A constricted opening in Kir channels does not impede potassium conduction

The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K + ions maintain a complete hydration shell while passing between the transmemb...

Full description

Saved in:
Bibliographic Details
Published inNature communications Vol. 11; no. 1; pp. 3024 - 13
Main Authors Black, Katrina A., He, Sitong, Jin, Ruitao, Miller, David M., Bolla, Jani R., Clarke, Oliver B., Johnson, Paul, Windley, Monique, Burns, Christopher J., Hill, Adam P., Laver, Derek, Robinson, Carol V., Smith, Brian J., Gulbis, Jacqueline M.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 15.06.2020
Nature Publishing Group
Nature Portfolio
Subjects
631/114
631/45/535
631/57
82/58
Channel gating
Channels
Computer simulation
Conduction
Conformation
Cytosol
Cytosol - chemistry
Cytosol - metabolism
Dehydration
Electric Conductivity
Electric Impedance
Free energy
G Protein-Coupled Inwardly-Rectifying Potassium Channels - chemistry
G Protein-Coupled Inwardly-Rectifying Potassium Channels - genetics
G Protein-Coupled Inwardly-Rectifying Potassium Channels - metabolism
Humanities and Social Sciences
Humans
Intracellular
Ion Transport
Ions
Ions - chemistry
Ions - metabolism
Model testing
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Potassium
Potassium - chemistry
Potassium - metabolism
Potassium channels
Potassium channels (inwardly-rectifying)
Potassium currents
Protein Conformation
Science
Science (multidisciplinary)
Water - metabolism
Water chemistry
Online AccessGet full text

Cover

Abstract The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K + ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K + channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K + ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K + permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism. The transition between conducting and non-conducting states of K + channels has been explained by conformational changes at the intracellular entrance to the conduction pathway. Here authors demonstrate that control over K + currents in Kir channels is not explained by the canonical pore-gating model, as conduction is not impaired by a constricted inner helix bundle.
AbstractList The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism.
The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K + ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K + channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K + ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K + permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism. The transition between conducting and non-conducting states of K + channels has been explained by conformational changes at the intracellular entrance to the conduction pathway. Here authors demonstrate that control over K + currents in Kir channels is not explained by the canonical pore-gating model, as conduction is not impaired by a constricted inner helix bundle.
The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K + ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K + channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K + ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K + permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism.
The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like intracellular entrance to the pore. It is based on the premise that K+ ions maintain a complete hydration shell while passing between the transmembrane cavity and cytosol, which must be accommodated. To put the canonical model to the test, we locked the conformation of a Kir K+ channel to prevent widening of the narrow collar. Unexpectedly, conduction was unimpaired in the locked channels. In parallel, we employed all-atom molecular dynamics to simulate K+ ions moving along the conduction pathway between the lower cavity and cytosol. During simulations, the constriction did not significantly widen. Instead, transient loss of some water molecules facilitated K+ permeation through the collar. The low free energy barrier to partial dehydration in the absence of conformational change indicates Kir channels are not gated by the canonical mechanism.The transition between conducting and non-conducting states of K+ channels has been explained by conformational changes at the intracellular entrance to the conduction pathway. Here authors demonstrate that control over K+ currents in Kir channels is not explained by the canonical pore-gating model, as conduction is not impaired by a constricted inner helix bundle.
The transition between conducting and non-conducting states of K+ channels has been explained by conformational changes at the intracellular entrance to the conduction pathway. Here authors demonstrate that control over K+ currents in Kir channels is not explained by the canonical pore-gating model, as conduction is not impaired by a constricted inner helix bundle.
ArticleNumber 3024
Author Hill, Adam P.
Gulbis, Jacqueline M.
Miller, David M.
Clarke, Oliver B.
Johnson, Paul
Laver, Derek
Burns, Christopher J.
Black, Katrina A.
Jin, Ruitao
He, Sitong
Windley, Monique
Robinson, Carol V.
Smith, Brian J.
Bolla, Jani R.
Author_xml – sequence: 1
  givenname: Katrina A.
  surname: Black
  fullname: Black, Katrina A.
  organization: Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne
– sequence: 2
  givenname: Sitong
  surname: He
  fullname: He, Sitong
  organization: La Trobe Institute for Molecular Science, La Trobe University
– sequence: 3
  givenname: Ruitao
  orcidid: 0000-0002-7934-250X
  surname: Jin
  fullname: Jin, Ruitao
  organization: La Trobe Institute for Molecular Science, La Trobe University
– sequence: 4
  givenname: David M.
  surname: Miller
  fullname: Miller, David M.
  organization: Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne
– sequence: 5
  givenname: Jani R.
  orcidid: 0000-0003-4346-182X
  surname: Bolla
  fullname: Bolla, Jani R.
  organization: Physical and Theoretical Chemistry Laboratory, University of Oxford
– sequence: 6
  givenname: Oliver B.
  surname: Clarke
  fullname: Clarke, Oliver B.
  organization: Biochemistry and Molecular Biophysics, Columbia University
– sequence: 7
  givenname: Paul
  surname: Johnson
  fullname: Johnson, Paul
  organization: School of Biomedical Sciences and Pharmacy, The University of Newcastle
– sequence: 8
  givenname: Monique
  surname: Windley
  fullname: Windley, Monique
  organization: Computational Cardiology Laboratory, Victor Chang Cardiac Research Institute
– sequence: 9
  givenname: Christopher J.
  orcidid: 0000-0002-4463-4916
  surname: Burns
  fullname: Burns, Christopher J.
  organization: Department of Medical Biology, The University of Melbourne, Chemical Biology Division, The Walter and Eliza Hall Institute of Medical Research
– sequence: 10
  givenname: Adam P.
  surname: Hill
  fullname: Hill, Adam P.
  organization: Computational Cardiology Laboratory, Victor Chang Cardiac Research Institute
– sequence: 11
  givenname: Derek
  surname: Laver
  fullname: Laver, Derek
  organization: School of Biomedical Sciences and Pharmacy, The University of Newcastle
– sequence: 12
  givenname: Carol V.
  orcidid: 0000-0001-7829-5505
  surname: Robinson
  fullname: Robinson, Carol V.
  organization: Physical and Theoretical Chemistry Laboratory, University of Oxford
– sequence: 13
  givenname: Brian J.
  orcidid: 0000-0003-0498-1910
  surname: Smith
  fullname: Smith, Brian J.
  email: brian.smith@latrobe.edu.au
  organization: La Trobe Institute for Molecular Science, La Trobe University
– sequence: 14
  givenname: Jacqueline M.
  orcidid: 0000-0003-2091-2237
  surname: Gulbis
  fullname: Gulbis, Jacqueline M.
  email: jgulbis@wehi.edu.au
  organization: Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, Department of Medical Biology, The University of Melbourne
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32541684$$D View this record in MEDLINE/PubMed
BookMark eNp9kUlPHDEQha0IFJbwB3KILOXcxFt7uURCKAsBiQs5WzVeBo9m7I7djZR_nx6aELjEF1tV731V1jtBB7nkgNB7Ss4p4fpTE1RI1RFGOiq1YB15g44ZEbSjivGDF-8jdNbahsyHG6qFeIuOOOvF3nWMflxgV3Iba3Jj8LgMIae8xinj61Sxu4ecw7ZhX0LDuYw47YbgAx7KCK2labd3-8mNqeR36DDCtoWzp_sU_fz65e7ye3dz--3q8uKmc70gYydXkkqAyBUXmqgofHTQM2ViVCo4Ar1zXoOXEoRw2gkFsTdOBibAhMj5KbpauL7Axg417aD-tgWSfSyUurZQx-S2wVIfe65WRmnHhdfR8BX0wUlDlQRD4sz6vLCGabUL3oU8Vti-gr7u5HRv1-XBKmZ6pfQM-PgEqOXXFNpoN2Wqef6_ZYJyxgVnZFaxReVqaa2G-DyBEruP0y5x2jlO-xin3Zs-vNzt2fI3vFnAF0GbW3kd6r_Z_8H-AVJSrcY
CitedBy_id crossref_primary_10_1016_j_celrep_2021_109619
crossref_primary_10_1038_s41467_023_37260_y
crossref_primary_10_1016_j_sbi_2023_102541
crossref_primary_10_1152_ajpcell_00093_2022
crossref_primary_10_1085_jgp_202213196
crossref_primary_10_3389_fphys_2024_1386645
crossref_primary_10_3390_cells9091956
crossref_primary_10_1038_s41586_022_04637_w
crossref_primary_10_1016_j_chaos_2023_114333
crossref_primary_10_1038_s41467_022_28148_4
crossref_primary_10_1002_qua_27100
crossref_primary_10_3389_fmolb_2021_711975
Cites_doi 10.1038/srep34325
10.1038/sj.emboj.7601828
10.1038/nature20812
10.1038/nature10370
10.1038/349305a0
10.1007/s00894-017-3302-3
10.1074/jbc.273.27.16946
10.1016/S0076-6879(97)76066-X
10.1016/j.nbd.2011.03.016
10.1113/jphysiol.1985.sp015585
10.1126/science.7973666
10.18632/oncotarget.16949
10.1085/jgp.200609579
10.1107/S0907444911056058
10.1126/science.1085028
10.1038/s41598-017-04681-x
10.1021/ac0110552
10.1002/cpbi.3
10.1016/j.jmb.2009.02.034
10.1038/nature12241
10.1085/jgp.201912359
10.1107/S0907444902016657
10.1056/NEJMoa1110740
10.1107/S0021889807021206
10.1038/nature19767
10.1139/cjpp-2012-0413
10.1002/jcc.23702
10.1107/S0907444904019158
10.1126/science.273.5277.956
10.1073/pnas.1602815113
10.1016/j.lfs.2018.10.012
10.1016/j.cell.2011.07.046
10.1038/nmeth.4067
10.1016/j.bpc.2006.07.002
10.1038/368255a0
10.1016/0263-7855(96)00018-5
10.1074/jbc.M503503200
10.1107/S0909049502015170
10.1073/pnas.2635314100
10.1016/S0022-2836(02)00380-7
10.1085/jgp.201711801
10.1038/emboj.2011.268
10.1002/glia.21205
10.1038/nsmb.2473
10.1038/35882
10.1074/jbc.M113.501833
10.1529/biophysj.105.077073
10.1038/nsmb.2208
10.1038/nmeth.3771
10.1073/pnas.1003072107
10.1107/S0907444908043795
10.1016/j.bpc.2006.04.015
10.1126/science.1228757
10.1038/nprot.2007.73
10.1038/nature25752
10.1107/S0907444909047337
10.1126/science.1213808
10.1038/nature22988
10.1107/S0907444994003112
10.1016/j.softx.2015.06.001
10.1021/ct100494z
10.1074/jbc.272.9.5388
10.1038/372366a0
10.1073/pnas.0700554104
10.1038/nn.3691
10.1016/j.coph.2013.11.002
10.1016/j.cell.2010.05.003
10.7554/eLife.32481
ContentType Journal Article
Copyright The Author(s) 2020
The Author(s) 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml – notice: The Author(s) 2020
– notice: The Author(s) 2020. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
DBID C6C
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
3V.
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7X7
7XB
88E
8AO
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABUWG
AFKRA
ARAPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
LK8
M0S
M1P
M7P
P5Z
P62
P64
PIMPY
PQEST
PQQKQ
PQUKI
PRINS
RC3
SOI
5PM
DOA
DOI 10.1038/s41467-020-16842-0
DatabaseName SpringerOpen
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
ProQuest Central (Corporate)
Bacteriology Abstracts (Microbiology B)
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Ecology Abstracts
Entomology Abstracts (Full archive)
Environment Abstracts
Immunology Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
Nucleic Acids Abstracts
Oncogenes and Growth Factors Abstracts
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
ProQuest Pharma Collection
Technology Research Database
ProQuest SciTech Collection
ProQuest Technology Collection
ProQuest Natural Science Collection
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest Central
Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology Collection
Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One Community College
ProQuest Central Korea
Engineering Research Database
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
AIDS and Cancer Research Abstracts
SciTech Premium Collection
ProQuest Health & Medical Complete (Alumni)
Biological Sciences
Health & Medical Collection (Alumni Edition)
Medical Database
Biological Science Database
Advanced Technologies & Aerospace Database
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
Publicly Available Content Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
Genetics Abstracts
Environment Abstracts
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Publicly Available Content Database
ProQuest Central Student
Oncogenes and Growth Factors Abstracts
ProQuest Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Nucleic Acids Abstracts
SciTech Premium Collection
ProQuest Central China
Environmental Sciences and Pollution Management
Health Research Premium Collection
Natural Science Collection
Biological Science Collection
Chemoreception Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
ProQuest Medical Library (Alumni)
Advanced Technologies & Aerospace Collection
ProQuest Biological Science Collection
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
ProQuest Technology Collection
Health Research Premium Collection (Alumni)
Biological Science Database
Ecology Abstracts
ProQuest Hospital Collection (Alumni)
Biotechnology and BioEngineering Abstracts
Entomology Abstracts
ProQuest Health & Medical Complete
ProQuest One Academic UKI Edition
Engineering Research Database
ProQuest One Academic
Calcium & Calcified Tissue Abstracts
Technology Collection
Technology Research Database
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
Genetics Abstracts
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Bacteriology Abstracts (Microbiology B)
AIDS and Cancer Research Abstracts
ProQuest SciTech Collection
Advanced Technologies & Aerospace Database
ProQuest Medical Library
Immunology Abstracts
Environment Abstracts
ProQuest Central (Alumni)
DatabaseTitleList MEDLINE

CrossRef
Publicly Available Content Database
Database_xml – sequence: 1
  dbid: C6C
  name: SpringerOpen
  url: http://www.springeropen.com/
  sourceTypes: Publisher
– sequence: 2
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 3
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 4
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 5
  dbid: 8FG
  name: ProQuest Technology Collection
  url: https://search.proquest.com/technologycollection1
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 2041-1723
EndPage 13
ExternalDocumentID oai_doaj_org_article_1df537b978c34d8f93ba5ec69176a90f
10_1038_s41467_020_16842_0
32541684
Genre Research Support, Non-U.S. Gov't
Journal Article
GrantInformation_xml – fundername: RCUK | Medical Research Council (MRC)
  grantid: MR/N020413/1
  funderid: https://doi.org/10.13039/501100000265
– fundername: Department of Health | National Health and Medical Research Council (NHMRC)
  grantid: 1006624 and 1080682
  funderid: https://doi.org/10.13039/501100000925
– fundername: Medical Research Council
  grantid: MR/N020413/1
– fundername: ;
  grantid: MR/N020413/1
– fundername: ;
  grantid: 1006624 and 1080682
GroupedDBID ---
0R~
39C
3V.
53G
5VS
70F
7X7
88E
8AO
8FE
8FG
8FH
8FI
8FJ
AAHBH
AAJSJ
ABUWG
ACGFO
ACGFS
ACIWK
ACMJI
ACPRK
ACSMW
ADBBV
ADFRT
ADRAZ
AENEX
AFKRA
AFRAH
AHMBA
AJTQC
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AMTXH
AOIJS
ARAPS
ASPBG
AVWKF
AZFZN
BBNVY
BCNDV
BENPR
BGLVJ
BHPHI
BPHCQ
BVXVI
C6C
CCPQU
DIK
EBLON
EBS
EE.
EMOBN
F5P
FEDTE
FYUFA
GROUPED_DOAJ
HCIFZ
HMCUK
HVGLF
HYE
HZ~
KQ8
LK8
M1P
M48
M7P
M~E
NAO
O9-
OK1
P2P
P62
PIMPY
PQQKQ
PROAC
PSQYO
RNS
RNT
RNTTT
RPM
SNYQT
SV3
TSG
UKHRP
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7XB
8FD
8FK
AZQEC
C1K
DWQXO
FR3
GNUQQ
H94
K9.
P64
PQEST
PQUKI
PRINS
RC3
SOI
5PM
ID FETCH-LOGICAL-c540t-6b616aaf3734807f4dfca5279ff77ec0a5ccd8ad66a44c8c47af59c6e24a9ef33
IEDL.DBID RPM
ISSN 2041-1723
IngestDate Tue Oct 22 15:12:31 EDT 2024
Tue Sep 17 20:57:41 EDT 2024
Thu Oct 10 18:03:10 EDT 2024
Thu Nov 21 21:02:13 EST 2024
Sat Sep 28 08:20:17 EDT 2024
Fri Oct 11 20:38:17 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Language English
License Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c540t-6b616aaf3734807f4dfca5279ff77ec0a5ccd8ad66a44c8c47af59c6e24a9ef33
ORCID 0000-0003-2091-2237
0000-0001-7829-5505
0000-0002-7934-250X
0000-0002-4463-4916
0000-0003-4346-182X
0000-0003-0498-1910
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7295778/
PMID 32541684
PQID 2413234320
PQPubID 546298
PageCount 13
ParticipantIDs doaj_primary_oai_doaj_org_article_1df537b978c34d8f93ba5ec69176a90f
pubmedcentral_primary_oai_pubmedcentral_nih_gov_7295778
proquest_journals_2413234320
crossref_primary_10_1038_s41467_020_16842_0
pubmed_primary_32541684
springer_journals_10_1038_s41467_020_16842_0
PublicationCentury 2000
PublicationDate 2020-06-15
PublicationDateYYYYMMDD 2020-06-15
PublicationDate_xml – month: 06
  year: 2020
  text: 2020-06-15
  day: 15
PublicationDecade 2020
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
PublicationTitle Nature communications
PublicationTitleAbbrev Nat Commun
PublicationTitleAlternate Nat Commun
PublicationYear 2020
Publisher Nature Publishing Group UK
Nature Publishing Group
Nature Portfolio
Publisher_xml – name: Nature Publishing Group UK
– name: Nature Publishing Group
– name: Nature Portfolio
References Allen, Andersen, Roux (CR29) 2004; 101
Hilgemann, Ball (CR52) 1996; 273
Sobott, Hernández, McCammon, Tito, Robinson (CR71) 2002; 74
Sun (CR1) 2018; 213
Fan (CR11) 2018; 37
Fan, Makielski (CR53) 1997; 272
Wickman (CR23) 1994; 368
Bostick, Brooks (CR31) 2007; 104
Thuringer (CR9) 2017; 8
McPhillips (CR55) 2002; 9
Szuts (CR12) 2013; 91
Otwinowski, Minor (CR56) 1997; 276
Piechotta (CR46) 2011; 30
CR34
Lopatin, Makhina, Nichols (CR16) 1994; 372
Wilkens, Aldrich (CR44) 2006; 128
Gault (CR72) 2016; 13
Wu (CR66) 2014; 35
McCoy (CR59) 2007; 40
Sicca (CR3) 2011; 43
Papazian, Timpe, Jan, Jan (CR43) 1991; 349
Reichold (CR7) 2010; 107
Rapedius (CR54) 2005; 280
Kuo (CR17) 2003; 300
Brohawn, del Mármol, Mackinnon (CR37) 2012; 335
Hou, Pedi, Diver, Long (CR38) 2012; 338
Smart (CR63) 2012; 68
Swale, Kharade, Denton (CR10) 2014; 15
Hansen, Tao, Mackinnon (CR20) 2011; 477
Bavro (CR27) 2012; 19
Pašalić (CR50) 2017; 23
Adams (CR62) 2002; 58
Zubcevic (CR28) 2014; 289
Abraham (CR67) 2015; 1-2
Huang (CR68) 2017; 14
Emsley, Cowtan (CR61) 2004; 60
Varma, Rempe (CR33) 2006; 124
Humphrey, Dalke, Schulten (CR69) 1996; 14
Tong (CR8) 2014; 17
Whorton, Mackinnon (CR19) 2011; 147
Yang (CR39) 2016; 538
Sicca (CR2) 2016; 6
Nishida, Cadene, Chait, Mackinnon (CR21) 2007; 26
Hub, de Groot, van der Spoel (CR30) 2010; 6
Whorton, Mackinnon (CR25) 2013; 498
Lee, Letts, Mackinnon (CR35) 2009; 387
Hernández, Robinson (CR70) 2007; 2
Katz (CR13) 1949; 3
Brunger, DeLaBarre, Davies, Weis (CR60) 2009; 65
Krapivinsky (CR24) 1998; 273
Srivastava (CR6) 2012; 367
Im, Roux (CR32) 2002; 319
Haj-Yasein (CR4) 2011; 59
Ficker, Taglialatela, Wible, Henley, Brown (CR15) 1994; 266
Lacin (CR36) 2017; 149
CR26
Kabsch (CR57) 2010; 66
Clarke (CR18) 2010; 141
Glaaser, Slesinger (CR41) 2017; 7
(CR58) 1994; 50
Allen, Andersen, Roux (CR49) 2006; 124
Huang, Feng, Hilgemann (CR22) 1998; 391
Posson, McCoy, Nimigean (CR45) 2013; 20
CR64
Bernsteiner, Zangerl-Plessl, Chen, Stary-Weinzinger (CR51) 2019; 151
Lolicato (CR47) 2017; 547
Allen, Andersen, Roux (CR48) 2006; 90
Webb, Sali (CR65) 2016; 54
Park, Campbell, Mackinnon (CR40) 2017; 541
Ashcroft, Heiny, Vergara (CR14) 1985; 359
Su, Brown, Wang, Mackinnon (CR42) 2016; 113
Cui (CR5) 2018; 554
IW Glaaser (16842_CR41) 2017; 7
TW Allen (16842_CR49) 2006; 124
F Sobott (16842_CR71) 2002; 74
G Krapivinsky (16842_CR24) 1998; 273
S Varma (16842_CR33) 2006; 124
Z Otwinowski (16842_CR56) 1997; 276
MJ Abraham (16842_CR67) 2015; 1-2
J Gault (16842_CR72) 2016; 13
A Kuo (16842_CR17) 2003; 300
D Thuringer (16842_CR9) 2017; 8
TM McPhillips (16842_CR55) 2002; 9
F Sicca (16842_CR3) 2011; 43
H Yang (16842_CR39) 2016; 538
AJ McCoy (16842_CR59) 2007; 40
W Kabsch (16842_CR57) 2010; 66
KD Wickman (16842_CR23) 1994; 368
W Im (16842_CR32) 2002; 319
OS Smart (16842_CR63) 2012; 68
NN Haj-Yasein (16842_CR4) 2011; 59
L Zubcevic (16842_CR28) 2014; 289
B Katz (16842_CR13) 1949; 3
M Lolicato (16842_CR47) 2017; 547
X Hou (16842_CR38) 2012; 338
M Reichold (16842_CR7) 2010; 107
SB Hansen (16842_CR20) 2011; 477
16842_CR34
DR Swale (16842_CR10) 2014; 15
TW Allen (16842_CR29) 2004; 101
H Pašalić (16842_CR50) 2017; 23
16842_CR26
B Webb (16842_CR65) 2016; 54
M Rapedius (16842_CR54) 2005; 280
Y Cui (16842_CR5) 2018; 554
Z Su (16842_CR42) 2016; 113
AN Lopatin (16842_CR16) 1994; 372
J Huang (16842_CR68) 2017; 14
M Nishida (16842_CR21) 2007; 26
JS Hub (16842_CR30) 2010; 6
TW Allen (16842_CR48) 2006; 90
CM Wilkens (16842_CR44) 2006; 128
FM Ashcroft (16842_CR14) 1985; 359
EL Wu (16842_CR66) 2014; 35
C Fan (16842_CR11) 2018; 37
MR Whorton (16842_CR25) 2013; 498
16842_CR64
E Park (16842_CR40) 2017; 541
AT Brunger (16842_CR60) 2009; 65
PL Piechotta (16842_CR46) 2011; 30
V Szuts (16842_CR12) 2013; 91
SG Brohawn (16842_CR37) 2012; 335
DL Bostick (16842_CR31) 2007; 104
R Srivastava (16842_CR6) 2012; 367
H Hernández (16842_CR70) 2007; 2
Collaborative Computational Project, Number 4. (16842_CR58) 1994; 50
E Lacin (16842_CR36) 2017; 149
H Bernsteiner (16842_CR51) 2019; 151
S-Y Lee (16842_CR35) 2009; 387
OB Clarke (16842_CR18) 2010; 141
DJ Posson (16842_CR45) 2013; 20
P Emsley (16842_CR61) 2004; 60
E Ficker (16842_CR15) 1994; 266
VN Bavro (16842_CR27) 2012; 19
CL Huang (16842_CR22) 1998; 391
C Sun (16842_CR1) 2018; 213
MR Whorton (16842_CR19) 2011; 147
W Humphrey (16842_CR69) 1996; 14
X Tong (16842_CR8) 2014; 17
Z Fan (16842_CR53) 1997; 272
F Sicca (16842_CR2) 2016; 6
DM Papazian (16842_CR43) 1991; 349
DW Hilgemann (16842_CR52) 1996; 273
PD Adams (16842_CR62) 2002; 58
References_xml – volume: 6
  year: 2016
  ident: CR2
  article-title: Gain-of-function defects of astrocytic Kir4.1 channels in children with autism spectrum disorders and epilepsy
  publication-title: Sci. Rep.
  doi: 10.1038/srep34325
  contributor:
    fullname: Sicca
– volume: 26
  start-page: 4005
  year: 2007
  end-page: 4015
  ident: CR21
  article-title: Crystal structure of a Kir3.1-prokaryotic Kir channel chimera
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7601828
  contributor:
    fullname: Mackinnon
– volume: 541
  start-page: 500
  year: 2017
  end-page: 505
  ident: CR40
  article-title: Structure of a CLC chloride ion channel by cryo-electron microscopy
  publication-title: Nature
  doi: 10.1038/nature20812
  contributor:
    fullname: Mackinnon
– volume: 477
  start-page: 495
  year: 2011
  end-page: 498
  ident: CR20
  article-title: Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2
  publication-title: Nature
  doi: 10.1038/nature10370
  contributor:
    fullname: Mackinnon
– volume: 349
  start-page: 305
  year: 1991
  end-page: 310
  ident: CR43
  article-title: Alteration of voltage-dependence of Shaker potassium channel by mutations in the S4 sequence
  publication-title: Nature
  doi: 10.1038/349305a0
  contributor:
    fullname: Jan
– volume: 23
  start-page: 131
  year: 2017
  ident: CR50
  article-title: Cation-π interactions in competition with cation microhydration: a theoretical study of alkali metal cation-pyrene complexes
  publication-title: J. Mol. Model
  doi: 10.1007/s00894-017-3302-3
  contributor:
    fullname: Pašalić
– volume: 273
  start-page: 16946
  year: 1998
  end-page: 16952
  ident: CR24
  article-title: Gβγ binding to GIRK4 subunit is critical for G protein-gated K channel activation
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.27.16946
  contributor:
    fullname: Krapivinsky
– volume: 276
  start-page: 307
  year: 1997
  end-page: 326
  ident: CR56
  article-title: Processing of X-ray diffraction data collected in oscillation mode
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(97)76066-X
  contributor:
    fullname: Minor
– volume: 43
  start-page: 239
  year: 2011
  end-page: 247
  ident: CR3
  article-title: Autism with seizures and intellectual disability: possible causative role of gain-of-function of the inwardly-rectifying K+ channel Kir4.1
  publication-title: Neurobiol. Dis.
  doi: 10.1016/j.nbd.2011.03.016
  contributor:
    fullname: Sicca
– volume: 359
  start-page: 269
  year: 1985
  end-page: 291
  ident: CR14
  article-title: Inward rectification in the transverse tubular system of frog skeletal muscle studied with potentiometric dyes
  publication-title: J. Physiol.
  doi: 10.1113/jphysiol.1985.sp015585
  contributor:
    fullname: Vergara
– volume: 266
  start-page: 1068
  year: 1994
  end-page: 1072
  ident: CR15
  article-title: Spermine and spermidine as gating molecules for inward rectifier K+ channels
  publication-title: Science
  doi: 10.1126/science.7973666
  contributor:
    fullname: Brown
– volume: 8
  start-page: 37681
  year: 2017
  end-page: 37693
  ident: CR9
  article-title: Modulation of the inwardly rectifying potassium channel Kir4.1 by the pro-invasive miR-5096 in glioblastoma cells
  publication-title: Oncotarget
  doi: 10.18632/oncotarget.16949
  contributor:
    fullname: Thuringer
– volume: 128
  start-page: 347
  year: 2006
  end-page: 364
  ident: CR44
  article-title: State-independent block of BK channels by an intracellular quaternary ammonium
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.200609579
  contributor:
    fullname: Aldrich
– volume: 68
  start-page: 368
  year: 2012
  end-page: 380
  ident: CR63
  article-title: Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444911056058
  contributor:
    fullname: Smart
– volume: 300
  start-page: 1922
  year: 2003
  end-page: 1926
  ident: CR17
  article-title: Crystal structure of the potassium channel KirBac1.1 in the closed state
  publication-title: Science
  doi: 10.1126/science.1085028
  contributor:
    fullname: Kuo
– volume: 7
  year: 2017
  ident: CR41
  article-title: Dual activation of neuronal G protein-gated inwardly rectifying potassium (GIRK) channels by cholesterol and alcohol
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-017-04681-x
  contributor:
    fullname: Slesinger
– volume: 37
  start-page: 193
  year: 2018
  end-page: 203
  ident: CR11
  article-title: Kir2.2 p.Thr140Met: a genetic susceptibility to sporadic periodic paralysis
  publication-title: Acta Myol.
  contributor:
    fullname: Fan
– volume: 74
  start-page: 1402
  year: 2002
  end-page: 1407
  ident: CR71
  article-title: A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
  publication-title: Anal. Chem.
  doi: 10.1021/ac0110552
  contributor:
    fullname: Robinson
– volume: 54
  start-page: 5.6.1
  year: 2016
  end-page: 5.6.37
  ident: CR65
  article-title: Comparative Protein Structure Modeling Using MODELLER
  publication-title: Curr. Protoc. Bioinformatics
  doi: 10.1002/cpbi.3
  contributor:
    fullname: Sali
– volume: 387
  start-page: 1055
  year: 2009
  end-page: 1060
  ident: CR35
  article-title: Functional reconstitution of purified human Hv1 H channels
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.02.034
  contributor:
    fullname: Mackinnon
– volume: 498
  start-page: 190
  year: 2013
  end-page: 197
  ident: CR25
  article-title: X-ray structure of the mammalian GIRK2-βγ G-protein complex
  publication-title: Nature
  doi: 10.1038/nature12241
  contributor:
    fullname: Mackinnon
– volume: 151
  start-page: 1231
  year: 2019
  end-page: 1246
  ident: CR51
  article-title: Conduction through a narrow inward-rectifier K channel pore
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.201912359
  contributor:
    fullname: Stary-Weinzinger
– volume: 58
  start-page: 1948
  year: 2002
  end-page: 1954
  ident: CR62
  article-title: PHENIX: building new software for automated crystallographic structure determination
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444902016657
  contributor:
    fullname: Adams
– volume: 367
  start-page: 115
  year: 2012
  end-page: 123
  ident: CR6
  article-title: Potassium channel KIR4.1 as an immune target in multiple sclerosis
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJMoa1110740
  contributor:
    fullname: Srivastava
– volume: 40
  start-page: 658
  year: 2007
  end-page: 674
  ident: CR59
  article-title: Phaser crystallographic software
  publication-title: J. Appl Crystallogr
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: McCoy
– volume: 538
  start-page: 537
  year: 2016
  end-page: 541
  ident: CR39
  article-title: Pore architecture of TRIC channels and insights into their gating mechanism
  publication-title: Nature
  doi: 10.1038/nature19767
  contributor:
    fullname: Yang
– volume: 91
  start-page: 648
  year: 2013
  end-page: 656
  ident: CR12
  article-title: Altered expression of genes for Kir ion channels in dilated cardiomyopathy
  publication-title: Can. J. Physiol. Pharmacol.
  doi: 10.1139/cjpp-2012-0413
  contributor:
    fullname: Szuts
– volume: 35
  start-page: 1997
  year: 2014
  end-page: 2004
  ident: CR66
  article-title: CHARMM-GUI Membrane Builder toward realistic biological membrane simulations
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.23702
  contributor:
    fullname: Wu
– volume: 60
  start-page: 2126
  year: 2004
  end-page: 2132
  ident: CR61
  article-title: IUCr. Coot: model-building tools for molecular graphics
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444904019158
  contributor:
    fullname: Cowtan
– volume: 273
  start-page: 956
  year: 1996
  end-page: 959
  ident: CR52
  article-title: Regulation of cardiac Na ,Ca exchange and KATP potassium channels by PIP2
  publication-title: Science
  doi: 10.1126/science.273.5277.956
  contributor:
    fullname: Ball
– volume: 113
  start-page: 5748
  year: 2016
  end-page: 5753
  ident: CR42
  article-title: Novel cell-free high-throughput screening method for pharmacological tools targeting K+ channels
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1602815113
  contributor:
    fullname: Mackinnon
– volume: 213
  start-page: 183
  year: 2018
  end-page: 189
  ident: CR1
  article-title: Association study between inwardly rectifying potassium channels 2.1 and 4.1 and autism spectrum disorders
  publication-title: Life Sci.
  doi: 10.1016/j.lfs.2018.10.012
  contributor:
    fullname: Sun
– volume: 147
  start-page: 199
  year: 2011
  end-page: 208
  ident: CR19
  article-title: Crystal structure of the mammalian GIRK2 K+ channel and gating regulation by G proteins, PIP2, and sodium
  publication-title: Cell
  doi: 10.1016/j.cell.2011.07.046
  contributor:
    fullname: Mackinnon
– volume: 14
  start-page: 71
  year: 2017
  end-page: 73
  ident: CR68
  article-title: CHARMM36m: an improved force field for folded and intrinsically disordered proteins
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4067
  contributor:
    fullname: Huang
– volume: 124
  start-page: 192
  year: 2006
  end-page: 199
  ident: CR33
  article-title: Coordination numbers of alkali metal ions in aqueous solutions
  publication-title: Biophys. Chem.
  doi: 10.1016/j.bpc.2006.07.002
  contributor:
    fullname: Rempe
– volume: 368
  start-page: 255
  year: 1994
  end-page: 257
  ident: CR23
  article-title: Recombinant G-protein beta gamma-subunits activate the muscarinic-gated atrial potassium channel
  publication-title: Nature
  doi: 10.1038/368255a0
  contributor:
    fullname: Wickman
– volume: 14
  start-page: 27
  year: 1996
  end-page: 28
  ident: CR69
  article-title: VMD: visual molecular dynamic
  publication-title: J. Mol. Graph.
  doi: 10.1016/0263-7855(96)00018-5
  contributor:
    fullname: Schulten
– ident: CR64
– ident: CR26
– volume: 280
  start-page: 30760
  year: 2005
  end-page: 30767
  ident: CR54
  article-title: Long chain CoA esters as competitive antagonists of phosphatidylinositol 4,5-bisphosphate activation in Kir channels
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M503503200
  contributor:
    fullname: Rapedius
– volume: 9
  start-page: 401
  year: 2002
  end-page: 406
  ident: CR55
  article-title: Blu-Ice and the Distributed Control System: software for data acquisition and instrument control at macromolecular crystallography beamlines
  publication-title: J. Synchrotron Radiat.
  doi: 10.1107/S0909049502015170
  contributor:
    fullname: McPhillips
– volume: 101
  start-page: 117
  year: 2004
  end-page: 122
  ident: CR29
  article-title: Energetics of ion conduction through the gramicidin channel
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.2635314100
  contributor:
    fullname: Roux
– volume: 319
  start-page: 1177
  year: 2002
  end-page: 1197
  ident: CR32
  article-title: Ions and counterions in a biological channel: a molecular dynamics simulation of OmpF porin from in an explicit membrane with 1 M KCl aqueous salt solution
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(02)00380-7
  contributor:
    fullname: Roux
– volume: 149
  start-page: 799
  year: 2017
  end-page: 811
  ident: CR36
  article-title: Dynamic role of the tether helix in PIP2-dependent gating of a G protein-gated potassium channel
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.201711801
  contributor:
    fullname: Lacin
– volume: 30
  start-page: 3607
  year: 2011
  end-page: 3619
  ident: CR46
  article-title: The pore structure and gating mechanism of K2P channels
  publication-title: EMBO J.
  doi: 10.1038/emboj.2011.268
  contributor:
    fullname: Piechotta
– volume: 59
  start-page: 1635
  year: 2011
  end-page: 1642
  ident: CR4
  article-title: Evidence that compromised K+ spatial buffering contributes to the epileptogenic effect of mutations in the human Kir4.1 gene (KCNJ10)
  publication-title: Glia
  doi: 10.1002/glia.21205
  contributor:
    fullname: Haj-Yasein
– volume: 20
  start-page: 159
  year: 2013
  end-page: 166
  ident: CR45
  article-title: The voltage-dependent gate in MthK potassium channels is located at the selectivity filter
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2473
  contributor:
    fullname: Nimigean
– volume: 391
  start-page: 803
  year: 1998
  end-page: 806
  ident: CR22
  article-title: Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbg
  publication-title: Nature
  doi: 10.1038/35882
  contributor:
    fullname: Hilgemann
– volume: 289
  start-page: 143
  year: 2014
  end-page: 151
  ident: CR28
  article-title: Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.501833
  contributor:
    fullname: Zubcevic
– volume: 90
  start-page: 3447
  year: 2006
  end-page: 3468
  ident: CR48
  article-title: Ion permeation through a narrow channel: using gramicidin to ascertain all-atom molecular dynamics potential of mean force methodology and biomolecular force fields
  publication-title: Biophysj
  doi: 10.1529/biophysj.105.077073
  contributor:
    fullname: Roux
– volume: 19
  start-page: 158
  year: 2012
  end-page: 163
  ident: CR27
  article-title: Structure of a KirBac potassium channel with an open bundle crossing indicates a mechanism of channel gating
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2208
  contributor:
    fullname: Bavro
– volume: 13
  start-page: 333
  year: 2016
  end-page: 336
  ident: CR72
  article-title: High-resolution mass spectrometry of small molecules bound to membrane proteins
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.3771
  contributor:
    fullname: Gault
– volume: 107
  start-page: 14490
  year: 2010
  end-page: 14495
  ident: CR7
  article-title: KCNJ10 gene mutations causing EAST syndrome (epilepsy, ataxia, sensorineural deafness, and tubulopathy) disrupt channel function
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1003072107
  contributor:
    fullname: Reichold
– volume: 65
  start-page: 128
  year: 2009
  end-page: 133
  ident: CR60
  article-title: IUCr. X-ray structure determination at low resolution
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444908043795
  contributor:
    fullname: Weis
– volume: 124
  start-page: 251
  year: 2006
  end-page: 267
  ident: CR49
  article-title: Molecular dynamics—potential of mean force calculations as a tool for understanding ion permeation and selectivity in narrow channels
  publication-title: Biophys. Chem.
  doi: 10.1016/j.bpc.2006.04.015
  contributor:
    fullname: Roux
– volume: 338
  start-page: 1308
  year: 2012
  end-page: 1313
  ident: CR38
  article-title: Crystal structure of the calcium release-activated calcium channel Orai
  publication-title: Science
  doi: 10.1126/science.1228757
  contributor:
    fullname: Long
– volume: 2
  start-page: 715
  year: 2007
  end-page: 726
  ident: CR70
  article-title: Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2007.73
  contributor:
    fullname: Robinson
– volume: 554
  start-page: 323
  year: 2018
  end-page: 327
  ident: CR5
  article-title: Astroglial Kir4.1 in the lateral habenula drives neuronal bursts in depression
  publication-title: Nature
  doi: 10.1038/nature25752
  contributor:
    fullname: Cui
– volume: 66
  start-page: 125
  year: 2010
  end-page: 132
  ident: CR57
  article-title: XDS
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: Kabsch
– volume: 335
  start-page: 436
  year: 2012
  end-page: 441
  ident: CR37
  article-title: Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K ion channel
  publication-title: Science
  doi: 10.1126/science.1213808
  contributor:
    fullname: Mackinnon
– volume: 3
  start-page: 285
  year: 1949
  end-page: 299
  ident: CR13
  article-title: Les constantes electriques de la membrane du muscle
  publication-title: Arch. Sci. Physiol.
  contributor:
    fullname: Katz
– volume: 547
  start-page: 364
  year: 2017
  end-page: 368
  ident: CR47
  article-title: K2P2.1 (TREK-1)–activator complexes reveal a cryptic selectivity filter binding site
  publication-title: Nature
  doi: 10.1038/nature22988
  contributor:
    fullname: Lolicato
– volume: 50
  start-page: 760
  year: 1994
  end-page: 763
  ident: CR58
  article-title: The CCP4 suite: programs for protein crystallography
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444994003112
– volume: 1-2
  start-page: 19
  year: 2015
  end-page: 25
  ident: CR67
  article-title: GROMACS: high performance molecular simulations through multi-level parallelism from laptops to supercomputers
  publication-title: SoftwareX
  doi: 10.1016/j.softx.2015.06.001
  contributor:
    fullname: Abraham
– volume: 6
  start-page: 3713
  year: 2010
  end-page: 3720
  ident: CR30
  article-title: g_wham-A free weighted histogram analysis implementation including robust error and autocorrelation estimates
  publication-title: J. Chem. Theory Comput.
  doi: 10.1021/ct100494z
  contributor:
    fullname: van der Spoel
– volume: 272
  start-page: 5388
  year: 1997
  end-page: 5395
  ident: CR53
  article-title: Anionic phospholipids activate ATP-sensitive potassium channels
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.9.5388
  contributor:
    fullname: Makielski
– volume: 372
  start-page: 366
  year: 1994
  end-page: 369
  ident: CR16
  article-title: Potassium channel block by cytoplasmic polyamines as the mechanism of intrinsic rectification
  publication-title: Nature
  doi: 10.1038/372366a0
  contributor:
    fullname: Nichols
– volume: 104
  start-page: 9260
  year: 2007
  end-page: 9265
  ident: CR31
  article-title: Selectivity in K channels is due to topological control of the permeant ion's coordinated state
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.0700554104
  contributor:
    fullname: Brooks
– ident: CR34
– volume: 17
  start-page: 694
  year: 2014
  end-page: 703
  ident: CR8
  article-title: Astrocyte Kir4.1 ion channel deficits contribute to neuronal dysfunction in Huntington's disease model mice
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.3691
  contributor:
    fullname: Tong
– volume: 15
  start-page: 7
  year: 2014
  end-page: 15
  ident: CR10
  article-title: Cardiac and renal inward rectifier potassium channel pharmacology: emerging tools for integrative physiology and therapeutics
  publication-title: Curr. Opin. Pharm.
  doi: 10.1016/j.coph.2013.11.002
  contributor:
    fullname: Denton
– volume: 141
  start-page: 1018
  year: 2010
  end-page: 1029
  ident: CR18
  article-title: Domain reorientation and rotation of an intracellular assembly regulate conduction in Kir potassium channels
  publication-title: Cell
  doi: 10.1016/j.cell.2010.05.003
  contributor:
    fullname: Clarke
– volume: 35
  start-page: 1997
  year: 2014
  ident: 16842_CR66
  publication-title: J. Comput. Chem.
  doi: 10.1002/jcc.23702
  contributor:
    fullname: EL Wu
– volume: 128
  start-page: 347
  year: 2006
  ident: 16842_CR44
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.200609579
  contributor:
    fullname: CM Wilkens
– volume: 6
  year: 2016
  ident: 16842_CR2
  publication-title: Sci. Rep.
  doi: 10.1038/srep34325
  contributor:
    fullname: F Sicca
– volume: 15
  start-page: 7
  year: 2014
  ident: 16842_CR10
  publication-title: Curr. Opin. Pharm.
  doi: 10.1016/j.coph.2013.11.002
  contributor:
    fullname: DR Swale
– volume: 498
  start-page: 190
  year: 2013
  ident: 16842_CR25
  publication-title: Nature
  doi: 10.1038/nature12241
  contributor:
    fullname: MR Whorton
– volume: 54
  start-page: 5.6.1
  year: 2016
  ident: 16842_CR65
  publication-title: Curr. Protoc. Bioinformatics
  doi: 10.1002/cpbi.3
  contributor:
    fullname: B Webb
– volume: 66
  start-page: 125
  year: 2010
  ident: 16842_CR57
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444909047337
  contributor:
    fullname: W Kabsch
– volume: 59
  start-page: 1635
  year: 2011
  ident: 16842_CR4
  publication-title: Glia
  doi: 10.1002/glia.21205
  contributor:
    fullname: NN Haj-Yasein
– volume: 335
  start-page: 436
  year: 2012
  ident: 16842_CR37
  publication-title: Science
  doi: 10.1126/science.1213808
  contributor:
    fullname: SG Brohawn
– volume: 289
  start-page: 143
  year: 2014
  ident: 16842_CR28
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.501833
  contributor:
    fullname: L Zubcevic
– ident: 16842_CR64
– volume: 147
  start-page: 199
  year: 2011
  ident: 16842_CR19
  publication-title: Cell
  doi: 10.1016/j.cell.2011.07.046
  contributor:
    fullname: MR Whorton
– volume: 37
  start-page: 193
  year: 2018
  ident: 16842_CR11
  publication-title: Acta Myol.
  contributor:
    fullname: C Fan
– volume: 338
  start-page: 1308
  year: 2012
  ident: 16842_CR38
  publication-title: Science
  doi: 10.1126/science.1228757
  contributor:
    fullname: X Hou
– volume: 90
  start-page: 3447
  year: 2006
  ident: 16842_CR48
  publication-title: Biophysj
  doi: 10.1529/biophysj.105.077073
  contributor:
    fullname: TW Allen
– volume: 538
  start-page: 537
  year: 2016
  ident: 16842_CR39
  publication-title: Nature
  doi: 10.1038/nature19767
  contributor:
    fullname: H Yang
– volume: 17
  start-page: 694
  year: 2014
  ident: 16842_CR8
  publication-title: Nat. Neurosci.
  doi: 10.1038/nn.3691
  contributor:
    fullname: X Tong
– volume: 149
  start-page: 799
  year: 2017
  ident: 16842_CR36
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.201711801
  contributor:
    fullname: E Lacin
– volume: 541
  start-page: 500
  year: 2017
  ident: 16842_CR40
  publication-title: Nature
  doi: 10.1038/nature20812
  contributor:
    fullname: E Park
– volume: 391
  start-page: 803
  year: 1998
  ident: 16842_CR22
  publication-title: Nature
  doi: 10.1038/35882
  contributor:
    fullname: CL Huang
– volume: 3
  start-page: 285
  year: 1949
  ident: 16842_CR13
  publication-title: Arch. Sci. Physiol.
  contributor:
    fullname: B Katz
– volume: 141
  start-page: 1018
  year: 2010
  ident: 16842_CR18
  publication-title: Cell
  doi: 10.1016/j.cell.2010.05.003
  contributor:
    fullname: OB Clarke
– volume: 8
  start-page: 37681
  year: 2017
  ident: 16842_CR9
  publication-title: Oncotarget
  doi: 10.18632/oncotarget.16949
  contributor:
    fullname: D Thuringer
– volume: 151
  start-page: 1231
  year: 2019
  ident: 16842_CR51
  publication-title: J. Gen. Physiol.
  doi: 10.1085/jgp.201912359
  contributor:
    fullname: H Bernsteiner
– volume: 14
  start-page: 71
  year: 2017
  ident: 16842_CR68
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.4067
  contributor:
    fullname: J Huang
– volume: 74
  start-page: 1402
  year: 2002
  ident: 16842_CR71
  publication-title: Anal. Chem.
  doi: 10.1021/ac0110552
  contributor:
    fullname: F Sobott
– volume: 280
  start-page: 30760
  year: 2005
  ident: 16842_CR54
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M503503200
  contributor:
    fullname: M Rapedius
– volume: 1-2
  start-page: 19
  year: 2015
  ident: 16842_CR67
  publication-title: SoftwareX
  doi: 10.1016/j.softx.2015.06.001
  contributor:
    fullname: MJ Abraham
– volume: 372
  start-page: 366
  year: 1994
  ident: 16842_CR16
  publication-title: Nature
  doi: 10.1038/372366a0
  contributor:
    fullname: AN Lopatin
– volume: 124
  start-page: 251
  year: 2006
  ident: 16842_CR49
  publication-title: Biophys. Chem.
  doi: 10.1016/j.bpc.2006.04.015
  contributor:
    fullname: TW Allen
– volume: 19
  start-page: 158
  year: 2012
  ident: 16842_CR27
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2208
  contributor:
    fullname: VN Bavro
– ident: 16842_CR26
  doi: 10.7554/eLife.32481
– volume: 6
  start-page: 3713
  year: 2010
  ident: 16842_CR30
  publication-title: J. Chem. Theory Comput.
  doi: 10.1021/ct100494z
  contributor:
    fullname: JS Hub
– volume: 50
  start-page: 760
  year: 1994
  ident: 16842_CR58
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444994003112
  contributor:
    fullname: Collaborative Computational Project, Number 4.
– volume: 104
  start-page: 9260
  year: 2007
  ident: 16842_CR31
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.0700554104
  contributor:
    fullname: DL Bostick
– volume: 477
  start-page: 495
  year: 2011
  ident: 16842_CR20
  publication-title: Nature
  doi: 10.1038/nature10370
  contributor:
    fullname: SB Hansen
– volume: 107
  start-page: 14490
  year: 2010
  ident: 16842_CR7
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1003072107
  contributor:
    fullname: M Reichold
– volume: 13
  start-page: 333
  year: 2016
  ident: 16842_CR72
  publication-title: Nat. Methods
  doi: 10.1038/nmeth.3771
  contributor:
    fullname: J Gault
– volume: 65
  start-page: 128
  year: 2009
  ident: 16842_CR60
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444908043795
  contributor:
    fullname: AT Brunger
– volume: 124
  start-page: 192
  year: 2006
  ident: 16842_CR33
  publication-title: Biophys. Chem.
  doi: 10.1016/j.bpc.2006.07.002
  contributor:
    fullname: S Varma
– volume: 387
  start-page: 1055
  year: 2009
  ident: 16842_CR35
  publication-title: J. Mol. Biol.
  doi: 10.1016/j.jmb.2009.02.034
  contributor:
    fullname: S-Y Lee
– volume: 58
  start-page: 1948
  year: 2002
  ident: 16842_CR62
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444902016657
  contributor:
    fullname: PD Adams
– volume: 300
  start-page: 1922
  year: 2003
  ident: 16842_CR17
  publication-title: Science
  doi: 10.1126/science.1085028
  contributor:
    fullname: A Kuo
– volume: 276
  start-page: 307
  year: 1997
  ident: 16842_CR56
  publication-title: Methods Enzymol.
  doi: 10.1016/S0076-6879(97)76066-X
  contributor:
    fullname: Z Otwinowski
– volume: 43
  start-page: 239
  year: 2011
  ident: 16842_CR3
  publication-title: Neurobiol. Dis.
  doi: 10.1016/j.nbd.2011.03.016
  contributor:
    fullname: F Sicca
– volume: 368
  start-page: 255
  year: 1994
  ident: 16842_CR23
  publication-title: Nature
  doi: 10.1038/368255a0
  contributor:
    fullname: KD Wickman
– volume: 273
  start-page: 16946
  year: 1998
  ident: 16842_CR24
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.273.27.16946
  contributor:
    fullname: G Krapivinsky
– volume: 20
  start-page: 159
  year: 2013
  ident: 16842_CR45
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2473
  contributor:
    fullname: DJ Posson
– volume: 23
  start-page: 131
  year: 2017
  ident: 16842_CR50
  publication-title: J. Mol. Model
  doi: 10.1007/s00894-017-3302-3
  contributor:
    fullname: H Pašalić
– volume: 272
  start-page: 5388
  year: 1997
  ident: 16842_CR53
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.272.9.5388
  contributor:
    fullname: Z Fan
– volume: 91
  start-page: 648
  year: 2013
  ident: 16842_CR12
  publication-title: Can. J. Physiol. Pharmacol.
  doi: 10.1139/cjpp-2012-0413
  contributor:
    fullname: V Szuts
– volume: 26
  start-page: 4005
  year: 2007
  ident: 16842_CR21
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7601828
  contributor:
    fullname: M Nishida
– volume: 7
  year: 2017
  ident: 16842_CR41
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-017-04681-x
  contributor:
    fullname: IW Glaaser
– volume: 68
  start-page: 368
  year: 2012
  ident: 16842_CR63
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444911056058
  contributor:
    fullname: OS Smart
– volume: 367
  start-page: 115
  year: 2012
  ident: 16842_CR6
  publication-title: N. Engl. J. Med.
  doi: 10.1056/NEJMoa1110740
  contributor:
    fullname: R Srivastava
– volume: 213
  start-page: 183
  year: 2018
  ident: 16842_CR1
  publication-title: Life Sci.
  doi: 10.1016/j.lfs.2018.10.012
  contributor:
    fullname: C Sun
– volume: 101
  start-page: 117
  year: 2004
  ident: 16842_CR29
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.2635314100
  contributor:
    fullname: TW Allen
– volume: 30
  start-page: 3607
  year: 2011
  ident: 16842_CR46
  publication-title: EMBO J.
  doi: 10.1038/emboj.2011.268
  contributor:
    fullname: PL Piechotta
– volume: 359
  start-page: 269
  year: 1985
  ident: 16842_CR14
  publication-title: J. Physiol.
  doi: 10.1113/jphysiol.1985.sp015585
  contributor:
    fullname: FM Ashcroft
– volume: 349
  start-page: 305
  year: 1991
  ident: 16842_CR43
  publication-title: Nature
  doi: 10.1038/349305a0
  contributor:
    fullname: DM Papazian
– volume: 273
  start-page: 956
  year: 1996
  ident: 16842_CR52
  publication-title: Science
  doi: 10.1126/science.273.5277.956
  contributor:
    fullname: DW Hilgemann
– volume: 554
  start-page: 323
  year: 2018
  ident: 16842_CR5
  publication-title: Nature
  doi: 10.1038/nature25752
  contributor:
    fullname: Y Cui
– volume: 60
  start-page: 2126
  year: 2004
  ident: 16842_CR61
  publication-title: Acta Crystallogr. D. Biol. Crystallogr
  doi: 10.1107/S0907444904019158
  contributor:
    fullname: P Emsley
– volume: 113
  start-page: 5748
  year: 2016
  ident: 16842_CR42
  publication-title: Proc. Natl Acad. Sci. USA
  doi: 10.1073/pnas.1602815113
  contributor:
    fullname: Z Su
– volume: 266
  start-page: 1068
  year: 1994
  ident: 16842_CR15
  publication-title: Science
  doi: 10.1126/science.7973666
  contributor:
    fullname: E Ficker
– ident: 16842_CR34
– volume: 9
  start-page: 401
  year: 2002
  ident: 16842_CR55
  publication-title: J. Synchrotron Radiat.
  doi: 10.1107/S0909049502015170
  contributor:
    fullname: TM McPhillips
– volume: 14
  start-page: 27
  year: 1996
  ident: 16842_CR69
  publication-title: J. Mol. Graph.
  doi: 10.1016/0263-7855(96)00018-5
  contributor:
    fullname: W Humphrey
– volume: 2
  start-page: 715
  year: 2007
  ident: 16842_CR70
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2007.73
  contributor:
    fullname: H Hernández
– volume: 319
  start-page: 1177
  year: 2002
  ident: 16842_CR32
  publication-title: J. Mol. Biol.
  doi: 10.1016/S0022-2836(02)00380-7
  contributor:
    fullname: W Im
– volume: 40
  start-page: 658
  year: 2007
  ident: 16842_CR59
  publication-title: J. Appl Crystallogr
  doi: 10.1107/S0021889807021206
  contributor:
    fullname: AJ McCoy
– volume: 547
  start-page: 364
  year: 2017
  ident: 16842_CR47
  publication-title: Nature
  doi: 10.1038/nature22988
  contributor:
    fullname: M Lolicato
SSID ssj0000391844
Score 2.447908
Snippet The canonical mechanistic model explaining potassium channel gating is of a conformational change that alternately dilates and constricts a collar-like...
The transition between conducting and non-conducting states of K+ channels has been explained by conformational changes at the intracellular entrance to the...
SourceID doaj
pubmedcentral
proquest
crossref
pubmed
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 3024
SubjectTerms 631/114
631/45/535
631/57
82/58
Channel gating
Channels
Computer simulation
Conduction
Conformation
Cytosol
Cytosol - chemistry
Cytosol - metabolism
Dehydration
Electric Conductivity
Electric Impedance
Free energy
G Protein-Coupled Inwardly-Rectifying Potassium Channels - chemistry
G Protein-Coupled Inwardly-Rectifying Potassium Channels - genetics
G Protein-Coupled Inwardly-Rectifying Potassium Channels - metabolism
Humanities and Social Sciences
Humans
Intracellular
Ion Transport
Ions
Ions - chemistry
Ions - metabolism
Model testing
Molecular dynamics
Molecular Dynamics Simulation
multidisciplinary
Potassium
Potassium - chemistry
Potassium - metabolism
Potassium channels
Potassium channels (inwardly-rectifying)
Potassium currents
Protein Conformation
Science
Science (multidisciplinary)
Water - metabolism
Water chemistry
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1JS8UwEA4iCF7E3edGDt602DZbc1RRRMGTgreQZsEe7BNfPfjvnUn71OeCF6_dksyXzHzTSWYIOdBOay6szaIOecY5qzNdiSoDfSkCd0WsQ9ptcSMv7_jVvbj_VOoL94T16YF7wR0XPgqmanB2HOO-iprVVgQnwc2QVucxad-8_ORMJR3MNLgufDglk7PqeMKTTkBvqcDYU5bPWKKUsP8nlvl9s-SXiGkyRBfLZGlgkPSk7_kKmQvtKlnoa0q-rpGrE-qQ84F-AzJJsToWfIY2Lb1unime823BHFI_DhPajjvaAG_2gT6NO6DRzcsjvu37lLLr5O7i_PbsMhsKJmQOiFeXyVoW0trIMGVNriL30VlRKvwvq4LLrXDOV9ZLaTl3lePKRqGdDCW3OkTGNsh8O27DFqFlbZ0SuOaj53UJD0qmAFjBwaD5ohqRw6nwzFOfF8OkeDarTC9qA6I2SdQmH5FTlO_7k5jTOl0ApM2AtPkL6RHZnaJjhoU2MRgWLPFwLLSx2QP13goD5xc7MCJqBsKZbszeaZuHlGIbXA6hFIzyaAr2R5O_D3P7P4a5QxZLnKVYH0nskvnu-SXsAfHp6v00x98AT8P-_g
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Technology Collection
  dbid: 8FG
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELagCIkL4k2gIB-4gdUkfp9QQSxVkThRqTfL8QNyIFl20wP_nhknu9XyuiZObM_Y428eniHklQ3WCuk9yzbVTAjeMWukYSAvZRKhyV0q0Raf1dmFOL-Ul4vBbbuEVe5kYhHUcQxoIz9B_0-LtyDrt-sfDKtGoXd1KaFxk9xqWq0wpM-sPu5tLJj93Aix3JWpuTnZiiIZUGdq0APF6oPzqKTt_xvW_DNk8je_aTmOVvfI3QVH0tOZ8ffJjTQ8ILfnypI_H5LzUxoQ-YGUA0hJsUYW_Ib2A_3Ubyje9h3gUKRxTFs6jBPtAT3HRNfjBGC6v_qOX8c5sewjcrH68OX9GVvKJrAA8GtiqlON8j5zTFxT6yxiDl62Gq2zOoXayxCi8VEpL0QwQWifpQ0qtcLblDl_TI6GcUhPCW07H7TEnZ-j6FpoqLgG9koBx1psTEVe74jn1nN2DFe82ty4mdQOSO0KqV1dkXdI331LzGxdHoybr27ZKK6JWXLdgXIbuIgmW955mYICtVJ5W-eKHO-445bttnXXi6MiT2ZG7XvhoALjACqiD1h4MIzDN0P_rSTaBsVDag2zfLNj9nWX_57ms_-P8Dm50-L6w_pH8pgcTZur9AKAzdS9LKv3F6aU9hk
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELaqIlAvqLyXFuQDNwgk8fuAqoKoqiI4sVJvluMHRIKk7KYS_ffMOEmrheXCMYkdxzPj8ffF9gwhL4w3hgvnimRiWXDOmsJooQvwlyJyX6Um5t0Wn-Xpkp-di_MdMqc7mgS43krtMJ_UcvX99a-fV0cw4N-OR8b1mzXPwx2JUIXLSgVQ-Fs1zIy4xevTBPezZ2YGCA2fzs5sr7pH7jAgTXi1MVXliP7bYOjfuyn_WFLNM9XJPrk7QUx6PNrEPbITu_vk9ph08uoBOTumHkEhOEBAmxS7C6-hbUc_tiuKB4E7mC9p6OOadv1AWwDWIdKLfgCc3V7-wNphjDn7kCxPPnx5f1pMGRUKD8hsKGQjK-lcYhjTplSJh-SdqBX-uFXRl054H7QLUjrOvfZcuSSMl7HmzsTE2COy2_VdfEJo3TivBDqFFHhTQ0HJFGgeRFfrUOkFeTkLz16MgTNsXvBm2o5StyB1m6VuywV5h_K9LolBr_ONfvXVTmPIViEJphrgvZ7xoJNhjRPRS2Cc0pkyLcjhrB07G5LFdcMaT89CG49HRV23Mit6QdSGCjc-Y_NJ137LMbiBkwiloJevZmXfNPnvbj7974YOyF6NVopZk8Qh2R1Wl_EZwKGheZ5t_DfxEQbX
  priority: 102
  providerName: Scholars Portal
– databaseName: SpringerOpen
  dbid: C6C
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3NT90wDI8QCInLNGBsjwHKgRur1jbfR3gCIZA4gcQtSvOh9bA-xCsH_nvstO9N3eCwa5s0jR3HP8exTcip8cZw4VyRTCwLzllTGC10AfuliNxXqYn5tsWdvH7gN4_icUyTg7EwE_890z-XPIsyGjkVuowKMM-3QAcrXM1zOV-fp2Cmc835GBfzfteJ7skp-t_Dlf9ej_zLR5pVz9Vn8mnEjPR8YPIu2YjdHtkeqki-7pObc-oR5cGOBvCRYj0s-AxtO3rbPlOM7O1AAdKwiEvaLXraAlIOkT4tegDO7ctv7B2GJLJfyMPV5f38uhhLJBQeoFZfyEZW0rnEMElNqRIPyTtRKzyJVdGXTngftAtSOs699ly5JIyXsebOxMTYAdnsFl38RmjdOK8ESnkKvKmhoWQKWCk4qLBQ6Rk5WxHPPg2ZMGz2YDNtB1JbILXNpLbljFwgfdctMYt1fgDMtaNQ2CokwVQDhqxnPOhkWONE9BJMSOlMmWbkaMUdO4rW0qIjsMZwWBjj68Co9SgMzF38gRlRExZOfmP6pmt_5aTaYGQIpWCWP1bM_jPkx9M8_L_m38lOjesRax-JI7LZP7_EYwA1fXOSV_MbeZbvFg
  priority: 102
  providerName: Springer Nature
Title A constricted opening in Kir channels does not impede potassium conduction
URI https://link.springer.com/article/10.1038/s41467-020-16842-0
https://www.ncbi.nlm.nih.gov/pubmed/32541684
https://www.proquest.com/docview/2413234320
https://pubmed.ncbi.nlm.nih.gov/PMC7295778
https://doaj.org/article/1df537b978c34d8f93ba5ec69176a90f
Volume 11
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELbaIiQuiDeBsvKBG6SbxO_jdtWlWtSqAirtLXL8KJHYZLWbHvj3jJ2ksDwuXBzFcWJnxh5_Y49nEHqrjFKUaZ165bKUUlKlSjKZgrxkjprcVy5aW1zy82u6XLHVAWLjWZhotG-q-qT5tj5p6q_RtnKzNtPRTmx6dTEHQMiEkNNDdAjT7y8qehS_RIHWQocDMhmR0x2N4iAoSnnYdkpD-DcCmlG425uPotv-v2HNP00mf9s3jdPR4hF6OOBIPOvb-xgduOYJut9Hlvz-FC1n2ATkB1IOICUOMbLgM7hu8Md6i8Np3wYmRWxbt8NN2-Ea0LN1eNN2AKbr23V42_aOZZ-h68XZl_l5OoRNSA3Ary7lFc-51p4ExzWZ8NR6o1khwuqscCbTzBgrteVcU2qkoUJ7pgx3BdXKeUKeo6OmbdxLhItKG8HCyPeWVgUU5EQAe4F0hbS5TNC7kXjlpveOUcZdbSLLnuolUL2MVC-zBJ0G-t6VDJ6tY0a7vSkH_pa59YyICpRbQ6iVXpFKM2c4qJVcq8wn6HjkTjkMt10ZNgeLcEQW6njRM-qulpHRCRJ7LNxrxv4T6HfR0fbQzxL0fmT2zyr__Zuv_rui1-hBEXppCI3EjtFRt711bwDzdNUEevpKQCoXHybo3my2_LyE6-nZ5dUnyJ3z-SSuJkB6QeUkjogfADoG_w
link.rule.ids 230,314,727,780,784,864,885,2102,12056,12765,21388,24318,27924,27925,31719,33373,33744,41120,42189,43310,43600,43805,51576,53791,53793,73745,74035,74302
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwEB7BVoheUHkHWvCBG0RN4ld8Qm3VamnLCqFW6s1y_Cg5kGx30wP_Hk-S3WqhcE2c2J6xZ76ZsWcAPiirFOPGpEH5LGWMVqkqeZlGeck9s3mofH_aYiaml-z0il-NDrfleKxyJRN7Qe1aiz7yfYz_FHgLMvs8v0mxahRGV8cSGg9hCzOn8wlsHR7Pvn1fe1kw_3nJ2HhbJqPl_pL1sgGtphxjUGm2oZH6xP33oc2_D03-ETntFdLJDjwZkSQ5GFj_FB745hk8GmpL_noOpwfEIvaLci6CSoJVsuJvSN2Qs3pB8L5vE9Uica1fkqbtSB3xs_Nk3nYRTte3P_FrN6SWfQGXJ8cXR9N0LJyQ2gjAulRUIhfGBIqpazIZmAvW8EKif1Z6mxlurSuNE8IwZkvLpAlcWeELZpQPlL6ESdM2_jWQojJWctz7wbGqiA0FlZHBnEXF5vIygY8r4un5kB9D93FtWuqB1DqSWvek1lkCh0jfdUvMbd0_aBfXetwqOneBU1lF89ZS5sqgaGW4tyIalsKoLCSwu-KOHjfcUt8tjwReDYxa90KjEYwDSEBusHBjGJtvmvpHn2o7mh5cyjjLTytm33X572m--f8I38Pj6cXXc33-ZXb2FrYLXItYDYnvwqRb3Pq9CHO66t24ln8DhOb6ag
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwELZgKxAXxLMEWvCBG0SbxK_khFroqrRoVSEq9WY5fkAOTba76aH_npnEu9UC5Zo4sTMzmfnGM54h5H1lq4oLY9JQ-SzlnNVpVYoyBX0pPLd5qP2QbTGXx-f85EJcxPynVUyrXOvEQVG7zuIe-RTjPwWegsymIaZFnH2ZfVpcpdhBCiOtsZ3GfbIDVjErJmTn8Gh-9n2z44K10EvO48mZjJXTFR_0BHpQOcaj0mzLOg1F_P-FPP9OoPwjijoYp9kT8jiiSnowisFTcs-3z8iDsc_kzXNyckAt4kDQeQAwKXbMgtfQpqWnzZLi2d8WTCR1nV_RtutpA1jaebroeoDWzfUlPu3GMrMvyPns6Mfn4zQ2UUgtgLE-lbXMpTGBYRmbTAXugjWiULhXq7zNjLDWlcZJaTi3peXKBFFZ6QtuKh8Ye0kmbdf6V4QWtbFKoB4IjtcFDJRMAbMFByPn8jIhH9bE04uxVoYeYtys1COpNZBaD6TWWUIOkb6bkVjnerjQLX_q-Nvo3AXBVA2urmXclaFitRHeSnAypamykJC9NXd0_PlW-lZUErI7MmozCwOHGBeQELXFwq1lbN9pm19D2W1wQ4RS8JUf18y-nfLuz3z9_xW-Iw9BjPW3r_PTN-RRgaKIjZHEHpn0y2u_D4inr99GUf4NNdP-lw
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=A+constricted+opening+in+Kir+channels+does+not+impede+potassium+conduction&rft.jtitle=Nature+communications&rft.au=Black%2C+Katrina+A.&rft.au=He%2C+Sitong&rft.au=Jin%2C+Ruitao&rft.au=Miller%2C+David+M.&rft.date=2020-06-15&rft.pub=Nature+Publishing+Group+UK&rft.eissn=2041-1723&rft.volume=11&rft_id=info:doi/10.1038%2Fs41467-020-16842-0&rft_id=info%3Apmid%2F32541684&rft.externalDBID=PMC7295778
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=2041-1723&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=2041-1723&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=2041-1723&client=summon