Identification of Glu173 as the critical amino acid residue for the ADP-ribosyltransferase activity of Clostridium botulinum C3 exoenzyme.
about
Structural basis for the NAD-hydrolysis mechanism and the ARTT-loop plasticity of C3 exoenzymesActivation of the osmo-sensitive chloride conductance involves P21rho and is accompanied by a transient reorganization of the F-actin cytoskeleton.Evidence that Arg-295, Glu-378, and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin.Structure-function discrepancy in Clostridium botulinum C3 toxin for its rational prioritization as a subunit vaccine.
P2860
Identification of Glu173 as the critical amino acid residue for the ADP-ribosyltransferase activity of Clostridium botulinum C3 exoenzyme.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@en
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@nl
type
label
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@en
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@nl
prefLabel
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@en
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@nl
P2093
P2860
P1433
P1476
Identification of Glu173 as th ...... ridium botulinum C3 exoenzyme.
@en
P2093
P2860
P304
P356
10.1016/0014-5793(95)00851-Y
P407
P577
1995-09-01T00:00:00Z