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NSF N-terminal domain crystal structure: models of NSF function
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scholarly article
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title
NSF N-terminal domain crystal structure: models of NSF function
(English)
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main subject
crystal structure
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author
Reinhard Jahn
object named as
R Jahn
series ordinal
2
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author name string
R C Yu
series ordinal
1
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A T Brunger
series ordinal
3
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publication date
July 1999
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published in
Molecular Cell
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volume
4
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page(s)
97-107
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issue
1
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cites work
Methods used in the structure determination of bovine mitochondrial F1 ATPase
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Domains of alpha-SNAP required for the stimulation of exocytosis and for N-ethylmalemide-sensitive fusion protein (NSF) binding and activation
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Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis
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Direct observation of protein solvation and discrete disorder with experimental crystallographic phases
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A six-stranded double-psi beta barrel is shared by several protein superfamilies.
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A 200-amino acid ATPase module in search of a basic function
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Vesicle fusion from yeast to man
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A revised model for the oligomeric state of the N-ethylmaleimide-sensitive fusion protein, NSF.
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Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
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SNAREs and NSF in targeted membrane fusion
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Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly
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Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro.
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Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes.
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Protein structure comparison by alignment of distance matrices
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Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures.
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Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein
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Each Domain of theN-Ethylmaleimide-sensitive Fusion Protein Contributes to Its Transport Activity
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Identifiers
DOI
10.1016/S1097-2765(00)80191-4
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2937555
OpenCitations bibliographic resource ID
2937555
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2937555
PubMed ID
10445031
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
2937555
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