(Q28141448)

1

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A P Joglekar

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A L Williams

3

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J C Hay

Journal of Biological Chemistry

4

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language of work or name

English

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publication date

15 December 2000

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published in

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volume

275

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page(s)

39631-9

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issue

50

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cites work

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SNAREs and NSF in targeted membrane fusion

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

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The synaptic SNARE complex is a parallel four-stranded helical bundle

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

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Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain

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

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Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion.

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Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport

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A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles

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Protein interactions regulating vesicle transport between the endoplasmic reticulum and Golgi apparatus in mammalian cells

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Localization, dynamics, and protein interactions reveal distinct roles for ER and Golgi SNAREs

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Role of vesicle-associated syntaxin 5 in the assembly of pre-Golgi intermediates

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Asymmetric requirements for a Rab GTPase and SNARE proteins in fusion of COPII vesicles with acceptor membranes

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Characteristics of endoplasmic reticulum-derived transport vesicles

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Bos1p, an integral membrane protein of the endoplasmic reticulum to Golgi transport vesicles, is required for their fusion competence

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Reconstitution of retrograde transport from the Golgi to the ER in vitro

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Bet1p activates the v-SNARE Bos1p

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Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase

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Mammalian vesicle trafficking proteins of the endoplasmic reticulum and Golgi apparatus

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The syntaxin family of vesicular transport receptors

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An isoform of the Golgi t-SNARE, syntaxin 5, with an endoplasmic reticulum retrieval signal

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Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins

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Specificity and regulation of a synaptic vesicle docking complex

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Protein-protein interactions contributing to the specificity of intracellular vesicular trafficking

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Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p.

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Structural Changes Are Associated with SolubleN-Ethylmaleimide-sensitive Fusion Protein Attachment Protein Receptor Complex Formation

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

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nSec1 binds a closed conformation of syntaxin1A.

21 January 2018

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Sec1p binds to SNARE complexes and concentrates at sites of secretion

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SNARE complex formation is triggered by Ca2+ and drives membrane fusion

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Morphological and functional association of Sec22b/ERS-24 with the pre-Golgi intermediate compartment

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Assembly of the ER to Golgi SNARE complex requires Uso1p

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SNAREpins: minimal machinery for membrane fusion

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