Structural Basis of Neutralization of the Major Toxic Component from the Scorpion Centruroides noxius Hoffmann by a Human-derived Single-chain Antibody Fragment (Q27667506)

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Language	Label	Description	Also known as
English	Structural Basis of Neutralization of the Major Toxic Component from the Scorpion Centruroides noxius Hoffmann by a Human-derived Single-chain Antibody Fragment	scientific article

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scholarly article

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Structural Basis of Neutralization of the Major Toxic Component from the Scorpion Centruroides noxius Hoffmann by a Human-derived Single-chain Antibody Fragment (English)

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based on heuristic

inferred from title

Centruroides noxius

object named as

Centruroides noxius

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based on heuristic

inferred from title

Enrique Rudiño-Piñera

3

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Lourival Possani Postay

5

object named as

Lourival D Possani

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Baltazar Becerril

4

object named as

Baltazar Becerril

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Lidia Riaño-Umbarila

2

object named as

Lidia Riaño-Umbarila

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author name string

Juan Carlos Canul-Tec

1

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Alfredo Torres-Larios

6

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language of work or name

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publication date

10 June 2011

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Journal of Biological Chemistry

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286

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23

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20892-900

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describes a project that uses

1 reference

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Solution structure of toxin 2 from centruroides noxius Hoffmann, a beta-scorpion neurotoxin acting on sodium channels

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20 March 2017

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Scorpion toxins specific for Na+-channels

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29 September 2017

Heterologous expressed toxic and non-toxic peptide variants of toxin CssII are capable to produce neutralizing antibodies against the venom of the scorpion Centruroides suffusus suffusus.

1 reference

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Four disulfide-bridged scorpion beta neurotoxin CssII: heterologous expression and proper folding in vitro

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Structural basis of neutralization by a human anti-severe acute respiratory syndrome spike protein antibody, 80R.

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Resurgent current and voltage sensor trapping enhanced activation by a beta-scorpion toxin solely in Nav1.6 channel. Significance in mice Purkinje neurons.

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29 September 2017

Structure and function of the voltage sensor of sodium channels probed by a beta-scorpion toxin.

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29 September 2017

Subtype specificity of scorpion beta-toxin Tz1 interaction with voltage-gated sodium channels is determined by the pore loop of domain 3.

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Overview of scorpion toxins specific for Na+ channels and related peptides: biodiversity, structure-function relationships and evolution

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Anchor residues in protein-protein interactions

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Voltage sensor-trapping: enhanced activation of sodium channels by beta-scorpion toxin bound to the S3-S4 loop in domain II.

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Two types of scorpion neurotoxins characterized by their binding to two separate receptor sites on rat brain synaptosomes

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29 September 2017

Two types of scorpion toxin receptor sites, one related to the activation, the other to the inactivation of the action potential sodium channel

1 reference

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29 September 2017

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29 September 2017

3dSS: 3D structural superposition

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2 June 2018

Amino acid sequence and immunological characterization with monoclonal antibodies of two toxins from the venom of the scorpion Centruroides noxius Hoffmann

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2 June 2018

Functional Anatomy of Scorpion Toxins Affecting Sodium Channels

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21 January 2018

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21 January 2018

Common features in the functional surface of scorpion beta-toxins and elements that confer specificity for insect and mammalian voltage-gated sodium channels.

1 reference

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21 January 2018

Design of a specific activator for skeletal muscle sodium channels uncovers channel architecture.

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Small exterior hydrophobic cluster contributes to conformational stability and steroid binding in ketosteroid isomerase from Pseudomonas putida biotype B.

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An 'Old World' scorpion beta-toxin that recognizes both insect and mammalian sodium channels

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21 January 2018

Protein stabilization by hydrophobic interactions at the surface

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based on heuristic

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ProtorP: a protein-protein interaction analysis server

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M111.238410

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PubMed publication ID

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