Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states.

Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states.

Item
http://www.wikidata.org/entity/Q42728419
What macromolecular crowding can do to a proteinStructural 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 secretionBacterial kinesin light chain (Bklc) links the Btub cytoskeleton to membranes.Calcium, acylation, and molecular confinement favor folding of Bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic formStructural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Single-molecule Force Spectroscopy Reveals the Calcium Dependence of the Alternative Conformations in the Native State of a βγ-Crystallin Protein.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.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Characterization of Post-Translational Modifications and Cytotoxic Properties of the Adenylate-Cyclase Hemolysin Produced by Various Bordetella pertussis and Bordetella parapertussis Isolates.Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region.Calcium-Binding Proteins with Disordered Structure and Their Role in Secretion, Storage, and Cellular Signaling.From bulk to plasmonic nanoparticle surfaces: the behavior of two potent therapeutic peptides, octreotide and pasireotideLarge size citrate-reduced gold colloids appear as optimal SERS substrates for cationic peptides
P2860

Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states.

Item
http://www.wikidata.org/entity/Q42728419
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Calcium-induced folding of int ...... es and oligomerization states.
@en
Calcium-induced folding of intrinsically disordered repeat-in-toxin
@nl
type
label
Calcium-induced folding of int ...... es and oligomerization states.
@en
Calcium-induced folding of intrinsically disordered repeat-in-toxin
@nl
prefLabel
Calcium-induced folding of int ...... es and oligomerization states.
@en
Calcium-induced folding of intrinsically disordered repeat-in-toxin
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932
P356
P1433
P1476
Calcium-induced folding of int ...... es and oligomerization states.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932