Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly

The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of...

Full description

Saved in:
Bibliographic Details
Published inNature communications Vol. 10; no. 1; pp. 69 - 14
Main Authors Wang, Shen, Li, Yun, Gong, Jihong, Ye, Sheng, Yang, Xiaofei, Zhang, Rongguang, Ma, Cong
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 08.01.2019
Nature Publishing Group
Nature Portfolio
Subjects
631/378/548/2589
631/535/1266
631/80/313/2104
82/80
82/83
9/74
Animals
Assembly
BASIC BIOLOGICAL SCIENCES
Biophysics
Complex formation
Exocytosis
Gene Knockdown Techniques
HEK293 Cells
Humanities and Social Sciences
Humans
Laboratories
Membrane vesicles
Mice
multidisciplinary
Munc18 Proteins - metabolism
Mutation
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurons
Primary Cell Culture
Protein Binding - physiology
Protein Domains - physiology
Proteins
Science
Science (multidisciplinary)
SNAP receptors
SNAP-25 protein
SNARE
Synaptic vesicle exocytosis
Synaptobrevin
Synaptosomal-Associated Protein 25 - metabolism
Syntaxin
Syntaxin 1
Syntaxin 1 - metabolism
Vesicle-Associated Membrane Protein 2 - metabolism
X-ray crystallography
Online AccessGet full text

Cover

Abstract The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly. Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction between Munc13-1 and synaptobrevin-2 that is critical for the transition of the Munc18-1/syntaxin-1 complex to the SNARE complex.
AbstractList The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly. Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction between Munc13-1 and synaptobrevin-2 that is critical for the transition of the Munc18-1/syntaxin-1 complex to the SNARE complex.
The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.
Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction between Munc13-1 and synaptobrevin-2 that is critical for the transition of the Munc18-1/syntaxin-1 complex to the SNARE complex.
The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.
The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Furthermore, our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.
The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and synaptobrevin-2, but the underlying mechanism remains elusive. Here, we identify an interaction between Munc13-1 and the membrane-proximal linker region of synaptobrevin-2, and reveal its essential role in transition and exocytosis. Upon this interaction, Munc13-1 not only recruits synaptobrevin-2-embedded vesicles to the target membrane but also renders the synaptobrevin-2 SNARE motif more accessible to the Munc18-1/syntaxin-1 complex. Afterward, the entry of SNAP-25 leads to a half-zippered SNARE assembly, which eventually dissociates the Munc18-1/syntaxin-1 complex to complete SNARE complex formation. Our data suggest that Munc18-1 and Munc13-1 together serve as a functional template to orchestrate SNARE complex assembly.Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction between Munc13-1 and synaptobrevin-2 that is critical for the transition of the Munc18-1/syntaxin-1 complex to the SNARE complex.
ArticleNumber 69
Author Ma, Cong
Wang, Shen
Li, Yun
Yang, Xiaofei
Ye, Sheng
Gong, Jihong
Zhang, Rongguang
Author_xml – sequence: 1
  givenname: Shen
  orcidid: 0000-0002-5013-1039
  surname: Wang
  fullname: Wang, Shen
  organization: Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology
– sequence: 2
  givenname: Yun
  surname: Li
  fullname: Li, Yun
  organization: Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology
– sequence: 3
  givenname: Jihong
  surname: Gong
  fullname: Gong, Jihong
  organization: Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology
– sequence: 4
  givenname: Sheng
  surname: Ye
  fullname: Ye, Sheng
  organization: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences
– sequence: 5
  givenname: Xiaofei
  surname: Yang
  fullname: Yang, Xiaofei
  organization: Key Laboratory of Cognitive Science, Hubei Key Laboratory of Medical Information Analysis and Tumor Diagnosis and Treatment, Laboratory of Membrane Ion Channels and Medicine, College of Biomedical Engineering, South-Central University for Nationalities
– sequence: 6
  givenname: Rongguang
  surname: Zhang
  fullname: Zhang, Rongguang
  organization: National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, National Center for Protein Science Shanghai, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Science, Chinese Academy of Sciences
– sequence: 7
  givenname: Cong
  surname: Ma
  fullname: Ma, Cong
  email: cong.ma@hust.edu.cn
  organization: Key Laboratory of Molecular Biophysics of the Ministry of Education, College of Life Science and Technology, and the Collaborative Innovation Center for Brain Science, Huazhong University of Science and Technology
BackLink https://www.ncbi.nlm.nih.gov/pubmed/30622273$$D View this record in MEDLINE/PubMed
https://www.osti.gov/servlets/purl/1510246$$D View this record in Osti.gov
BookMark eNp9kktv1DAUhSNUREvpH2CBItiwCfj92CBVVYFKBSQea8txbmYyytiD7VT03-NMWmi7qDfx4zsn59r3eXXgg4eqeonRO4yoep8YZkI2CKsGKURUI55URwQx3GBJ6MGd-WF1ktIGlUE1Vow9qw4pEoQQSY8q82XyDqva-q7eT2mdIF5BbVNt677s5CF4O9YZtrvRZqhzqEN0a0g5zksPU9wDP76efj-vXSgY_CnyBNt2vH5RPe3tmODk5ntc_fp4_vPsc3P57dPF2ell47iQueFE21YphnRLrWaOMCEUhb5zCHWSYkocwiBpr3kvKVDJrRRa86IiHbY9Pa4uFt8u2I3ZxWFr47UJdjD7jRBXxsY8uBGMsgj3BFqhiGaylxqEAoKFc1h00Oni9WHx2k3tFjoHvpQ63jO9f-KHtVmFKyMo4YTOBq8Xg5DyYJIbMri1C96DywZzjEp5BXp785cYfk_lOs12SA7G0XoIUzIlERdcMiwL-uYBuglTLJe-UEgLrlihXt2N_S_v7WMXQC2AiyGlCL0pyez8vqWKYTQYmbm1zNJaprSW2beWmcOSB9Jb90dFdBGlAvsVxP-xH1H9BXc-3lE
CitedBy_id crossref_primary_10_1038_s41596_024_01014_x
crossref_primary_10_3389_fimmu_2020_545414
crossref_primary_10_3389_fnins_2023_1123561
crossref_primary_10_1080_10409238_2022_2121804
crossref_primary_10_1002_pro_3844
crossref_primary_10_1016_j_mcn_2019_103452
crossref_primary_10_1073_pnas_2016276118
crossref_primary_10_1186_s43556_022_00090_3
crossref_primary_10_3389_fnsyn_2021_798204
crossref_primary_10_1038_s41467_024_46828_1
crossref_primary_10_1073_pnas_2309516120
crossref_primary_10_1093_brain_awae019
crossref_primary_10_1038_s42003_024_07317_9
crossref_primary_10_1155_2022_9176923
crossref_primary_10_7554_eLife_90775_3
crossref_primary_10_1073_pnas_2306086120
crossref_primary_10_7554_eLife_79926
crossref_primary_10_1021_acs_biochem_4c00148
crossref_primary_10_1039_D4TA00778F
crossref_primary_10_1016_j_jnrt_2024_100134
crossref_primary_10_1038_s41467_019_11873_8
crossref_primary_10_7554_eLife_42806
crossref_primary_10_1126_sciadv_adi7024
crossref_primary_10_1016_j_celrep_2020_108611
crossref_primary_10_1055_s_0041_1727259
crossref_primary_10_3389_fneur_2021_806506
crossref_primary_10_3390_ijms23042378
crossref_primary_10_3389_fnmol_2021_785696
crossref_primary_10_1002_1873_3468_13570
crossref_primary_10_1111_febs_16528
crossref_primary_10_3389_fcell_2020_609708
crossref_primary_10_1007_s12035_022_02916_1
crossref_primary_10_1113_JP286651
crossref_primary_10_1186_s12915_023_01655_6
crossref_primary_10_3389_fendo_2023_1096365
crossref_primary_10_1016_j_bpj_2022_07_013
crossref_primary_10_1002_pro_4870
crossref_primary_10_1073_pnas_1813194116
crossref_primary_10_1016_j_jbc_2024_105782
crossref_primary_10_1007_s00018_020_03688_4
crossref_primary_10_1038_s41598_022_09654_3
crossref_primary_10_3390_ijms222111775
crossref_primary_10_1073_pnas_1914361117
crossref_primary_10_1136_jnnp_2022_330504
crossref_primary_10_7554_eLife_88619
crossref_primary_10_7554_eLife_88619_3
crossref_primary_10_3390_biomedicines10071593
crossref_primary_10_1016_j_isci_2022_104506
crossref_primary_10_1146_annurev_biochem_081820_103615
crossref_primary_10_1073_pnas_2121259119
crossref_primary_10_1523_ENEURO_0278_20_2020
crossref_primary_10_1038_s41598_020_68476_3
crossref_primary_10_1016_j_celrep_2019_11_107
crossref_primary_10_1016_j_neuron_2022_06_010
crossref_primary_10_1002_1873_3468_14157
crossref_primary_10_1371_journal_pone_0229799
crossref_primary_10_1016_j_celrep_2024_114026
crossref_primary_10_1038_s41467_024_46965_7
crossref_primary_10_1016_j_isci_2024_109793
crossref_primary_10_1016_j_jbc_2024_108001
crossref_primary_10_3389_fnmol_2022_948160
crossref_primary_10_1146_annurev_biophys_111821_104732
crossref_primary_10_1073_pnas_2311484120
crossref_primary_10_15252_embj_2019103631
crossref_primary_10_7554_eLife_90775
crossref_primary_10_3389_fimmu_2024_1460882
crossref_primary_10_1111_jnc_15120
crossref_primary_10_1002_2211_5463_13473
crossref_primary_10_1016_j_neuropharm_2024_110247
crossref_primary_10_7554_eLife_82041
crossref_primary_10_1002_1873_3468_14006
Cites_doi 10.1038/35006120
10.1126/science.1233801
10.1523/JNEUROSCI.6282-11.2012
10.1016/S0896-6273(00)80520-6
10.15252/embj.201695775
10.1002/anie.201406359
10.1371/journal.pone.0067409
10.1126/science.aac7906
10.1091/mbc.e09-04-0284
10.1038/nature11320
10.1083/jcb.201508118
10.1107/S0907444910007493
10.1038/26412
10.1038/nsmb.2101
10.1073/pnas.0702290104
10.1038/sj.emboj.7601003
10.3389/fcell.2016.00042
10.1073/pnas.91.4.1445
10.1002/1873-3468.13018
10.1038/srep13875
10.1038/nprot.2012.020
10.1073/pnas.0914906108
10.1083/jcb.200705145
10.1038/nsmb.3038
10.1016/j.cell.2009.11.002
10.1091/mbc.e07-05-0461
10.1038/ncomms15915
10.1126/science.1230473
10.3389/fnmol.2017.00256
10.1016/j.bpj.2015.08.051
10.1038/msb.2011.75
10.1016/j.neuron.2017.07.004
10.1038/emboj.2008.37
10.1242/jcs.126862
10.1091/mbc.e08-01-0077
10.1021/ja407392n
10.1038/nsmb.1450
10.1038/nrm2002
10.1038/nature08156
10.1016/S0092-8674(00)81404-X
10.1016/j.tins.2007.08.008
10.1091/mbc.e07-03-0193
10.1074/jbc.M113.514273
10.1126/science.1129486
10.1016/j.neuron.2013.10.022
10.1146/annurev-biophys-060414-034057
10.1074/jbc.M209428200
10.1074/jbc.M312064200
10.1016/S0896-6273(00)80146-4
10.1038/ncomms14236
10.1038/nature23484
10.1107/S0021889807021206
10.1074/jbc.M114.584805
10.1073/pnas.1303753110
10.1038/nsmb.2047
10.1523/JNEUROSCI.0007-16.2016
10.7554/eLife.22567
10.7554/eLife.14211
10.7554/eLife.24278
ContentType Journal Article
Copyright The Author(s) 2019
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) 2019
– notice: 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.
CorporateAuthor Argonne National Laboratory (ANL), Argonne, IL (United States)
CorporateAuthor_xml – name: Argonne National Laboratory (ANL), Argonne, IL (United States)
DBID C6C
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
3V.
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7X7
7XB
88E
8AO
8FD
8FE
8FG
8FH
8FI
8FJ
8FK
ABUWG
AEUYN
AFKRA
ARAPS
AZQEC
BBNVY
BENPR
BGLVJ
BHPHI
C1K
CCPQU
DWQXO
FR3
FYUFA
GHDGH
GNUQQ
H94
HCIFZ
K9.
LK8
M0S
M1P
M7P
P5Z
P62
P64
PHGZM
PHGZT
PIMPY
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQQKQ
PQUKI
PRINS
RC3
SOI
7X8
OIOZB
OTOTI
5PM
DOA
DOI 10.1038/s41467-018-08028-6
DatabaseName Springer Nature OA Free Journals
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
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 One Sustainability
ProQuest Central UK/Ireland
Advanced Technologies & Aerospace Collection
ProQuest Central Essentials
Biological Science Collection
ProQuest Central
Technology Collection
Natural Science Collection
Environmental Sciences and Pollution Management
ProQuest One
ProQuest Central
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)
Medical Database
Biological Science Database
ProQuest advanced technologies & aerospace journals
ProQuest Advanced Technologies & Aerospace Collection
Biotechnology and BioEngineering Abstracts
ProQuest Central Premium
ProQuest One Academic (New)
ProQuest Publicly Available Content Database
ProQuest Health & Medical Research Collection
ProQuest One Academic Middle East (New)
ProQuest One Health & Nursing
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Applied & Life Sciences
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
Genetics Abstracts
Environment Abstracts
MEDLINE - Academic
OSTI.GOV - Hybrid
OSTI.GOV
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
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
ProQuest One Applied & Life Sciences
ProQuest One Sustainability
Health Research Premium Collection
Natural Science Collection
Health & Medical Research Collection
Biological Science Collection
Chemoreception Abstracts
Industrial and Applied Microbiology Abstracts (Microbiology A)
ProQuest Central (New)
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
ProQuest One Academic (New)
Technology Collection
Technology Research Database
ProQuest One Academic Middle East (New)
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest One Health & Nursing
ProQuest Natural Science Collection
ProQuest Pharma Collection
ProQuest Central
ProQuest Health & Medical Research Collection
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)
MEDLINE - Academic
DatabaseTitleList
MEDLINE - Academic


CrossRef
MEDLINE

Publicly Available Content Database
Database_xml – sequence: 1
  dbid: C6C
  name: Springer Nature OA Free Journals
  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 14
ExternalDocumentID oai_doaj_org_article_8a01f2eb682947f79e68e216cc16ded9
PMC6325239
1510246
30622273
10_1038_s41467_018_08028_6
Genre Research Support, Non-U.S. Gov't
Journal Article
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
ADMLS
ADRAZ
AENEX
AEUYN
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
AASML
AAYXX
CITATION
PHGZM
PHGZT
CGR
CUY
CVF
ECM
EIF
NPM
7QL
7QP
7QR
7SN
7SS
7ST
7T5
7T7
7TM
7TO
7XB
8FD
8FK
AARCD
AZQEC
C1K
DWQXO
FR3
GNUQQ
H94
K9.
P64
PJZUB
PKEHL
PPXIY
PQEST
PQGLB
PQUKI
PRINS
RC3
SOI
7X8
OIOZB
OTOTI
5PM
PUEGO
ID FETCH-LOGICAL-c567t-529ab88409b3a94c246683efdc00d73132c01e73f95f73e375a769959ab2d1af3
IEDL.DBID M48
ISSN 2041-1723
IngestDate Wed Aug 27 01:32:12 EDT 2025
Thu Aug 21 13:22:44 EDT 2025
Mon Nov 25 02:42:02 EST 2024
Fri Jul 11 15:05:57 EDT 2025
Wed Aug 13 06:32:55 EDT 2025
Thu Apr 03 07:10:08 EDT 2025
Thu Apr 24 22:55:23 EDT 2025
Tue Jul 01 02:21:21 EDT 2025
Fri Feb 21 02:38:59 EST 2025
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-c567t-529ab88409b3a94c246683efdc00d73132c01e73f95f73e375a769959ab2d1af3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
31670846; 31721002; 31670850; 2015CB910800
National Natural Science Foundation of China (NSFC)
National Key Basic Research Program of China
ORCID 0000-0002-5013-1039
0000000250131039
OpenAccessLink http://journals.scholarsportal.info/openUrl.xqy?doi=10.1038/s41467-018-08028-6
PMID 30622273
PQID 2165096584
PQPubID 546298
PageCount 14
ParticipantIDs doaj_primary_oai_doaj_org_article_8a01f2eb682947f79e68e216cc16ded9
pubmedcentral_primary_oai_pubmedcentral_nih_gov_6325239
osti_scitechconnect_1510246
proquest_miscellaneous_2165657417
proquest_journals_2165096584
pubmed_primary_30622273
crossref_citationtrail_10_1038_s41467_018_08028_6
crossref_primary_10_1038_s41467_018_08028_6
springer_journals_10_1038_s41467_018_08028_6
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2019-01-08
PublicationDateYYYYMMDD 2019-01-08
PublicationDate_xml – month: 01
  year: 2019
  text: 2019-01-08
  day: 08
PublicationDecade 2010
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
– name: United States
PublicationTitle Nature communications
PublicationTitleAbbrev Nat Commun
PublicationTitleAlternate Nat Commun
PublicationYear 2019
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 Williams, Vicogne, Zaitseva, McLaughlin, Pessin (CR53) 2009; 20
Han (CR24) 2014; 289
Sudhof (CR1) 2014; 53
Rizo, Xu (CR13) 2015; 44
CR37
Yang (CR22) 2015; 22
McCoy (CR55) 2007; 40
CR30
Diao (CR35) 2013; 135
Starai, Hickey, Wickner (CR45) 2008; 19
Sudhof (CR11) 2013; 80
Tarafdar, Chakraborty, Bruno, Lentz (CR52) 2015; 109
Kummel (CR48) 2011; 18
Li, Wang, Li, Zhu, Ma (CR57) 2018; 592
Rosenmund, Stevens (CR34) 1996; 16
Pobbati, Stein, Fasshauer (CR8) 2006; 313
Zhou (CR50) 2017; 548
Kasula (CR26) 2016; 214
Munch (CR25) 2016; 36
Sievers (CR59) 2011; 7
Fasshauer, Margittai (CR7) 2004; 279
Wang (CR21) 2017; 36
Stein, Weber, Wahl, Jahn (CR6) 2009; 460
Diao (CR36) 2012; 7
Li (CR49) 2017; 10
Ma, Li, Xu, Rizo (CR19) 2011; 18
Hu (CR23) 2011; 108
Yue (CR41) 2017; 8
Shestakova, Suvorova, Pavliv, Khaidakova, Lupashin (CR43) 2007; 179
Rizo, Rosenmund (CR3) 2008; 15
Baker (CR28) 2015; 349
Liu, Zuo, Yue, Guo (CR40) 2007; 18
CR54
Burkhardt, Hattendorf, Weis, Fasshauer (CR17) 2008; 27
Colbert (CR47) 2013; 110
Sutton, Fasshauer, Jahn, Brunger (CR5) 1998; 395
Jahn, Fasshauer (CR12) 2012; 490
Toonen, Verhage (CR16) 2007; 30
Sorensen (CR9) 2006; 25
Kloepper, Kienle, Fasshauer (CR4) 2007; 18
Misura, Scheller, Weis (CR18) 2000; 404
Han, Bin, Kang, Han, Sugita (CR27) 2013; 126
Dubuke, Munson (CR38) 2016; 4
Jahn, Scheller (CR2) 2006; 7
Pevsner, Hsu, Scheller (CR14) 1994; 91
Betz (CR15) 1998; 21
Baker, Jeffrey, Hughson (CR46) 2013; 8
Borisovska (CR51) 2012; 32
Collins, Wickner (CR44) 2007; 104
Lai (CR32) 2017; 95
Ma, Su, Seven, Xu, Rizo (CR20) 2013; 339
Jiang (CR58) 2015; 5
Emsley, Lohkamp, Scott, Cowtan (CR56) 2010; 66
Parisotto (CR29) 2014; 289
He (CR31) 2017; 8
Hughson (CR33) 2013; 339
Ren (CR39) 2009; 139
Weber (CR10) 1998; 92
Siniossoglou, Pelham (CR42) 2002; 277
TC Sudhof (8028_CR1) 2014; 53
T Weber (8028_CR10) 1998; 92
J Diao (8028_CR35) 2013; 135
FM Hughson (8028_CR33) 2013; 339
J Pevsner (8028_CR14) 1994; 91
C Ma (8028_CR19) 2011; 18
KN Colbert (8028_CR47) 2013; 110
J Rizo (8028_CR13) 2015; 44
SH Hu (8028_CR23) 2011; 108
A Stein (8028_CR6) 2009; 460
D Kummel (8028_CR48) 2011; 18
Y Ren (8028_CR39) 2009; 139
R Kasula (8028_CR26) 2016; 214
S Siniossoglou (8028_CR42) 2002; 277
R Jahn (8028_CR2) 2006; 7
VJ Starai (8028_CR45) 2008; 19
GA Han (8028_CR24) 2014; 289
D Fasshauer (8028_CR7) 2004; 279
PK Tarafdar (8028_CR52) 2015; 109
A Betz (8028_CR15) 1998; 21
J Rizo (8028_CR3) 2008; 15
JB Sorensen (8028_CR9) 2006; 25
Y Lai (8028_CR32) 2017; 95
Q Zhou (8028_CR50) 2017; 548
RW Baker (8028_CR28) 2015; 349
RF Toonen (8028_CR16) 2007; 30
RB Sutton (8028_CR5) 1998; 395
Y Li (8028_CR57) 2018; 592
8028_CR54
C Rosenmund (8028_CR34) 1996; 16
AV Pobbati (8028_CR8) 2006; 313
ML Dubuke (8028_CR38) 2016; 4
GA Han (8028_CR27) 2013; 126
TC Sudhof (8028_CR11) 2013; 80
KM Misura (8028_CR18) 2000; 404
F Sievers (8028_CR59) 2011; 7
P Yue (8028_CR41) 2017; 8
RW Baker (8028_CR46) 2013; 8
M Borisovska (8028_CR51) 2012; 32
S Wang (8028_CR21) 2017; 36
W Jiang (8028_CR58) 2015; 5
TH Kloepper (8028_CR4) 2007; 18
C Ma (8028_CR20) 2013; 339
KM Collins (8028_CR44) 2007; 104
P Emsley (8028_CR56) 2010; 66
AS Munch (8028_CR25) 2016; 36
A Shestakova (8028_CR43) 2007; 179
J Liu (8028_CR40) 2007; 18
P Burkhardt (8028_CR17) 2008; 27
8028_CR37
R Jahn (8028_CR12) 2012; 490
X Yang (8028_CR22) 2015; 22
D Williams (8028_CR53) 2009; 20
J Diao (8028_CR36) 2012; 7
AJ McCoy (8028_CR55) 2007; 40
E He (8028_CR31) 2017; 8
D Parisotto (8028_CR29) 2014; 289
Y Li (8028_CR49) 2017; 10
8028_CR30
References_xml – volume: 404
  start-page: 355
  year: 2000
  end-page: 362
  ident: CR18
  article-title: Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex
  publication-title: Nature
  doi: 10.1038/35006120
– volume: 339
  start-page: 406
  year: 2013
  end-page: 407
  ident: CR33
  article-title: Neuroscience. Chaperones that SNARE neurotransmitter release
  publication-title: Science
  doi: 10.1126/science.1233801
– volume: 32
  start-page: 15983
  year: 2012
  end-page: 15997
  ident: CR51
  article-title: Membrane-proximal tryptophans of synaptobrevin II stabilize priming of secretory vesicles
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.6282-11.2012
– volume: 21
  start-page: 123
  year: 1998
  end-page: 136
  ident: CR15
  article-title: Munc13-1 is a presynaptic phorbol ester receptor that enhances neurotransmitter release
  publication-title: Neuron
  doi: 10.1016/S0896-6273(00)80520-6
– volume: 36
  start-page: 816
  year: 2017
  end-page: 829
  ident: CR21
  article-title: Conformational change of syntaxin linker region induced by Munc13s initiates SNARE complex formation in synaptic exocytosis
  publication-title: EMBO J.
  doi: 10.15252/embj.201695775
– volume: 53
  start-page: 12696
  year: 2014
  end-page: 12717
  ident: CR1
  article-title: The molecular machinery of neurotransmitter release (Nobel lecture)
  publication-title: Angew. Chem. Int. Ed. Engl.
  doi: 10.1002/anie.201406359
– volume: 8
  start-page: e67409
  year: 2013
  ident: CR46
  article-title: Crystal structures of the Sec1/Munc18 (SM) protein Vps33, alone and bound to the homotypic fusion and vacuolar protein sorting (HOPS) subunit Vps16*
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0067409
– volume: 349
  start-page: 1111
  year: 2015
  end-page: 1114
  ident: CR28
  article-title: A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
  publication-title: Science
  doi: 10.1126/science.aac7906
– volume: 20
  start-page: 4910
  year: 2009
  end-page: 4919
  ident: CR53
  article-title: Evidence that electrostatic interactions between vesicle-associated membrane protein 2 and acidic phospholipids may modulate the fusion of transport vesicles with the plasma membrane
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e09-04-0284
– volume: 490
  start-page: 201
  year: 2012
  end-page: 207
  ident: CR12
  article-title: Molecular machines governing exocytosis of synaptic vesicles
  publication-title: Nature
  doi: 10.1038/nature11320
– volume: 214
  start-page: 847
  year: 2016
  end-page: 858
  ident: CR26
  article-title: The Munc18-1 domain 3a hinge-loop controls syntaxin-1A nanodomain assembly and engagement with the SNARE complex during secretory vesicle priming
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201508118
– ident: CR54
– volume: 66
  start-page: 486
  year: 2010
  end-page: 501
  ident: CR56
  article-title: Features and development of Coot
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444910007493
– volume: 395
  start-page: 347
  year: 1998
  end-page: 353
  ident: CR5
  article-title: Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
  publication-title: Nature
  doi: 10.1038/26412
– volume: 18
  start-page: 927
  year: 2011
  end-page: 933
  ident: CR48
  article-title: Complexin cross-links prefusion SNAREs into a zigzag array
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2101
– volume: 104
  start-page: 8755
  year: 2007
  end-page: 8760
  ident: CR44
  article-title: Trans-SNARE complex assembly and yeast vacuole membrane fusion
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0702290104
– volume: 25
  start-page: 955
  year: 2006
  end-page: 966
  ident: CR9
  article-title: Sequential N- to C-terminal SNARE complex assembly drives priming and fusion of secretory vesicles
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7601003
– volume: 4
  start-page: 42
  year: 2016
  ident: CR38
  article-title: The secret life of tethers: the role of tethering factors in SNARE complex regulation
  publication-title: Front. Cell. Dev. Biol.
  doi: 10.3389/fcell.2016.00042
– volume: 91
  start-page: 1445
  year: 1994
  end-page: 1449
  ident: CR14
  article-title: n-Sec1: a neural-specific syntaxin-binding protein
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.91.4.1445
– volume: 592
  start-page: 1161
  year: 2018
  end-page: 1172
  ident: CR57
  article-title: Tomosyn guides SNARE complex formation in coordination with Munc18 and Munc13
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.13018
– volume: 5
  year: 2015
  ident: CR58
  article-title: An optimized method for high-titer lentivirus preparations without ultracentrifugation
  publication-title: Sci. Rep.
  doi: 10.1038/srep13875
– volume: 7
  start-page: 921
  year: 2012
  end-page: 934
  ident: CR36
  article-title: A single vesicle–vesicle fusion assay for in vitro studies of SNAREs and accessory proteins
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2012.020
– volume: 108
  start-page: 1040
  year: 2011
  end-page: 1045
  ident: CR23
  article-title: Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0914906108
– volume: 179
  start-page: 1179
  year: 2007
  end-page: 1192
  ident: CR43
  article-title: Interaction of the conserved oligomeric Golgi complex with t-SNARE syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200705145
– volume: 22
  start-page: 547
  year: 2015
  end-page: 554
  ident: CR22
  article-title: Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.3038
– volume: 139
  start-page: 1119
  year: 2009
  end-page: 1129
  ident: CR39
  article-title: A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
  publication-title: Cell
  doi: 10.1016/j.cell.2009.11.002
– volume: 18
  start-page: 4483
  year: 2007
  end-page: 4492
  ident: CR40
  article-title: Phosphatidylinositol 4,5-bisphosphate mediates the targeting of the exocyst to the plasma membrane for exocytosis in mammalian cells
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e07-05-0461
– volume: 8
  year: 2017
  ident: CR31
  article-title: Munc13-1 and Munc18-1 together prevent NSF-dependent de-priming of synaptic vesicles
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms15915
– volume: 339
  start-page: 421
  year: 2013
  end-page: 425
  ident: CR20
  article-title: Reconstitution of the vital functions of Munc18 and Munc13 in neurotransmitter release
  publication-title: Science
  doi: 10.1126/science.1230473
– volume: 10
  start-page: 256
  year: 2017
  ident: CR49
  article-title: A stimulation function of synaptotagmin-1 in ternary SNARE complex formation dependent on Munc18 and Munc13
  publication-title: Front. Mol. Neurosci.
  doi: 10.3389/fnmol.2017.00256
– volume: 109
  start-page: 1863
  year: 2015
  end-page: 1872
  ident: CR52
  article-title: Phosphatidylserine-dependent catalysis of stalk and pore formation by synaptobrevin JMR-TMD peptide
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2015.08.051
– volume: 7
  start-page: 539
  year: 2011
  ident: CR59
  article-title: Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb.2011.75
– ident: CR37
– ident: CR30
– volume: 95
  start-page: 591
  year: 2017
  end-page: 607 e10
  ident: CR32
  article-title: Molecular mechanisms of synaptic vesicle priming by Munc13 and Munc18
  publication-title: Neuron
  doi: 10.1016/j.neuron.2017.07.004
– volume: 27
  start-page: 923
  year: 2008
  end-page: 933
  ident: CR17
  article-title: Munc18a controls SNARE assembly through its interaction with the syntaxin N-peptide
  publication-title: EMBO J.
  doi: 10.1038/emboj.2008.37
– volume: 126
  start-page: 2361
  year: 2013
  end-page: 2371
  ident: CR27
  article-title: Domain 3a of Munc18-1 plays a crucial role at the priming stage of exocytosis
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.126862
– volume: 19
  start-page: 2500
  year: 2008
  end-page: 2508
  ident: CR45
  article-title: HOPS proofreads the -SNARE complex for yeast vacuole fusion
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e08-01-0077
– volume: 135
  start-page: 15274
  year: 2013
  end-page: 15277
  ident: CR35
  article-title: Complexin-1 enhances the on-rate of vesicle docking via simultaneous SNARE and membrane interactions
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja407392n
– volume: 15
  start-page: 665
  year: 2008
  end-page: 674
  ident: CR3
  article-title: Synaptic vesicle fusion
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1450
– volume: 7
  start-page: 631
  year: 2006
  end-page: 643
  ident: CR2
  article-title: SNAREs—engines for membrane fusion
  publication-title: Nat. Rev. Mol. Cell. Biol.
  doi: 10.1038/nrm2002
– volume: 460
  start-page: 525
  year: 2009
  end-page: 528
  ident: CR6
  article-title: Helical extension of the neuronal SNARE complex into the membrane
  publication-title: Nature
  doi: 10.1038/nature08156
– volume: 92
  start-page: 759
  year: 1998
  end-page: 772
  ident: CR10
  article-title: SNAREpins: minimal machinery for membrane fusion
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81404-X
– volume: 30
  start-page: 564
  year: 2007
  end-page: 572
  ident: CR16
  article-title: Munc18-1 in secretion: lonely Munc joins SNARE team and takes control
  publication-title: Trends Neurosci.
  doi: 10.1016/j.tins.2007.08.008
– volume: 18
  start-page: 3463
  year: 2007
  end-page: 3471
  ident: CR4
  article-title: An elaborate classification of SNARE proteins sheds light on the conservation of the eukaryotic endomembrane system
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e07-03-0193
– volume: 289
  start-page: 9639
  year: 2014
  end-page: 9650
  ident: CR29
  article-title: An extended helical conformation in domain 3a of Munc18-1 provides a template for SNARE (soluble -ethylmaleimide-sensitive factor attachment protein receptor) complex assembly
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.514273
– volume: 313
  start-page: 673
  year: 2006
  end-page: 676
  ident: CR8
  article-title: N- to C-terminal SNARE complex assembly promotes rapid membrane fusion
  publication-title: Science
  doi: 10.1126/science.1129486
– volume: 80
  start-page: 675
  year: 2013
  end-page: 690
  ident: CR11
  article-title: Neurotransmitter release: the last millisecond in the life of a synaptic vesicle
  publication-title: Neuron
  doi: 10.1016/j.neuron.2013.10.022
– volume: 44
  start-page: 339
  year: 2015
  end-page: 367
  ident: CR13
  article-title: The synaptic vesicle release machinery
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev-biophys-060414-034057
– volume: 277
  start-page: 48318
  year: 2002
  end-page: 48324
  ident: CR42
  article-title: Vps51p links the VFT complex to the SNARE Tlg1p
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M209428200
– volume: 279
  start-page: 7613
  year: 2004
  end-page: 7621
  ident: CR7
  article-title: A transient N-terminal interaction of SNAP-25 and syntaxin nucleates SNARE assembly
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M312064200
– volume: 16
  start-page: 1197
  year: 1996
  end-page: 1207
  ident: CR34
  article-title: Definition of the readily releasable pool of vesicles at hippocampal synapses
  publication-title: Neuron
  doi: 10.1016/S0896-6273(00)80146-4
– volume: 8
  year: 2017
  ident: CR41
  article-title: Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms14236
– volume: 548
  start-page: 420
  year: 2017
  end-page: 425
  ident: CR50
  article-title: The primed SNARE–complexin–synaptotagmin complex for neuronal exocytosis
  publication-title: Nature
  doi: 10.1038/nature23484
– volume: 40
  start-page: 658
  year: 2007
  end-page: 674
  ident: CR55
  article-title: Phaser crystallographic software
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
– volume: 289
  start-page: 33617
  year: 2014
  end-page: 33628
  ident: CR24
  article-title: A pivotal role for pro-335 in balancing the dual functions of Munc18-1 domain-3a in regulated exocytosis
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M114.584805
– volume: 110
  start-page: 12637
  year: 2013
  end-page: 12642
  ident: CR47
  article-title: Syntaxin1a variants lacking an N-peptide or bearing the LE mutation bind to Munc18a in a closed conformation
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1303753110
– volume: 18
  start-page: 542
  year: 2011
  end-page: 549
  ident: CR19
  article-title: Munc13 mediates the transition from the closed syntaxin-Munc18 complex to the SNARE complex
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2047
– volume: 36
  start-page: 6881
  year: 2016
  end-page: 6891
  ident: CR25
  article-title: Extension of Helix 12 in Munc18-1 Induces Vesicle Priming
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.0007-16.2016
– volume: 15
  start-page: 665
  year: 2008
  ident: 8028_CR3
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.1450
– volume: 490
  start-page: 201
  year: 2012
  ident: 8028_CR12
  publication-title: Nature
  doi: 10.1038/nature11320
– ident: 8028_CR37
  doi: 10.7554/eLife.22567
– volume: 36
  start-page: 6881
  year: 2016
  ident: 8028_CR25
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.0007-16.2016
– volume: 5
  year: 2015
  ident: 8028_CR58
  publication-title: Sci. Rep.
  doi: 10.1038/srep13875
– volume: 110
  start-page: 12637
  year: 2013
  ident: 8028_CR47
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.1303753110
– volume: 20
  start-page: 4910
  year: 2009
  ident: 8028_CR53
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e09-04-0284
– volume: 8
  start-page: e67409
  year: 2013
  ident: 8028_CR46
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0067409
– volume: 109
  start-page: 1863
  year: 2015
  ident: 8028_CR52
  publication-title: Biophys. J.
  doi: 10.1016/j.bpj.2015.08.051
– volume: 53
  start-page: 12696
  year: 2014
  ident: 8028_CR1
  publication-title: Angew. Chem. Int. Ed. Engl.
  doi: 10.1002/anie.201406359
– volume: 44
  start-page: 339
  year: 2015
  ident: 8028_CR13
  publication-title: Annu. Rev. Biophys.
  doi: 10.1146/annurev-biophys-060414-034057
– volume: 135
  start-page: 15274
  year: 2013
  ident: 8028_CR35
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja407392n
– volume: 349
  start-page: 1111
  year: 2015
  ident: 8028_CR28
  publication-title: Science
  doi: 10.1126/science.aac7906
– volume: 548
  start-page: 420
  year: 2017
  ident: 8028_CR50
  publication-title: Nature
  doi: 10.1038/nature23484
– volume: 25
  start-page: 955
  year: 2006
  ident: 8028_CR9
  publication-title: EMBO J.
  doi: 10.1038/sj.emboj.7601003
– volume: 339
  start-page: 421
  year: 2013
  ident: 8028_CR20
  publication-title: Science
  doi: 10.1126/science.1230473
– volume: 279
  start-page: 7613
  year: 2004
  ident: 8028_CR7
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M312064200
– volume: 10
  start-page: 256
  year: 2017
  ident: 8028_CR49
  publication-title: Front. Mol. Neurosci.
  doi: 10.3389/fnmol.2017.00256
– volume: 7
  start-page: 631
  year: 2006
  ident: 8028_CR2
  publication-title: Nat. Rev. Mol. Cell. Biol.
  doi: 10.1038/nrm2002
– volume: 289
  start-page: 9639
  year: 2014
  ident: 8028_CR29
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.514273
– volume: 108
  start-page: 1040
  year: 2011
  ident: 8028_CR23
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0914906108
– volume: 22
  start-page: 547
  year: 2015
  ident: 8028_CR22
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.3038
– volume: 18
  start-page: 4483
  year: 2007
  ident: 8028_CR40
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e07-05-0461
– volume: 313
  start-page: 673
  year: 2006
  ident: 8028_CR8
  publication-title: Science
  doi: 10.1126/science.1129486
– volume: 139
  start-page: 1119
  year: 2009
  ident: 8028_CR39
  publication-title: Cell
  doi: 10.1016/j.cell.2009.11.002
– volume: 18
  start-page: 927
  year: 2011
  ident: 8028_CR48
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2101
– volume: 18
  start-page: 3463
  year: 2007
  ident: 8028_CR4
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e07-03-0193
– volume: 27
  start-page: 923
  year: 2008
  ident: 8028_CR17
  publication-title: EMBO J.
  doi: 10.1038/emboj.2008.37
– volume: 126
  start-page: 2361
  year: 2013
  ident: 8028_CR27
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.126862
– ident: 8028_CR54
  doi: 10.7554/eLife.14211
– volume: 7
  start-page: 921
  year: 2012
  ident: 8028_CR36
  publication-title: Nat. Protoc.
  doi: 10.1038/nprot.2012.020
– volume: 214
  start-page: 847
  year: 2016
  ident: 8028_CR26
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201508118
– volume: 7
  start-page: 539
  year: 2011
  ident: 8028_CR59
  publication-title: Mol. Syst. Biol.
  doi: 10.1038/msb.2011.75
– volume: 66
  start-page: 486
  year: 2010
  ident: 8028_CR56
  publication-title: Acta Crystallogr. D
  doi: 10.1107/S0907444910007493
– volume: 395
  start-page: 347
  year: 1998
  ident: 8028_CR5
  publication-title: Nature
  doi: 10.1038/26412
– volume: 21
  start-page: 123
  year: 1998
  ident: 8028_CR15
  publication-title: Neuron
  doi: 10.1016/S0896-6273(00)80520-6
– volume: 40
  start-page: 658
  year: 2007
  ident: 8028_CR55
  publication-title: J. Appl. Crystallogr.
  doi: 10.1107/S0021889807021206
– volume: 404
  start-page: 355
  year: 2000
  ident: 8028_CR18
  publication-title: Nature
  doi: 10.1038/35006120
– volume: 18
  start-page: 542
  year: 2011
  ident: 8028_CR19
  publication-title: Nat. Struct. Mol. Biol.
  doi: 10.1038/nsmb.2047
– volume: 179
  start-page: 1179
  year: 2007
  ident: 8028_CR43
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200705145
– volume: 91
  start-page: 1445
  year: 1994
  ident: 8028_CR14
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.91.4.1445
– volume: 95
  start-page: 591
  year: 2017
  ident: 8028_CR32
  publication-title: Neuron
  doi: 10.1016/j.neuron.2017.07.004
– volume: 104
  start-page: 8755
  year: 2007
  ident: 8028_CR44
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.0702290104
– volume: 277
  start-page: 48318
  year: 2002
  ident: 8028_CR42
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M209428200
– volume: 19
  start-page: 2500
  year: 2008
  ident: 8028_CR45
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e08-01-0077
– volume: 8
  year: 2017
  ident: 8028_CR31
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms15915
– volume: 289
  start-page: 33617
  year: 2014
  ident: 8028_CR24
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M114.584805
– volume: 460
  start-page: 525
  year: 2009
  ident: 8028_CR6
  publication-title: Nature
  doi: 10.1038/nature08156
– ident: 8028_CR30
  doi: 10.7554/eLife.24278
– volume: 339
  start-page: 406
  year: 2013
  ident: 8028_CR33
  publication-title: Science
  doi: 10.1126/science.1233801
– volume: 4
  start-page: 42
  year: 2016
  ident: 8028_CR38
  publication-title: Front. Cell. Dev. Biol.
  doi: 10.3389/fcell.2016.00042
– volume: 36
  start-page: 816
  year: 2017
  ident: 8028_CR21
  publication-title: EMBO J.
  doi: 10.15252/embj.201695775
– volume: 32
  start-page: 15983
  year: 2012
  ident: 8028_CR51
  publication-title: J. Neurosci.
  doi: 10.1523/JNEUROSCI.6282-11.2012
– volume: 8
  year: 2017
  ident: 8028_CR41
  publication-title: Nat. Commun.
  doi: 10.1038/ncomms14236
– volume: 92
  start-page: 759
  year: 1998
  ident: 8028_CR10
  publication-title: Cell
  doi: 10.1016/S0092-8674(00)81404-X
– volume: 16
  start-page: 1197
  year: 1996
  ident: 8028_CR34
  publication-title: Neuron
  doi: 10.1016/S0896-6273(00)80146-4
– volume: 592
  start-page: 1161
  year: 2018
  ident: 8028_CR57
  publication-title: FEBS Lett.
  doi: 10.1002/1873-3468.13018
– volume: 30
  start-page: 564
  year: 2007
  ident: 8028_CR16
  publication-title: Trends Neurosci.
  doi: 10.1016/j.tins.2007.08.008
– volume: 80
  start-page: 675
  year: 2013
  ident: 8028_CR11
  publication-title: Neuron
  doi: 10.1016/j.neuron.2013.10.022
SSID ssj0000391844
Score 2.661792
Snippet The transition of the Munc18-1/syntaxin-1 complex to the SNARE complex, a key step involved in exocytosis, is regulated by Munc13-1, SNAP-25 and...
Synaptic exocytosis depends on formation of the SNARE complex but its assembly mechanism is still under debate. Here, the authors identify an interaction...
SourceID doaj
pubmedcentral
osti
proquest
pubmed
crossref
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Enrichment Source
Publisher
StartPage 69
SubjectTerms 631/378/548/2589
631/535/1266
631/80/313/2104
82/80
82/83
9/74
Animals
Assembly
BASIC BIOLOGICAL SCIENCES
Biophysics
Complex formation
Exocytosis
Gene Knockdown Techniques
HEK293 Cells
Humanities and Social Sciences
Humans
Laboratories
Membrane vesicles
Mice
multidisciplinary
Munc18 Proteins - metabolism
Mutation
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Neurons
Primary Cell Culture
Protein Binding - physiology
Protein Domains - physiology
Proteins
Science
Science (multidisciplinary)
SNAP receptors
SNAP-25 protein
SNARE
Synaptic vesicle exocytosis
Synaptobrevin
Synaptosomal-Associated Protein 25 - metabolism
Syntaxin
Syntaxin 1
Syntaxin 1 - metabolism
Vesicle-Associated Membrane Protein 2 - metabolism
X-ray crystallography
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1La9wwEBYlUOil9F03aVGht3aJJdl6HNOSEArJoW0gN6EnLWztkHWg-fedkbzbbJ-XnrzYEivPjDzfSJpvCHnlVNK-02zhReaLjuH-Lo9gy5oHZ3pnQsJ855NTeXzWvT_vz2-U-sIzYZUeuApuX7uWZZ681Nx0KiuTpE6cyRCYjCmW1D3weTeCqfINFgZCl27OkmmF3l915ZvQMiRkxiUlueWJCmE_XEaYWL8Dm7-emfxp47T4o6N75O4MJOlBfYH75FYaHpDbtbTk9UNiT8BhMU3dEGn5KSiuvybqVtRR9GZ1EZAiN9USACedRjpelvJZyB5BC9ElNvh4evDhkJaj5-kbdF-lr355_YicHR1-ene8mIspLEIv1QQBp3FeYzjnhTNd4J2UWqQcQ9tGhQSOoWVJiWz6rEQSqndKIhmZ8zwyl8VjsjOMQ3pKqAfZxxSEx0woFrNhQYFctIo6O5b7hrC1YG2Ymcax4MXSlh1voW1VhgVl2KIMKxvyetPnovJs_LX1W9TXpiVyZJcbYDl2thz7L8tpyC5q2wLUQL7cgAeLwmQBAgFugb_YWxuBnaf1ykLvSpfTNeTl5jFMSNxlcUMar2ob2QNQUw15Um1mM06IzzD3WDREbVnT1otsPxm-fC6k31LwngsY9Ju13f0Y1p8F9ex_CGqX3AGYaMrCk94jO9PlVXoOUGzyL8qs-w6QFS16
  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/eLvHCXMwfV1Lb9QwELagCIkL4k1oQUbiBqvGduLHCRXUpUJqD0Cl3iy_AkhLUjapRP89M0421fLoKVHiKLZnxjOeGX9DyCunkvaVZgsvGr6oGMZ3eQRe1jw4UzsTEp53Pj6RR6fVx7P6bHK49VNa5WZNzAt17AL6yPc5kyNSSfX2_OcCq0ZhdHUqoXGT3GKgaTClSy8_zD4WRD_XVTWdlSmF3u-rvDKUDGGZ0bEkt_RRhu2HSwfi9S-T8-_MyT_Cp1krLe-Ru5M5SQ9G-t8nN1L7gNweC0xePiT2GNQW09S1keZbQdELm6jrqaOo00ZXIEWEqhWYnXToaLfORbQQQ4JmuEts8Pnk4NMhzQno6Rd83qcffnX5iJwuD7-8P1pMJRUWoZZqgG2ncV7jps4LZ6rAK5g1kZoYyjIqhHEMJUtKNKZulEhC1U5JhCRznkfmGvGY7LRdm54S6kNgMQXh8TwUi41hQcG8aBV141hTF4RtJtaGCW8cy16sbI57C21HYlgghs3EsLIgr-dvzke0jWtbv0N6zS0RKTs_6NZf7SR4VruSNTx5qbmpVKNMkjoBM0HvZUzRFGQXqW3B4EDU3IDpRWGwYAiB9QK_2NswgZ2Eu7dXrFiQl_NrEEuMtbg2dRdjG1mDuaYK8mTkmbmfsEvDE8iiIGqLm7YGsv2m_f4tQ39LwWsuoNNvNnx31a3_T9Sz60exS-6AGWiyY0nvkZ1hfZGeg6k1-BdZnn4D0KQkwA
  priority: 102
  providerName: ProQuest
– databaseName: HAS SpringerNature Open Access 2022
  dbid: AAJSJ
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3daxQxEA-1RfBF_HbbKhF808NNsptkH09pKQftg7XQt5BPFa67crcF-993Jrt7cloFn-64nXBzmZnLL5OZXwh5a1XUrtJs5kTis4rh-S4P4Muae9vUtvER-51Pz-TJRbW4rC93CJ96YXLRfqa0zH_TU3XYh3WVQ7pkyKeMGSF5j-whVTv49t58vjhfbDIryHmuq2rskCmFvmPw1iqUyfrhpYOgugto_lkv-duhaV6Ljh-RhyOIpPNB7cdkJ7ZPyP3hWsmbp8ScwmLFNLVtoPmtoJh7jdSuqaW4kg0JQIq8VEsAm7TvaLfKV2chcwTNJJcocH42_3xEc9l5_AnD1_HKLW-ekYvjoy-fTmbjRQozX0vVw2azsU7jVs4J21SeV1JqEVPwZRkUkjf6kkUlUlMnJaJQtVUSicis44HZJJ6T3bZr40tCnfcsRC8cdkGxkBrmFcyLVkEny1JdEDZNrPEjyzhedrE0-bRbaDMYw4AxTDaGkQV5txnzY-DY-Kf0R7TXRhL5sfMH3eqrGf3FaFuyxKOTmjeVSqqJUkfOJGgvQwxNQQ7Q2gZgBnLleiwq8r0B-AOYBb7icHICM4b02sDogSqnKsibzWMIRjxhsW3srgcZWQNIUwV5MfjMRk_Ym2HfsSiI2vKmrR-y_aT9_i0TfkvBay5A6feT3_1S6-8Ttf9_4gfkAYDBJqeX9CHZ7VfX8RUArt69HiPsFqR5I-U
  priority: 102
  providerName: Springer Nature
Title Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly
URI https://link.springer.com/article/10.1038/s41467-018-08028-6
https://www.ncbi.nlm.nih.gov/pubmed/30622273
https://www.proquest.com/docview/2165096584
https://www.proquest.com/docview/2165657417
https://www.osti.gov/servlets/purl/1510246
https://pubmed.ncbi.nlm.nih.gov/PMC6325239
https://doaj.org/article/8a01f2eb682947f79e68e216cc16ded9
Volume 10
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV3db9MwELf2ISReJr4JG5WReINCHCf-eECoq1qmSq3QRqW-WY7jDKSSjLaT1v-eOyctKpS9JFFit459F_985_sdIW-t9CpPFevmvEy6KUP_blKALKvEWZ1Z7TzGO48n4mKajmbZ7IBs0h21Hbjcu7TDfFLTxfzD3a_1Z1D4T03IuPq4TIO6xwy5ltFaJA7JMcxMEjMajFu4H77MXMOCBh3NSZyyLhTgbRzN_p_ZmasCpT-calC9fXD0312Vf7lWw4w1fEROWqhJe41sPCYHvnpCHjTJJ9dPiRnDlMYUtVVBwyWnaKH11C6ppTjfNWZCiuxVc4CkdFXTehESbCG_BA1UmFjgatK7HNCwOd3fQfWl_5nP18_IdDj41r_otukWui4TcgVLUm1zhQu-nFuduiQVQnFfFi6OC4kUjy5mXvJSZ6XknsvMSoF0ZTZPCmZL_pwcVXXlXxKaO8cK73iOsVKsKDVzEvpFyUKVlpVZRNimY41rucgxJcbcBJ84V6YZDAODYcJgGBGRd9s6Nw0Tx72lz3G8tiWRRTvcqBfXplVKo2zMysTnQiU6laXUXiifMAGtF4UvdEROcbQNgBFk1HW49citDIAkQDbwF2cbITAbuTVQuyHUSSPyZvsYVBb9MLby9W1TRmQA5WREXjQys20nrOAwOplHRO5I086L7D6pfnwPtOCCJ1nCodHvN3L3p1n_76hX977jKXkICFEHm5M6I0erxa1_DShslXfIoZxJOKrhlw457vVGVyM4nw8mXy_hbl_0O8G-0Qkq-BsDljBx
linkProvider Scholars Portal
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwELZKEYIL4k1oASPBCVaNH7GdA0IFWra0uwdopd6M4ziAtCRldyvYP8VvZMZJtloevfWUKHESxzOeGc94viHkqdPBFNKwQSEqPpAM47u8BF423Ls8c7kPmO88GqvhkXx_nB2vkV99Lgxuq-xlYhTUZePRR77FmWqRSuSrk-8DrBqF0dW-hEbLFvth8QOWbLOXe2-Bvs843905fDMcdFUFBj5Teg4rr9wVBtc1hXC59FwqZUSoSp-mpUYkQ5-yoEWVZ5UWQejMaYWoXK7gJXOVgPdeIpelAE2Omem775Y-HURbN1J2uTmpMFszGSVRyhAGGh1ZakX_xTIBcGhgOv_LxP17p-Yf4dqoBXdvkOud-Uq3W367SdZCfYtcaQtaLm4TOwI1yQx1dUnjqaDo9Q3UzaijqENb1yNFRKwJmLl03tBmGot2IWYFjfCa2ODjePvDDo0b3sNPeHwWvhWTxR1ydCGDfZes100d7hNaeM_K4EWB-VesrHLmNYyL0aWpHKuyhLB-YK3v8M2xzMbExji7MLYlhgVi2EgMqxLyfPnMSYvucW7r10ivZUtE5o4Xmuln2010a1zKKh4KZXgudaXzoEwA5oXeqzKUeUI2kNoWDBxE6fW4ncnPLRheYC3BJzZ7JrCdMJnZM9ZPyJPlbRADGNtxdWhO2zYqA_NQJ-ReyzPLfsKqEDOeRUL0Cjet_Mjqnfrrlwg1rgTPuIBOv-j57qxb_x-oB-f_xWNydXg4OrAHe-P9DXINTNA8OrXMJlmfT0_DQzDz5sWjOLco-XTRk_k3QtpgdA
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV3db9MwELdGJxAviG_CBhgJnqBqbCe284DQxlptjFXTYNLePMdxAKkko-0E_df467hzkk7lY297atU4jeO7s-_zd4S8sMrrPNGsn4uS9xOG8V1eAC9r7myW2sx5rHc-GMvd4-T9SXqyRn51tTCYVtntiWGjLmqHPvIBZ7JBKkkGZZsWcbgzenv2vY8dpDDS2rXTaFhk3y9-gPk2e7O3A7R-yflo-Ondbr_tMNB3qVRzsMIym2u0cXJhs8TxREotfFm4OC4Uohq6mHklyiwtlfBCpVZJROiyOS-YLQX87zWyrtAq6pH17eH48Gjp4UHsdZ0kbaVOLPRgloR9KWYICo1uLblyGoamAfBRg3D_S-H9O2_zj-BtOBNHt8mtVpmlWw333SFrvrpLrjftLRf3iDmAQ5NpaquChq-Cog_YUzujluKJ2jgiKeJjTUDppfOa1tPQwgsRLGgA28QBH8dbR0Ma0t_9T7h95r_lk8V9cnwly_2A9Kq68o8IzZ1jhXcix2osVpQZcwrWRatCl5aVaURYt7DGtWjn2HRjYkLUXWjTEMMAMUwghpERebW856zB-rh09DbSazkScbrDD_X0s2nF3mgbs5L7XGqeJapUmZfaAyvD7GXhiywiG0htA-oOYvY6TG5ycwNqGOhO8IjNjglMu7XMzIUgROT58jJsChjpsZWvz5sxMgVlUUXkYcMzy3mCjYj1zyIiaoWbVl5k9Ur19UsAHpeCp1zApF93fHcxrf8v1OPL3-IZuQGCbD7sjfc3yE3QR7Pg4dKbpDefnvsnoPPN86etcFFyetXy_BvW_WYG
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=Munc18+and+Munc13+serve+as+a+functional+template+to+orchestrate+neuronal+SNARE+complex+assembly&rft.jtitle=Nature+communications&rft.au=Wang%2C+Shen&rft.au=Li%2C+Yun&rft.au=Gong%2C+Jihong&rft.au=Ye%2C+Sheng&rft.date=2019-01-08&rft.pub=Nature+Publishing+Group&rft.issn=2041-1723&rft.eissn=2041-1723&rft.volume=10&rft.issue=1&rft_id=info:doi/10.1038%2Fs41467-018-08028-6&rft.externalDocID=1510246
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