Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly. (Q30518000)

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English	Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly.	scientific article

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20 January 2020

Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly (English)

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20 January 2020

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20 January 2020

Michael G Fried

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20 January 2020

Bridget Carragher

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20 January 2020

Sidney Whiteheart

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20 January 2020

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Chunxia Zhao

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20 January 2020

Elizabeth M Wilson-Kubalek

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5 January 2012

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20 January 2020

Journal of Structural Biology

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20 January 2020

177

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20 January 2020

335-343

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20 January 2020

Requirements for the catalytic cycle of the N-ethylmaleimide-Sensitive Factor (NSF).

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A clustering approach to multireference alignment of single-particle projections in electron microscopy

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Dissecting the N-ethylmaleimide-sensitive factor: required elements of the N and D1 domains

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Improved structures of full-length p97, an AAA ATPase: implications for mechanisms of nucleotide-dependent conformational change

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20 June 2018

NSF and p97/VCP: similar at first, different at last

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Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains

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Electron cryomicroscopy structure of N-ethyl maleimide sensitive factor at 11 A resolution

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Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model

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Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle

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Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein

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NSF N-terminal domain crystal structure: models of NSF function

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Arrangement of subunits in 20 S particles consisting of NSF, SNAPs, and SNARE complexes.

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Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein

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Stimulation of NSF ATPase activity by alpha-SNAP is required for SNARE complex disassembly and exocytosis

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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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Domain structure of an N-ethylmaleimide-sensitive fusion protein involved in vesicular transport.

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Each Domain of theN-Ethylmaleimide-sensitive Fusion Protein Contributes to Its Transport Activity

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

N-Ethylmaleimide-sensitive Fusion Protein Contains High and Low Affinity ATP-binding Sites That Are Functionally Distinct

1 reference

https://pubmed.ncbi.nlm.nih.gov/22245547

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Defining the SNARE complex binding surface of alpha-SNAP: implications for SNARE complex disassembly

1 reference

https://pubmed.ncbi.nlm.nih.gov/22245547

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1016/J.JSB.2011.12.018

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20 January 2020

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20 January 2020

1 reference

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20 January 2020

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