(Q74769349)

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Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation

scientific article published on 01 September 2002

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13 November 2019

Spectroscopic analysis of low pH and lipid-induced structural changes in type A botulinum neurotoxin relevant to membrane channel formation and translocation (English)

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13 November 2019

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Fen-Ni Fu

1

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13 November 2019

David D Busath

2

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13 November 2019

Bal Ram Singh

3

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13 November 2019

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1 September 2002

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13 November 2019

Biophysical Chemistry

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13 November 2019

99

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13 November 2019

1

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13 November 2019

17-29

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13 November 2019

Critical aspects of bacterial protein toxins

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Identification of an ion channel-forming motif in the primary structure of tetanus and botulinum neurotoxins

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Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A.

1 reference

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Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes

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Ion-conducting channels produced by botulinum toxin in planar lipid membranes

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A 50-kDa fragment from the NH2-terminus of the heavy subunit of Clostridium botulinum type A neurotoxin forms channels in lipid vesicles

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Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charge, and transmembrane potential on the kinetics of channel formation

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The N-terminal half of the heavy chain of botulinum type A neurotoxin forms channels in planar phospholipid bilayers

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A protease-resistant novel hemagglutinin purified from type A Clostridium botulinum

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Low conductance gramicidin A channels are head-to-head dimers of beta 6.3-helices

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Calcein permeability of liposomes mediated by type A botulinum neurotoxin and its light and heavy chains

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Role of zinc in the structure and toxic activity of botulinum neurotoxin

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Calculation of protein conformation from circular dichroism

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Near-UV circular dichroism of band 3. Evidence for intradomain conformational changes and interdomain interactions

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Changes in the molecular topography of the light and heavy chains of type A botulinum neurotoxin following their separation

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Aromatic Contributions To Circular Dichroism Spectra Of Protein

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Tetanus toxin fragment forms channels in lipid vesicles at low pH

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Low pH-induced changes in Pseudomonas exotoxin and its domains: increased binding of Triton X-114.

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Structural studies on the zinc-endopeptidase light chain of tetanus neurotoxin

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Botulinum neurotoxin A selectively cleaves the synaptic protein SNAP-25

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7 January 2021

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Spectroscopic analysis of pH-induced changes in the molecular features of type A botulinum neurotoxin light chain

1 reference

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7 January 2021

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The light chain of botulinum neurotoxin forms channels in a lipid membrane.

1 reference

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7 January 2021

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Effect of pH on the interaction of botulinum neurotoxins A, B and E with liposomes

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Molecular structure of tetanus neurotoxin as revealed by Fourier transform infrared and circular dichroic spectroscopy

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A correlation between differential structural features and the degree of endopeptidase activity of type A botulinum neurotoxin in aqueous solution

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Crystal structure of botulinum neurotoxin type A and implications for toxicity

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Identifiers

10.1016/S0301-4622(02)00135-7

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12223236%20AND%20SRC:MED&resulttype=core&format=json

13 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12223236%20AND%20SRC:MED&resulttype=core&format=json

13 November 2019

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