The riddle of the Sec1/Munc-18 proteins – new twists added to their interactions with SNAREs (Q57978966)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12633987%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

title

The riddle of the Sec1/Munc-18 proteins - new twists added to their interactions with SNAREs (English)

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1 November 2019

2

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1 November 2019

author name string

Dieter Gallwitz

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12633987%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

publication date

1 March 2003

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12633987%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

number of pages

4

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Trends in Biochemical Sciences

inferred from page(s)

published in

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1 November 2019

volume

28

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1 November 2019

issue

3

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1 November 2019

page(s)

113-116

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

1 November 2019

cites work

1 reference

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7 January 2021

Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs

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7 January 2021

Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy

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7 January 2021

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

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7 January 2021

SNARE-mediated membrane fusion

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7 January 2021

Snares and Munc18 in synaptic vesicle fusion

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A family of proteins involved in intracellular transport

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7 January 2021

The Sec1 family: a novel family of proteins involved in synaptic transmission and general secretion.

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7 January 2021

Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin

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7 January 2021

Specificity and regulation of a synaptic vesicle docking complex

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A rat brain Sec1 homologue related to Rop and UNC18 interacts with syntaxin

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

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ROP, the Drosophila Sec1 homolog, interacts with syntaxin and regulates neurotransmitter release in a dosage-dependent manner.

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7 January 2021

An open form of syntaxin bypasses the requirement for UNC-13 in vesicle priming

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7 January 2021

Munc18-1 promotes large dense-core vesicle docking

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7 January 2021

Sec1p binds to SNARE complexes and concentrates at sites of secretion

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7 January 2021

Vam3p structure reveals conserved and divergent properties of syntaxins

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7 January 2021

How Tlg2p/syntaxin 16 'snares' Vps45

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7 January 2021

The Sec1p homologue Vps45p binds to the syntaxin Tlg2p

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7 January 2021

A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae

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7 January 2021

High-affinity binding of the yeast cis-Golgi t-SNARE, Sed5p, to wild-type and mutant Sly1p, a modulator of transport vesicle docking.

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7 January 2021

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

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7 January 2021

Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p

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7 January 2021

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

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7 January 2021

Crystallization and preliminary X-ray analysis of squid neuronal Sec1

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7 January 2021

Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily

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7 January 2021

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

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7 January 2021

A Ypt/Rab effector complex containing the Sec1 homolog Vps33p is required for homotypic vacuole fusion

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7 January 2021

Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion

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7 January 2021

10.1016/S0968-0004(03)00028-8

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12633987%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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