---
_id: '14794'
abstract:
- lang: eng
text: "Mosaic analysis with double markers (MADM) technology enables the sparse
labeling of genetically defined neurons. We present a protocol for time-lapse
imaging of cortical projection neuron migration in mice using MADM. We describe
steps for the isolation, culturing, and 4D imaging of neuronal dynamics in MADM-labeled
brain tissue. While this protocol is compatible with other single-cell labeling
methods, the MADM approach provides a genetic platform for the functional assessment
of cell-autonomous candidate gene function and the relative contribution of non-cell-autonomous
effects.\r\n\r\nFor complete details on the use and execution of this protocol,
please refer to Hansen et al. (2022),1 Contreras et al. (2021),2 and Amberg and
Hippenmeyer (2021).3"
acknowledged_ssus:
- _id: Bio
- _id: PreCl
acknowledgement: We thank Florian Pauler for discussion and his expert technical support.
This research was supported by the Scientific Service Units (SSU) at IST Austria
through resources provided by the Imaging and Optics Facility (IOF) and Preclinical
Facility (PCF). A.H.H. was a recipient of a DOC Fellowship (24812) of the Austrian
Academy of Sciences.
article_number: '102795'
article_processing_charge: Yes
article_type: review
author:
- first_name: Andi H
full_name: Hansen, Andi H
id: 38853E16-F248-11E8-B48F-1D18A9856A87
last_name: Hansen
- first_name: Simon
full_name: Hippenmeyer, Simon
id: 37B36620-F248-11E8-B48F-1D18A9856A87
last_name: Hippenmeyer
orcid: 0000-0003-2279-1061
citation:
ama: Hansen AH, Hippenmeyer S. Time-lapse imaging of cortical projection neuron
migration in mice using mosaic analysis with double markers. STAR Protocols.
2024;5(1). doi:10.1016/j.xpro.2023.102795
apa: Hansen, A. H., & Hippenmeyer, S. (2024). Time-lapse imaging of cortical
projection neuron migration in mice using mosaic analysis with double markers.
STAR Protocols. Elsevier. https://doi.org/10.1016/j.xpro.2023.102795
chicago: Hansen, Andi H, and Simon Hippenmeyer. “Time-Lapse Imaging of Cortical
Projection Neuron Migration in Mice Using Mosaic Analysis with Double Markers.”
STAR Protocols. Elsevier, 2024. https://doi.org/10.1016/j.xpro.2023.102795.
ieee: A. H. Hansen and S. Hippenmeyer, “Time-lapse imaging of cortical projection
neuron migration in mice using mosaic analysis with double markers,” STAR Protocols,
vol. 5, no. 1. Elsevier, 2024.
ista: Hansen AH, Hippenmeyer S. 2024. Time-lapse imaging of cortical projection
neuron migration in mice using mosaic analysis with double markers. STAR Protocols.
5(1), 102795.
mla: Hansen, Andi H., and Simon Hippenmeyer. “Time-Lapse Imaging of Cortical Projection
Neuron Migration in Mice Using Mosaic Analysis with Double Markers.” STAR Protocols,
vol. 5, no. 1, 102795, Elsevier, 2024, doi:10.1016/j.xpro.2023.102795.
short: A.H. Hansen, S. Hippenmeyer, STAR Protocols 5 (2024).
date_created: 2024-01-14T23:00:56Z
date_published: 2024-01-01T00:00:00Z
date_updated: 2024-01-17T10:32:31Z
day: '01'
department:
- _id: SiHi
doi: 10.1016/j.xpro.2023.102795
external_id:
pmid:
- '38165800'
intvolume: ' 5'
issue: '1'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.xpro.2023.102795
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: 2625A13E-B435-11E9-9278-68D0E5697425
grant_number: '24812'
name: Molecular Mechanisms of Radial Neuronal Migration
publication: STAR Protocols
publication_identifier:
eissn:
- 2666-1667
publication_status: epub_ahead
publisher: Elsevier
quality_controlled: '1'
related_material:
link:
- relation: software
url: http://github.com/hippenmeyerlab
scopus_import: '1'
status: public
title: Time-lapse imaging of cortical projection neuron migration in mice using mosaic
analysis with double markers
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 5
year: '2024'
...
---
_id: '14826'
abstract:
- lang: eng
text: The plant-signaling molecule auxin triggers fast and slow cellular responses
across land plants and algae. The nuclear auxin pathway mediates gene expression
and controls growth and development in land plants, but this pathway is absent
from algal sister groups. Several components of rapid responses have been identified
in Arabidopsis, but it is unknown if these are part of a conserved mechanism.
We recently identified a fast, proteome-wide phosphorylation response to auxin.
Here, we show that this response occurs across 5 land plant and algal species
and converges on a core group of shared targets. We found conserved rapid physiological
responses to auxin in the same species and identified rapidly accelerated fibrosarcoma
(RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation
across species. Genetic analysis connects this kinase to both auxin-triggered
protein phosphorylation and rapid cellular response, thus identifying an ancient
mechanism for fast auxin responses in the green lineage.
acknowledgement: 'We are grateful to Asuka Shitaku and Eri Koide for generating and
sharing the Marchantia PRAF-mCitrine line and Peng-Cheng Wang for sharing the Arabidopsis
raf mutant. We are grateful to our team members for discussions and helpful advice.
This work was supported by funding from the Netherlands Organization for Scientific
Research (NWO): VICI grant 865.14.001 and ENW-KLEIN OCENW.KLEIN.027 grants to D.W.;
VENI grant VI.VENI.212.003 to A.K.; the European Research Council AdG DIRNDL (contract
number 833867) to D.W.; CoG CATCH to J.S.; StG CELLONGATE (contract 803048) to M.F.;
and AdG ETAP (contract 742985) to J.F.; MEXT KAKENHI grant number JP19H05675 to
T.K.; JSPS KAKENHI grant number JP20H03275 to R.N.; Takeda Science Foundation to
R.N.; and the Austrian Science Fund (FWF, P29988) to J.F.'
article_processing_charge: Yes (in subscription journal)
article_type: original
author:
- first_name: Andre
full_name: Kuhn, Andre
last_name: Kuhn
- first_name: Mark
full_name: Roosjen, Mark
last_name: Roosjen
- first_name: Sumanth
full_name: Mutte, Sumanth
last_name: Mutte
- first_name: Shiv Mani
full_name: Dubey, Shiv Mani
last_name: Dubey
- first_name: Vanessa Polet
full_name: Carrillo Carrasco, Vanessa Polet
last_name: Carrillo Carrasco
- first_name: Sjef
full_name: Boeren, Sjef
last_name: Boeren
- first_name: Aline
full_name: Monzer, Aline
id: 2DB5D88C-D7B3-11E9-B8FD-7907E6697425
last_name: Monzer
- first_name: Jasper
full_name: Koehorst, Jasper
last_name: Koehorst
- first_name: Takayuki
full_name: Kohchi, Takayuki
last_name: Kohchi
- first_name: Ryuichi
full_name: Nishihama, Ryuichi
last_name: Nishihama
- first_name: Matyas
full_name: Fendrych, Matyas
id: 43905548-F248-11E8-B48F-1D18A9856A87
last_name: Fendrych
orcid: 0000-0002-9767-8699
- first_name: Joris
full_name: Sprakel, Joris
last_name: Sprakel
- first_name: Jiří
full_name: Friml, Jiří
id: 4159519E-F248-11E8-B48F-1D18A9856A87
last_name: Friml
orcid: 0000-0002-8302-7596
- first_name: Dolf
full_name: Weijers, Dolf
last_name: Weijers
citation:
ama: Kuhn A, Roosjen M, Mutte S, et al. RAF-like protein kinases mediate a deeply
conserved, rapid auxin response. Cell. 2024;187(1):130-148.e17. doi:10.1016/j.cell.2023.11.021
apa: Kuhn, A., Roosjen, M., Mutte, S., Dubey, S. M., Carrillo Carrasco, V. P., Boeren,
S., … Weijers, D. (2024). RAF-like protein kinases mediate a deeply conserved,
rapid auxin response. Cell. Elsevier. https://doi.org/10.1016/j.cell.2023.11.021
chicago: Kuhn, Andre, Mark Roosjen, Sumanth Mutte, Shiv Mani Dubey, Vanessa Polet
Carrillo Carrasco, Sjef Boeren, Aline Monzer, et al. “RAF-like Protein Kinases
Mediate a Deeply Conserved, Rapid Auxin Response.” Cell. Elsevier, 2024.
https://doi.org/10.1016/j.cell.2023.11.021.
ieee: A. Kuhn et al., “RAF-like protein kinases mediate a deeply conserved,
rapid auxin response,” Cell, vol. 187, no. 1. Elsevier, p. 130–148.e17,
2024.
ista: Kuhn A, Roosjen M, Mutte S, Dubey SM, Carrillo Carrasco VP, Boeren S, Monzer
A, Koehorst J, Kohchi T, Nishihama R, Fendrych M, Sprakel J, Friml J, Weijers
D. 2024. RAF-like protein kinases mediate a deeply conserved, rapid auxin response.
Cell. 187(1), 130–148.e17.
mla: Kuhn, Andre, et al. “RAF-like Protein Kinases Mediate a Deeply Conserved, Rapid
Auxin Response.” Cell, vol. 187, no. 1, Elsevier, 2024, p. 130–148.e17,
doi:10.1016/j.cell.2023.11.021.
short: A. Kuhn, M. Roosjen, S. Mutte, S.M. Dubey, V.P. Carrillo Carrasco, S. Boeren,
A. Monzer, J. Koehorst, T. Kohchi, R. Nishihama, M. Fendrych, J. Sprakel, J. Friml,
D. Weijers, Cell 187 (2024) 130–148.e17.
date_created: 2024-01-17T12:45:40Z
date_published: 2024-01-04T00:00:00Z
date_updated: 2024-01-22T13:43:40Z
day: '04'
ddc:
- '580'
department:
- _id: JiFr
doi: 10.1016/j.cell.2023.11.021
ec_funded: 1
external_id:
pmid:
- '38128538'
file:
- access_level: open_access
checksum: 06fd236a9ee0b46ccb05f44695bfc34b
content_type: application/pdf
creator: dernst
date_created: 2024-01-22T13:41:41Z
date_updated: 2024-01-22T13:41:41Z
file_id: '14874'
file_name: 2024_Cell_Kuhn.pdf
file_size: 13194060
relation: main_file
success: 1
file_date_updated: 2024-01-22T13:41:41Z
has_accepted_license: '1'
intvolume: ' 187'
issue: '1'
keyword:
- General Biochemistry
- Genetics and Molecular Biology
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '01'
oa: 1
oa_version: Published Version
page: 130-148.e17
pmid: 1
project:
- _id: 261099A6-B435-11E9-9278-68D0E5697425
call_identifier: H2020
grant_number: '742985'
name: Tracing Evolution of Auxin Transport and Polarity in Plants
- _id: 262EF96E-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: P29988
name: RNA-directed DNA methylation in plant development
publication: Cell
publication_identifier:
eissn:
- 1097-4172
issn:
- 0092-8674
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: RAF-like protein kinases mediate a deeply conserved, rapid auxin response
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
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 187
year: '2024'
...
---
_id: '14828'
abstract:
- lang: eng
text: Production of hydrogen at large scale requires development of non-noble, inexpensive,
and high-performing catalysts for constructing water-splitting devices. Herein,
we report the synthesis of Zn-doped NiO heterostructure (ZnNiO) catalysts at room
temperature via a coprecipitation method followed by drying (at 80 °C, 6 h) and
calcination at an elevated temperature of 400 °C for 5 h under three distinct
conditions, namely, air, N2, and vacuum. The vacuum-synthesized catalyst demonstrates
a low overpotential of 88 mV at −10 mA cm–2 and a small Tafel slope of 73 mV dec–1
suggesting relatively higher charge transfer kinetics for hydrogen evolution reactions
(HER) compared with the specimens synthesized under N2 or O2 atmosphere. It also
demonstrates an oxygen evolution (OER) overpotential of 260 mV at 10 mA cm–2 with
a low Tafel slope of 63 mV dec–1. In a full-cell water-splitting device, the vacuum-synthesized
ZnNiO heterostructure demonstrates a cell voltage of 1.94 V at 50 mA cm–2 and
shows remarkable stability over 24 h at a high current density of 100 mA cm–2.
It is also demonstrated in this study that Zn-doping, surface, and interface engineering
in transition-metal oxides play a crucial role in efficient electrocatalytic water
splitting. Also, the results obtained from density functional theory (DFT + U
= 0–8 eV), where U is the on-site Coulomb repulsion parameter also known as Hubbard
U, based electronic structure calculations confirm that Zn doping constructively
modifies the electronic structure, in both the valence band and the conduction
band, and found to be suitable in tailoring the carrier’s effective masses of
electrons and holes. The decrease in electron’s effective masses together with
large differences between the effective masses of electrons and holes is noticed,
which is found to be mainly responsible for achieving the best water-splitting
performance from a 9% Zn-doped NiO sample prepared under vacuum.
acknowledgement: This work was supported by the Technology Innovation Program (20011622,
Development of Battery System Applied High-Efficiency Heat Control Polymer and Part
Component) funded by the Ministry of Trade, Industry & Energy (MOTIE, Korea). Author
acknowledge to Prof. Tsunehiro Takeuchi from Toyota Technological Institute, Nagoya,
Japan for the support of computational resources.
article_processing_charge: No
article_type: original
author:
- first_name: Gundegowda Kalligowdanadoddi
full_name: Kiran, Gundegowda Kalligowdanadoddi
last_name: Kiran
- first_name: Saurabh
full_name: Singh, Saurabh
id: 12d625da-9cb3-11ed-9667-af09d37d3f0a
last_name: Singh
orcid: 0000-0003-2209-5269
- first_name: Neelima
full_name: Mahato, Neelima
last_name: Mahato
- first_name: Thupakula Venkata Madhukar
full_name: Sreekanth, Thupakula Venkata Madhukar
last_name: Sreekanth
- first_name: Gowra Raghupathy
full_name: Dillip, Gowra Raghupathy
last_name: Dillip
- first_name: Kisoo
full_name: Yoo, Kisoo
last_name: Yoo
- first_name: Jonghoon
full_name: Kim, Jonghoon
last_name: Kim
citation:
ama: Kiran GK, Singh S, Mahato N, et al. Interface engineering modulation combined
with electronic structure modification of Zn-doped NiO heterostructure for efficient
water-splitting activity. ACS Applied Energy Materials. 2024;7(1):214-229.
doi:10.1021/acsaem.3c02519
apa: Kiran, G. K., Singh, S., Mahato, N., Sreekanth, T. V. M., Dillip, G. R., Yoo,
K., & Kim, J. (2024). Interface engineering modulation combined with electronic
structure modification of Zn-doped NiO heterostructure for efficient water-splitting
activity. ACS Applied Energy Materials. American Chemical Society. https://doi.org/10.1021/acsaem.3c02519
chicago: Kiran, Gundegowda Kalligowdanadoddi, Saurabh Singh, Neelima Mahato, Thupakula
Venkata Madhukar Sreekanth, Gowra Raghupathy Dillip, Kisoo Yoo, and Jonghoon Kim.
“Interface Engineering Modulation Combined with Electronic Structure Modification
of Zn-Doped NiO Heterostructure for Efficient Water-Splitting Activity.” ACS
Applied Energy Materials. American Chemical Society, 2024. https://doi.org/10.1021/acsaem.3c02519.
ieee: G. K. Kiran et al., “Interface engineering modulation combined with
electronic structure modification of Zn-doped NiO heterostructure for efficient
water-splitting activity,” ACS Applied Energy Materials, vol. 7, no. 1.
American Chemical Society, pp. 214–229, 2024.
ista: Kiran GK, Singh S, Mahato N, Sreekanth TVM, Dillip GR, Yoo K, Kim J. 2024.
Interface engineering modulation combined with electronic structure modification
of Zn-doped NiO heterostructure for efficient water-splitting activity. ACS Applied
Energy Materials. 7(1), 214–229.
mla: Kiran, Gundegowda Kalligowdanadoddi, et al. “Interface Engineering Modulation
Combined with Electronic Structure Modification of Zn-Doped NiO Heterostructure
for Efficient Water-Splitting Activity.” ACS Applied Energy Materials,
vol. 7, no. 1, American Chemical Society, 2024, pp. 214–29, doi:10.1021/acsaem.3c02519.
short: G.K. Kiran, S. Singh, N. Mahato, T.V.M. Sreekanth, G.R. Dillip, K. Yoo, J.
Kim, ACS Applied Energy Materials 7 (2024) 214–229.
date_created: 2024-01-17T12:48:35Z
date_published: 2024-01-08T00:00:00Z
date_updated: 2024-01-22T13:47:39Z
day: '08'
department:
- _id: MaIb
doi: 10.1021/acsaem.3c02519
external_id:
isi:
- '001138342900001'
intvolume: ' 7'
isi: 1
issue: '1'
keyword:
- Electrical and Electronic Engineering
- Materials Chemistry
- Electrochemistry
- Energy Engineering and Power Technology
- Chemical Engineering (miscellaneous)
language:
- iso: eng
month: '01'
oa_version: None
page: 214-229
publication: ACS Applied Energy Materials
publication_identifier:
issn:
- 2574-0962
publication_status: published
publisher: American Chemical Society
quality_controlled: '1'
scopus_import: '1'
status: public
title: Interface engineering modulation combined with electronic structure modification
of Zn-doped NiO heterostructure for efficient water-splitting activity
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 7
year: '2024'
...
---
_id: '14834'
abstract:
- lang: eng
text: Bacteria divide by binary fission. The protein machine responsible for this
process is the divisome, a transient assembly of more than 30 proteins in and
on the surface of the cytoplasmic membrane. Together, they constrict the cell
envelope and remodel the peptidoglycan layer to eventually split the cell into
two. For Escherichia coli, most molecular players involved in this process have
probably been identified, but obtaining the quantitative information needed for
a mechanistic understanding can often not be achieved from experiments in vivo
alone. Since the discovery of the Z-ring more than 30 years ago, in vitro reconstitution
experiments have been crucial to shed light on molecular processes normally hidden
in the complex environment of the living cell. In this review, we summarize how
rebuilding the divisome from purified components – or at least parts of it - have
been instrumental to obtain the detailed mechanistic understanding of the bacterial
cell division machinery that we have today.
acknowledgement: We acknowledge members of the Loose laboratory at ISTA for helpful
discussions—in particular M. Kojic for his insightful comments. This work was supported
by the Austrian Science Fund (FWF P34607) to M.L.
article_number: '151380'
article_processing_charge: Yes
article_type: review
author:
- first_name: Philipp
full_name: Radler, Philipp
id: 40136C2A-F248-11E8-B48F-1D18A9856A87
last_name: Radler
orcid: '0000-0001-9198-2182 '
- first_name: Martin
full_name: Loose, Martin
id: 462D4284-F248-11E8-B48F-1D18A9856A87
last_name: Loose
orcid: 0000-0001-7309-9724
citation:
ama: 'Radler P, Loose M. A dynamic duo: Understanding the roles of FtsZ and FtsA
for Escherichia coli cell division through in vitro approaches. European Journal
of Cell Biology. 2024;103(1). doi:10.1016/j.ejcb.2023.151380'
apa: 'Radler, P., & Loose, M. (2024). A dynamic duo: Understanding the roles
of FtsZ and FtsA for Escherichia coli cell division through in vitro approaches.
European Journal of Cell Biology. Elsevier. https://doi.org/10.1016/j.ejcb.2023.151380'
chicago: 'Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles
of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.”
European Journal of Cell Biology. Elsevier, 2024. https://doi.org/10.1016/j.ejcb.2023.151380.'
ieee: 'P. Radler and M. Loose, “A dynamic duo: Understanding the roles of FtsZ and
FtsA for Escherichia coli cell division through in vitro approaches,” European
Journal of Cell Biology, vol. 103, no. 1. Elsevier, 2024.'
ista: 'Radler P, Loose M. 2024. A dynamic duo: Understanding the roles of FtsZ and
FtsA for Escherichia coli cell division through in vitro approaches. European
Journal of Cell Biology. 103(1), 151380.'
mla: 'Radler, Philipp, and Martin Loose. “A Dynamic Duo: Understanding the Roles
of FtsZ and FtsA for Escherichia Coli Cell Division through in Vitro Approaches.”
European Journal of Cell Biology, vol. 103, no. 1, 151380, Elsevier, 2024,
doi:10.1016/j.ejcb.2023.151380.'
short: P. Radler, M. Loose, European Journal of Cell Biology 103 (2024).
date_created: 2024-01-18T08:16:43Z
date_published: 2024-01-12T00:00:00Z
date_updated: 2024-01-23T08:37:13Z
day: '12'
ddc:
- '570'
department:
- _id: MaLo
doi: 10.1016/j.ejcb.2023.151380
external_id:
pmid:
- '38218128'
has_accepted_license: '1'
intvolume: ' 103'
issue: '1'
keyword:
- Cell Biology
- General Medicine
- Histology
- Pathology and Forensic Medicine
language:
- iso: eng
main_file_link:
- open_access: '1'
url: https://doi.org/10.1016/j.ejcb.2023.151380
month: '01'
oa: 1
oa_version: Published Version
pmid: 1
project:
- _id: fc38323b-9c52-11eb-aca3-ff8afb4a011d
grant_number: P34607
name: "Understanding bacterial cell division by in vitro\r\nreconstitution"
publication: European Journal of Cell Biology
publication_identifier:
issn:
- 0171-9335
publication_status: epub_ahead
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: 'A dynamic duo: Understanding the roles of FtsZ and FtsA for Escherichia coli
cell division through in vitro approaches'
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: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 103
year: '2024'
...
---
_id: '14841'
abstract:
- lang: eng
text: De novo heterozygous variants in KCNC2 encoding the voltage-gated potassium
(K+) channel subunit Kv3.2 are a recently described cause of developmental and
epileptic encephalopathy (DEE). A de novo variant in KCNC2 c.374G > A (p.Cys125Tyr)
was identified via exome sequencing in a patient with DEE. Relative to wild-type
Kv3.2, Kv3.2-p.Cys125Tyr induces K+ currents exhibiting a large hyperpolarizing
shift in the voltage dependence of activation, accelerated activation, and delayed
deactivation consistent with a relative stabilization of the open conformation,
along with increased current density. Leveraging the cryogenic electron microscopy
(cryo-EM) structure of Kv3.1, molecular dynamic simulations suggest that a strong
π-π stacking interaction between the variant Tyr125 and Tyr156 in the α-6 helix
of the T1 domain promotes a relative stabilization of the open conformation of
the channel, which underlies the observed gain of function. A multicompartment
computational model of a Kv3-expressing parvalbumin-positive cerebral cortex fast-spiking
γ-aminobutyric acidergic (GABAergic) interneuron (PV-IN) demonstrates how the
Kv3.2-Cys125Tyr variant impairs neuronal excitability and dysregulates inhibition
in cerebral cortex circuits to explain the resulting epilepsy.
acknowledgement: This work was supported by an ERC Consolidator Grant (SYNAPSEEK)
to T.P.V., the NOMIS Foundation through the NOMIS Fellowships program at IST Austria
to C.B.C., a Jefferson Synaptic Biology Center Pilot Project Grant to M.C., NIH
NINDS U54 NS108874 (PI, Alfred L. George), and NIH NINDS R01 NS122887 to E.M.G.
The computations were enabled by resources provided by the Swedish National Infrastructure
for Computing (SNIC) at the PDC Center for High-Performance Computing, KTH Royal
Institute of Technology, partially funded by the Swedish Research Council through
grant agreement no. 2018-05973. We thank Akshay Sridhar for the fruitful discussion
of the project.
article_number: e2307776121
article_processing_charge: No
article_type: original
author:
- first_name: Jerome
full_name: Clatot, Jerome
last_name: Clatot
- first_name: Christopher
full_name: Currin, Christopher
id: e8321fc5-3091-11eb-8a53-83f309a11ac9
last_name: Currin
orcid: 0000-0002-4809-5059
- first_name: Qiansheng
full_name: Liang, Qiansheng
last_name: Liang
- first_name: Tanadet
full_name: Pipatpolkai, Tanadet
last_name: Pipatpolkai
- first_name: Shavonne L.
full_name: Massey, Shavonne L.
last_name: Massey
- first_name: Ingo
full_name: Helbig, Ingo
last_name: Helbig
- first_name: Lucie
full_name: Delemotte, Lucie
last_name: Delemotte
- first_name: Tim P
full_name: Vogels, Tim P
id: CB6FF8D2-008F-11EA-8E08-2637E6697425
last_name: Vogels
orcid: 0000-0003-3295-6181
- first_name: Manuel
full_name: Covarrubias, Manuel
last_name: Covarrubias
- first_name: Ethan M.
full_name: Goldberg, Ethan M.
last_name: Goldberg
citation:
ama: Clatot J, Currin C, Liang Q, et al. A structurally precise mechanism links
an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction.
Proceedings of the National Academy of Sciences of the United States of America.
2024;121(3). doi:10.1073/pnas.2307776121
apa: Clatot, J., Currin, C., Liang, Q., Pipatpolkai, T., Massey, S. L., Helbig,
I., … Goldberg, E. M. (2024). A structurally precise mechanism links an epilepsy-associated
KCNC2 potassium channel mutation to interneuron dysfunction. Proceedings of
the National Academy of Sciences of the United States of America. Proceedings
of the National Academy of Sciences. https://doi.org/10.1073/pnas.2307776121
chicago: Clatot, Jerome, Christopher Currin, Qiansheng Liang, Tanadet Pipatpolkai,
Shavonne L. Massey, Ingo Helbig, Lucie Delemotte, Tim P Vogels, Manuel Covarrubias,
and Ethan M. Goldberg. “A Structurally Precise Mechanism Links an Epilepsy-Associated
KCNC2 Potassium Channel Mutation to Interneuron Dysfunction.” Proceedings of
the National Academy of Sciences of the United States of America. Proceedings
of the National Academy of Sciences, 2024. https://doi.org/10.1073/pnas.2307776121.
ieee: J. Clatot et al., “A structurally precise mechanism links an epilepsy-associated
KCNC2 potassium channel mutation to interneuron dysfunction,” Proceedings of
the National Academy of Sciences of the United States of America, vol. 121,
no. 3. Proceedings of the National Academy of Sciences, 2024.
ista: Clatot J, Currin C, Liang Q, Pipatpolkai T, Massey SL, Helbig I, Delemotte
L, Vogels TP, Covarrubias M, Goldberg EM. 2024. A structurally precise mechanism
links an epilepsy-associated KCNC2 potassium channel mutation to interneuron dysfunction.
Proceedings of the National Academy of Sciences of the United States of America.
121(3), e2307776121.
mla: Clatot, Jerome, et al. “A Structurally Precise Mechanism Links an Epilepsy-Associated
KCNC2 Potassium Channel Mutation to Interneuron Dysfunction.” Proceedings of
the National Academy of Sciences of the United States of America, vol. 121,
no. 3, e2307776121, Proceedings of the National Academy of Sciences, 2024, doi:10.1073/pnas.2307776121.
short: J. Clatot, C. Currin, Q. Liang, T. Pipatpolkai, S.L. Massey, I. Helbig, L.
Delemotte, T.P. Vogels, M. Covarrubias, E.M. Goldberg, Proceedings of the National
Academy of Sciences of the United States of America 121 (2024).
date_created: 2024-01-21T23:00:56Z
date_published: 2024-01-16T00:00:00Z
date_updated: 2024-01-23T10:20:40Z
day: '16'
department:
- _id: TiVo
doi: 10.1073/pnas.2307776121
ec_funded: 1
external_id:
pmid:
- '38194456'
intvolume: ' 121'
issue: '3'
language:
- iso: eng
month: '01'
oa_version: None
pmid: 1
project:
- _id: 0aacfa84-070f-11eb-9043-d7eb2c709234
call_identifier: H2020
grant_number: '819603'
name: Learning the shape of synaptic plasticity rules for neuronal architectures
and function through machine learning.
publication: Proceedings of the National Academy of Sciences of the United States
of America
publication_identifier:
eissn:
- 1091-6490
publication_status: published
publisher: Proceedings of the National Academy of Sciences
quality_controlled: '1'
related_material:
link:
- relation: software
url: 'https://github.com/ChrisCurrin/pv-kcnc2 '
scopus_import: '1'
status: public
title: A structurally precise mechanism links an epilepsy-associated KCNC2 potassium
channel mutation to interneuron dysfunction
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 121
year: '2024'
...