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Structure of membrane tethers and their role in fusion
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/bies.201600062openalex-snapshot
Coiled‐coils: The long and short of it
inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb01039.xopenalex-snapshot
The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae.
inferredcites →https://doi.org/10.1002/pro.3445openalex-snapshot
Mechanism of neurotransmitter release coming into focus
inferredcites →https://doi.org/10.1006/jsbi.1996.0053openalex-snapshot
Uso1 Protein Is a Dimer with Two Globular Heads and a Long Coiled-Coil Tail
inferredcites →https://doi.org/10.1007/s00418-013-1117-6openalex-snapshot
The Golgi puppet master: COG complex at center stage of membrane trafficking interactions
inferredcites →https://doi.org/10.1016/j.cell.2006.12.016openalex-snapshot
Selective Activation of Cognate SNAREpins by Sec1/Munc18 Proteins
inferredcites →https://doi.org/10.1016/j.cell.2007.11.048openalex-snapshot
Rab and Arl GTPase Family Members Cooperate in the Localization of the Golgin GCC185
inferredcites →https://doi.org/10.1016/j.cell.2009.05.048openalex-snapshot
The Localization of the Golgin GCC185 Is Independent of Rab6A/A' and Arl1
inferredcites →https://doi.org/10.1016/j.cell.2009.11.002openalex-snapshot
A Structure-Based Mechanism for Vesicle Capture by the Multisubunit Tethering Complex Dsl1
inferredcites →https://doi.org/10.1016/j.cell.2017.01.004openalex-snapshot
The In Vivo Architecture of the Exocyst Provides Structural Basis for Exocytosis
inferredcites →https://doi.org/10.1016/j.cub.2010.08.002openalex-snapshot
The Mon1-Ccz1 Complex Is the GEF of the Late Endosomal Rab7 Homolog Ypt7
inferredcites →https://doi.org/10.1016/j.devcel.2007.03.006openalex-snapshot
The CORVET Tethering Complex Interacts with the Yeast Rab5 Homolog Vps21 and Is Involved in Endo-Lysosomal Biogenesis
inferredcites →https://doi.org/10.1016/j.devcel.2009.07.012openalex-snapshot
A Link between ER Tethering and COP-I Vesicle Uncoating
inferredcites →https://doi.org/10.1016/j.devcel.2014.10.007openalex-snapshot
Toward a Comprehensive Map of the Effectors of Rab GTPases
inferredcites →https://doi.org/10.1016/j.jmb.2005.09.099openalex-snapshot
Crystal Structure of the S.cerevisiae Exocyst Component Exo70p
inferredcites →https://doi.org/10.1016/j.jmb.2017.12.007openalex-snapshot
A Completely Reimplemented MPI Bioinformatics Toolkit with a New HHpred Server at its Core
inferredcites →https://doi.org/10.1016/j.neuron.2017.07.004openalex-snapshot
Molecular Mechanisms of Synaptic Vesicle Priming by Munc13 and Munc18
inferredcites →https://doi.org/10.1016/j.str.2011.07.012openalex-snapshot
The Crystal Structure of a Munc13 C-terminal Module Exhibits a Remarkable Similarity to Vesicle Tethering Factors
inferredcites →https://doi.org/10.1016/j.tcb.2010.11.003openalex-snapshot
Transport according to GARP: receiving retrograde cargo at the trans-Golgi network
inferredcites →https://doi.org/10.1016/j.tcb.2013.09.006openalex-snapshot
Tethering the assembly of SNARE complexes
inferredcites →https://doi.org/10.1016/j.tcb.2016.02.005openalex-snapshot
Finding the Golgi: Golgin Coiled-Coil Proteins Show the Way
inferredcites →https://doi.org/10.1016/j.tibs.2018.06.012openalex-snapshot
Exposing the Elusive Exocyst Structure
inferredcites →https://doi.org/10.1016/j.yjsbx.2019.100003openalex-snapshot
SmartBac, a new baculovirus system for large protein complex production
inferredcites →https://doi.org/10.1016/s0092-8674(03)01079-1openalex-snapshot
The Mechanisms of Vesicle Budding and Fusion
inferredcites →https://doi.org/10.1016/s0896-6273(00)80493-6openalex-snapshot
Subunit Composition, Protein Interactions, and Structures of the Mammalian Brain sec6/8 Complex and Septin Filaments
inferredcites →https://doi.org/10.1016/s0960-9822(07)00351-xopenalex-snapshot
Involvement of the endosomal autoantigen EEA1 in homotypic fusion of early endosomes
inferredcites →https://doi.org/10.1016/s1097-2765(01)00385-9openalex-snapshot
Multivalent Endosome Targeting by Homodimeric EEA1
inferredcites →https://doi.org/10.1016/s1097-2765(03)00356-3openalex-snapshot
Structural Basis for Arl1-Dependent Targeting of Homodimeric GRIP Domains to the Golgi Apparatus
inferredcites →https://doi.org/10.1017/s0033583505004051openalex-snapshot
Structure and function of SNARE and SNARE-interacting proteins
inferredcites →https://doi.org/10.1038/35006120openalex-snapshot
Three-dimensional structure of the neuronal-Sec1–syntaxin 1a complex
inferredcites →https://doi.org/10.1038/85012openalex-snapshot
Vam3p structure reveals conserved and divergent properties of syntaxins.
inferredcites →https://doi.org/10.1038/emboj.2008.139openalex-snapshot
Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones
inferredcites →https://doi.org/10.1038/emboj.2009.168openalex-snapshot
Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing
inferredcites →https://doi.org/10.1038/nature08107openalex-snapshot
Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes
inferredcites →https://doi.org/10.1038/nature19326openalex-snapshot
An endosomal tether undergoes an entropic collapse to bring vesicles together
inferredcites →https://doi.org/10.1038/nature24469openalex-snapshot
A tethering complex drives the terminal stage of SNARE-dependent membrane fusion
inferredcites →https://doi.org/10.1038/ncb2226openalex-snapshot
Exocyst function regulated by effector phosphorylation
inferredcites →https://doi.org/10.1038/ncomms14236openalex-snapshot
Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion
inferredcites →https://doi.org/10.1038/nsmb.1548openalex-snapshot
Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
inferredcites →https://doi.org/10.1038/nsmb.1722openalex-snapshot
Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3
inferredcites →https://doi.org/10.1038/nsmb.1917openalex-snapshot
Molecular organization of the COG vesicle tethering complex
inferredcites →https://doi.org/10.1038/nsmb.3038openalex-snapshot
Syntaxin opening by the MUN domain underlies the function of Munc13 in synaptic-vesicle priming
inferredcites →https://doi.org/10.1038/nsmb.3146openalex-snapshot
Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex
inferredcites →https://doi.org/10.1038/nsmb.3263openalex-snapshot
Molecular architecture of the complete COG tethering complex
inferredcites →https://doi.org/10.1038/nsmb.3264openalex-snapshot
CATCHR, HOPS and CORVET tethering complexes share a similar architecture
inferredcites →https://doi.org/10.1038/nsmb1017openalex-snapshot
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
inferredcites →https://doi.org/10.1038/nsmb1096openalex-snapshot
The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
inferredcites →https://doi.org/10.1038/nsmb714openalex-snapshot
Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Arl1
inferredcites →https://doi.org/10.1038/nsmb987openalex-snapshot
Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
inferredcites →https://doi.org/10.1038/s41467-018-07467-5openalex-snapshot
Exocyst dynamics during vesicle tethering and fusion
inferredcites →https://doi.org/10.1038/s41467-018-08028-6openalex-snapshot
Munc18 and Munc13 serve as a functional template to orchestrate neuronal SNARE complex assembly
inferredcites →https://doi.org/10.1038/s41594-017-0016-2openalex-snapshot
Cryo-EM structure of the exocyst complex
inferredcites →https://doi.org/10.1038/sj.emboj.7600699openalex-snapshot
Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase
inferredcites →https://doi.org/10.1038/srep40909openalex-snapshot
Crystal structure of Sec10, a subunit of the exocyst complex
inferredcites →https://doi.org/10.1073/pnas.0901966106openalex-snapshot
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene
inferredcites →https://doi.org/10.1073/pnas.0903801106openalex-snapshot
Minimal membrane docking requirements revealed by reconstitution of Rab GTPase-dependent membrane fusion from purified components
inferredcites →https://doi.org/10.1073/pnas.1000843107openalex-snapshot
Structural basis for Rab GTPase recognition and endosome tethering by the C 2 H 2 zinc finger of Early Endosomal Autoantigen 1 (EEA1)
inferredcites →https://doi.org/10.1073/pnas.1004756107openalex-snapshot
Structural basis for the wobbler mouse neurodegenerative disorder caused by mutation in the Vps54 subunit of the GARP complex
inferredcites →https://doi.org/10.1073/pnas.1009419107openalex-snapshot
Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes
inferredcites →https://doi.org/10.1073/pnas.1117797109openalex-snapshot
Molecular architecture of the multisubunit homotypic fusion and vacuole protein sorting (HOPS) tethering complex
inferredcites →https://doi.org/10.1073/pnas.1221785110openalex-snapshot
The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes
inferredcites →https://doi.org/10.1073/pnas.1307074110openalex-snapshot
Structural basis of Vps33A recruitment to the human HOPS complex by Vps16
inferredcites →https://doi.org/10.1073/pnas.1414829111openalex-snapshot
Cog5–Cog7 crystal structure reveals interactions essential for the function of a multisubunit tethering complex
inferredcites →https://doi.org/10.1073/pnas.92.2.522openalex-snapshot
p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p.
inferredcites →https://doi.org/10.1073/pnas.97.17.9402openalex-snapshot
A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion
inferredcites →https://doi.org/10.1074/jbc.m109.000737openalex-snapshot
The Major Role of the Rab Ypt7p in Vacuole Fusion Is Supporting HOPS Membrane Association
inferredcites →https://doi.org/10.1074/jbc.m109.096966openalex-snapshot
Structure-Function Study of the N-terminal Domain of Exocyst Subunit Sec3
inferredcites →https://doi.org/10.1074/jbc.m111729200openalex-snapshot
Conformational Regulation of SNARE Assembly and Disassembly in Vivo
inferredcites →https://doi.org/10.1074/jbc.m114.602714openalex-snapshot
Structural Identification of the Vps18 β-Propeller Reveals a Critical Role in the HOPS Complex Stability and Function
inferredcites →https://doi.org/10.1074/jbc.m114.631465openalex-snapshot
The Habc Domain of the SNARE Vam3 Interacts with the HOPS Tethering Complex to Facilitate Vacuole Fusion
inferredcites →https://doi.org/10.1074/jbc.m115.688440openalex-snapshot
Characterization of the Mammalian CORVET and HOPS Complexes and Their Modular Restructuring for Endosome Specificity
inferredcites →https://doi.org/10.1074/jbc.m308702200openalex-snapshot
Ral GTPases Regulate Exocyst Assembly through Dual Subunit Interactions
inferredcites →https://doi.org/10.1074/jbc.m308740200openalex-snapshot
Dsl1p, an Essential Component of the Golgi-Endoplasmic Reticulum Retrieval System in Yeast, Uses the Same Sequence Motif to Interact with Different Subunits of the COPI Vesicle Coat
inferredcites →https://doi.org/10.1074/jbc.m503925200openalex-snapshot
A Cryptic Rab1-binding Site in the p115 TetheringProtein
inferredcites →https://doi.org/10.1074/jbc.m504590200openalex-snapshot
Subunit Architecture of the Conserved Oligomeric Golgi Complex
inferredcites →https://doi.org/10.1074/jbc.m703716200openalex-snapshot
Structural Analysis of Conserved Oligomeric Golgi Complex Subunit 2
inferredcites →https://doi.org/10.1083/jcb.151.3.551openalex-snapshot
New Component of the Vacuolar Class C-Vps Complex Couples Nucleotide Exchange on the Ypt7 Gtpase to Snare-Dependent Docking and Fusion
inferredcites →https://doi.org/10.1083/jcb.200111081openalex-snapshot
The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins
inferredcites →https://doi.org/10.1083/jcb.200408124openalex-snapshot
Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p
inferredcites →https://doi.org/10.1083/jcb.200705145openalex-snapshot
Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability
inferredcites →https://doi.org/10.1083/jcb.200808018openalex-snapshot
Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins
inferredcites →https://doi.org/10.1083/jcb.201611027openalex-snapshot
Rab2 promotes autophagic and endocytic lysosomal degradation
inferredcites →https://doi.org/10.1091/mbc.11.1.305openalex-snapshot
Vps52p, Vps53p, and Vps54p Form a Novel Multisubunit Complex Required for Protein Sorting at the Yeast Late Golgi
inferredcites →https://doi.org/10.1091/mbc.e05-01-0056openalex-snapshot
Dsl1p, Tip20p, and the Novel Dsl3(Sec39) Protein Are Required for the Stability of the Q/t-SNARE Complex at the Endoplasmic Reticulum in Yeast
inferredcites →https://doi.org/10.1091/mbc.e08-07-0740openalex-snapshot
Multiple Rab GTPase Binding Sites in GCC185 Suggest a Model for Vesicle Tethering at the Trans -Golgi
inferredcites →https://doi.org/10.1091/mbc.e09-06-0521openalex-snapshot
The CORVET Subunit Vps8 Cooperates with the Rab5 Homolog Vps21 to Induce Clustering of Late Endosomal Compartments
inferredcites →https://doi.org/10.1091/mbc.e10-03-0260openalex-snapshot
Subunit organization and Rab interactions of Vps-C protein complexes that control endolysosomal membrane traffic
inferredcites →https://doi.org/10.1091/mbc.e11-02-0104openalex-snapshot
HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites
inferredcites →https://doi.org/10.1091/mbc.e11-08-0670openalex-snapshot
Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1
inferredcites →https://doi.org/10.1091/mbc.e12-05-0343openalex-snapshot
Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex
inferredcites →https://doi.org/10.1091/mbc.e14-04-0907openalex-snapshot
The role of Sec3p in secretory vesicle targeting and exocyst complex assembly
inferredcites →https://doi.org/10.1091/mbc.e16-07-0517openalex-snapshot
A cascade of multiple proteins and lipids catalyzes membrane fusion
inferredcites →https://doi.org/10.1091/mbc.e16-11-0764openalex-snapshot
Multivalent Rab interactions determine tether-mediated membrane fusion
inferredcites →https://doi.org/10.1093/bioinformatics/18.4.617openalex-snapshot
An HMM model for coiled-coil domains and a comparison with PSSM-based predictions
inferredcites →https://doi.org/10.1093/emboj/cdg329openalex-snapshot
Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex
inferredcites →https://doi.org/10.1111/j.1600-0854.2005.00374.xopenalex-snapshot
Structural Analysis of the Interaction Between the SNARE Tlg1 and Vps51
inferredcites →https://doi.org/10.1111/j.1600-0854.2012.01362.xopenalex-snapshot
The DSL1 Complex: The Smallest but Not the Least CATCHR
inferredcites →https://doi.org/10.1111/tra.12232openalex-snapshot
Mammalian CORVET Is Required for Fusion and Conversion of Distinct Early Endosome Subpopulations
inferredcites →https://doi.org/10.1126/science.1161748openalex-snapshot
Membrane Fusion: Grappling with SNARE and SM Proteins
inferredcites →https://doi.org/10.1126/science.1230473openalex-snapshot
Reconstitution of the Vital Functions of Munc18 and Munc13 in Neurotransmitter Release
inferredcites →https://doi.org/10.1126/science.1256898openalex-snapshot
The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins
inferredcites →https://doi.org/10.1126/science.291.5509.1793openalex-snapshot
Structural Mechanism of Endosome Docking by the FYVE Domain
inferredcites →https://doi.org/10.1126/science.aac7906openalex-snapshot
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly
inferredcites →https://doi.org/10.1126/scisignal.aah5085openalex-snapshot
Phosphorylation of the exocyst protein Exo84 by TBK1 promotes insulin-stimulated GLUT4 trafficking
inferredcites →https://doi.org/10.1128/ec.00286-09openalex-snapshot
Mapping of Vps21 and HOPS Binding Sites in Vps8 and Effect of Binding Site Mutants on Endocytic Trafficking
inferredcites →https://doi.org/10.1146/annurev.cellbio.042308.113327openalex-snapshot
Tethering Factors as Organizers of Intracellular Vesicular Traffic
inferredcites →https://doi.org/10.1242/jcs.115.13.2627openalex-snapshot
Vesicle tethering complexes in membrane traffic
inferredcites →https://doi.org/10.1242/jcs.162651openalex-snapshot
The small GTPase Arl8b regulates assembly of the mammalian HOPS complex to lysosomes
inferredcites →https://doi.org/10.1371/journal.pbio.0040192openalex-snapshot
Structural Basis for a Munc13–1 Homodimer to Munc13–1/RIM Heterodimer Switch
inferredcites →https://doi.org/10.1371/journal.pone.0067409openalex-snapshot
Crystal Structures of the Sec1/Munc18 (SM) Protein Vps33, Alone and Bound to the Homotypic Fusion and Vacuolar Protein Sorting (HOPS) Subunit Vps16*
inferredcites →https://doi.org/10.15252/embr.201642032openalex-snapshot
RAB2A controls MT1‐MMP endocytic and E‐cadherin polarized Golgi trafficking to promote invasive breast cancer programs
inferredcites →https://doi.org/10.3389/fcell.2016.00035openalex-snapshot
Membrane Tethering Complexes in the Endosomal System
inferredcites →https://doi.org/10.7554/elife.10982openalex-snapshot
TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export
inferredcites →https://doi.org/10.7554/elife.12790openalex-snapshot
Protein flexibility is required for vesicle tethering at the Golgi
inferredcites →https://doi.org/10.7554/elife.22567openalex-snapshot
Mechanistic insights into neurotransmitter release and presynaptic plasticity from the crystal structure of Munc13-1 C1C2BMUN
inferredcites →https://doi.org/10.7554/elife.23367openalex-snapshot
Genetic screen in Drosophila muscle identifies autophagy-mediated T-tubule remodeling and a Rab2 role in autophagy
inferredcites →https://doi.org/10.7554/elife.26646openalex-snapshot
Sec17/Sec18 act twice, enhancing membrane fusion and then disassembling cis-SNARE complexes
inferredcites →https://doi.org/10.7554/elife.41771openalex-snapshot
Munc18-1 catalyzes neuronal SNARE assembly by templating SNARE association
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Synergism of Vesicle Trafficking and Cytoskeleton During Regulation of Plant Growth and Development: A Mechanistic Outlook
inferred← citeshttps://doi.org/10.1002/1873-3468.14553openalex-snapshot
The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11
inferred← citeshttps://doi.org/10.1002/jev2.70029openalex-snapshot
Distinct molecular properties and functions of small EV subpopulations isolated from human umbilical cord MSCs using tangential flow filtration combined with size exclusion chromatography
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From plants to antimicrobials: Natural products against bacterial membranes
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Establishment and Maintenance of Epithelial Polarization
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SNARE Proteins in Synaptic Vesicle Fusion
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siRNA screening reveals that SNAP29 contributes to exosome release
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Localization of SNARE proteins in the brain and corpus allatum of Bombyx mori
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Modulating intracellular pathways to improve non-viral delivery of RNA therapeutics
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Golgi inCOGnito: From vesicle tethering to human disease
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The machinery of vesicle fusion
inferred← citeshttps://doi.org/10.1016/j.cub.2020.03.068openalex-snapshot
Evolution and Natural History of Membrane Trafficking in Eukaryotes
inferred← citeshttps://doi.org/10.1016/j.heliyon.2023.e21976openalex-snapshot
RETRACTED: Synergism of vesicle trafficking and cytoskeleton during regulation of plant growth and development: A mechanistic outlook
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Three live-imaging techniques for comprehensively understanding the initial trigger for insulin-responsive intracellular GLUT4 trafficking
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S-acylation of YKT61 modulates its unconventional participation in the formation of SNARE complexes in Arabidopsis
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Cancer-driving mutations and variants of components of the membrane trafficking core machinery
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Vesicle dynamics during the egress of malaria gametocytes from the red blood cell
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Cytosolic Protein Delivery Using Modular Biotin–Streptavidin Assembly of Nanocomposites
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Functionalization and higher-order organization of liposomes with DNA nanostructures
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Structural insight into an Arl1–ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin
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Structure of the endosomal CORVET tethering complex
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Mechanisms of SNARE proteins in membrane fusion
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Structure of a membrane tethering complex incorporating multiple SNAREs
inferred← citeshttps://doi.org/10.1038/s41594-024-01388-2openalex-snapshot
Exocyst stimulates multiple steps of exocytic SNARE complex assembly and vesicle fusion
inferred← citeshttps://doi.org/10.1038/s42003-021-01830-xopenalex-snapshot
Insights on autophagosome–lysosome tethering from structural and biochemical characterization of human autophagy factor EPG5
inferred← citeshttps://doi.org/10.1042/bcj20190050openalex-snapshot
SNAREs, tethers and SM proteins: how to overcome the final barriers to membrane fusion?
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SNARE proteins: zip codes in vesicle targeting?
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Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering
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Pathogenic bacteria exploit transferrin receptor transcytosis to penetrate the blood–brain barrier
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Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1
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Structure of the human autophagy factor EPG5 and the molecular basis of its conserved mode of interaction with Atg8-family proteins
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A BLOC-1–AP-3 super-complex sorts a cis-SNARE complex into endosome-derived tubular transport carriers
inferred← citeshttps://doi.org/10.1083/jcb.202105120openalex-snapshot
Who’s in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond
inferred← citeshttps://doi.org/10.1091/mbc.e21-05-0227openalex-snapshot
Subunit exchange among endolysosomal tethering complexes is linked to contact site formation at the vacuole
inferred← citeshttps://doi.org/10.1091/mbc.e23-01-0029openalex-snapshot
Multiple tethers of organelle contact sites are involved in α-synuclein toxicity in yeast
inferred← citeshttps://doi.org/10.1091/mbc.e25-11-0531openalex-snapshot
A GUV-based assay to reconstitute membrane tethering in vitro
inferred← citeshttps://doi.org/10.1101/2023.06.21.546015openalex-snapshot
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.1101/2023.10.13.562242openalex-snapshot
Structure of the endosomal CORVET tethering complex
inferred← citeshttps://doi.org/10.1101/2023.11.21.568162openalex-snapshot
A Potent Kalihinol Analogue Disrupts Apicoplast Function and Vesicular Trafficking in P. falciparum Malaria
inferred← citeshttps://doi.org/10.1111/jeu.12919openalex-snapshot
Molecular evolutionary analysis of the SM and SNARE vesicle fusion machinery in ciliates shows concurrent expansions in late secretory machinery
inferred← citeshttps://doi.org/10.1111/jnc.70495openalex-snapshot
Septins in the Middle—Makers and Breakers of Membrane Contact Sites
inferred← citeshttps://doi.org/10.1111/mmi.14851openalex-snapshot
The Nma1 protein promotes long distance transport mediated by early endosomes in Ustilago maydis
inferred← citeshttps://doi.org/10.1111/tra.12699openalex-snapshot
Overview: Traffic at atomic resolution
inferred← citeshttps://doi.org/10.1111/tra.12871openalex-snapshot
Developmental program‐independent secretory granule degradation in larval salivary gland cells of Drosophila
inferred← citeshttps://doi.org/10.1126/sciadv.adl0608openalex-snapshot
Cargo selective vesicle tethering: The structural basis for binding of specific cargo proteins by the Golgi tether component TBC1D23
inferred← citeshttps://doi.org/10.1126/science.adm7966openalex-snapshot
A kalihinol analog disrupts apicoplast function and vesicular trafficking in P. falciparum malaria
inferred← citeshttps://doi.org/10.1146/annurev-biochem-081820-103615openalex-snapshot
Chaperoning SNARE Folding and Assembly
inferred← citeshttps://doi.org/10.1242/jcs.263788openalex-snapshot
Vps41 functions as a molecular ruler for HOPS tethering complex-mediated membrane fusion
inferred← citeshttps://doi.org/10.1515/revneuro-2021-0020openalex-snapshot
Defects in early secretory pathway transport machinery components and neurodevelopmental disorders
inferred← citeshttps://doi.org/10.15252/embr.202357758openalex-snapshot
Orchestrating vesicular and nonvesicular membrane dynamics by intrinsically disordered proteins
inferred← citeshttps://doi.org/10.3389/fcell.2019.00146openalex-snapshot
Models of Intracellular Transport: Pros and Cons
inferred← citeshttps://doi.org/10.3389/fcell.2020.00539openalex-snapshot
Lipid Rafts, Sphingolipids, and Ergosterol in Yeast Vacuole Fusion and Maturation
inferred← citeshttps://doi.org/10.3389/fcell.2025.1574638openalex-snapshot
A tale of Rabs and the exocyst complex in ciliary trafficking and biogenesis
inferred← citeshttps://doi.org/10.3389/fgene.2021.709666openalex-snapshot
Establishment of an Endocytosis-Related Prognostic Signature for Patients With Low-Grade Glioma
inferred← citeshttps://doi.org/10.3390/cells10082021openalex-snapshot
Quantitative Proteomics Reveals Significant Differences between Mouse Brain Formations in Expression of Proteins Involved in Neuronal Plasticity during Aging
inferred← citeshttps://doi.org/10.3390/cells15111013openalex-snapshot
Annexin A6 Modulates the Secretion of Pro-Inflammatory Cytokines and Exosomes via Interaction with SNAP23 in Triple-Negative Breast Cancer Cells
inferred← citeshttps://doi.org/10.3390/cells9112402openalex-snapshot
Glutamatergic Receptor Trafficking and Delivery: Role of the Exocyst Complex
inferred← citeshttps://doi.org/10.3390/cells9122652openalex-snapshot
The Close Relationship between the Golgi Trafficking Machinery and Protein Glycosylation
inferred← citeshttps://doi.org/10.3390/ijms21207594openalex-snapshot
Membrane Curvature, Trans-Membrane Area Asymmetry, Budding, Fission and Organelle Geometry
inferred← citeshttps://doi.org/10.3390/jof10090614openalex-snapshot
Emerging Roles of Exocyst Complex in Fungi: A Review
inferred← citeshttps://doi.org/10.3390/jof12060431openalex-snapshot
Knockout of SsArl1 Leading to Enhanced Virulence in Sclerotinia sclerotiorum
inferred← citeshttps://doi.org/10.3390/plants13050684openalex-snapshot
Distributing Plant Developmental Regulatory Proteins via Plasmodesmata
inferred← citeshttps://doi.org/10.64898/2025.12.11.693622openalex-snapshot
Structural studies suggest CCDC127 as a novel membrane contact site protein in the mitochondrial intermembrane space
inferred← citeshttps://doi.org/10.64898/2026.04.02.716088openalex-snapshot
GRAF1-dependent endocytotic processes and the Golgi apparatus contribute to novel intermediate stages of early ciliogenesis
inferred← citeshttps://doi.org/10.64898/2026.05.20.726668openalex-snapshot
Functional assignment of Golgi-associated vesicle tethers to specific membrane recycling pathways
inferred← citeshttps://doi.org/10.7554/elife.80901openalex-snapshot
Structure of the HOPS tethering complex, a lysosomal membrane fusion machinery
inferred← citeshttps://doi.org/10.7554/elife.82041openalex-snapshot
Double NPY motifs at the N-terminus of the yeast t-SNARE Sso2 synergistically bind Sec3 to promote membrane fusion
inferred← citeshttps://doi.org/10.7554/elife.89938openalex-snapshot
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.1openalex-snapshot
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.1.sa3openalex-snapshot
eLife Assessment: Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.2openalex-snapshot
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.2.sa0openalex-snapshot
Reviewer #3 (Public Review): Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.2.sa1openalex-snapshot
Reviewer #2 (Public Review): Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.2.sa2openalex-snapshot
Reviewer #1 (Public Review): Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.2.sa3openalex-snapshot
eLife Assessment: Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.2.sa4openalex-snapshot
Author Response: Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.3openalex-snapshot
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
inferred← citeshttps://doi.org/10.7554/elife.89938.4openalex-snapshot
Membrane contact sites regulate vacuolar fission via sphingolipid metabolism
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