Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin
about
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretionDisorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretionCharge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.Albumin, in the Presence of Calcium, Elicits a Massive Increase in Extracellular Bordetella Adenylate Cyclase Toxin.Calcium, acylation, and molecular confinement favor folding of Bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic formThe Translocation Domain of Botulinum Neurotoxin A Moderates the Propensity of the Catalytic Domain to Interact with Membranes at Acidic pHMolecular Modeling of the Catalytic Domain of CyaA Deepened the Knowledge of Its Functional Dynamics.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Rearranging and concatenating a native RTX domain to understand sequence modularity.Bordetella Adenylate Cyclase-Hemolysin Toxins.Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications.Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.Allosteric activation of Bordetella pertussis adenylyl cyclase by calmodulin: molecular dynamics and mutagenesis studiesCalcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Self-assembly of pH and calcium dual-responsive peptide-amphiphilic hydrogel.Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region.Bacterial Translocation Ratchets: Shared Physical Principles with Different Molecular Implementations: How bacterial secretion systems bias Brownian motion for efficient translocation of macromolecules.Probing the Ca(2+)-assisted π-π interaction during Ca(2+)-dependent protein folding.SEC-SAXS and HDX-MS: A powerful combination. The case of the calcium-binding domain of a bacterial toxin.The catalytic domains of Clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid.
P2860
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P2860
Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxin
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@ast
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@en
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@nl
type
label
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@ast
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@en
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@nl
prefLabel
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@ast
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@en
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@nl
P2093
P2860
P1433
P1476
Calcium-induced folding and st ...... d RTX domain of the CyaA toxin
@en
P2093
Ana Cristina Sotomayor Pérez
Anna Katarzyna Wozniak
Bruno Baron
Johanna C Karst
Patrick England
P2860
P304
P356
10.1016/J.BPJ.2010.10.016
P407
P577
2010-12-01T00:00:00Z