(Q27656103)

English

Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F

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title

Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F (English)

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main subject

Clostridium botulinum

object named as

Clostridium botulinum

1 reference

Rakhi Agarwal

1

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James J Schmidt

series ordinal

2

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Robert G Stafford

series ordinal

3

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Subramanyam Swaminathan

series ordinal

4

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publication date

July 2009

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published in

Nature Structural & Molecular Biology

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volume

16

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issue

7

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page(s)

789-94

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cites work

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SNAP-25 Substrate Peptide (Residues 180-183) Binds to but Bypasses Cleavage by Catalytically Active Clostridium botulinum Neurotoxin E

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Substrate Binding Mode and Its Implication on Drug Design for Botulinum Neurotoxin A

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21 April 2017

Catalytic features of the botulinum neurotoxin A light chain revealed by high resolution structure of an inhibitory peptide complex

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Structural predictions of the channel-forming region of botulinum neurotoxin heavy chain

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21 January 2018

Substrate recognition strategy for botulinum neurotoxin serotype A.

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21 January 2018

Botulinum neurotoxin serotype F: identification of substrate recognition requirements and development of inhibitors with low nanomolar affinity

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21 January 2018

Substrate recognition mechanism of VAMP/synaptobrevin-cleaving clostridial neurotoxins

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21 January 2018

Cloning, high level expression, purification, and crystallization of the full length Clostridium botulinum neurotoxin type E light chain

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An approach to multi-copy search in molecular replacement

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Multiple Pocket Recognition of SNAP25 by Botulinum Neurotoxin Serotype E

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Neurotoxins affecting neuroexocytosis

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31 March 2020

Cocrystal structure of synaptobrevin-II bound to botulinum neurotoxin type B at 2.0 A resolution

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Questions about the structure of the botulinum neurotoxin B light chain in complex with a target peptide

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31 March 2020

Structural analysis of botulinum neurotoxin serotype F light chain: implications on substrate binding and inhibitor design

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The interaction of synaptic vesicle-associated membrane protein/synaptobrevin with botulinum neurotoxins D and F

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Minimal essential domains specifying toxicity of the light chains of tetanus toxin and botulinum neurotoxin type A.

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retrieved

12 December 2020

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Identifiers

DOI

10.1038/NSMB.1626

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Dimensions Publication ID

1052263198

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PubMed publication ID

19543288

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(Q27656103)

Mode of VAMP substrate recognition and inhibition of Clostridium botulinum neurotoxin F

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