---
_id: '8246'
abstract:
- lang: eng
  text: The Staphylococcus aureus cell wall stress stimulon (CWSS) is activated by
    cell envelope-targeting antibiotics or depletion of essential cell wall biosynthesis
    enzymes. The functionally uncharacterized S. aureus LytR-CpsA-Psr (LCP) proteins,
    MsrR, SA0908 and SA2103, all belong to the CWSS. Although not essential, deletion
    of all three LCP proteins severely impairs cell division. We show here that VraSR-dependent
    CWSS expression was up to 250-fold higher in single, double and triple LCP mutants
    than in wild type S. aureus in the absence of external stress. The LCP triple
    mutant was virtually depleted of wall teichoic acids (WTA), which could be restored
    to different degrees by any of the single LCP proteins. Subinhibitory concentrations
    of tunicamycin, which inhibits the first WTA synthesis enzyme TarO (TagO), could
    partially complement the severe growth defect of the LCP triple mutant. Both of
    the latter findings support a role for S. aureus LCP proteins in late WTA synthesis,
    as in Bacillus subtilis where LCP proteins were recently proposed to transfer
    WTA from lipid carriers to the cell wall peptidoglycan. Intrinsic activation of
    the CWSS upon LCP deletion and the fact that LCP proteins were essential for WTA-loading
    of the cell wall, highlight their important role(s) in S. aureus cell envelope
    biogenesis.
article_processing_charge: No
article_type: original
author:
- first_name: Vanina
  full_name: Dengler, Vanina
  last_name: Dengler
- first_name: Patricia Stutzmann
  full_name: Meier, Patricia Stutzmann
  last_name: Meier
- first_name: Ronald
  full_name: Heusser, Ronald
  last_name: Heusser
- first_name: Peter
  full_name: Kupferschmied, Peter
  last_name: Kupferschmied
- first_name: Judit
  full_name: Fazekas, Judit
  id: 36432834-F248-11E8-B48F-1D18A9856A87
  last_name: Fazekas
  orcid: 0000-0002-8777-3502
- first_name: Sarah
  full_name: Friebe, Sarah
  last_name: Friebe
- first_name: Sibylle Burger
  full_name: Staufer, Sibylle Burger
  last_name: Staufer
- first_name: Paul A.
  full_name: Majcherczyk, Paul A.
  last_name: Majcherczyk
- first_name: Philippe
  full_name: Moreillon, Philippe
  last_name: Moreillon
- first_name: Brigitte
  full_name: Berger-Bächi, Brigitte
  last_name: Berger-Bächi
- first_name: Nadine
  full_name: McCallum, Nadine
  last_name: McCallum
citation:
  ama: Dengler V, Meier PS, Heusser R, et al. Deletion of hypothetical wall teichoic
    acid ligases in Staphylococcus aureus activates the cell wall stress response.
    <i>FEMS Microbiology Letters</i>. 2012;333(2):109-120. doi:<a href="https://doi.org/10.1111/j.1574-6968.2012.02603.x">10.1111/j.1574-6968.2012.02603.x</a>
  apa: Dengler, V., Meier, P. S., Heusser, R., Kupferschmied, P., Singer, J., Friebe,
    S., … McCallum, N. (2012). Deletion of hypothetical wall teichoic acid ligases
    in Staphylococcus aureus activates the cell wall stress response. <i>FEMS Microbiology
    Letters</i>. Oxford University Press. <a href="https://doi.org/10.1111/j.1574-6968.2012.02603.x">https://doi.org/10.1111/j.1574-6968.2012.02603.x</a>
  chicago: Dengler, Vanina, Patricia Stutzmann Meier, Ronald Heusser, Peter Kupferschmied,
    Judit Singer, Sarah Friebe, Sibylle Burger Staufer, et al. “Deletion of Hypothetical
    Wall Teichoic Acid Ligases in Staphylococcus Aureus Activates the Cell Wall Stress
    Response.” <i>FEMS Microbiology Letters</i>. Oxford University Press, 2012. <a
    href="https://doi.org/10.1111/j.1574-6968.2012.02603.x">https://doi.org/10.1111/j.1574-6968.2012.02603.x</a>.
  ieee: V. Dengler <i>et al.</i>, “Deletion of hypothetical wall teichoic acid ligases
    in Staphylococcus aureus activates the cell wall stress response,” <i>FEMS Microbiology
    Letters</i>, vol. 333, no. 2. Oxford University Press, pp. 109–120, 2012.
  ista: Dengler V, Meier PS, Heusser R, Kupferschmied P, Singer J, Friebe S, Staufer
    SB, Majcherczyk PA, Moreillon P, Berger-Bächi B, McCallum N. 2012. Deletion of
    hypothetical wall teichoic acid ligases in Staphylococcus aureus activates the
    cell wall stress response. FEMS Microbiology Letters. 333(2), 109–120.
  mla: Dengler, Vanina, et al. “Deletion of Hypothetical Wall Teichoic Acid Ligases
    in Staphylococcus Aureus Activates the Cell Wall Stress Response.” <i>FEMS Microbiology
    Letters</i>, vol. 333, no. 2, Oxford University Press, 2012, pp. 109–20, doi:<a
    href="https://doi.org/10.1111/j.1574-6968.2012.02603.x">10.1111/j.1574-6968.2012.02603.x</a>.
  short: V. Dengler, P.S. Meier, R. Heusser, P. Kupferschmied, J. Singer, S. Friebe,
    S.B. Staufer, P.A. Majcherczyk, P. Moreillon, B. Berger-Bächi, N. McCallum, FEMS
    Microbiology Letters 333 (2012) 109–120.
date_created: 2020-08-10T11:54:47Z
date_published: 2012-08-01T00:00:00Z
date_updated: 2021-01-12T08:17:43Z
day: '01'
doi: 10.1111/j.1574-6968.2012.02603.x
extern: '1'
external_id:
  pmid:
  - '22640011'
intvolume: '       333'
issue: '2'
language:
- iso: eng
month: '08'
oa_version: None
page: 109-120
pmid: 1
publication: FEMS Microbiology Letters
publication_identifier:
  issn:
  - 0378-1097
publication_status: published
publisher: Oxford University Press
quality_controlled: '1'
status: public
title: Deletion of hypothetical wall teichoic acid ligases in Staphylococcus aureus
  activates the cell wall stress response
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 333
year: '2012'
...
---
_id: '826'
abstract:
- lang: eng
  text: Plants exhibit a unique developmental flexibility to ever-changing environmental
    conditions. To achieve their profound adaptability, plants are able to maintain
    permanent stem cell populations and form new organs during the entire plant life
    cycle. Signaling substances, called plant hormones, such as auxin, cytokinin,
    abscisic acid, brassinosteroid, ethylene, gibberellin, jasmonic acid, and strigolactone,
    govern and coordinate these developmental processes. Physiological and genetic
    studies have dissected the molecular components of signal perception and transduction
    of the individual hormonal pathways. However, over recent years it has become
    evident that hormones do not act only in a linear pathway. Hormonal pathways are
    interconnected by a complex network of interactions and feedback circuits that
    determines the final outcome of the individual hormone actions. This raises questions
    about the molecular mechanisms underlying hormonal cross talk and about how these
    hormonal networks are established, maintained, and modulated throughout plant
    development.
acknowledgement: We would like to thank Annick Bleys for help in preparing the manuscript.
  This work was supported by the European Research Council with a Starting Independent
  Research grant (ERC-2007-Stg-207362-HCPO) and the project CZ.1.07/2.3.00/20.0043
  (to the Central European Institute of Technology, CEITEC) to E.B. M.V. is a postdoctoral
  fellow of the Research Foundation Flanders. We apologize that, because of space
  restrictions, the scientific contributions of only a limited number of original
  articles could be cited and discussed.
author:
- first_name: Marleen
  full_name: Vanstraelen, Marleen
  last_name: Vanstraelen
- first_name: Eva
  full_name: Eva Benková
  id: 38F4F166-F248-11E8-B48F-1D18A9856A87
  last_name: Benková
  orcid: 0000-0002-8510-9739
citation:
  ama: Vanstraelen M, Benková E. Hormonal interactions in the regulation of plant
    development. <i>Annual Review of Cell and Developmental Biology</i>. 2012;28:463-487.
    doi:<a href="https://doi.org/10.1146/annurev-cellbio-101011-155741">10.1146/annurev-cellbio-101011-155741</a>
  apa: Vanstraelen, M., &#38; Benková, E. (2012). Hormonal interactions in the regulation
    of plant development. <i>Annual Review of Cell and Developmental Biology</i>.
    Annual Reviews. <a href="https://doi.org/10.1146/annurev-cellbio-101011-155741">https://doi.org/10.1146/annurev-cellbio-101011-155741</a>
  chicago: Vanstraelen, Marleen, and Eva Benková. “Hormonal Interactions in the Regulation
    of Plant Development.” <i>Annual Review of Cell and Developmental Biology</i>.
    Annual Reviews, 2012. <a href="https://doi.org/10.1146/annurev-cellbio-101011-155741">https://doi.org/10.1146/annurev-cellbio-101011-155741</a>.
  ieee: M. Vanstraelen and E. Benková, “Hormonal interactions in the regulation of
    plant development,” <i>Annual Review of Cell and Developmental Biology</i>, vol.
    28. Annual Reviews, pp. 463–487, 2012.
  ista: Vanstraelen M, Benková E. 2012. Hormonal interactions in the regulation of
    plant development. Annual Review of Cell and Developmental Biology. 28, 463–487.
  mla: Vanstraelen, Marleen, and Eva Benková. “Hormonal Interactions in the Regulation
    of Plant Development.” <i>Annual Review of Cell and Developmental Biology</i>,
    vol. 28, Annual Reviews, 2012, pp. 463–87, doi:<a href="https://doi.org/10.1146/annurev-cellbio-101011-155741">10.1146/annurev-cellbio-101011-155741</a>.
  short: M. Vanstraelen, E. Benková, Annual Review of Cell and Developmental Biology
    28 (2012) 463–487.
date_created: 2018-12-11T11:48:43Z
date_published: 2012-11-01T00:00:00Z
date_updated: 2021-01-12T08:17:46Z
day: '01'
doi: 10.1146/annurev-cellbio-101011-155741
extern: 1
intvolume: '        28'
month: '11'
page: 463 - 487
publication: Annual Review of Cell and Developmental Biology
publication_status: published
publisher: Annual Reviews
publist_id: '6822'
quality_controlled: 0
status: public
title: Hormonal interactions in the regulation of plant development
type: journal_article
volume: 28
year: '2012'
...
---
_id: '829'
abstract:
- lang: eng
  text: The architecture of a plant's root system, established postembryonically,
    results from both coordinated root growth and lateral root branching. The plant
    hormones auxin and cytokinin are central endogenous signaling molecules that regulate
    lateral root organogenesis positively and negatively, respectively. Tight control
    and mutual balance of their antagonistic activities are particularly important
    during the early phases of lateral root organogenesis to ensure continuous lateral
    root initiation (LRI) and proper development of lateral root primordia (LRP).
    Here, we show that the early phases of lateral root organogenesis, including priming
    and initiation, take place in root zones with a repressed cytokinin response.
    Accordingly, ectopic overproduction of cytokinin in the root basal meristem most
    efficiently inhibits LRI. Enhanced cytokinin responses in pericycle cells between
    existing LRP might restrict LRI near existing LRP and, when compromised, ectopic
    LRI occurs. Furthermore, our results demonstrate that young LRP are more sensitive
    to perturbations in the cytokinin activity than are developmentally more advanced
    primordia. We hypothesize that the effect of cytokinin on the development of primordia
    possibly depends on the robustness and stability of the auxin gradient.
acknowledgement: We thank Jen Sheen, Dolf Weijers, Tatsuo Kakimoto, Stephen Depuydt,
  and Laurent Laplaze for sharing published material, Jiri Friml for discussions,
  and Martine De Cock and Annick Bleys for help in preparing the manuscript. This
  work was supported by a Starting Independent Research grant from the European Research
  Council (ERC-2007-Stg-207362-HCPO) and the project CZ.1.07/2.3.00/20.0043 to the
  Central European Institute of Technology to E.B. and grants from the Ministry of
  Education, Youth, and Sports of the Czech Republic (MSM 6198959216) and the Centre
  of the Region Haná for Biotechnological and Agricultural Research (ED0007/01/01)
  to P.T.
author:
- first_name: Agnieszka
  full_name: Bielach, Agnieszka
  last_name: Bielach
- first_name: Katerina
  full_name: Podlesakova, Katerina
  last_name: Podlesakova
- first_name: Peter
  full_name: Peter Marhavy
  id: 3F45B078-F248-11E8-B48F-1D18A9856A87
  last_name: Marhavy
  orcid: 0000-0001-5227-5741
- first_name: Jérôme
  full_name: Duclercq, Jérôme
  last_name: Duclercq
- first_name: Candela
  full_name: Candela Cuesta
  id: 33A3C818-F248-11E8-B48F-1D18A9856A87
  last_name: Cuesta
  orcid: 0000-0003-1923-2410
- first_name: Bruno
  full_name: Muller, Bruno
  last_name: Muller
- first_name: Wim
  full_name: Grunewald, Wim
  last_name: Grunewald
- first_name: Petr
  full_name: Tarkowski, Petr
  last_name: Tarkowski
- first_name: Eva
  full_name: Eva Benková
  id: 38F4F166-F248-11E8-B48F-1D18A9856A87
  last_name: Benková
  orcid: 0000-0002-8510-9739
citation:
  ama: Bielach A, Podlesakova K, Marhavý P, et al. Spatiotemporal regulation of lateral
    root organogenesis in Arabidopsis by cytokinin. <i>The Plant Cell</i>. 2012;24(10):3967-3981.
    doi:<a href="https://doi.org/10.1105/tpc.112.103044">10.1105/tpc.112.103044</a>
  apa: Bielach, A., Podlesakova, K., Marhavý, P., Duclercq, J., Cuesta, C., Muller,
    B., … Benková, E. (2012). Spatiotemporal regulation of lateral root organogenesis
    in Arabidopsis by cytokinin. <i>The Plant Cell</i>. American Society of Plant
    Biologists. <a href="https://doi.org/10.1105/tpc.112.103044">https://doi.org/10.1105/tpc.112.103044</a>
  chicago: Bielach, Agnieszka, Katerina Podlesakova, Peter Marhavý, Jérôme Duclercq,
    Candela Cuesta, Bruno Muller, Wim Grunewald, Petr Tarkowski, and Eva Benková.
    “Spatiotemporal Regulation of Lateral Root Organogenesis in Arabidopsis by Cytokinin.”
    <i>The Plant Cell</i>. American Society of Plant Biologists, 2012. <a href="https://doi.org/10.1105/tpc.112.103044">https://doi.org/10.1105/tpc.112.103044</a>.
  ieee: A. Bielach <i>et al.</i>, “Spatiotemporal regulation of lateral root organogenesis
    in Arabidopsis by cytokinin,” <i>The Plant Cell</i>, vol. 24, no. 10. American
    Society of Plant Biologists, pp. 3967–3981, 2012.
  ista: Bielach A, Podlesakova K, Marhavý P, Duclercq J, Cuesta C, Muller B, Grunewald
    W, Tarkowski P, Benková E. 2012. Spatiotemporal regulation of lateral root organogenesis
    in Arabidopsis by cytokinin. The Plant Cell. 24(10), 3967–3981.
  mla: Bielach, Agnieszka, et al. “Spatiotemporal Regulation of Lateral Root Organogenesis
    in Arabidopsis by Cytokinin.” <i>The Plant Cell</i>, vol. 24, no. 10, American
    Society of Plant Biologists, 2012, pp. 3967–81, doi:<a href="https://doi.org/10.1105/tpc.112.103044">10.1105/tpc.112.103044</a>.
  short: A. Bielach, K. Podlesakova, P. Marhavý, J. Duclercq, C. Cuesta, B. Muller,
    W. Grunewald, P. Tarkowski, E. Benková, The Plant Cell 24 (2012) 3967–3981.
date_created: 2018-12-11T11:48:43Z
date_published: 2012-10-01T00:00:00Z
date_updated: 2021-01-12T08:17:55Z
day: '01'
doi: 10.1105/tpc.112.103044
extern: 1
intvolume: '        24'
issue: '10'
month: '10'
page: 3967 - 3981
publication: The Plant Cell
publication_status: published
publisher: American Society of Plant Biologists
publist_id: '6819'
quality_controlled: 0
status: public
title: Spatiotemporal regulation of lateral root organogenesis in Arabidopsis by cytokinin
type: journal_article
volume: 24
year: '2012'
...
---
_id: '846'
abstract:
- lang: eng
  text: Whether or not evolutionary change is inherently irreversible remains a controversial
    topic. Some examples of evolutionary irreversibility are known; however, this
    question has not been comprehensively addressed at the molecular level. Here,
    we use data from 221 human genes with known pathogenic mutations to estimate the
    rate of irreversibility in protein evolution. For these genes, we reconstruct
    ancestral amino acid sequences along the mammalian phylogeny and identify ancestral
    amino acid states that match known pathogenic mutations. Such cases represent
    inherent evolutionary irreversibility because, at the present moment, reversals
    to these ancestral amino acid states are impossible for the human lineage. We
    estimate that approximately 10% of all amino acid substitutions along the mammalian
    phylogeny are irreversible, such that a return to the ancestral amino acid state
    would lead to a pathogenic phenotype. For a subset of 51 genes with high rates
    of irreversibility, as much as 40% of all amino acid evolution was estimated to
    be irreversible. Because pathogenic phenotypes do not resemble ancestral phenotypes,
    the molecular nature of the high rate of irreversibility in proteins is best explained
    by evolution with a high prevalence of compensatory, epistatic interactions between
    amino acid sites. Under such mode of protein evolution, once an amino acid substitution
    is fixed, the probability of its reversal declines as the protein sequence accumulates
    changes that affect the phenotypic manifestation of the ancestral state. The prevalence
    of epistasis in evolution indicates that the observed high rate of irreversibility
    in protein evolution is an inherent property of protein structure and function.
acknowledgement: This work was supported by Plan Nacional grant BFU2009-09271 from
  the Spanish Ministry of Science and Innovation and by FPU (Formación del Profesorado
  Universitario) program grant AP2008-01888 from the Spanish Ministry of Education
  to O.S. F.A.K. is a European Molecular Biology Organization Young Investigator and
  Howard Hughes Medical Institute International Early Career Scientist.
author:
- first_name: Onuralp
  full_name: Soylemez, Onuralp
  last_name: Soylemez
- first_name: Fyodor
  full_name: Fyodor Kondrashov
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
citation:
  ama: Soylemez O, Kondrashov F. Estimating the rate of irreversibility in protein
    evolution. <i>Genome Biology and Evolution</i>. 2012;4(12):1213-1222. doi:<a href="https://doi.org/10.1093/gbe/evs096">10.1093/gbe/evs096</a>
  apa: Soylemez, O., &#38; Kondrashov, F. (2012). Estimating the rate of irreversibility
    in protein evolution. <i>Genome Biology and Evolution</i>. Oxford University Press.
    <a href="https://doi.org/10.1093/gbe/evs096">https://doi.org/10.1093/gbe/evs096</a>
  chicago: Soylemez, Onuralp, and Fyodor Kondrashov. “Estimating the Rate of Irreversibility
    in Protein Evolution.” <i>Genome Biology and Evolution</i>. Oxford University
    Press, 2012. <a href="https://doi.org/10.1093/gbe/evs096">https://doi.org/10.1093/gbe/evs096</a>.
  ieee: O. Soylemez and F. Kondrashov, “Estimating the rate of irreversibility in
    protein evolution,” <i>Genome Biology and Evolution</i>, vol. 4, no. 12. Oxford
    University Press, pp. 1213–1222, 2012.
  ista: Soylemez O, Kondrashov F. 2012. Estimating the rate of irreversibility in
    protein evolution. Genome Biology and Evolution. 4(12), 1213–1222.
  mla: Soylemez, Onuralp, and Fyodor Kondrashov. “Estimating the Rate of Irreversibility
    in Protein Evolution.” <i>Genome Biology and Evolution</i>, vol. 4, no. 12, Oxford
    University Press, 2012, pp. 1213–22, doi:<a href="https://doi.org/10.1093/gbe/evs096">10.1093/gbe/evs096</a>.
  short: O. Soylemez, F. Kondrashov, Genome Biology and Evolution 4 (2012) 1213–1222.
date_created: 2018-12-11T11:48:49Z
date_published: 2012-01-01T00:00:00Z
date_updated: 2021-01-12T08:19:25Z
day: '01'
doi: 10.1093/gbe/evs096
extern: 1
intvolume: '         4'
issue: '12'
month: '01'
page: 1213 - 1222
publication: Genome Biology and Evolution
publication_status: published
publisher: Oxford University Press
publist_id: '6802'
quality_controlled: 0
status: public
title: Estimating the rate of irreversibility in protein evolution
tmp:
  image: /images/cc_by_nc.png
  legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
  name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
  short: CC BY-NC (4.0)
type: journal_article
volume: 4
year: '2012'
...
---
_id: '8463'
abstract:
- lang: eng
  text: The 1H dipolar network, which is the major obstacle for applying proton detection
    in the solid-state, can be reduced by deuteration, employing the RAP (Reduced
    Adjoining Protonation) labeling scheme, which yields random protonation at non-exchangeable
    sites. We present here a systematic study on the optimal degree of random sidechain
    protonation in RAP samples as a function of the MAS (magic angle spinning) frequency.
    In particular, we compare 1H sensitivity and linewidth of a microcrystalline protein,
    the SH3 domain of chicken α-spectrin, for samples, prepared with 5–25 % H2O in
    the E. coli growth medium, in the MAS frequency range of 20–60 kHz. At an external
    field of 19.96 T (850 MHz), we find that using a proton concentration between
    15 and 25 % in the M9 medium yields the best compromise in terms of sensitivity
    and resolution, with an achievable average 1H linewidth on the order of 40–50
    Hz. Comparing sensitivities at a MAS frequency of 60 versus 20 kHz, a gain in
    sensitivity by a factor of 4–4.5 is observed in INEPT-based 1H detected 1D 1H,13C
    correlation experiments. In total, we find that spectra recorded with a 1.3 mm
    rotor at 60 kHz have almost the same sensitivity as spectra recorded with a fully
    packed 3.2 mm rotor at 20 kHz, even though ~20× less material is employed. The
    improved sensitivity is attributed to 1H line narrowing due to fast MAS and to
    the increased efficiency of the 1.3 mm coil.
article_processing_charge: No
article_type: original
author:
- first_name: Sam
  full_name: Asami, Sam
  last_name: Asami
- first_name: Kathrin
  full_name: Szekely, Kathrin
  last_name: Szekely
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Beat H.
  full_name: Meier, Beat H.
  last_name: Meier
- first_name: Bernd
  full_name: Reif, Bernd
  last_name: Reif
citation:
  ama: Asami S, Szekely K, Schanda P, Meier BH, Reif B. Optimal degree of protonation
    for 1H detection of aliphatic sites in randomly deuterated proteins as a function
    of the MAS frequency. <i>Journal of Biomolecular NMR</i>. 2012;54(2):155-168.
    doi:<a href="https://doi.org/10.1007/s10858-012-9659-9">10.1007/s10858-012-9659-9</a>
  apa: Asami, S., Szekely, K., Schanda, P., Meier, B. H., &#38; Reif, B. (2012). Optimal
    degree of protonation for 1H detection of aliphatic sites in randomly deuterated
    proteins as a function of the MAS frequency. <i>Journal of Biomolecular NMR</i>.
    Springer Nature. <a href="https://doi.org/10.1007/s10858-012-9659-9">https://doi.org/10.1007/s10858-012-9659-9</a>
  chicago: Asami, Sam, Kathrin Szekely, Paul Schanda, Beat H. Meier, and Bernd Reif.
    “Optimal Degree of Protonation for 1H Detection of Aliphatic Sites in Randomly
    Deuterated Proteins as a Function of the MAS Frequency.” <i>Journal of Biomolecular
    NMR</i>. Springer Nature, 2012. <a href="https://doi.org/10.1007/s10858-012-9659-9">https://doi.org/10.1007/s10858-012-9659-9</a>.
  ieee: S. Asami, K. Szekely, P. Schanda, B. H. Meier, and B. Reif, “Optimal degree
    of protonation for 1H detection of aliphatic sites in randomly deuterated proteins
    as a function of the MAS frequency,” <i>Journal of Biomolecular NMR</i>, vol.
    54, no. 2. Springer Nature, pp. 155–168, 2012.
  ista: Asami S, Szekely K, Schanda P, Meier BH, Reif B. 2012. Optimal degree of protonation
    for 1H detection of aliphatic sites in randomly deuterated proteins as a function
    of the MAS frequency. Journal of Biomolecular NMR. 54(2), 155–168.
  mla: Asami, Sam, et al. “Optimal Degree of Protonation for 1H Detection of Aliphatic
    Sites in Randomly Deuterated Proteins as a Function of the MAS Frequency.” <i>Journal
    of Biomolecular NMR</i>, vol. 54, no. 2, Springer Nature, 2012, pp. 155–68, doi:<a
    href="https://doi.org/10.1007/s10858-012-9659-9">10.1007/s10858-012-9659-9</a>.
  short: S. Asami, K. Szekely, P. Schanda, B.H. Meier, B. Reif, Journal of Biomolecular
    NMR 54 (2012) 155–168.
date_created: 2020-09-18T10:09:18Z
date_published: 2012-08-23T00:00:00Z
date_updated: 2021-01-12T08:19:27Z
day: '23'
doi: 10.1007/s10858-012-9659-9
extern: '1'
intvolume: '        54'
issue: '2'
language:
- iso: eng
month: '08'
oa_version: None
page: 155-168
publication: Journal of Biomolecular NMR
publication_identifier:
  issn:
  - 0925-2738
  - 1573-5001
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Optimal degree of protonation for 1H detection of aliphatic sites in randomly
  deuterated proteins as a function of the MAS frequency
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 54
year: '2012'
...
---
_id: '8465'
abstract:
- lang: eng
  text: We demonstrate that conformational exchange processes in proteins on microsecond-to-millisecond
    time scales can be detected and quantified by solid-state NMR spectroscopy. We
    show two independent approaches that measure the effect of conformational exchange
    on transverse relaxation parameters, namely Carr–Purcell–Meiboom–Gill relaxation-dispersion
    experiments and measurement of differential multiple-quantum coherence decay.
    Long coherence lifetimes, as required for these experiments, are achieved by the
    use of highly deuterated samples and fast magic-angle spinning. The usefulness
    of the approaches is demonstrated by application to microcrystalline ubiquitin.
    We detect a conformational exchange process in a region of the protein for which
    dynamics have also been observed in solution. Interestingly, quantitative analysis
    of the data reveals that the exchange process is more than 1 order of magnitude
    slower than in solution, and this points to the impact of the crystalline environment
    on free energy barriers.
article_processing_charge: No
article_type: original
author:
- first_name: Martin
  full_name: Tollinger, Martin
  last_name: Tollinger
- first_name: Astrid C.
  full_name: Sivertsen, Astrid C.
  last_name: Sivertsen
- first_name: Beat H.
  full_name: Meier, Beat H.
  last_name: Meier
- first_name: Matthias
  full_name: Ernst, Matthias
  last_name: Ernst
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. Site-resolved measurement
    of microsecond-to-millisecond conformational-exchange processes in proteins by
    solid-state NMR spectroscopy. <i>Journal of the American Chemical Society</i>.
    2012;134(36):14800-14807. doi:<a href="https://doi.org/10.1021/ja303591y">10.1021/ja303591y</a>
  apa: Tollinger, M., Sivertsen, A. C., Meier, B. H., Ernst, M., &#38; Schanda, P.
    (2012). Site-resolved measurement of microsecond-to-millisecond conformational-exchange
    processes in proteins by solid-state NMR spectroscopy. <i>Journal of the American
    Chemical Society</i>. American Chemical Society. <a href="https://doi.org/10.1021/ja303591y">https://doi.org/10.1021/ja303591y</a>
  chicago: Tollinger, Martin, Astrid C. Sivertsen, Beat H. Meier, Matthias Ernst,
    and Paul Schanda. “Site-Resolved Measurement of Microsecond-to-Millisecond Conformational-Exchange
    Processes in Proteins by Solid-State NMR Spectroscopy.” <i>Journal of the American
    Chemical Society</i>. American Chemical Society, 2012. <a href="https://doi.org/10.1021/ja303591y">https://doi.org/10.1021/ja303591y</a>.
  ieee: M. Tollinger, A. C. Sivertsen, B. H. Meier, M. Ernst, and P. Schanda, “Site-resolved
    measurement of microsecond-to-millisecond conformational-exchange processes in
    proteins by solid-state NMR spectroscopy,” <i>Journal of the American Chemical
    Society</i>, vol. 134, no. 36. American Chemical Society, pp. 14800–14807, 2012.
  ista: Tollinger M, Sivertsen AC, Meier BH, Ernst M, Schanda P. 2012. Site-resolved
    measurement of microsecond-to-millisecond conformational-exchange processes in
    proteins by solid-state NMR spectroscopy. Journal of the American Chemical Society.
    134(36), 14800–14807.
  mla: Tollinger, Martin, et al. “Site-Resolved Measurement of Microsecond-to-Millisecond
    Conformational-Exchange Processes in Proteins by Solid-State NMR Spectroscopy.”
    <i>Journal of the American Chemical Society</i>, vol. 134, no. 36, American Chemical
    Society, 2012, pp. 14800–07, doi:<a href="https://doi.org/10.1021/ja303591y">10.1021/ja303591y</a>.
  short: M. Tollinger, A.C. Sivertsen, B.H. Meier, M. Ernst, P. Schanda, Journal of
    the American Chemical Society 134 (2012) 14800–14807.
date_created: 2020-09-18T10:10:20Z
date_published: 2012-08-21T00:00:00Z
date_updated: 2021-01-12T08:19:27Z
day: '21'
doi: 10.1021/ja303591y
extern: '1'
intvolume: '       134'
issue: '36'
language:
- iso: eng
month: '08'
oa_version: None
page: 14800-14807
publication: Journal of the American Chemical Society
publication_identifier:
  issn:
  - 0002-7863
  - 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Site-resolved measurement of microsecond-to-millisecond conformational-exchange
  processes in proteins by solid-state NMR spectroscopy
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
year: '2012'
...
---
_id: '8466'
abstract:
- lang: eng
  text: Recent advances in NMR spectroscopy and the availability of high magnetic
    field strengths now offer the possibility to record real-time 3D NMR spectra of
    short-lived protein states, e.g., states that become transiently populated during
    protein folding. Here we present a strategy for obtaining sequential NMR assignments
    as well as atom-resolved information on structural and dynamic features within
    a folding intermediate of the amyloidogenic protein β2-microglobulin that has
    a half-lifetime of only 20 min.
article_processing_charge: No
article_type: original
author:
- first_name: Enrico
  full_name: Rennella, Enrico
  last_name: Rennella
- first_name: Thomas
  full_name: Cutuil, Thomas
  last_name: Cutuil
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: Isabel
  full_name: Ayala, Isabel
  last_name: Ayala
- first_name: Vincent
  full_name: Forge, Vincent
  last_name: Forge
- first_name: Bernhard
  full_name: Brutscher, Bernhard
  last_name: Brutscher
citation:
  ama: Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. Real-time NMR
    characterization of structure and dynamics in a transiently populated protein
    folding intermediate. <i>Journal of the American Chemical Society</i>. 2012;134(19):8066-8069.
    doi:<a href="https://doi.org/10.1021/ja302598j">10.1021/ja302598j</a>
  apa: Rennella, E., Cutuil, T., Schanda, P., Ayala, I., Forge, V., &#38; Brutscher,
    B. (2012). Real-time NMR characterization of structure and dynamics in a transiently
    populated protein folding intermediate. <i>Journal of the American Chemical Society</i>.
    American Chemical Society. <a href="https://doi.org/10.1021/ja302598j">https://doi.org/10.1021/ja302598j</a>
  chicago: Rennella, Enrico, Thomas Cutuil, Paul Schanda, Isabel Ayala, Vincent Forge,
    and Bernhard Brutscher. “Real-Time NMR Characterization of Structure and Dynamics
    in a Transiently Populated Protein Folding Intermediate.” <i>Journal of the American
    Chemical Society</i>. American Chemical Society, 2012. <a href="https://doi.org/10.1021/ja302598j">https://doi.org/10.1021/ja302598j</a>.
  ieee: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, and B. Brutscher,
    “Real-time NMR characterization of structure and dynamics in a transiently populated
    protein folding intermediate,” <i>Journal of the American Chemical Society</i>,
    vol. 134, no. 19. American Chemical Society, pp. 8066–8069, 2012.
  ista: Rennella E, Cutuil T, Schanda P, Ayala I, Forge V, Brutscher B. 2012. Real-time
    NMR characterization of structure and dynamics in a transiently populated protein
    folding intermediate. Journal of the American Chemical Society. 134(19), 8066–8069.
  mla: Rennella, Enrico, et al. “Real-Time NMR Characterization of Structure and Dynamics
    in a Transiently Populated Protein Folding Intermediate.” <i>Journal of the American
    Chemical Society</i>, vol. 134, no. 19, American Chemical Society, 2012, pp. 8066–69,
    doi:<a href="https://doi.org/10.1021/ja302598j">10.1021/ja302598j</a>.
  short: E. Rennella, T. Cutuil, P. Schanda, I. Ayala, V. Forge, B. Brutscher, Journal
    of the American Chemical Society 134 (2012) 8066–8069.
date_created: 2020-09-18T10:10:28Z
date_published: 2012-05-03T00:00:00Z
date_updated: 2021-01-12T08:19:28Z
day: '03'
doi: 10.1021/ja302598j
extern: '1'
intvolume: '       134'
issue: '19'
language:
- iso: eng
month: '05'
oa_version: None
page: 8066-8069
publication: Journal of the American Chemical Society
publication_identifier:
  issn:
  - 0002-7863
  - 1520-5126
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
status: public
title: Real-time NMR characterization of structure and dynamics in a transiently populated
  protein folding intermediate
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 134
year: '2012'
...
---
_id: '8467'
abstract:
- lang: eng
  text: Partial deuteration is a powerful tool to increase coherence life times and
    spectral resolution in proton solid-state NMR. The J coupling to deuterium needs,
    however, to be decoupled to maintain the good resolution in the (usually indirect)
    13C dimension(s). We present a simple and reversible way to expand a commercial
    1.3 mm HCN MAS probe with a 2H channel with sufficient field strength for J-decoupling
    of deuterium, namely 2–3 kHz. The coil is placed at the outside of the stator
    and requires no significant modifications to the probe. The performance and the
    realizable gains in sensitivity and resolution are demonstrated using perdeuterated
    ubiquitin, with selectively CHD2-labeled methyl groups.
article_processing_charge: No
article_type: original
author:
- first_name: Matthias
  full_name: Huber, Matthias
  last_name: Huber
- first_name: Oliver
  full_name: With, Oliver
  last_name: With
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
- first_name: René
  full_name: Verel, René
  last_name: Verel
- first_name: Matthias
  full_name: Ernst, Matthias
  last_name: Ernst
- first_name: Beat H.
  full_name: Meier, Beat H.
  last_name: Meier
citation:
  ama: Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. A supplementary coil
    for 2H decoupling with commercial HCN MAS probes. <i>Journal of Magnetic Resonance</i>.
    2012;214:76-80. doi:<a href="https://doi.org/10.1016/j.jmr.2011.10.010">10.1016/j.jmr.2011.10.010</a>
  apa: Huber, M., With, O., Schanda, P., Verel, R., Ernst, M., &#38; Meier, B. H.
    (2012). A supplementary coil for 2H decoupling with commercial HCN MAS probes.
    <i>Journal of Magnetic Resonance</i>. Elsevier. <a href="https://doi.org/10.1016/j.jmr.2011.10.010">https://doi.org/10.1016/j.jmr.2011.10.010</a>
  chicago: Huber, Matthias, Oliver With, Paul Schanda, René Verel, Matthias Ernst,
    and Beat H. Meier. “A Supplementary Coil for 2H Decoupling with Commercial HCN
    MAS Probes.” <i>Journal of Magnetic Resonance</i>. Elsevier, 2012. <a href="https://doi.org/10.1016/j.jmr.2011.10.010">https://doi.org/10.1016/j.jmr.2011.10.010</a>.
  ieee: M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, and B. H. Meier, “A supplementary
    coil for 2H decoupling with commercial HCN MAS probes,” <i>Journal of Magnetic
    Resonance</i>, vol. 214. Elsevier, pp. 76–80, 2012.
  ista: Huber M, With O, Schanda P, Verel R, Ernst M, Meier BH. 2012. A supplementary
    coil for 2H decoupling with commercial HCN MAS probes. Journal of Magnetic Resonance.
    214, 76–80.
  mla: Huber, Matthias, et al. “A Supplementary Coil for 2H Decoupling with Commercial
    HCN MAS Probes.” <i>Journal of Magnetic Resonance</i>, vol. 214, Elsevier, 2012,
    pp. 76–80, doi:<a href="https://doi.org/10.1016/j.jmr.2011.10.010">10.1016/j.jmr.2011.10.010</a>.
  short: M. Huber, O. With, P. Schanda, R. Verel, M. Ernst, B.H. Meier, Journal of
    Magnetic Resonance 214 (2012) 76–80.
date_created: 2020-09-18T10:10:36Z
date_published: 2012-01-01T00:00:00Z
date_updated: 2021-01-12T08:19:28Z
day: '01'
doi: 10.1016/j.jmr.2011.10.010
extern: '1'
intvolume: '       214'
language:
- iso: eng
month: '01'
oa_version: None
page: 76-80
publication: Journal of Magnetic Resonance
publication_identifier:
  issn:
  - 1090-7807
publication_status: published
publisher: Elsevier
quality_controlled: '1'
status: public
title: A supplementary coil for 2H decoupling with commercial HCN MAS probes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 214
year: '2012'
...
---
_id: '8502'
abstract:
- lang: eng
  text: 'The famous ergodic hypothesis suggests that for a typical Hamiltonian on
    a typical energy surface nearly all trajectories are dense. KAM theory disproves
    it. Ehrenfest (The Conceptual Foundations of the Statistical Approach in Mechanics.
    Ithaca, NY: Cornell University Press, 1959) and Birkhoff (Collected Math Papers.
    Vol 2, New York: Dover, pp 462–465, 1968) stated the quasi-ergodic hypothesis
    claiming that a typical Hamiltonian on a typical energy surface has a dense orbit.
    This question is wide open. Herman (Proceedings of the International Congress
    of Mathematicians, Vol II (Berlin, 1998). Doc Math 1998, Extra Vol II, Berlin:
    Int Math Union, pp 797–808, 1998) proposed to look for an example of a Hamiltonian
    near H0(I)=⟨I,I⟩2 with a dense orbit on the unit energy surface. In this paper
    we construct a Hamiltonian H0(I)+εH1(θ,I,ε) which has an orbit dense in a set
    of maximal Hausdorff dimension equal to 5 on the unit energy surface.'
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: Maria
  full_name: Saprykina, Maria
  last_name: Saprykina
citation:
  ama: Kaloshin V, Saprykina M. An example of a nearly integrable Hamiltonian system
    with a trajectory dense in a set of maximal Hausdorff dimension. <i>Communications
    in Mathematical Physics</i>. 2012;315(3):643-697. doi:<a href="https://doi.org/10.1007/s00220-012-1532-x">10.1007/s00220-012-1532-x</a>
  apa: Kaloshin, V., &#38; Saprykina, M. (2012). An example of a nearly integrable
    Hamiltonian system with a trajectory dense in a set of maximal Hausdorff dimension.
    <i>Communications in Mathematical Physics</i>. Springer Nature. <a href="https://doi.org/10.1007/s00220-012-1532-x">https://doi.org/10.1007/s00220-012-1532-x</a>
  chicago: Kaloshin, Vadim, and Maria Saprykina. “An Example of a Nearly Integrable
    Hamiltonian System with a Trajectory Dense in a Set of Maximal Hausdorff Dimension.”
    <i>Communications in Mathematical Physics</i>. Springer Nature, 2012. <a href="https://doi.org/10.1007/s00220-012-1532-x">https://doi.org/10.1007/s00220-012-1532-x</a>.
  ieee: V. Kaloshin and M. Saprykina, “An example of a nearly integrable Hamiltonian
    system with a trajectory dense in a set of maximal Hausdorff dimension,” <i>Communications
    in Mathematical Physics</i>, vol. 315, no. 3. Springer Nature, pp. 643–697, 2012.
  ista: Kaloshin V, Saprykina M. 2012. An example of a nearly integrable Hamiltonian
    system with a trajectory dense in a set of maximal Hausdorff dimension. Communications
    in Mathematical Physics. 315(3), 643–697.
  mla: Kaloshin, Vadim, and Maria Saprykina. “An Example of a Nearly Integrable Hamiltonian
    System with a Trajectory Dense in a Set of Maximal Hausdorff Dimension.” <i>Communications
    in Mathematical Physics</i>, vol. 315, no. 3, Springer Nature, 2012, pp. 643–97,
    doi:<a href="https://doi.org/10.1007/s00220-012-1532-x">10.1007/s00220-012-1532-x</a>.
  short: V. Kaloshin, M. Saprykina, Communications in Mathematical Physics 315 (2012)
    643–697.
date_created: 2020-09-18T10:47:16Z
date_published: 2012-11-01T00:00:00Z
date_updated: 2021-01-12T08:19:44Z
day: '01'
doi: 10.1007/s00220-012-1532-x
extern: '1'
intvolume: '       315'
issue: '3'
keyword:
- Mathematical Physics
- Statistical and Nonlinear Physics
language:
- iso: eng
month: '11'
oa_version: None
page: 643-697
publication: Communications in Mathematical Physics
publication_identifier:
  issn:
  - 0010-3616
  - 1432-0916
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: An example of a nearly integrable Hamiltonian system with a trajectory dense
  in a set of maximal Hausdorff dimension
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 315
year: '2012'
...
---
_id: '8503'
abstract:
- lang: eng
  text: We prove there are finitely many isometry classes of planar central configurations
    (also called relative equilibria) in the Newtonian 5-body problem, except perhaps
    if the 5-tuple of positive masses belongs to a given codimension 2 subvariety
    of the mass space.
article_processing_charge: No
article_type: original
author:
- first_name: Alain
  full_name: Albouy, Alain
  last_name: Albouy
- first_name: Vadim
  full_name: Kaloshin, Vadim
  id: FE553552-CDE8-11E9-B324-C0EBE5697425
  last_name: Kaloshin
  orcid: 0000-0002-6051-2628
citation:
  ama: Albouy A, Kaloshin V. Finiteness of central configurations of five bodies in
    the plane. <i>Annals of Mathematics</i>. 2012;176(1):535-588. doi:<a href="https://doi.org/10.4007/annals.2012.176.1.10">10.4007/annals.2012.176.1.10</a>
  apa: Albouy, A., &#38; Kaloshin, V. (2012). Finiteness of central configurations
    of five bodies in the plane. <i>Annals of Mathematics</i>. Princeton University
    Press. <a href="https://doi.org/10.4007/annals.2012.176.1.10">https://doi.org/10.4007/annals.2012.176.1.10</a>
  chicago: Albouy, Alain, and Vadim Kaloshin. “Finiteness of Central Configurations
    of Five Bodies in the Plane.” <i>Annals of Mathematics</i>. Princeton University
    Press, 2012. <a href="https://doi.org/10.4007/annals.2012.176.1.10">https://doi.org/10.4007/annals.2012.176.1.10</a>.
  ieee: A. Albouy and V. Kaloshin, “Finiteness of central configurations of five bodies
    in the plane,” <i>Annals of Mathematics</i>, vol. 176, no. 1. Princeton University
    Press, pp. 535–588, 2012.
  ista: Albouy A, Kaloshin V. 2012. Finiteness of central configurations of five bodies
    in the plane. Annals of Mathematics. 176(1), 535–588.
  mla: Albouy, Alain, and Vadim Kaloshin. “Finiteness of Central Configurations of
    Five Bodies in the Plane.” <i>Annals of Mathematics</i>, vol. 176, no. 1, Princeton
    University Press, 2012, pp. 535–88, doi:<a href="https://doi.org/10.4007/annals.2012.176.1.10">10.4007/annals.2012.176.1.10</a>.
  short: A. Albouy, V. Kaloshin, Annals of Mathematics 176 (2012) 535–588.
date_created: 2020-09-18T10:47:24Z
date_published: 2012-07-01T00:00:00Z
date_updated: 2021-01-12T08:19:44Z
day: '01'
doi: 10.4007/annals.2012.176.1.10
extern: '1'
intvolume: '       176'
issue: '1'
language:
- iso: eng
month: '07'
oa_version: None
page: 535-588
publication: Annals of Mathematics
publication_identifier:
  issn:
  - 0003-486X
publication_status: published
publisher: Princeton University Press
quality_controlled: '1'
status: public
title: Finiteness of central configurations of five bodies in the plane
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 176
year: '2012'
...
---
_id: '8504'
abstract:
- lang: eng
  text: In this paper we present a surprising example of a Cr unimodal map of an interval
    f:I→I whose number of periodic points Pn(f)=∣{x∈I:fnx=x}∣ grows faster than any
    ahead given sequence along a subsequence nk=3k. This example also shows that ‘non-flatness’
    of critical points is necessary for the Martens–de Melo–van Strien theorem [M.
    Martens, W. de Melo and S. van Strien. Julia–Fatou–Sullivan theory for real one-dimensional
    dynamics. Acta Math.168(3–4) (1992), 273–318] to hold.
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: O. S.
  full_name: KOZLOVSKI, O. S.
  last_name: KOZLOVSKI
citation:
  ama: Kaloshin V, KOZLOVSKI OS. A Cr unimodal map with an arbitrary fast growth of
    the number of periodic points. <i>Ergodic Theory and Dynamical Systems</i>. 2012;32(1):159-165.
    doi:<a href="https://doi.org/10.1017/s0143385710000817">10.1017/s0143385710000817</a>
  apa: Kaloshin, V., &#38; KOZLOVSKI, O. S. (2012). A Cr unimodal map with an arbitrary
    fast growth of the number of periodic points. <i>Ergodic Theory and Dynamical
    Systems</i>. Cambridge University Press. <a href="https://doi.org/10.1017/s0143385710000817">https://doi.org/10.1017/s0143385710000817</a>
  chicago: Kaloshin, Vadim, and O. S. KOZLOVSKI. “A Cr Unimodal Map with an Arbitrary
    Fast Growth of the Number of Periodic Points.” <i>Ergodic Theory and Dynamical
    Systems</i>. Cambridge University Press, 2012. <a href="https://doi.org/10.1017/s0143385710000817">https://doi.org/10.1017/s0143385710000817</a>.
  ieee: V. Kaloshin and O. S. KOZLOVSKI, “A Cr unimodal map with an arbitrary fast
    growth of the number of periodic points,” <i>Ergodic Theory and Dynamical Systems</i>,
    vol. 32, no. 1. Cambridge University Press, pp. 159–165, 2012.
  ista: Kaloshin V, KOZLOVSKI OS. 2012. A Cr unimodal map with an arbitrary fast growth
    of the number of periodic points. Ergodic Theory and Dynamical Systems. 32(1),
    159–165.
  mla: Kaloshin, Vadim, and O. S. KOZLOVSKI. “A Cr Unimodal Map with an Arbitrary
    Fast Growth of the Number of Periodic Points.” <i>Ergodic Theory and Dynamical
    Systems</i>, vol. 32, no. 1, Cambridge University Press, 2012, pp. 159–65, doi:<a
    href="https://doi.org/10.1017/s0143385710000817">10.1017/s0143385710000817</a>.
  short: V. Kaloshin, O.S. KOZLOVSKI, Ergodic Theory and Dynamical Systems 32 (2012)
    159–165.
date_created: 2020-09-18T10:47:33Z
date_published: 2012-02-01T00:00:00Z
date_updated: 2021-01-12T08:19:44Z
day: '01'
doi: 10.1017/s0143385710000817
extern: '1'
intvolume: '        32'
issue: '1'
keyword:
- Applied Mathematics
- General Mathematics
language:
- iso: eng
month: '02'
oa_version: None
page: 159-165
publication: Ergodic Theory and Dynamical Systems
publication_identifier:
  issn:
  - 0143-3857
  - 1469-4417
publication_status: published
publisher: Cambridge University Press
quality_controlled: '1'
status: public
title: A Cr unimodal map with an arbitrary fast growth of the number of periodic points
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2012'
...
---
_id: '858'
abstract:
- lang: eng
  text: 'ackground: The evolution and genomic stop codon frequencies have not been
    rigorously studied with the exception of coding of non-canonical amino acids.
    Here we study the rate of evolution and frequency distribution of stop codons
    in bacterial genomes.Results: We show that in bacteria stop codons evolve slower
    than synonymous sites, suggesting the action of weak negative selection. However,
    the frequency of stop codons relative to genomic nucleotide content indicated
    that this selection regime is not straightforward. The frequency of TAA and TGA
    stop codons is GC-content dependent, with TAA decreasing and TGA increasing with
    GC-content, while TAG frequency is independent of GC-content. Applying a formal,
    analytical model to these data we found that the relationship between stop codon
    frequencies and nucleotide content cannot be explained by mutational biases or
    selection on nucleotide content. However, with weak nucleotide content-dependent
    selection on TAG, -0.5 < Nes < 1.5, the model fits all of the data and recapitulates
    the relationship between TAG and nucleotide content. For biologically plausible
    rates of mutations we show that, in bacteria, TAG stop codon is universally associated
    with lower fitness, with TAA being the optimal for G-content < 16% while for G-content
    > 16% TGA has a higher fitness than TAG.Conclusions: Our data indicate that TAG
    codon is universally suboptimal in the bacterial lineage, such that TAA is likely
    to be the preferred stop codon for low GC content while the TGA is the preferred
    stop codon for high GC content. The optimization of stop codon usage may therefore
    be useful in genome engineering or gene expression optimization applications.Reviewers:
    This article was reviewed by Michail Gelfand, Arcady Mushegian and Shamil Sunyaev.
    For the full reviews, please go to the Reviewers'' Comments section.'
acknowledgement: |
  We thank Elena Alkalaeva and Peter Kolosov for insightful discussion and Brian Charlesworth for a critical reading of our manuscript. The work has been supported by a Plan Nacional grant from the Spanish Ministry of Science and Innovation, EMBO Young Investigator and Howard Hughes Medical Institute International Early Career Scientist awards.
author:
- first_name: Inna
  full_name: Povolotskaya, Inna
  last_name: Povolotskaya
- first_name: Fyodor
  full_name: Fyodor Kondrashov
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
- first_name: Alice
  full_name: Ledda, Alice
  last_name: Ledda
- first_name: Peter
  full_name: Vlasov, Peter K
  last_name: Vlasov
citation:
  ama: Povolotskaya I, Kondrashov F, Ledda A, Vlasov P. Stop codons in bacteria are
    not selectively equivalent. <i>Biology Direct</i>. 2012;7. doi:<a href="https://doi.org/10.1186/1745-6150-7-30">10.1186/1745-6150-7-30</a>
  apa: Povolotskaya, I., Kondrashov, F., Ledda, A., &#38; Vlasov, P. (2012). Stop
    codons in bacteria are not selectively equivalent. <i>Biology Direct</i>. BioMed
    Central. <a href="https://doi.org/10.1186/1745-6150-7-30">https://doi.org/10.1186/1745-6150-7-30</a>
  chicago: Povolotskaya, Inna, Fyodor Kondrashov, Alice Ledda, and Peter Vlasov. “Stop
    Codons in Bacteria Are Not Selectively Equivalent.” <i>Biology Direct</i>. BioMed
    Central, 2012. <a href="https://doi.org/10.1186/1745-6150-7-30">https://doi.org/10.1186/1745-6150-7-30</a>.
  ieee: I. Povolotskaya, F. Kondrashov, A. Ledda, and P. Vlasov, “Stop codons in bacteria
    are not selectively equivalent,” <i>Biology Direct</i>, vol. 7. BioMed Central,
    2012.
  ista: Povolotskaya I, Kondrashov F, Ledda A, Vlasov P. 2012. Stop codons in bacteria
    are not selectively equivalent. Biology Direct. 7.
  mla: Povolotskaya, Inna, et al. “Stop Codons in Bacteria Are Not Selectively Equivalent.”
    <i>Biology Direct</i>, vol. 7, BioMed Central, 2012, doi:<a href="https://doi.org/10.1186/1745-6150-7-30">10.1186/1745-6150-7-30</a>.
  short: I. Povolotskaya, F. Kondrashov, A. Ledda, P. Vlasov, Biology Direct 7 (2012).
date_created: 2018-12-11T11:48:52Z
date_published: 2012-09-01T00:00:00Z
date_updated: 2021-01-12T08:20:08Z
day: '01'
doi: 10.1186/1745-6150-7-30
extern: 1
intvolume: '         7'
month: '09'
publication: Biology Direct
publication_status: published
publisher: BioMed Central
publist_id: '6792'
quality_controlled: 0
status: public
title: Stop codons in bacteria are not selectively equivalent
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
volume: 7
year: '2012'
...
---
_id: '887'
abstract:
- lang: eng
  text: A subject of extensive study in evolutionary theory has been the issue of
    how neutral, redundant copies can be maintained in the genome for long periods
    of time. Concurrently, examples of adaptive gene duplications to various environmental
    conditions in different species have been described. At this point, it is too
    early to tell whether or not a substantial fraction of gene copies have initially
    achieved fixation by positive selection for increased dosage. Nevertheless, enough
    examples have accumulated in the literature that such a possibility should be
    considered. Here, I review the recent examples of adaptive gene duplications and
    make an attempt to draw generalizations on what types of genes may be particularly
    prone to be selected for under certain environmental conditions. The identification
    of copy-number variation in ecological field studies of species adapting to stressful
    or novel environmental conditions may improve our understanding of gene duplications
    as a mechanism of adaptation and its relevance to the long-term persistence of
    gene duplications.
acknowledgement: The work was supported by a Plan Nacional grant no. BFU2009-09271
  from the Spanish Ministry of Science and Innovation. The author is a European Molecular
  Biology Organization Young Investigator and Howard Hughes Medical Institute International
  Early Career Scientist.
author:
- first_name: Fyodor
  full_name: Fyodor Kondrashov
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
citation:
  ama: Kondrashov F. Gene duplication as a mechanism of genomic adaptation to a changing
    environment. <i>Proceedings of the Royal Society of London Series B Biological
    Sciences</i>. 2012;279(1749):5048-5057. doi:<a href="https://doi.org/10.1098/rspb.2012.1108">10.1098/rspb.2012.1108</a>
  apa: Kondrashov, F. (2012). Gene duplication as a mechanism of genomic adaptation
    to a changing environment. <i>Proceedings of the Royal Society of London Series
    B Biological Sciences</i>. Royal Society, The. <a href="https://doi.org/10.1098/rspb.2012.1108">https://doi.org/10.1098/rspb.2012.1108</a>
  chicago: Kondrashov, Fyodor. “Gene Duplication as a Mechanism of Genomic Adaptation
    to a Changing Environment.” <i>Proceedings of the Royal Society of London Series
    B Biological Sciences</i>. Royal Society, The, 2012. <a href="https://doi.org/10.1098/rspb.2012.1108">https://doi.org/10.1098/rspb.2012.1108</a>.
  ieee: F. Kondrashov, “Gene duplication as a mechanism of genomic adaptation to a
    changing environment,” <i>Proceedings of the Royal Society of London Series B
    Biological Sciences</i>, vol. 279, no. 1749. Royal Society, The, pp. 5048–5057,
    2012.
  ista: Kondrashov F. 2012. Gene duplication as a mechanism of genomic adaptation
    to a changing environment. Proceedings of the Royal Society of London Series B
    Biological Sciences. 279(1749), 5048–5057.
  mla: Kondrashov, Fyodor. “Gene Duplication as a Mechanism of Genomic Adaptation
    to a Changing Environment.” <i>Proceedings of the Royal Society of London Series
    B Biological Sciences</i>, vol. 279, no. 1749, Royal Society, The, 2012, pp. 5048–57,
    doi:<a href="https://doi.org/10.1098/rspb.2012.1108">10.1098/rspb.2012.1108</a>.
  short: F. Kondrashov, Proceedings of the Royal Society of London Series B Biological
    Sciences 279 (2012) 5048–5057.
date_created: 2018-12-11T11:49:01Z
date_published: 2012-01-01T00:00:00Z
date_updated: 2021-01-12T08:21:16Z
day: '01'
doi: 10.1098/rspb.2012.1108
extern: 1
intvolume: '       279'
issue: '1749'
month: '01'
page: 5048 - 5057
publication: Proceedings of the Royal Society of London Series B Biological Sciences
publication_status: published
publisher: Royal Society, The
publist_id: '6765'
quality_controlled: 0
status: public
title: Gene duplication as a mechanism of genomic adaptation to a changing environment
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
volume: 279
year: '2012'
...
---
_id: '900'
abstract:
- lang: eng
  text: 'The main forces directing long-term molecular evolution remain obscure. A
    sizable fraction of amino-acid substitutions seem to be fixed by positive selection,
    but it is unclear to what degree long-term protein evolution is constrained by
    epistasis, that is, instances when substitutions that are accepted in one genotype
    are deleterious in another. Here we obtain a quantitative estimate of the prevalence
    of epistasis in long-term protein evolution by relating data on amino-acid usage
    in 14 organelle proteins and 2 nuclear-encoded proteins to their rates of short-term
    evolution. We studied multiple alignments of at least 1,000 orthologues for each
    of these 16 proteins from species from a diverse phylogenetic background and found
    that an average site contained approximately eight different amino acids. Thus,
    without epistasis an average site should accept two-fifths of all possible amino
    acids, and the average rate of amino-acid substitutions should therefore be about
    three-fifths lower than the rate of neutral evolution. However, we found that
    the measured rate of amino-acid substitution in recent evolution is 20 times lower
    than the rate of neutral evolution and an order of magnitude lower than that expected
    in the absence of epistasis. These data indicate that epistasis is pervasive throughout
    protein evolution: about 90 per cent of all amino-acid substitutions have a neutral
    or beneficial impact only in the genetic backgrounds in which they occur, and
    must therefore be deleterious in a different background of other species. Our
    findings show that most amino-acid substitutions have different fitness effects
    in different species and that epistasis provides the primary conceptual framework
    to describe the tempo and mode of long-term protein evolution.'
acknowledgement: |
  The work was supported by Plan Nacional grants from the Spanish Ministry of Science and Innovation, to F.A.K. and C.N. C.K. was supported by the European Union FP7 project Quantomics (KBBE2A222664). F.A.K. is a European Molecular Biology Organization Young Investigator and Howard Hughes Medical Institute International Early Career Scientist. We thank B. Lehner and T. Warnecke for input and a critical reading of the manuscript.
author:
- first_name: Michael
  full_name: Breen, Michael S
  last_name: Breen
- first_name: Carsten
  full_name: Kemena, Carsten
  last_name: Kemena
- first_name: Peter
  full_name: Vlasov, Peter K
  last_name: Vlasov
- first_name: Cédric
  full_name: Notredame, Cédric
  last_name: Notredame
- first_name: Fyodor
  full_name: Fyodor Kondrashov
  id: 44FDEF62-F248-11E8-B48F-1D18A9856A87
  last_name: Kondrashov
  orcid: 0000-0001-8243-4694
citation:
  ama: Breen M, Kemena C, Vlasov P, Notredame C, Kondrashov F. Epistasis as the primary
    factor in molecular evolution. <i>Nature</i>. 2012;490(7421):535-538. doi:<a href="https://doi.org/10.1038/nature11510">10.1038/nature11510</a>
  apa: Breen, M., Kemena, C., Vlasov, P., Notredame, C., &#38; Kondrashov, F. (2012).
    Epistasis as the primary factor in molecular evolution. <i>Nature</i>. Nature
    Publishing Group. <a href="https://doi.org/10.1038/nature11510">https://doi.org/10.1038/nature11510</a>
  chicago: Breen, Michael, Carsten Kemena, Peter Vlasov, Cédric Notredame, and Fyodor
    Kondrashov. “Epistasis as the Primary Factor in Molecular Evolution.” <i>Nature</i>.
    Nature Publishing Group, 2012. <a href="https://doi.org/10.1038/nature11510">https://doi.org/10.1038/nature11510</a>.
  ieee: M. Breen, C. Kemena, P. Vlasov, C. Notredame, and F. Kondrashov, “Epistasis
    as the primary factor in molecular evolution,” <i>Nature</i>, vol. 490, no. 7421.
    Nature Publishing Group, pp. 535–538, 2012.
  ista: Breen M, Kemena C, Vlasov P, Notredame C, Kondrashov F. 2012. Epistasis as
    the primary factor in molecular evolution. Nature. 490(7421), 535–538.
  mla: Breen, Michael, et al. “Epistasis as the Primary Factor in Molecular Evolution.”
    <i>Nature</i>, vol. 490, no. 7421, Nature Publishing Group, 2012, pp. 535–38,
    doi:<a href="https://doi.org/10.1038/nature11510">10.1038/nature11510</a>.
  short: M. Breen, C. Kemena, P. Vlasov, C. Notredame, F. Kondrashov, Nature 490 (2012)
    535–538.
date_created: 2018-12-11T11:49:06Z
date_published: 2012-10-25T00:00:00Z
date_updated: 2021-01-12T08:21:45Z
day: '25'
doi: 10.1038/nature11510
extern: 1
intvolume: '       490'
issue: '7421'
month: '10'
page: 535 - 538
publication: Nature
publication_status: published
publisher: Nature Publishing Group
publist_id: '6748'
quality_controlled: 0
status: public
title: Epistasis as the primary factor in molecular evolution
type: journal_article
volume: 490
year: '2012'
...
---
_id: '9014'
abstract:
- lang: eng
  text: In this Letter, we explore experimentally the phase behavior of a dense active
    suspension of self-propelled colloids. In addition to a solidlike and gaslike
    phase observed for high and low densities, a novel cluster phase is reported at
    intermediate densities. This takes the form of a stationary assembly of dense
    aggregates—resulting from a permanent dynamical merging and separation of active
    colloids—whose average size grows with activity as a linear function of the self-propelling
    velocity. While different possible scenarios can be considered to account for
    these observations—such as a generic velocity weakening instability recently put
    forward—we show that the experimental results are reproduced mathematically by
    a chemotactic aggregation mechanism, originally introduced to account for bacterial
    aggregation and accounting here for diffusiophoretic chemical interaction between
    colloidal swimmers.
article_number: '268303'
article_processing_charge: No
article_type: letter_note
arxiv: 1
author:
- first_name: I.
  full_name: Theurkauff, I.
  last_name: Theurkauff
- first_name: C.
  full_name: Cottin-Bizonne, C.
  last_name: Cottin-Bizonne
- first_name: Jérémie A
  full_name: Palacci, Jérémie A
  id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
  last_name: Palacci
  orcid: 0000-0002-7253-9465
- first_name: C.
  full_name: Ybert, C.
  last_name: Ybert
- first_name: L.
  full_name: Bocquet, L.
  last_name: Bocquet
citation:
  ama: Theurkauff I, Cottin-Bizonne C, Palacci JA, Ybert C, Bocquet L. Dynamic clustering
    in active colloidal suspensions with chemical signaling. <i>Physical Review Letters</i>.
    2012;108(26). doi:<a href="https://doi.org/10.1103/physrevlett.108.268303">10.1103/physrevlett.108.268303</a>
  apa: Theurkauff, I., Cottin-Bizonne, C., Palacci, J. A., Ybert, C., &#38; Bocquet,
    L. (2012). Dynamic clustering in active colloidal suspensions with chemical signaling.
    <i>Physical Review Letters</i>. American Physical Society . <a href="https://doi.org/10.1103/physrevlett.108.268303">https://doi.org/10.1103/physrevlett.108.268303</a>
  chicago: Theurkauff, I., C. Cottin-Bizonne, Jérémie A Palacci, C. Ybert, and L.
    Bocquet. “Dynamic Clustering in Active Colloidal Suspensions with Chemical Signaling.”
    <i>Physical Review Letters</i>. American Physical Society , 2012. <a href="https://doi.org/10.1103/physrevlett.108.268303">https://doi.org/10.1103/physrevlett.108.268303</a>.
  ieee: I. Theurkauff, C. Cottin-Bizonne, J. A. Palacci, C. Ybert, and L. Bocquet,
    “Dynamic clustering in active colloidal suspensions with chemical signaling,”
    <i>Physical Review Letters</i>, vol. 108, no. 26. American Physical Society ,
    2012.
  ista: Theurkauff I, Cottin-Bizonne C, Palacci JA, Ybert C, Bocquet L. 2012. Dynamic
    clustering in active colloidal suspensions with chemical signaling. Physical Review
    Letters. 108(26), 268303.
  mla: Theurkauff, I., et al. “Dynamic Clustering in Active Colloidal Suspensions
    with Chemical Signaling.” <i>Physical Review Letters</i>, vol. 108, no. 26, 268303,
    American Physical Society , 2012, doi:<a href="https://doi.org/10.1103/physrevlett.108.268303">10.1103/physrevlett.108.268303</a>.
  short: I. Theurkauff, C. Cottin-Bizonne, J.A. Palacci, C. Ybert, L. Bocquet, Physical
    Review Letters 108 (2012).
date_created: 2021-01-19T10:26:59Z
date_published: 2012-06-29T00:00:00Z
date_updated: 2023-02-23T13:46:45Z
day: '29'
doi: 10.1103/physrevlett.108.268303
extern: '1'
external_id:
  arxiv:
  - '1202.6264'
  pmid:
  - '23005020'
intvolume: '       108'
issue: '26'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1202.6264
month: '06'
oa: 1
oa_version: Preprint
pmid: 1
publication: Physical Review Letters
publication_identifier:
  eissn:
  - '10797114'
  issn:
  - '00319007'
publication_status: published
publisher: 'American Physical Society '
quality_controlled: '1'
scopus_import: '1'
status: public
title: Dynamic clustering in active colloidal suspensions with chemical signaling
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 108
year: '2012'
...
---
_id: '9049'
abstract:
- lang: eng
  text: 'Diffusiophoretic motion of colloids and macromolecules under salt gradients
    exhibits a logarithmic-sensing, i.e. the particle velocity is proportional to
    the spatial gradient of the logarithm of the salt concentration, as VDP = DDP∇logc.
    Here we explore experimentally the implications of this log-sensing behavior,
    on the basis of a hydrogel microfluidic device allowing to build spatially and
    temporally controlled gradients. We first demonstrate that the non-linearity of
    the salt-taxis leads to a trapping of particles under concentration gradient oscillations
    via a rectification of the motion. As an alternative, we make use of the high
    sensitivity of diffusiophoretic migration to vanishing salt concentration due
    to the log-sensing: in a counter-intuitive way, a vanishing gradient can lead
    to measurable velocity provided that the solute concentration is low enough, thus
    keeping ∇c/c finite. We show that this leads to a strong segregation of particles
    in osmotic shock configuration, resulting from a step change of the salt concentration
    at the boundaries. These various phenomena are rationalized on the basis of a
    theoretical description for the time-dependent Smoluchowski equation for the colloidal
    density.'
article_processing_charge: No
article_type: original
author:
- first_name: Jérémie A
  full_name: Palacci, Jérémie A
  id: 8fb92548-2b22-11eb-b7c1-a3f0d08d7c7d
  last_name: Palacci
  orcid: 0000-0002-7253-9465
- first_name: Cécile
  full_name: Cottin-Bizonne, Cécile
  last_name: Cottin-Bizonne
- first_name: Christophe
  full_name: Ybert, Christophe
  last_name: Ybert
- first_name: Lydéric
  full_name: Bocquet, Lydéric
  last_name: Bocquet
citation:
  ama: Palacci JA, Cottin-Bizonne C, Ybert C, Bocquet L. Osmotic traps for colloids
    and macromolecules based on logarithmic sensing in salt taxis. <i>Soft Matter</i>.
    2012;8(4):980-994. doi:<a href="https://doi.org/10.1039/c1sm06395b">10.1039/c1sm06395b</a>
  apa: Palacci, J. A., Cottin-Bizonne, C., Ybert, C., &#38; Bocquet, L. (2012). Osmotic
    traps for colloids and macromolecules based on logarithmic sensing in salt taxis.
    <i>Soft Matter</i>. Royal Society of Chemistry. <a href="https://doi.org/10.1039/c1sm06395b">https://doi.org/10.1039/c1sm06395b</a>
  chicago: Palacci, Jérémie A, Cécile Cottin-Bizonne, Christophe Ybert, and Lydéric
    Bocquet. “Osmotic Traps for Colloids and Macromolecules Based on Logarithmic Sensing
    in Salt Taxis.” <i>Soft Matter</i>. Royal Society of Chemistry, 2012. <a href="https://doi.org/10.1039/c1sm06395b">https://doi.org/10.1039/c1sm06395b</a>.
  ieee: J. A. Palacci, C. Cottin-Bizonne, C. Ybert, and L. Bocquet, “Osmotic traps
    for colloids and macromolecules based on logarithmic sensing in salt taxis,” <i>Soft
    Matter</i>, vol. 8, no. 4. Royal Society of Chemistry, pp. 980–994, 2012.
  ista: Palacci JA, Cottin-Bizonne C, Ybert C, Bocquet L. 2012. Osmotic traps for
    colloids and macromolecules based on logarithmic sensing in salt taxis. Soft Matter.
    8(4), 980–994.
  mla: Palacci, Jérémie A., et al. “Osmotic Traps for Colloids and Macromolecules
    Based on Logarithmic Sensing in Salt Taxis.” <i>Soft Matter</i>, vol. 8, no. 4,
    Royal Society of Chemistry, 2012, pp. 980–94, doi:<a href="https://doi.org/10.1039/c1sm06395b">10.1039/c1sm06395b</a>.
  short: J.A. Palacci, C. Cottin-Bizonne, C. Ybert, L. Bocquet, Soft Matter 8 (2012)
    980–994.
date_created: 2021-02-01T13:43:10Z
date_published: 2012-01-28T00:00:00Z
date_updated: 2023-02-23T13:47:31Z
day: '28'
doi: 10.1039/c1sm06395b
extern: '1'
intvolume: '         8'
issue: '4'
language:
- iso: eng
month: '01'
oa_version: None
page: 980-994
publication: Soft Matter
publication_identifier:
  eissn:
  - 1744-6848
  issn:
  - 1744-683X
publication_status: published
publisher: Royal Society of Chemistry
quality_controlled: '1'
scopus_import: '1'
status: public
title: Osmotic traps for colloids and macromolecules based on logarithmic sensing
  in salt taxis
type: journal_article
user_id: D865714E-FA4E-11E9-B85B-F5C5E5697425
volume: 8
year: '2012'
...
---
_id: '91'
abstract:
- lang: eng
  text: 'We demonstrate how to appropriately estimate the zero-frequency (static)
    hyperpolarizability of an organic molecule from its charge distribution, and we
    explore applications of these estimates for identifying and evaluating new organic
    nonlinear optical (NLO) materials. First, we calculate hyperpolarizabilities from
    Hartree-Fock-derived charge distributions and find order-of-magnitude agreement
    with experimental values. We show that these simple arithmetic calculations will
    enable systematic searches for new organic NLO molecules. Second, we derive hyperpolarizabilities
    from crystallographic data using a multipolar charge-density analysis and find
    good agreement with empirical calculations. This demonstrates an experimental
    determination of the full static hyperpolarizability tensor in a solid-state sample. '
acknowledgement: This work was supported by The Winston Churchill Foundation of the
  United States (A.P.H., M.A.B.F., D.D.H.), The Royal Society via a University Research
  Fellowship (J.M.C.), and the University of New Brunswick via The Vice-Chancellor’s
  Research Chair (J.M.C.).
article_number: '033512'
author:
- first_name: Andrew P
  full_name: Higginbotham, Andrew P
  id: 4AD6785A-F248-11E8-B48F-1D18A9856A87
  last_name: Higginbotham
  orcid: 0000-0003-2607-2363
- first_name: Jacqueline
  full_name: Cole, Jacqueline
  last_name: Cole
- first_name: Martin
  full_name: Blood Forsythe, Martin
  last_name: Blood Forsythe
- first_name: Daniel
  full_name: Hickstein, Daniel
  last_name: Hickstein
citation:
  ama: Higginbotham AP, Cole J, Blood Forsythe M, Hickstein D. Identifying and evaluating
    organic nonlinear optical materials via molecular moments. <i>Journal of Applied
    Physics</i>. 2012;111(3). doi:<a href="https://doi.org/10.1063/1.3678593">10.1063/1.3678593</a>
  apa: Higginbotham, A. P., Cole, J., Blood Forsythe, M., &#38; Hickstein, D. (2012).
    Identifying and evaluating organic nonlinear optical materials via molecular moments.
    <i>Journal of Applied Physics</i>. American Institute of Physics. <a href="https://doi.org/10.1063/1.3678593">https://doi.org/10.1063/1.3678593</a>
  chicago: Higginbotham, Andrew P, Jacqueline Cole, Martin Blood Forsythe, and Daniel
    Hickstein. “Identifying and Evaluating Organic Nonlinear Optical Materials via
    Molecular Moments.” <i>Journal of Applied Physics</i>. American Institute of Physics,
    2012. <a href="https://doi.org/10.1063/1.3678593">https://doi.org/10.1063/1.3678593</a>.
  ieee: A. P. Higginbotham, J. Cole, M. Blood Forsythe, and D. Hickstein, “Identifying
    and evaluating organic nonlinear optical materials via molecular moments,” <i>Journal
    of Applied Physics</i>, vol. 111, no. 3. American Institute of Physics, 2012.
  ista: Higginbotham AP, Cole J, Blood Forsythe M, Hickstein D. 2012. Identifying
    and evaluating organic nonlinear optical materials via molecular moments. Journal
    of Applied Physics. 111(3), 033512.
  mla: Higginbotham, Andrew P., et al. “Identifying and Evaluating Organic Nonlinear
    Optical Materials via Molecular Moments.” <i>Journal of Applied Physics</i>, vol.
    111, no. 3, 033512, American Institute of Physics, 2012, doi:<a href="https://doi.org/10.1063/1.3678593">10.1063/1.3678593</a>.
  short: A.P. Higginbotham, J. Cole, M. Blood Forsythe, D. Hickstein, Journal of Applied
    Physics 111 (2012).
date_created: 2018-12-11T11:44:35Z
date_published: 2012-02-07T00:00:00Z
date_updated: 2021-01-12T08:21:50Z
day: '07'
doi: 10.1063/1.3678593
extern: '1'
intvolume: '       111'
issue: '3'
language:
- iso: eng
month: '02'
oa_version: None
publication: Journal of Applied Physics
publication_status: published
publisher: American Institute of Physics
publist_id: '7963'
quality_controlled: '1'
status: public
title: Identifying and evaluating organic nonlinear optical materials via molecular
  moments
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 111
year: '2012'
...
---
_id: '9142'
abstract:
- lang: eng
  text: "In models of radiative–convective equilibrium it is known that convection
    can spontaneously aggregate into one single localized moist region if the domain
    is large enough. The large changes in the mean climate state and radiative fluxes
    accompanying this self-aggregation raise questions as to what simulations at lower
    resolutions with parameterized convection, in similar homogeneous geometries,
    should be expected to produce to be considered successful in mimicking a cloud-resolving
    model.\r\nThe authors investigate this self-aggregation in a nonrotating, three-dimensional
    cloud-resolving model on a square domain without large-scale forcing. It is found
    that self-aggregation is sensitive not only to the domain size, but also to the
    horizontal resolution. With horizontally homogeneous initial conditions, convective
    aggregation only occurs on domains larger than about 200km and with resolutions
    coarser than about 2km in the model examined. The system exhibits hysteresis,
    so that with aggregated initial conditions, convection remains aggregated even
    at our finest resolution, 500m, as long as the domain is greater than 200–300km.\r\nThe
    sensitivity of self-aggregation to resolution and domain size in this model is
    due to the sensitivity of the distribution of low clouds to these two parameters.
    Indeed, the mechanism responsible for the aggregation of convection is the dynamical
    response to the longwave radiative cooling from low clouds. Strong longwave cooling
    near cloud top in dry regions forces downward motion, which by continuity generates
    inflow near cloud top and near-surface outflow from dry regions. This circulation
    results in the net export of moist static energy from regions with low moist static
    energy, yielding a positive feedback."
article_processing_charge: No
article_type: original
author:
- first_name: Caroline J
  full_name: Muller, Caroline J
  id: f978ccb0-3f7f-11eb-b193-b0e2bd13182b
  last_name: Muller
  orcid: 0000-0001-5836-5350
- first_name: Isaac M.
  full_name: Held, Isaac M.
  last_name: Held
citation:
  ama: Muller CJ, Held IM. Detailed investigation of the self-aggregation of convection
    in cloud-resolving simulations. <i>Journal of the Atmospheric Sciences</i>. 2012;69(8):2551-2565.
    doi:<a href="https://doi.org/10.1175/jas-d-11-0257.1">10.1175/jas-d-11-0257.1</a>
  apa: Muller, C. J., &#38; Held, I. M. (2012). Detailed investigation of the self-aggregation
    of convection in cloud-resolving simulations. <i>Journal of the Atmospheric Sciences</i>.
    American Meteorological Society. <a href="https://doi.org/10.1175/jas-d-11-0257.1">https://doi.org/10.1175/jas-d-11-0257.1</a>
  chicago: Muller, Caroline J, and Isaac M. Held. “Detailed Investigation of the Self-Aggregation
    of Convection in Cloud-Resolving Simulations.” <i>Journal of the Atmospheric Sciences</i>.
    American Meteorological Society, 2012. <a href="https://doi.org/10.1175/jas-d-11-0257.1">https://doi.org/10.1175/jas-d-11-0257.1</a>.
  ieee: C. J. Muller and I. M. Held, “Detailed investigation of the self-aggregation
    of convection in cloud-resolving simulations,” <i>Journal of the Atmospheric Sciences</i>,
    vol. 69, no. 8. American Meteorological Society, pp. 2551–2565, 2012.
  ista: Muller CJ, Held IM. 2012. Detailed investigation of the self-aggregation of
    convection in cloud-resolving simulations. Journal of the Atmospheric Sciences.
    69(8), 2551–2565.
  mla: Muller, Caroline J., and Isaac M. Held. “Detailed Investigation of the Self-Aggregation
    of Convection in Cloud-Resolving Simulations.” <i>Journal of the Atmospheric Sciences</i>,
    vol. 69, no. 8, American Meteorological Society, 2012, pp. 2551–65, doi:<a href="https://doi.org/10.1175/jas-d-11-0257.1">10.1175/jas-d-11-0257.1</a>.
  short: C.J. Muller, I.M. Held, Journal of the Atmospheric Sciences 69 (2012) 2551–2565.
date_created: 2021-02-15T14:39:03Z
date_published: 2012-08-01T00:00:00Z
date_updated: 2022-01-24T13:49:41Z
day: '01'
doi: 10.1175/jas-d-11-0257.1
extern: '1'
intvolume: '        69'
issue: '8'
keyword:
- Atmospheric Science
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://doi.org/10.1175/JAS-D-11-0257.1
month: '08'
oa: 1
oa_version: Published Version
page: 2551-2565
publication: Journal of the Atmospheric Sciences
publication_identifier:
  issn:
  - 0022-4928
  - 1520-0469
publication_status: published
publisher: American Meteorological Society
quality_controlled: '1'
status: public
title: Detailed investigation of the self-aggregation of convection in cloud-resolving
  simulations
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 69
year: '2012'
...
---
_id: '922'
abstract:
- lang: eng
  text: 'We study theoretically the morphologies of biological tubes affected by various
    pathologies. When epithelial cells grow, the negative tension produced by their
    division provokes a buckling instability. Several shapes are investigated: varicose,
    dilated, sinuous, or sausagelike. They are all found in pathologies of tracheal,
    renal tubes, or arteries. The final shape depends crucially on the mechanical
    parameters of the tissues: Young''s modulus, wall-to-lumen ratio, homeostatic
    pressure. We argue that since tissues must be in quasistatic mechanical equilibrium,
    abnormal shapes convey information as to what causes the pathology. We calculate
    a phase diagram of tubular instabilities which could be a helpful guide for investigating
    the underlying genetic regulation.'
article_processing_charge: No
arxiv: 1
author:
- first_name: Edouard B
  full_name: Hannezo, Edouard B
  id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
  last_name: Hannezo
  orcid: 0000-0001-6005-1561
- first_name: Jacques
  full_name: Prost, Jacques
  last_name: Prost
- first_name: Jean
  full_name: Joanny, Jean
  last_name: Joanny
citation:
  ama: Hannezo EB, Prost J, Joanny J. Mechanical instabilities of biological tubes.
    <i>Physical Review Letters</i>. 2012;109(1). doi:<a href="https://doi.org/10.1103/PhysRevLett.109.018101">10.1103/PhysRevLett.109.018101</a>
  apa: Hannezo, E. B., Prost, J., &#38; Joanny, J. (2012). Mechanical instabilities
    of biological tubes. <i>Physical Review Letters</i>. American Physical Society.
    <a href="https://doi.org/10.1103/PhysRevLett.109.018101">https://doi.org/10.1103/PhysRevLett.109.018101</a>
  chicago: Hannezo, Edouard B, Jacques Prost, and Jean Joanny. “Mechanical Instabilities
    of Biological Tubes.” <i>Physical Review Letters</i>. American Physical Society,
    2012. <a href="https://doi.org/10.1103/PhysRevLett.109.018101">https://doi.org/10.1103/PhysRevLett.109.018101</a>.
  ieee: E. B. Hannezo, J. Prost, and J. Joanny, “Mechanical instabilities of biological
    tubes,” <i>Physical Review Letters</i>, vol. 109, no. 1. American Physical Society,
    2012.
  ista: Hannezo EB, Prost J, Joanny J. 2012. Mechanical instabilities of biological
    tubes. Physical Review Letters. 109(1).
  mla: Hannezo, Edouard B., et al. “Mechanical Instabilities of Biological Tubes.”
    <i>Physical Review Letters</i>, vol. 109, no. 1, American Physical Society, 2012,
    doi:<a href="https://doi.org/10.1103/PhysRevLett.109.018101">10.1103/PhysRevLett.109.018101</a>.
  short: E.B. Hannezo, J. Prost, J. Joanny, Physical Review Letters 109 (2012).
date_created: 2018-12-11T11:49:13Z
date_published: 2012-07-03T00:00:00Z
date_updated: 2021-01-12T08:21:56Z
day: '03'
doi: 10.1103/PhysRevLett.109.018101
extern: '1'
external_id:
  arxiv:
  - '1207.1516'
intvolume: '       109'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
  url: https://arxiv.org/abs/1207.1516
month: '07'
oa: 1
oa_version: Preprint
publication: Physical Review Letters
publication_status: published
publisher: American Physical Society
publist_id: '6519'
status: public
title: Mechanical instabilities of biological tubes
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 109
year: '2012'
...
---
_id: '7074'
abstract:
- lang: eng
  text: The Seebeck coefficients, electrical resistivities, total thermal conductivities,
    and magnetization are reported for temperatures between 5 and 350 K for n-type
    Bi0.88Sb0.12 nano-composite alloys made by Ho-doping at the 0, 1, and 3 % atomic
    levels. The alloys were prepared using a dc hot-pressing method, and are shown
    to be single phase for both Ho contents with grain sizes on the average of 900
    nm. We find the parent compound has a maximum of ZT = 0.28 at 231 K, while doping
    1 % Ho increases the maximum ZT to 0.31 at 221 K and the 3 % doped sample suppresses
    the maximum ZT = 0.24 at a temperature of 260 K.
article_processing_charge: No
article_type: original
author:
- first_name: K. C.
  full_name: Lukas, K. C.
  last_name: Lukas
- first_name: G.
  full_name: Joshi, G.
  last_name: Joshi
- first_name: Kimberly A
  full_name: Modic, Kimberly A
  id: 13C26AC0-EB69-11E9-87C6-5F3BE6697425
  last_name: Modic
  orcid: 0000-0001-9760-3147
- first_name: Z. F.
  full_name: Ren, Z. F.
  last_name: Ren
- first_name: C. P.
  full_name: Opeil, C. P.
  last_name: Opeil
citation:
  ama: Lukas KC, Joshi G, Modic KA, Ren ZF, Opeil CP. Thermoelectric properties of
    Ho-doped Bi0.88Sb0.12. <i>Journal of Materials Science</i>. 2012;47(15):5729-5734.
    doi:<a href="https://doi.org/10.1007/s10853-012-6463-6">10.1007/s10853-012-6463-6</a>
  apa: Lukas, K. C., Joshi, G., Modic, K. A., Ren, Z. F., &#38; Opeil, C. P. (2012).
    Thermoelectric properties of Ho-doped Bi0.88Sb0.12. <i>Journal of Materials Science</i>.
    Springer Nature. <a href="https://doi.org/10.1007/s10853-012-6463-6">https://doi.org/10.1007/s10853-012-6463-6</a>
  chicago: Lukas, K. C., G. Joshi, Kimberly A Modic, Z. F. Ren, and C. P. Opeil. “Thermoelectric
    Properties of Ho-Doped Bi0.88Sb0.12.” <i>Journal of Materials Science</i>. Springer
    Nature, 2012. <a href="https://doi.org/10.1007/s10853-012-6463-6">https://doi.org/10.1007/s10853-012-6463-6</a>.
  ieee: K. C. Lukas, G. Joshi, K. A. Modic, Z. F. Ren, and C. P. Opeil, “Thermoelectric
    properties of Ho-doped Bi0.88Sb0.12,” <i>Journal of Materials Science</i>, vol.
    47, no. 15. Springer Nature, pp. 5729–5734, 2012.
  ista: Lukas KC, Joshi G, Modic KA, Ren ZF, Opeil CP. 2012. Thermoelectric properties
    of Ho-doped Bi0.88Sb0.12. Journal of Materials Science. 47(15), 5729–5734.
  mla: Lukas, K. C., et al. “Thermoelectric Properties of Ho-Doped Bi0.88Sb0.12.”
    <i>Journal of Materials Science</i>, vol. 47, no. 15, Springer Nature, 2012, pp.
    5729–34, doi:<a href="https://doi.org/10.1007/s10853-012-6463-6">10.1007/s10853-012-6463-6</a>.
  short: K.C. Lukas, G. Joshi, K.A. Modic, Z.F. Ren, C.P. Opeil, Journal of Materials
    Science 47 (2012) 5729–5734.
date_created: 2019-11-19T13:36:54Z
date_published: 2012-08-01T00:00:00Z
date_updated: 2021-01-12T08:11:43Z
day: '01'
doi: 10.1007/s10853-012-6463-6
extern: '1'
intvolume: '        47'
issue: '15'
language:
- iso: eng
month: '08'
oa_version: None
page: 5729-5734
publication: Journal of Materials Science
publication_identifier:
  eissn:
  - 1573-4803
  issn:
  - 0022-2461
publication_status: published
publisher: Springer Nature
quality_controlled: '1'
status: public
title: Thermoelectric properties of Ho-doped Bi0.88Sb0.12
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 47
year: '2012'
...
