Membrane fusion (Q81623456)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18618939%20AND%20SRC:MED&resulttype=core&format=json

10 January 2020

review article

1 reference

title

Membrane fusion (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18618939%20AND%20SRC:MED&resulttype=core&format=json

10 January 2020

0 references

William Wickner

1

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18618939%20AND%20SRC:MED&resulttype=core&format=json

10 January 2020

Randy Schekman

series ordinal

2

1 reference

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10 January 2020

publication date

1 July 2008

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18618939%20AND%20SRC:MED&resulttype=core&format=json

Nature Structural & Molecular Biology

10 January 2020

published in

1 reference

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10 January 2020

volume

15

1 reference

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10 January 2020

issue

7

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10 January 2020

page(s)

658-664

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Mechanics of membrane fusion

10 January 2020

cites work

1 reference

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Osmotic and curvature stress affect PEG-induced fusion of lipid vesicles but not mixing of their lipids.

31 March 2020

1 reference

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Physiological levels of diacylglycerols in phospholipid membranes induce membrane fusion and stabilize inverted phases

31 March 2020

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Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: importance of interbilayer separation.

31 March 2020

1 reference

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Evolution of Lipidic Structures during Model Membrane Fusion and the Relation of This Process to Cell Membrane Fusion†

31 March 2020

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31 March 2020

Viral membrane fusion

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The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation

31 March 2020

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Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion

31 March 2020

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Membrane Fusion by Peptide Analogues of Influenza Virus Haemagglutinin

31 March 2020

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Membrane permeability changes at early stages of influenza hemagglutinin-mediated fusion

31 March 2020

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Coiled coils in both intracellular vesicle and viral membrane fusion

31 March 2020

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Genetic analysis of membrane differentiation in Paramecium. Freeze-fracture study of the trichocyst cycle in wild-type and mutant strains

31 March 2020

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Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae

31 March 2020

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Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway

31 March 2020

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Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway

31 March 2020

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Transport of vesicular stomatitis virus glycoprotein in a cell-free extract

31 March 2020

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Reconstitution of SEC gene product-dependent intercompartmental protein transport

31 March 2020

1 reference

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Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway

31 March 2020

1 reference

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Organelle assembly in yeast: characterization of yeast mutants defective in vacuolar biogenesis and protein sorting

31 March 2020

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A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast

31 March 2020

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The synaptic vesicle cycle

31 March 2020

1 reference

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VAMP-1: a synaptic vesicle-associated integral membrane protein

31 March 2020

1 reference

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Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain

31 March 2020

1 reference

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Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones

31 March 2020

1 reference

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Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin

31 March 2020

1 reference

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Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release

31 March 2020

1 reference

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SNARE complex oligomerization by synaphin/complexin is essential for synaptic vesicle exocytosis.

31 March 2020

1 reference

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Complexin/synaptotagmin interplay controls acrosomal exocytosis

31 March 2020

1 reference

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A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion

31 March 2020

1 reference

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SNAP receptors implicated in vesicle targeting and fusion

31 March 2020

1 reference

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Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs

31 March 2020

1 reference

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Mechanism of calcium-independent synaptotagmin binding to target SNAREs

31 March 2020

1 reference

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A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis

31 March 2020

1 reference

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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

31 March 2020

1 reference

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SNAREpins: minimal machinery for membrane fusion

31 March 2020

1 reference

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Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion.

31 March 2020

1 reference

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Selective activation of cognate SNAREpins by Sec1/Munc18 proteins

31 March 2020

1 reference

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Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport

31 March 2020

1 reference

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The evolution of the huntingtin-associated protein 40 (HAP40) in conjunction with huntingtin

31 March 2020

1 reference

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Phox domain interaction with PtdIns(3)P targets the Vam7 t-SNARE to vacuole membranes.

31 March 2020

1 reference

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SNAREs are concentrated in cholesterol-dependent clusters that define docking and fusion sites for exocytosis

31 March 2020

1 reference

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Vacuole fusion at a ring of vertex docking sites leaves membrane fragments within the organelle

31 March 2020

1 reference

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Trans-SNARE complex assembly and yeast vacuole membrane fusion.

31 March 2020

1 reference

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Homotypic vacuolar fusion mediated by t- and v-SNAREs

31 March 2020

1 reference

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SNAREs in opposing bilayers interact in a circular array to form conducting pores

31 March 2020

1 reference

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Snares and Munc18 in synaptic vesicle fusion

31 March 2020

1 reference

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Sec1p binds to SNARE complexes and concentrates at sites of secretion

31 March 2020

1 reference

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Sec1p directly stimulates SNARE-mediated membrane fusion in vitro

31 March 2020

1 reference

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How Tlg2p/syntaxin 16 'snares' Vps45

31 March 2020

1 reference

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Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif

31 March 2020

1 reference

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A conformational switch in syntaxin during exocytosis: role of munc18.

31 March 2020

1 reference

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Three-dimensional structure of the neuronal-Sec1-syntaxin 1a complex

31 March 2020

1 reference

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Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes

31 March 2020

1 reference

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A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast

31 March 2020

1 reference

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Interactions of Nucleotide Release Factor Dss4p with Sec4p in the Post-Golgi Secretory Pathway of Yeast

31 March 2020

1 reference

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Spatial regulation of exocytosis: lessons from yeast

31 March 2020

1 reference

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The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis

31 March 2020

1 reference

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TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion

31 March 2020

1 reference

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Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p

31 March 2020

1 reference

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New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion

31 March 2020

1 reference

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TRAPP stimulates guanine nucleotide exchange on Ypt1p

31 March 2020

1 reference

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The rab exchange factor Sec2p reversibly associates with the exocyst

31 March 2020

1 reference

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Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis

31 March 2020

1 reference

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Rabaptin-5 is a direct effector of the small GTPase Rab5 in endocytic membrane fusion

31 March 2020

1 reference

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A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function

31 March 2020

1 reference

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The Rab5 effector EEA1 is a core component of endosome docking

31 March 2020

1 reference

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Phosphatidylinositol-3-OH kinases are Rab5 effectors.

31 March 2020

1 reference

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Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes.

31 March 2020

1 reference

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EEA1 links PI(3)K function to Rab5 regulation of endosome fusion

31 March 2020

1 reference

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Mosaic organization of the endocytic pathway

31 March 2020

1 reference

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Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex

31 March 2020

1 reference

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An enzymatic cascade of Rab5 effectors regulates phosphoinositide turnover in the endocytic pathway

31 March 2020

1 reference

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Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13

31 March 2020

1 reference

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Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion

31 March 2020

1 reference

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Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles

31 March 2020

1 reference

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Reversible, cooperative reactions of yeast vacuole docking

31 March 2020

1 reference

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Use of resonance energy transfer to monitor membrane fusion

31 March 2020

1 reference

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Lipid mixing during membrane aggregation and fusion: why fusion assays disagree

31 March 2020

1 reference

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Novel inner monolayer fusion assays reveal differential monolayer mixing associated with cation-dependent membrane fusion

31 March 2020

1 reference

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Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

31 March 2020

1 reference

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Early endosomal SNAREs form a structurally conserved SNARE complex and fuse liposomes with multiple topologies

31 March 2020

1 reference

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Hemifusion in SNARE-mediated membrane fusion

31 March 2020

1 reference

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The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion

31 March 2020

1 reference

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Reconstitution of Ca2+-regulated membrane fusion by synaptotagmin and SNAREs.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

SNARE-mediated lipid mixing depends on the physical state of the vesicles

31 March 2020

1 reference

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Neuronal SNAREs do not trigger fusion between synthetic membranes but do promote PEG-mediated membrane fusion

31 March 2020

1 reference

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Excess vacuolar SNAREs drive lysis and Rab bypass fusion

31 March 2020

1 reference

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Sec18p and Vam7p remodel trans-SNARE complexes to permit a lipid-anchored R-SNARE to support yeast vacuole fusion

31 March 2020

1 reference

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Lipidic antagonists to SNARE-mediated fusion

31 March 2020

1 reference

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Phosphorylation of synaptic vesicle proteins: modulation of the alpha SNAP interaction with the core complex

31 March 2020

1 reference

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Phosphorylation of Munc-18/n-Sec1/rbSec1 by protein kinase C: its implication in regulating the interaction of Munc-18/n-Sec1/rbSec1 with syntaxin

31 March 2020

1 reference

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The vacuolar kinase Yck3 maintains organelle fragmentation by regulating the HOPS tethering complex

31 March 2020

1 reference

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Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins

31 March 2020

1 reference

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Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Vam2/Vps41p and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Conformation of the synaptobrevin transmembrane domain

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Diacylglycerol causes major structural transitions in phospholipid bilayer membranes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Mitochondrial fusion in yeast requires the transmembrane GTPase Fzo1p

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Structural basis of mitochondrial tethering by mitofusin complexes.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Mitochondrial fusion intermediates revealed in vitro

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Ugo1p links the Fzo1p and Mgm1p GTPases for mitochondrial fusion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Mitochondrial inner-membrane fusion and crista maintenance requires the dynamin-related GTPase Mgm1.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

The type I membrane protein EFF-1 is essential for developmental cell fusion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

AFF-1, a FOS-1-regulated fusogen, mediates fusion of the anchor cell in C. elegans

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

The C. elegans developmental fusogen EFF-1 mediates homotypic fusion in heterologous cells and in vivo

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

EFF-1 is sufficient to initiate and execute tissue-specific cell fusion in C. elegans

31 March 2020

1 reference

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Fusogenic activity of EFF-1 is regulated via dynamic localization in fusing somatic cells of C. elegans

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Identification and regulation of a gene required for cell fusion during mating of the yeast Saccharomyces cerevisiae

31 March 2020

1 reference

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Fus2 localizes near the site of cell fusion and is required for both cell fusion and nuclear alignment during zygote formation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Distinct morphological phenotypes of cell fusion mutants

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Prm1p, a pheromone-regulated multispanning membrane protein, facilitates plasma membrane fusion during yeast mating

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Prm1 prevents contact-dependent lysis of yeast mating pairs

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Rabs and their effectors: achieving specificity in membrane traffic

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

A role for giantin in docking COPI vesicles to Golgi membranes

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

SNAREs--engines for membrane fusion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNSMB.1451

Crystal structure of the vesicular transport protein Sec17: implications for SNAP function in SNARE complex disassembly

31 March 2020

1 reference

https://pubmed.ncbi.nlm.nih.gov/18618939

12 December 2020

Mutational analysis of SEC4 suggests a cyclical mechanism for the regulation of vesicular traffic

1 reference

https://pubmed.ncbi.nlm.nih.gov/18618939

12 December 2020

Purification of three related peripheral membrane proteins needed for vesicular transport

1 reference

https://pubmed.ncbi.nlm.nih.gov/18618939

12 December 2020

Genes for directing vacuolar morphogenesis in Saccharomyces cerevisiae. I. Isolation and characterization of two classes of vam mutants

1 reference

https://pubmed.ncbi.nlm.nih.gov/18618939

12 December 2020

The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae

1 reference

https://pubmed.ncbi.nlm.nih.gov/18618939

12 December 2020

Identifiers

DOI

10.1038/NSMB.1451

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18618939%20AND%20SRC:MED&resulttype=core&format=json

10 January 2020

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18618939%20AND%20SRC:MED&resulttype=core&format=json

10 January 2020

PubMed publication ID

18618939

1 reference