---
_id: '6029'
abstract:
- lang: eng
text: Protein micropatterning has become an important tool for many biomedical applications
as well as in academic research. Current techniques that allow to reduce the feature
size of patterns below 1 μm are, however, often costly and require sophisticated
equipment. We present here a straightforward and convenient method to generate
highly condensed nanopatterns of proteins without the need for clean room facilities
or expensive equipment. Our approach is based on nanocontact printing and allows
for the fabrication of protein patterns with feature sizes of 80 nm and periodicities
down to 140 nm. This was made possible by the use of the material X-poly(dimethylsiloxane)
(X-PDMS) in a two-layer stamp layout for protein printing. In a proof of principle,
different proteins at various scales were printed and the pattern quality was
evaluated by atomic force microscopy (AFM) and super-resolution fluorescence microscopy.
article_number: '655'
article_processing_charge: No
author:
- first_name: Marco
full_name: Lindner, Marco
last_name: Lindner
- first_name: Aliz
full_name: Tresztenyak, Aliz
last_name: Tresztenyak
- first_name: Gergö
full_name: Fülöp, Gergö
last_name: Fülöp
- first_name: Wiebke
full_name: Jahr, Wiebke
id: 425C1CE8-F248-11E8-B48F-1D18A9856A87
last_name: Jahr
- first_name: Adrian
full_name: Prinz, Adrian
last_name: Prinz
- first_name: Iris
full_name: Prinz, Iris
last_name: Prinz
- 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: Gerhard J.
full_name: Schütz, Gerhard J.
last_name: Schütz
- first_name: Eva
full_name: Sevcsik, Eva
last_name: Sevcsik
citation:
ama: Lindner M, Tresztenyak A, Fülöp G, et al. A fast and simple contact printing
approach to generate 2D protein nanopatterns. Frontiers in Chemistry. 2019;6.
doi:10.3389/fchem.2018.00655
apa: Lindner, M., Tresztenyak, A., Fülöp, G., Jahr, W., Prinz, A., Prinz, I., …
Sevcsik, E. (2019). A fast and simple contact printing approach to generate 2D
protein nanopatterns. Frontiers in Chemistry. Frontiers Media S.A. https://doi.org/10.3389/fchem.2018.00655
chicago: Lindner, Marco, Aliz Tresztenyak, Gergö Fülöp, Wiebke Jahr, Adrian Prinz,
Iris Prinz, Johann G Danzl, Gerhard J. Schütz, and Eva Sevcsik. “A Fast and Simple
Contact Printing Approach to Generate 2D Protein Nanopatterns.” Frontiers in
Chemistry. Frontiers Media S.A., 2019. https://doi.org/10.3389/fchem.2018.00655.
ieee: M. Lindner et al., “A fast and simple contact printing approach to
generate 2D protein nanopatterns,” Frontiers in Chemistry, vol. 6. Frontiers
Media S.A., 2019.
ista: Lindner M, Tresztenyak A, Fülöp G, Jahr W, Prinz A, Prinz I, Danzl JG, Schütz
GJ, Sevcsik E. 2019. A fast and simple contact printing approach to generate 2D
protein nanopatterns. Frontiers in Chemistry. 6, 655.
mla: Lindner, Marco, et al. “A Fast and Simple Contact Printing Approach to Generate
2D Protein Nanopatterns.” Frontiers in Chemistry, vol. 6, 655, Frontiers
Media S.A., 2019, doi:10.3389/fchem.2018.00655.
short: M. Lindner, A. Tresztenyak, G. Fülöp, W. Jahr, A. Prinz, I. Prinz, J.G. Danzl,
G.J. Schütz, E. Sevcsik, Frontiers in Chemistry 6 (2019).
date_created: 2019-02-17T22:59:24Z
date_published: 2019-01-24T00:00:00Z
date_updated: 2023-08-24T14:45:38Z
day: '24'
ddc:
- '540'
department:
- _id: JoDa
doi: 10.3389/fchem.2018.00655
external_id:
isi:
- '000456718000001'
file:
- access_level: open_access
checksum: 7841301d7c53b56ef873791b4b6f7b24
content_type: application/pdf
creator: dernst
date_created: 2019-02-18T15:10:34Z
date_updated: 2020-07-14T12:47:17Z
file_id: '6039'
file_name: 2019_frontiers_Lindner.pdf
file_size: 1766820
relation: main_file
file_date_updated: 2020-07-14T12:47:17Z
has_accepted_license: '1'
intvolume: ' 6'
isi: 1
language:
- iso: eng
month: '01'
oa: 1
oa_version: Published Version
publication: Frontiers in Chemistry
publication_identifier:
eissn:
- '22962646'
publication_status: published
publisher: Frontiers Media S.A.
quality_controlled: '1'
scopus_import: '1'
status: public
title: A fast and simple contact printing approach to generate 2D protein nanopatterns
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: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 6
year: '2019'
...
---
_id: '6052'
abstract:
- lang: eng
text: 'Expansion microscopy is a relatively new approach to super-resolution imaging
that uses expandable hydrogels to isotropically increase the physical distance
between fluorophores in biological samples such as cell cultures or tissue slices.
The classic gel recipe results in an expansion factor of ~4×, with a resolution
of 60–80 nm. We have recently developed X10 microscopy, which uses a gel that
achieves an expansion factor of ~10×, with a resolution of ~25 nm. Here, we provide
a step-by-step protocol for X10 expansion microscopy. A typical experiment consists
of seven sequential stages: (i) immunostaining, (ii) anchoring, (iii) polymerization,
(iv) homogenization, (v) expansion, (vi) imaging, and (vii) validation. The protocol
presented here includes recommendations for optimization, pitfalls and their solutions,
and detailed guidelines that should increase reproducibility. Although our protocol
focuses on X10 expansion microscopy, we detail which of these suggestions are
also applicable to classic fourfold expansion microscopy. We exemplify our protocol
using primary hippocampal neurons from rats, but our approach can be used with
other primary cells or cultured cell lines of interest. This protocol will enable
any researcher with basic experience in immunostainings and access to an epifluorescence
microscope to perform super-resolution microscopy with X10. The procedure takes
3 d and requires ~5 h of actively handling the sample for labeling and expansion,
and another ~3 h for imaging and analysis.'
article_processing_charge: No
article_type: original
author:
- first_name: Sven M
full_name: Truckenbrodt, Sven M
id: 45812BD4-F248-11E8-B48F-1D18A9856A87
last_name: Truckenbrodt
- first_name: Christoph M
full_name: Sommer, Christoph M
id: 4DF26D8C-F248-11E8-B48F-1D18A9856A87
last_name: Sommer
orcid: 0000-0003-1216-9105
- first_name: Silvio O
full_name: Rizzoli, Silvio O
last_name: Rizzoli
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
citation:
ama: Truckenbrodt SM, Sommer CM, Rizzoli SO, Danzl JG. A practical guide to optimization
in X10 expansion microscopy. Nature Protocols. 2019;14(3):832–863. doi:10.1038/s41596-018-0117-3
apa: Truckenbrodt, S. M., Sommer, C. M., Rizzoli, S. O., & Danzl, J. G. (2019).
A practical guide to optimization in X10 expansion microscopy. Nature Protocols.
Nature Publishing Group. https://doi.org/10.1038/s41596-018-0117-3
chicago: Truckenbrodt, Sven M, Christoph M Sommer, Silvio O Rizzoli, and Johann
G Danzl. “A Practical Guide to Optimization in X10 Expansion Microscopy.” Nature
Protocols. Nature Publishing Group, 2019. https://doi.org/10.1038/s41596-018-0117-3.
ieee: S. M. Truckenbrodt, C. M. Sommer, S. O. Rizzoli, and J. G. Danzl, “A practical
guide to optimization in X10 expansion microscopy,” Nature Protocols, vol.
14, no. 3. Nature Publishing Group, pp. 832–863, 2019.
ista: Truckenbrodt SM, Sommer CM, Rizzoli SO, Danzl JG. 2019. A practical guide
to optimization in X10 expansion microscopy. Nature Protocols. 14(3), 832–863.
mla: Truckenbrodt, Sven M., et al. “A Practical Guide to Optimization in X10 Expansion
Microscopy.” Nature Protocols, vol. 14, no. 3, Nature Publishing Group,
2019, pp. 832–863, doi:10.1038/s41596-018-0117-3.
short: S.M. Truckenbrodt, C.M. Sommer, S.O. Rizzoli, J.G. Danzl, Nature Protocols
14 (2019) 832–863.
date_created: 2019-02-24T22:59:20Z
date_published: 2019-03-01T00:00:00Z
date_updated: 2023-08-24T14:48:33Z
day: '01'
ddc:
- '570'
department:
- _id: JoDa
- _id: Bio
doi: 10.1038/s41596-018-0117-3
ec_funded: 1
external_id:
isi:
- '000459890700008'
pmid:
- '30778205'
file:
- access_level: open_access
checksum: 7efb9951e7ddf3e3dcc2fb92b859c623
content_type: application/vnd.openxmlformats-officedocument.wordprocessingml.document
creator: kschuh
date_created: 2021-06-29T14:41:46Z
date_updated: 2021-06-29T14:41:46Z
file_id: '9619'
file_name: 181031_Truckenbrodt_ExM_NatProtoc.docx
file_size: 84478958
relation: main_file
success: 1
file_date_updated: 2021-06-29T14:41:46Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
issue: '3'
language:
- iso: eng
month: '03'
oa: 1
oa_version: Submitted Version
page: 832–863
pmid: 1
project:
- _id: 260C2330-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '754411'
name: ISTplus - Postdoctoral Fellowships
- _id: 265CB4D0-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I03600
name: Optical control of synaptic function via adhesion molecules
publication: Nature Protocols
publication_status: published
publisher: Nature Publishing Group
quality_controlled: '1'
scopus_import: '1'
status: public
title: A practical guide to optimization in X10 expansion microscopy
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 14
year: '2019'
...
---
_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. Scientific Reports. 2018;8. doi:10.1038/s41598-018-19947-1
apa: Gregor, C., Sidenstein, S. C., Andresen, M., Sahl, S. J., Danzl, J. G., &
Hell, S. W. (2018). Novel reversibly switchable fluorescent proteins for RESOLFT
and STED nanoscopy engineered from the bacterial photoreceptor YtvA. Scientific
Reports. Springer Nature. https://doi.org/10.1038/s41598-018-19947-1
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.”
Scientific Reports. Springer Nature, 2018. https://doi.org/10.1038/s41598-018-19947-1.
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,” Scientific Reports,
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.”
Scientific Reports, vol. 8, 2724, Springer Nature, 2018, doi:10.1038/s41598-018-19947-1.
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: '5998'
abstract:
- lang: eng
text: Genome amplification and cellular senescence are commonly associated with
pathological processes. While physiological roles for polyploidization and senescence
have been described in mouse development, controversy exists over their significance
in humans. Here, we describe tetraploidization and senescence as phenomena of
normal human placenta development. During pregnancy, placental extravillous trophoblasts
(EVTs) invade the pregnant endometrium, termed decidua, to establish an adapted
microenvironment required for the developing embryo. This process is critically
dependent on continuous cell proliferation and differentiation, which is thought
to follow the classical model of cell cycle arrest prior to terminal differentiation.
Strikingly, flow cytometry and DNAseq revealed that EVT formation is accompanied
with a genome-wide polyploidization, independent of mitotic cycles. DNA replication
in these cells was analysed by a fluorescent cell-cycle indicator reporter system,
cell cycle marker expression and EdU incorporation. Upon invasion into the decidua,
EVTs widely lose their replicative potential and enter a senescent state characterized
by high senescence-associated (SA) β-galactosidase activity, induction of a SA
secretory phenotype as well as typical metabolic alterations. Furthermore, we
show that the shift from endocycle-dependent genome amplification to growth arrest
is disturbed in androgenic complete hydatidiform moles (CHM), a hyperplastic pregnancy
disorder associated with increased risk of developing choriocarinoma. Senescence
is decreased in CHM-EVTs, accompanied by exacerbated endoreduplication and hyperploidy.
We propose induction of cellular senescence as a ploidy-limiting mechanism during
normal human placentation and unravel a link between excessive polyploidization
and reduced senescence in CHM.
article_number: e1007698
article_processing_charge: No
author:
- first_name: Philipp
full_name: Velicky, Philipp
id: 39BDC62C-F248-11E8-B48F-1D18A9856A87
last_name: Velicky
orcid: 0000-0002-2340-7431
- first_name: Gudrun
full_name: Meinhardt, Gudrun
last_name: Meinhardt
- first_name: Kerstin
full_name: Plessl, Kerstin
last_name: Plessl
- first_name: Sigrid
full_name: Vondra, Sigrid
last_name: Vondra
- first_name: Tamara
full_name: Weiss, Tamara
last_name: Weiss
- first_name: Peter
full_name: Haslinger, Peter
last_name: Haslinger
- first_name: Thomas
full_name: Lendl, Thomas
last_name: Lendl
- first_name: Karin
full_name: Aumayr, Karin
last_name: Aumayr
- first_name: Mario
full_name: Mairhofer, Mario
last_name: Mairhofer
- first_name: Xiaowei
full_name: Zhu, Xiaowei
last_name: Zhu
- first_name: Birgit
full_name: Schütz, Birgit
last_name: Schütz
- first_name: Roberta L.
full_name: Hannibal, Roberta L.
last_name: Hannibal
- first_name: Robert
full_name: Lindau, Robert
last_name: Lindau
- first_name: Beatrix
full_name: Weil, Beatrix
last_name: Weil
- first_name: Jan
full_name: Ernerudh, Jan
last_name: Ernerudh
- first_name: Jürgen
full_name: Neesen, Jürgen
last_name: Neesen
- first_name: Gerda
full_name: Egger, Gerda
last_name: Egger
- first_name: Mario
full_name: Mikula, Mario
last_name: Mikula
- first_name: Clemens
full_name: Röhrl, Clemens
last_name: Röhrl
- first_name: Alexander E.
full_name: Urban, Alexander E.
last_name: Urban
- first_name: Julie
full_name: Baker, Julie
last_name: Baker
- first_name: Martin
full_name: Knöfler, Martin
last_name: Knöfler
- first_name: Jürgen
full_name: Pollheimer, Jürgen
last_name: Pollheimer
citation:
ama: Velicky P, Meinhardt G, Plessl K, et al. Genome amplification and cellular
senescence are hallmarks of human placenta development. PLOS Genetics.
2018;14(10). doi:10.1371/journal.pgen.1007698
apa: Velicky, P., Meinhardt, G., Plessl, K., Vondra, S., Weiss, T., Haslinger, P.,
… Pollheimer, J. (2018). Genome amplification and cellular senescence are hallmarks
of human placenta development. PLOS Genetics. Public Library of Science.
https://doi.org/10.1371/journal.pgen.1007698
chicago: Velicky, Philipp, Gudrun Meinhardt, Kerstin Plessl, Sigrid Vondra, Tamara
Weiss, Peter Haslinger, Thomas Lendl, et al. “Genome Amplification and Cellular
Senescence Are Hallmarks of Human Placenta Development.” PLOS Genetics.
Public Library of Science, 2018. https://doi.org/10.1371/journal.pgen.1007698.
ieee: P. Velicky et al., “Genome amplification and cellular senescence are
hallmarks of human placenta development,” PLOS Genetics, vol. 14, no. 10.
Public Library of Science, 2018.
ista: Velicky P, Meinhardt G, Plessl K, Vondra S, Weiss T, Haslinger P, Lendl T,
Aumayr K, Mairhofer M, Zhu X, Schütz B, Hannibal RL, Lindau R, Weil B, Ernerudh
J, Neesen J, Egger G, Mikula M, Röhrl C, Urban AE, Baker J, Knöfler M, Pollheimer
J. 2018. Genome amplification and cellular senescence are hallmarks of human placenta
development. PLOS Genetics. 14(10), e1007698.
mla: Velicky, Philipp, et al. “Genome Amplification and Cellular Senescence Are
Hallmarks of Human Placenta Development.” PLOS Genetics, vol. 14, no. 10,
e1007698, Public Library of Science, 2018, doi:10.1371/journal.pgen.1007698.
short: P. Velicky, G. Meinhardt, K. Plessl, S. Vondra, T. Weiss, P. Haslinger, T.
Lendl, K. Aumayr, M. Mairhofer, X. Zhu, B. Schütz, R.L. Hannibal, R. Lindau, B.
Weil, J. Ernerudh, J. Neesen, G. Egger, M. Mikula, C. Röhrl, A.E. Urban, J. Baker,
M. Knöfler, J. Pollheimer, PLOS Genetics 14 (2018).
date_created: 2019-02-14T13:07:45Z
date_published: 2018-10-12T00:00:00Z
date_updated: 2023-09-19T14:31:43Z
day: '12'
ddc:
- '570'
department:
- _id: JoDa
doi: 10.1371/journal.pgen.1007698
external_id:
isi:
- '000449328500025'
file:
- access_level: open_access
checksum: 34aa9a5972f61889c19f18be8ee787a0
content_type: application/pdf
creator: kschuh
date_created: 2019-02-14T13:14:35Z
date_updated: 2020-07-14T12:47:15Z
file_id: '6000'
file_name: 2018_PLOS_Velicky.pdf
file_size: 4592947
relation: main_file
file_date_updated: 2020-07-14T12:47:15Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
issue: '10'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Published Version
publication: PLOS Genetics
publication_identifier:
issn:
- 1553-7404
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Genome amplification and cellular senescence are hallmarks of human placenta
development
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: 14
year: '2018'
...
---
_id: '6499'
abstract:
- lang: eng
text: Expansion microscopy is a recently introduced imaging technique that achieves
super‐resolution through physically expanding the specimen by ~4×, after embedding
into a swellable gel. The resolution attained is, correspondingly, approximately
fourfold better than the diffraction limit, or ~70 nm. This is a major improvement
over conventional microscopy, but still lags behind modern STED or STORM setups,
whose resolution can reach 20–30 nm. We addressed this issue here by introducing
an improved gel recipe that enables an expansion factor of ~10× in each dimension,
which corresponds to an expansion of the sample volume by more than 1,000‐fold.
Our protocol, which we termed X10 microscopy, achieves a resolution of 25–30 nm
on conventional epifluorescence microscopes. X10 provides multi‐color images similar
or even superior to those produced with more challenging methods, such as STED,
STORM, and iterative expansion microscopy (iExM). X10 is therefore the cheapest
and easiest option for high‐quality super‐resolution imaging currently available.
X10 should be usable in any laboratory, irrespective of the machinery owned or
of the technical knowledge.
article_number: e45836
article_processing_charge: No
author:
- first_name: Sven M
full_name: Truckenbrodt, Sven M
id: 45812BD4-F248-11E8-B48F-1D18A9856A87
last_name: Truckenbrodt
- first_name: Manuel
full_name: Maidorn, Manuel
last_name: Maidorn
- first_name: Dagmar
full_name: Crzan, Dagmar
last_name: Crzan
- first_name: Hanna
full_name: Wildhagen, Hanna
last_name: Wildhagen
- first_name: Selda
full_name: Kabatas, Selda
last_name: Kabatas
- first_name: Silvio O
full_name: Rizzoli, Silvio O
last_name: Rizzoli
citation:
ama: Truckenbrodt SM, Maidorn M, Crzan D, Wildhagen H, Kabatas S, Rizzoli SO. X10
expansion microscopy enables 25‐nm resolution on conventional microscopes. EMBO
reports. 2018;19(9). doi:10.15252/embr.201845836
apa: Truckenbrodt, S. M., Maidorn, M., Crzan, D., Wildhagen, H., Kabatas, S., &
Rizzoli, S. O. (2018). X10 expansion microscopy enables 25‐nm resolution on conventional
microscopes. EMBO Reports. EMBO. https://doi.org/10.15252/embr.201845836
chicago: Truckenbrodt, Sven M, Manuel Maidorn, Dagmar Crzan, Hanna Wildhagen, Selda
Kabatas, and Silvio O Rizzoli. “X10 Expansion Microscopy Enables 25‐nm Resolution
on Conventional Microscopes.” EMBO Reports. EMBO, 2018. https://doi.org/10.15252/embr.201845836.
ieee: S. M. Truckenbrodt, M. Maidorn, D. Crzan, H. Wildhagen, S. Kabatas, and S.
O. Rizzoli, “X10 expansion microscopy enables 25‐nm resolution on conventional
microscopes,” EMBO reports, vol. 19, no. 9. EMBO, 2018.
ista: Truckenbrodt SM, Maidorn M, Crzan D, Wildhagen H, Kabatas S, Rizzoli SO. 2018.
X10 expansion microscopy enables 25‐nm resolution on conventional microscopes.
EMBO reports. 19(9), e45836.
mla: Truckenbrodt, Sven M., et al. “X10 Expansion Microscopy Enables 25‐nm Resolution
on Conventional Microscopes.” EMBO Reports, vol. 19, no. 9, e45836, EMBO,
2018, doi:10.15252/embr.201845836.
short: S.M. Truckenbrodt, M. Maidorn, D. Crzan, H. Wildhagen, S. Kabatas, S.O. Rizzoli,
EMBO Reports 19 (2018).
date_created: 2019-05-28T13:16:08Z
date_published: 2018-09-01T00:00:00Z
date_updated: 2023-09-19T14:52:32Z
day: '01'
ddc:
- '580'
department:
- _id: JoDa
doi: 10.15252/embr.201845836
external_id:
isi:
- '000443682200009'
file:
- access_level: open_access
checksum: 6ec90abc637f09cca3a7b6424d7e7a26
content_type: application/pdf
creator: kschuh
date_created: 2019-05-28T13:17:19Z
date_updated: 2020-07-14T12:47:32Z
file_id: '6500'
file_name: 2018_embo_Truckenbrodt.pdf
file_size: 2005572
relation: main_file
file_date_updated: 2020-07-14T12:47:32Z
has_accepted_license: '1'
intvolume: ' 19'
isi: 1
issue: '9'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
publication: EMBO reports
publication_identifier:
eissn:
- 1469-3178
issn:
- 1469-221X
publication_status: published
publisher: EMBO
quality_controlled: '1'
scopus_import: '1'
status: public
title: X10 expansion microscopy enables 25‐nm resolution on conventional microscopes
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: 19
year: '2018'
...
---
_id: '145'
abstract:
- lang: eng
text: Aged proteins can become hazardous to cellular function, by accumulating molecular
damage. This implies that cells should preferentially rely on newly produced ones.
We tested this hypothesis in cultured hippocampal neurons, focusing on synaptic
transmission. We found that newly synthesized vesicle proteins were incorporated
in the actively recycling pool of vesicles responsible for all neurotransmitter
release during physiological activity. We observed this for the calcium sensor
Synaptotagmin 1, for the neurotransmitter transporter VGAT, and for the fusion
protein VAMP2 (Synaptobrevin 2). Metabolic labeling of proteins and visualization
by secondary ion mass spectrometry enabled us to query the entire protein makeup
of the actively recycling vesicles, which we found to be younger than that of
non-recycling vesicles. The young vesicle proteins remained in use for up to ~
24 h, during which they participated in recycling a few hundred times. They were
afterward reluctant to release and were degraded after an additional ~ 24–48 h.
We suggest that the recycling pool of synaptic vesicles relies on newly synthesized
proteins, while the inactive reserve pool contains older proteins.
acknowledgement: We thank Reinhard Jahn for providing a plasmid for YFP-SNAP25. We
thank Erwin Neher for help with the development of the mathematical model of the
synaptic vesicle life cycle. We thank Martin Meschkat, Andreas Höbartner, Annedore
Punge, and Peer Hoopmann for help with the experiments. We thank Burkhard Rammner
for providing the illustrations of synaptic vesicle and protein dynamics. We thank
Manuel Maidorn, Martin Helm, and Katharina N. Richter for critically reading the
manuscript. S.T. was supported by an Excellence Stipend of the Göttingen Graduate
School for Neurosciences, Biophysics, and Molecular Biosciences (GGNB). E.F.F. is
a recipient of long-term fellowships from the European Molecular Biology Organization
(ALTF_797-2012) and from the Human Frontier Science Program (HFSP_LT000830/2013).
The work was supported by grants to S.O.R. from the European Research Council (ERC-2013-CoG
NeuroMolAnatomy) and from the Deutsche Forschungsgemeinschaft (Cluster of Excellence
Nanoscale Microscopy and Molecular Physiology of the Brain, SFB1190/P09, SFB889/A05,
and SFB1286/A03, and DFG RI 1967 7/1). The nanoSIMS instrument was funded by the
German Federal Ministry of Education and Research (03F0626A).
article_number: e98044
article_processing_charge: No
article_type: original
author:
- first_name: Sven M
full_name: Truckenbrodt, Sven M
id: 45812BD4-F248-11E8-B48F-1D18A9856A87
last_name: Truckenbrodt
- first_name: Abhiyan
full_name: Viplav, Abhiyan
last_name: Viplav
- first_name: Sebsatian
full_name: Jähne, Sebsatian
last_name: Jähne
- first_name: Angela
full_name: Vogts, Angela
last_name: Vogts
- first_name: Annette
full_name: Denker, Annette
last_name: Denker
- first_name: Hanna
full_name: Wildhagen, Hanna
last_name: Wildhagen
- first_name: Eugenio
full_name: Fornasiero, Eugenio
last_name: Fornasiero
- first_name: Silvio
full_name: Rizzoli, Silvio
last_name: Rizzoli
citation:
ama: Truckenbrodt SM, Viplav A, Jähne S, et al. Newly produced synaptic vesicle
proteins are preferentially used in synaptic transmission. The EMBO Journal.
2018;37(15). doi:10.15252/embj.201798044
apa: Truckenbrodt, S. M., Viplav, A., Jähne, S., Vogts, A., Denker, A., Wildhagen,
H., … Rizzoli, S. (2018). Newly produced synaptic vesicle proteins are preferentially
used in synaptic transmission. The EMBO Journal. Wiley. https://doi.org/10.15252/embj.201798044
chicago: Truckenbrodt, Sven M, Abhiyan Viplav, Sebsatian Jähne, Angela Vogts, Annette
Denker, Hanna Wildhagen, Eugenio Fornasiero, and Silvio Rizzoli. “Newly Produced
Synaptic Vesicle Proteins Are Preferentially Used in Synaptic Transmission.” The
EMBO Journal. Wiley, 2018. https://doi.org/10.15252/embj.201798044.
ieee: S. M. Truckenbrodt et al., “Newly produced synaptic vesicle proteins
are preferentially used in synaptic transmission,” The EMBO Journal, vol.
37, no. 15. Wiley, 2018.
ista: Truckenbrodt SM, Viplav A, Jähne S, Vogts A, Denker A, Wildhagen H, Fornasiero
E, Rizzoli S. 2018. Newly produced synaptic vesicle proteins are preferentially
used in synaptic transmission. The EMBO Journal. 37(15), e98044.
mla: Truckenbrodt, Sven M., et al. “Newly Produced Synaptic Vesicle Proteins Are
Preferentially Used in Synaptic Transmission.” The EMBO Journal, vol. 37,
no. 15, e98044, Wiley, 2018, doi:10.15252/embj.201798044.
short: S.M. Truckenbrodt, A. Viplav, S. Jähne, A. Vogts, A. Denker, H. Wildhagen,
E. Fornasiero, S. Rizzoli, The EMBO Journal 37 (2018).
date_created: 2018-12-11T11:44:52Z
date_published: 2018-08-01T00:00:00Z
date_updated: 2023-09-13T09:02:48Z
day: '01'
ddc:
- '570'
department:
- _id: JoDa
doi: 10.15252/embj.201798044
external_id:
isi:
- '000440416900005'
pmid:
- '29950309'
file:
- access_level: open_access
checksum: a540feb6c9af6aefc78de531461a8835
content_type: application/pdf
creator: dernst
date_created: 2018-12-17T14:17:29Z
date_updated: 2020-07-14T12:44:56Z
file_id: '5710'
file_name: 2018_EMBO_Truckenbrodt.pdf
file_size: 2846470
relation: main_file
file_date_updated: 2020-07-14T12:44:56Z
has_accepted_license: '1'
intvolume: ' 37'
isi: 1
issue: '15'
language:
- iso: eng
month: '08'
oa: 1
oa_version: Published Version
pmid: 1
publication: The EMBO Journal
publication_identifier:
issn:
- 0261-4189
publication_status: published
publisher: Wiley
publist_id: '7778'
quality_controlled: '1'
scopus_import: '1'
status: public
title: Newly produced synaptic vesicle proteins are preferentially used in synaptic
transmission
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: 37
year: '2018'
...
---
_id: '159'
abstract:
- lang: eng
text: L-type Ca2+ channels (LTCCs) play a crucial role in excitation-contraction
coupling and release of hormones from secretory cells. They are targets of antihypertensive
and antiarrhythmic drugs such as diltiazem. Here, we present a photoswitchable
diltiazem, FHU-779, which can be used to reversibly block endogenous LTCCs by
light. FHU-779 is as potent as diltiazem and can be used to place pancreatic β-cell
function and cardiac activity under optical control.
article_processing_charge: No
article_type: original
author:
- first_name: Timm
full_name: Fehrentz, Timm
last_name: Fehrentz
- first_name: Florian
full_name: Huber, Florian
last_name: Huber
- first_name: Nina
full_name: Hartrampf, Nina
last_name: Hartrampf
- first_name: Tobias
full_name: Bruegmann, Tobias
last_name: Bruegmann
- first_name: James
full_name: Frank, James
last_name: Frank
- first_name: Nicholas
full_name: Fine, Nicholas
last_name: Fine
- first_name: Daniela
full_name: Malan, Daniela
last_name: Malan
- 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: Denis
full_name: Tikhonov, Denis
last_name: Tikhonov
- first_name: Maritn
full_name: Sumser, Maritn
last_name: Sumser
- first_name: Philipp
full_name: Sasse, Philipp
last_name: Sasse
- first_name: David
full_name: Hodson, David
last_name: Hodson
- first_name: Boris
full_name: Zhorov, Boris
last_name: Zhorov
- first_name: Nikolaj
full_name: Klocker, Nikolaj
last_name: Klocker
- first_name: Dirk
full_name: Trauner, Dirk
last_name: Trauner
citation:
ama: Fehrentz T, Huber F, Hartrampf N, et al. Optical control of L-type Ca2+ channels
using a diltiazem photoswitch. Nature Chemical Biology. 2018;14(8):764-767.
doi:10.1038/s41589-018-0090-8
apa: Fehrentz, T., Huber, F., Hartrampf, N., Bruegmann, T., Frank, J., Fine, N.,
… Trauner, D. (2018). Optical control of L-type Ca2+ channels using a diltiazem
photoswitch. Nature Chemical Biology. Nature Publishing Group. https://doi.org/10.1038/s41589-018-0090-8
chicago: Fehrentz, Timm, Florian Huber, Nina Hartrampf, Tobias Bruegmann, James
Frank, Nicholas Fine, Daniela Malan, et al. “Optical Control of L-Type Ca2+ Channels
Using a Diltiazem Photoswitch.” Nature Chemical Biology. Nature Publishing
Group, 2018. https://doi.org/10.1038/s41589-018-0090-8.
ieee: T. Fehrentz et al., “Optical control of L-type Ca2+ channels using
a diltiazem photoswitch,” Nature Chemical Biology, vol. 14, no. 8. Nature
Publishing Group, pp. 764–767, 2018.
ista: Fehrentz T, Huber F, Hartrampf N, Bruegmann T, Frank J, Fine N, Malan D, Danzl
JG, Tikhonov D, Sumser M, Sasse P, Hodson D, Zhorov B, Klocker N, Trauner D. 2018.
Optical control of L-type Ca2+ channels using a diltiazem photoswitch. Nature
Chemical Biology. 14(8), 764–767.
mla: Fehrentz, Timm, et al. “Optical Control of L-Type Ca2+ Channels Using a Diltiazem
Photoswitch.” Nature Chemical Biology, vol. 14, no. 8, Nature Publishing
Group, 2018, pp. 764–67, doi:10.1038/s41589-018-0090-8.
short: T. Fehrentz, F. Huber, N. Hartrampf, T. Bruegmann, J. Frank, N. Fine, D.
Malan, J.G. Danzl, D. Tikhonov, M. Sumser, P. Sasse, D. Hodson, B. Zhorov, N.
Klocker, D. Trauner, Nature Chemical Biology 14 (2018) 764–767.
date_created: 2018-12-11T11:44:56Z
date_published: 2018-07-16T00:00:00Z
date_updated: 2023-09-13T09:36:35Z
day: '16'
ddc:
- '570'
department:
- _id: JoDa
doi: 10.1038/s41589-018-0090-8
external_id:
isi:
- '000438970200010'
file:
- access_level: open_access
checksum: d42935094ec845f54a0688bf12986d62
content_type: application/pdf
creator: dernst
date_created: 2020-05-14T12:14:09Z
date_updated: 2020-07-14T12:45:03Z
file_id: '7832'
file_name: 2018_NatureChemicalBiology_Fehrentz.pdf
file_size: 6321000
relation: main_file
file_date_updated: 2020-07-14T12:45:03Z
has_accepted_license: '1'
intvolume: ' 14'
isi: 1
issue: '8'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Submitted Version
page: 764 - 767
publication: Nature Chemical Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '7762'
quality_controlled: '1'
related_material:
link:
- relation: erratum
url: https://doi.org/10.1038/s41589-021-00744-3
scopus_import: '1'
status: public
title: Optical control of L-type Ca2+ channels using a diltiazem photoswitch
type: journal_article
user_id: c635000d-4b10-11ee-a964-aac5a93f6ac1
volume: 14
year: '2018'
...
---
_id: '9229'
alternative_title:
- Molecular and cellular neuroscience
article_processing_charge: No
article_type: letter_note
author:
- first_name: Johann G
full_name: Danzl, Johann G
id: 42EFD3B6-F248-11E8-B48F-1D18A9856A87
last_name: Danzl
orcid: 0000-0001-8559-3973
citation:
ama: Danzl JG. Diffraction-unlimited optical imaging for synaptic physiology. Opera
Medica et Physiologica. 2018;4(S1):11. doi:10.20388/omp2018.00s1.001
apa: Danzl, J. G. (2018). Diffraction-unlimited optical imaging for synaptic physiology.
Opera Medica et Physiologica. Lobachevsky State University of Nizhny Novgorod.
https://doi.org/10.20388/omp2018.00s1.001
chicago: Danzl, Johann G. “Diffraction-Unlimited Optical Imaging for Synaptic Physiology.”
Opera Medica et Physiologica. Lobachevsky State University of Nizhny Novgorod,
2018. https://doi.org/10.20388/omp2018.00s1.001.
ieee: J. G. Danzl, “Diffraction-unlimited optical imaging for synaptic physiology,”
Opera Medica et Physiologica, vol. 4, no. S1. Lobachevsky State University
of Nizhny Novgorod, p. 11, 2018.
ista: Danzl JG. 2018. Diffraction-unlimited optical imaging for synaptic physiology.
Opera Medica et Physiologica. 4(S1), 11.
mla: Danzl, Johann G. “Diffraction-Unlimited Optical Imaging for Synaptic Physiology.”
Opera Medica et Physiologica, vol. 4, no. S1, Lobachevsky State University
of Nizhny Novgorod, 2018, p. 11, doi:10.20388/omp2018.00s1.001.
short: J.G. Danzl, Opera Medica et Physiologica 4 (2018) 11.
date_created: 2021-03-07T23:01:25Z
date_published: 2018-06-30T00:00:00Z
date_updated: 2021-12-03T07:31:05Z
day: '30'
department:
- _id: JoDa
doi: 10.20388/omp2018.00s1.001
intvolume: ' 4'
issue: S1
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://operamedphys.org/content/molecular-and-cellular-neuroscience
month: '06'
oa: 1
oa_version: Published Version
page: '11'
publication: Opera Medica et Physiologica
publication_identifier:
eissn:
- 2500-2295
issn:
- 2500-2287
publication_status: published
publisher: Lobachevsky State University of Nizhny Novgorod
quality_controlled: '1'
scopus_import: '1'
status: public
title: Diffraction-unlimited optical imaging for synaptic physiology
type: journal_article
user_id: 8b945eb4-e2f2-11eb-945a-df72226e66a9
volume: 4
year: '2018'
...