Do Structural Deviations between Toxins Adopting the Same Fold Reflect Functional Differences?-Reference-Cited by-同舟云学术

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Do Structural Deviations between Toxins Adopting the Same Fold Reflect Functional Differences?

Published:2000-06 Issue:24 Volume:275 Page:18302-18310
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Ricciardi Alejandro,le Du Marie-Hélène,Khayati Mounira,Dajas Federico,Boulain Jean-Claude,Ménez André,Ducancel Frédéric

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference58 articles.

1. Snake Toxins;Endo,1991

2. Three-dimensional structure of the "long" neurotoxin from cobra venom.

3. The refined crystal structure of alpha-cobratoxin from Naja naja siamensis at 2.4-A resolution.

4. Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: sequence-specific assignments, secondary structure, and dimer formation

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1. A consensus recombinant elapid long-chain α-neurotoxin and how protein folding matters for antibody recognition and neutralization of elapid venoms;Biochemical and Biophysical Research Communications;2024-11

2. Blocking of negative charged carboxyl groups converts Naja atra neurotoxin to cardiotoxin-like protein;International Journal of Biological Macromolecules;2020-12

3. Snake three-finger α-neurotoxins and nicotinic acetylcholine receptors: molecules, mechanisms and medicine;Biochemical Pharmacology;2020-11

4. Fulditoxin, representing a new class of dimeric snake toxins, defines novel pharmacology at nicotinic ACh receptors;British Journal of Pharmacology;2020-02-09

5. Short-chain consensus alpha-neurotoxin: a synthetic 60-mer peptide with generic traits and enhanced immunogenic properties;Amino Acids;2018-04-06

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