Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity
about
cDNA cloning and sequence analysis of human pancreatic procarboxypeptidase A1The three-dimensional structure of human procarboxypeptidase A2. Deciphering the basis of the inhibition, activation and intrinsic activity of the zymogenStructure of human procathepsin L reveals the molecular basis of inhibition by the prosegmentNMR solution structure of the activation domain of human procarboxypeptidase A2Structural basis of profactor D activation: from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor DX-ray structure of nucleoside diphosphate kinaseThe NMR structure of the activation domain isolated from porcine procarboxypeptidase BFlexibility of the Thrombin-activatable Fibrinolysis Inhibitor Pro-domain Enables Productive Binding of Protein SubstratesThe three-dimensional structure of the native ternary complex of bovine pancreatic procarboxypeptidase A with proproteinase E and chymotrypsinogen CCarboxypeptidase O is a glycosylphosphatidylinositol-anchored intestinal peptidase with acidic amino acid specificityPurification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus.Structural basis of the resistance of an insect carboxypeptidase to plant protease inhibitorsTwo conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF.Molecular dynamics simulation of highly charged proteins: comparison of the particle-particle particle-mesh and reaction field methods for the calculation of electrostatic interactions.Sensitive luciferin derived probes for selective carboxypeptidase activity.The activation pathway of procarboxypeptidase B from porcine pancreas: participation of the active enzyme in the proteolytic processing.The crystal structure of thrombin-activable fibrinolysis inhibitor (TAFI) provides the structural basis for its intrinsic activity and the short half-life of TAFIa.Crystal structure and mechanism of human carboxypeptidase O: Insights into its specific activity for acidic residues.
P2860
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P2860
Three-dimensional structure of porcine procarboxypeptidase B: a structural basis of its inactivity
description
1991 nî lūn-bûn
@nan
1991 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Three-dimensional structure of ...... ctural basis of its inactivity
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Three-dimensional structure of ...... ctural basis of its inactivity
@en
Three-dimensional structure of ...... ctural basis of its inactivity
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type
label
Three-dimensional structure of ...... ctural basis of its inactivity
@ast
Three-dimensional structure of ...... ctural basis of its inactivity
@en
Three-dimensional structure of ...... ctural basis of its inactivity
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prefLabel
Three-dimensional structure of ...... ctural basis of its inactivity
@ast
Three-dimensional structure of ...... ctural basis of its inactivity
@en
Three-dimensional structure of ...... ctural basis of its inactivity
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P2093
P2860
P1433
P1476
Three-dimensional structure of ...... ctural basis of its inactivity
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P2093
P2860
P356
10.1002/J.1460-2075.1991.TB07914.X
P407
P577
1991-01-01T00:00:00Z