert, and Anton Nikitenko. “Random Inscribed Polytopes Have
    Similar Radius Functions as Poisson-Delaunay Mosaics.” <i>Annals of Applied Probability</i>,
    vol. 28, no. 5, Institute of Mathematical Statistics, 2018, pp. 3215–38, doi:<a
    href="https://doi.org/10.1214/18-AAP1389">10.1214/18-AAP1389</a>.
  short: H. Edelsbrunner, A. Nikitenko, Annals of Applied Probability 28 (2018) 3215–3238.
date_created: 2018-12-11T11:44:33Z
date_published: 2018-10-01T00:00:00Z
date_updated: 2023-09-15T12:10:35Z
day: '01'
department:
- _id: HeEd
doi: 10.1214/18-AAP1389
external_id:
  arxiv:
  - '1705.02870'
  isi:
  - '000442893500018'
intvolume: '        28'
isi: 1
issue: '5'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1705.02870
month: '10'
oa: 1
oa_version: Preprint
page: 3215 - 3238
project:
- _id: 2561EBF4-B435-11E9-9278-68D0E5697425
  call_identifier: FWF
  grant_number: I02979-N35
  name: Persistence and stability of geometric complexes
publication: Annals of Applied Probability
publication_status: published
publisher: Institute of Mathematical Statistics
publist_id: '7967'
quality_controlled: '1'
related_material:
  record:
  - id: '6287'
    relation: dissertation_contains
    status: public
scopus_import: '1'
status: public
title: Random inscribed polytopes have similar radius functions as Poisson-Delaunay
  mosaics
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 28
year: '2018'
...
---
_id: '9'
abstract:
- lang: eng
  text: 'Immune cells migrating to the sites of infection navigate through diverse
    tissue architectures and switch their migratory mechanisms upon demand. However,
    little is known about systemic regulators that could allow the acquisition of
    these mechanisms. We performed a genetic screen in Drosophila melanogaster to
    identify regulators of germband invasion by embryonic macrophages into the confined
    space between the ectoderm and mesoderm. We have found that bZIP circadian transcription
    factors (TFs) Kayak (dFos) and Vrille (dNFIL3) have opposite effects on macrophage
    germband infiltration: Kayak facilitated and Vrille inhibited it. These TFs are
    enriched in the macrophages during migration and genetically interact to control
    it. Kayak sets a less coordinated mode of migration of the macrophage group and
    increases the probability and length of Levy walks. Intriguingly, the motility
    of kayak mutant macrophages was also strongly affected during initial germband
    invasion but not along another less confined route. Inhibiting Rho1 signaling
    within the tail ectoderm partially rescued the Kayak mutant phenotype, strongly
    suggesting that migrating macrophages have to overcome a barrier imposed by the
    stiffness of the ectoderm. Also, Kayak appeared to be important for the maintenance
    of the round cell shape and the rear edge translocation of the macrophages invading
    the germband. Complementary to this, the cortical actin cytoskeleton of Kayak-
    deficient macrophages was strongly affected. RNA sequencing revealed the filamin
    Cheerio and tetraspanin TM4SF to be downstream of Kayak. Chromatin immunoprecipitation
    and immunostaining revealed that the formin Diaphanous is another downstream target
    of Kayak. Immunostaining revealed that the formin Diaphanous is another downstream
    target of Kayak. Indeed, Cheerio, TM4SF and Diaphanous are required within macrophages
    for germband invasion, and expression of constitutively active Diaphanous in macrophages
    was able to rescue the kayak mutant phenotype. Moreover, Cher and Diaphanous are
    also reduced in the macrophages overexpressing Vrille. We hypothesize that Kayak,
    through its targets, increases actin polymerization and cortical tension in macrophages
    and thus allows extra force generation necessary for macrophage dissemination
    and migration through confined stiff tissues, while Vrille counterbalances it.'
alternative_title:
- ISTA Thesis
article_processing_charge: No
author:
- first_name: Vera
  full_name: Belyaeva, Vera
  id: 47F080FE-F248-11E8-B48F-1D18A9856A87
  last_name: Belyaeva
citation:
  ama: Belyaeva V. Transcriptional regulation of macrophage migration in the Drosophila
    melanogaster embryo . 2018. doi:<a href="https://doi.org/10.15479/AT:ISTA:th1064">10.15479/AT:ISTA:th1064</a>
  apa: Belyaeva, V. (2018). <i>Transcriptional regulation of macrophage migration
    in the Drosophila melanogaster embryo </i>. Institute of Science and Technology
    Austria. <a href="https://doi.org/10.15479/AT:ISTA:th1064">https://doi.org/10.15479/AT:ISTA:th1064</a>
  chicago: Belyaeva, Vera. “Transcriptional Regulation of Macrophage Migration in
    the Drosophila Melanogaster Embryo .” Institute of Science and Technology Austria,
    2018. <a href="https://doi.org/10.15479/AT:ISTA:th1064">https://doi.org/10.15479/AT:ISTA:th1064</a>.
  ieee: V. Belyaeva, “Transcriptional regulation of macrophage migration in the Drosophila
    melanogaster embryo ,” Institute of Science and Technology Austria, 2018.
  ista: Belyaeva V. 2018. Transcriptional regulation of macrophage migration in the
    Drosophila melanogaster embryo . Institute of Science and Technology Austria.
  mla: Belyaeva, Vera. <i>Transcriptional Regulation of Macrophage Migration in the
    Drosophila Melanogaster Embryo </i>. Institute of Science and Technology Austria,
    2018, doi:<a href="https://doi.org/10.15479/AT:ISTA:th1064">10.15479/AT:ISTA:th1064</a>.
  short: V. Belyaeva, Transcriptional Regulation of Macrophage Migration in the Drosophila
    Melanogaster Embryo , Institute of Science and Technology Austria, 2018.
date_created: 2018-12-11T11:44:08Z
date_published: 2018-07-01T00:00:00Z
date_updated: 2023-09-07T12:43:10Z
day: '01'
ddc:
- '570'
degree_awarded: PhD
department:
- _id: DaSi
doi: 10.15479/AT:ISTA:th1064
file:
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  checksum: d27b2465cb70d0c9678a0381b9b6ced1
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  creator: dernst
  date_created: 2019-04-08T14:13:12Z
  date_updated: 2020-07-14T12:48:14Z
  embargo_to: open_access
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  date_created: 2019-04-08T14:14:08Z
  date_updated: 2021-02-11T11:17:16Z
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file_date_updated: 2021-02-11T11:17:16Z
has_accepted_license: '1'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: '96'
publication_identifier:
  issn:
  - 2663-337X
publication_status: published
publisher: Institute of Science and Technology Austria
publist_id: '8047'
pubrep_id: '1064'
status: public
supervisor:
- first_name: Daria E
  full_name: Siekhaus, Daria E
  id: 3D224B9E-F248-11E8-B48F-1D18A9856A87
  last_name: Siekhaus
  orcid: 0000-0001-8323-8353
title: 'Transcriptional regulation of macrophage migration in the Drosophila melanogaster
  embryo '
type: dissertation
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
year: '2018'
...
---
_id: '162'
abstract:
- lang: eng
  text: 'Facial shape is the basis for facial recognition and categorization. Facial
    features reflect the underlying geometry of the skeletal structures. Here, we
    reveal that cartilaginous nasal capsule (corresponding to upper jaw and face)
    is shaped by signals generated by neural structures: brain and olfactory epithelium.
    Brain-derived Sonic Hedgehog (SHH) enables the induction of nasal septum and posterior
    nasal capsule, whereas the formation of a capsule roof is controlled by signals
    from the olfactory epithelium. Unexpectedly, the cartilage of the nasal capsule
    turned out to be important for shaping membranous facial bones during development.
    This suggests that conserved neurosensory structures could benefit from protection
    and have evolved signals inducing cranial cartilages encasing them. Experiments
    with mutant mice revealed that the genomic regulatory regions controlling production
    of SHH in the nervous system contribute to facial cartilage morphogenesis, which
    might be a mechanism responsible for the adaptive evolution of animal faces and
    snouts.'
article_number: e34465
article_processing_charge: No
author:
- first_name: Marketa
  full_name: Kaucka, Marketa
  last_name: Kaucka
- first_name: Julian
  full_name: Petersen, Julian
  last_name: Petersen
- first_name: Marketa
  full_name: Tesarova, Marketa
  last_name: Tesarova
- first_name: Bara
  full_name: Szarowska, Bara
  last_name: Szarowska
- first_name: Maria
  full_name: Kastriti, Maria
  last_name: Kastriti
- first_name: Meng
  full_name: Xie, Meng
  last_name: Xie
- first_name: Anna
  full_name: Kicheva, Anna
  id: 3959A2A0-F248-11E8-B48F-1D18A9856A87
  last_name: Kicheva
  orcid: 0000-0003-4509-4998
- first_name: Karl
  full_name: Annusver, Karl
  last_name: Annusver
- first_name: Maria
  full_name: Kasper, Maria
  last_name: Kasper
- first_name: Orsolya
  full_name: Symmons, Orsolya
  last_name: Symmons
- first_name: Leslie
  full_name: Pan, Leslie
  last_name: Pan
- first_name: Francois
  full_name: Spitz, Francois
  last_name: Spitz
- first_name: Jozef
  full_name: Kaiser, Jozef
  last_name: Kaiser
- first_name: Maria
  full_name: Hovorakova, Maria
  last_name: Hovorakova
- first_name: Tomas
  full_name: Zikmund, Tomas
  last_name: Zikmund
- first_name: Kazunori
  full_name: Sunadome, Kazunori
  last_name: Sunadome
- first_name: Michael P
  full_name: Matise, Michael P
  last_name: Matise
- first_name: Hui
  full_name: Wang, Hui
  last_name: Wang
- first_name: Ulrika
  full_name: Marklund, Ulrika
  last_name: Marklund
- first_name: Hind
  full_name: Abdo, Hind
  last_name: Abdo
- first_name: Patrik
  full_name: Ernfors, Patrik
  last_name: Ernfors
- first_name: Pascal
  full_name: Maire, Pascal
  last_name: Maire
- first_name: Maud
  full_name: Wurmser, Maud
  last_name: Wurmser
- first_name: Andrei S
  full_name: Chagin, Andrei S
  last_name: Chagin
- first_name: Kaj
  full_name: Fried, Kaj
  last_name: Fried
- first_name: Igor
  full_name: Adameyko, Igor
  last_name: Adameyko
citation:
  ama: Kaucka M, Petersen J, Tesarova M, et al. Signals from the brain and olfactory
    epithelium control shaping of the mammalian nasal capsule cartilage. <i>eLife</i>.
    2018;7. doi:<a href="https://doi.org/10.7554/eLife.34465">10.7554/eLife.34465</a>
  apa: Kaucka, M., Petersen, J., Tesarova, M., Szarowska, B., Kastriti, M., Xie, M.,
    … Adameyko, I. (2018). Signals from the brain and olfactory epithelium control
    shaping of the mammalian nasal capsule cartilage. <i>ELife</i>. eLife Sciences
    Publications. <a href="https://doi.org/10.7554/eLife.34465">https://doi.org/10.7554/eLife.34465</a>
  chicago: Kaucka, Marketa, Julian Petersen, Marketa Tesarova, Bara Szarowska, Maria
    Kastriti, Meng Xie, Anna Kicheva, et al. “Signals from the Brain and Olfactory
    Epithelium Control Shaping of the Mammalian Nasal Capsule Cartilage.” <i>ELife</i>.
    eLife Sciences Publications, 2018. <a href="https://doi.org/10.7554/eLife.34465">https://doi.org/10.7554/eLife.34465</a>.
  ieee: M. Kaucka <i>et al.</i>, “Signals from the brain and olfactory epithelium
    control shaping of the mammalian nasal capsule cartilage,” <i>eLife</i>, vol.
    7. eLife Sciences Publications, 2018.
  ista: Kaucka M, Petersen J, Tesarova M, Szarowska B, Kastriti M, Xie M, Kicheva
    A, Annusver K, Kasper M, Symmons O, Pan L, Spitz F, Kaiser J, Hovorakova M, Zikmund
    T, Sunadome K, Matise MP, Wang H, Marklund U, Abdo H, Ernfors P, Maire P, Wurmser
    M, Chagin AS, Fried K, Adameyko I. 2018. Signals from the brain and olfactory
    epithelium control shaping of the mammalian nasal capsule cartilage. eLife. 7,
    e34465.
  mla: Kaucka, Marketa, et al. “Signals from the Brain and Olfactory Epithelium Control
    Shaping of the Mammalian Nasal Capsule Cartilage.” <i>ELife</i>, vol. 7, e34465,
    eLife Sciences Publications, 2018, doi:<a href="https://doi.org/10.7554/eLife.34465">10.7554/eLife.34465</a>.
  short: M. Kaucka, J. Petersen, M. Tesarova, B. Szarowska, M. Kastriti, M. Xie, A.
    Kicheva, K. Annusver, M. Kasper, O. Symmons, L. Pan, F. Spitz, J. Kaiser, M. Hovorakova,
    T. Zikmund, K. Sunadome, M.P. Matise, H. Wang, U. Marklund, H. Abdo, P. Ernfors,
    P. Maire, M. Wurmser, A.S. Chagin, K. Fried, I. Adameyko, ELife 7 (2018).
date_created: 2018-12-11T11:44:57Z
date_published: 2018-06-13T00:00:00Z
date_updated: 2023-09-18T09:29:07Z
day: '13'
ddc:
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department:
- _id: AnKi
doi: 10.7554/eLife.34465
ec_funded: 1
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title: Signals from the brain and olfactory epithelium control shaping of the mammalian
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