Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.
about
Functional Contributions of Positive Charges in the Pore-Lining Helix 3 of the Bordetella pertussis CyaA-Hemolysin to Hemolytic Activity and Ion-Channel Opening.The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin.Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes.Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes.Phosphoproteomics of cAMP signaling of Bordetella adenylate cyclase toxin in mouse dendritic cells.Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region.Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins.Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity; Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain.
P2860
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P2860
Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.
description
2016 nî lūn-bûn
@nan
2016年の論文
@ja
2016年論文
@yue
2016年論文
@zh-hant
2016年論文
@zh-hk
2016年論文
@zh-mo
2016年論文
@zh-tw
2016年论文
@wuu
2016年论文
@zh
2016年论文
@zh-cn
name
Negatively charged residues of ...... ty of adenylate cyclase toxin.
@en
type
label
Negatively charged residues of ...... ty of adenylate cyclase toxin.
@en
prefLabel
Negatively charged residues of ...... ty of adenylate cyclase toxin.
@en
P2093
P2860
P50
P356
P1433
P1476
Negatively charged residues of ...... ty of adenylate cyclase toxin.
@en
P2093
Irena Linhartova
Jiri Masin
Ladislav Bumba
Peter Sebo
Radovan Fiser
P2860
P2888
P356
10.1038/SREP29137
P407
P577
2016-09-01T00:00:00Z