Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis.
about
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloningStructure of the integral membrane protein CAAX protease Ste24p.Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localizationComparison of the Internal Dynamics of Metalloproteases Provides New Insights on Their Function and Evolution.Angiotensin I-converting enzyme transition state stabilization by HIS1089: evidence for a catalytic mechanism distinct from other gluzincin metalloproteinases.Structure, function, and regulation of leukotriene A4 hydrolase.Two thimet oligopeptidase-like Pz peptidases produced by a collagen-degrading thermophile, Geobacillus collagenovorans MO-1.Metal-coordinating substrate analogs as inhibitors of metalloenzymesThe catalytic mechanism of angiotensin converting enzyme.Energetics of enzyme catalysis.Product inhibition in native-state proteolysis.Purification and characterization of acidolysin, an acidic metalloprotease produced by Clostridium acetobutylicum ATCC 824Leukotriene A4 hydrolase/aminopeptidase, the gatekeeper of chemotactic leukotriene B4 biosynthesis.Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.Carboxypeptidase A mechanisms.Matrix metalloproteinases as potential targets in the venous dilation associated with varicose veins.Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation of glutamic acid-296.Evidence for the general base mechanism in carboxypeptidase A-catalyzed reactions: partitioning studies on nucleophiles and H2(18)O kinetic isotope effects.The structural and functional roles of metal ions in thermolysin.Alteration of specific activity and stability of thermostable neutral protease by site-directed mutagenesis.ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity.Structures of adamalysin II with peptidic inhibitors. Implications for the design of tumor necrosis factor alpha convertase inhibitors.The effect of changing the hydrophobic S1' subsite of thermolysin-like proteases on substrate specificity.Substrate specificity in the highly heterogeneous M4 peptidase family is determined by a small subset of amino acids
P2860
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P2860
Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis.
description
1977 nî lūn-bûn
@nan
1977 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1977 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1977年の論文
@ja
1977年論文
@yue
1977年論文
@zh-hant
1977年論文
@zh-hk
1977年論文
@zh-mo
1977年論文
@zh-tw
1977年论文
@wuu
name
Crystallographic study of the ...... or the mechanism of catalysis.
@ast
Crystallographic study of the ...... or the mechanism of catalysis.
@en
Crystallographic study of the ...... or the mechanism of catalysis.
@nl
type
label
Crystallographic study of the ...... or the mechanism of catalysis.
@ast
Crystallographic study of the ...... or the mechanism of catalysis.
@en
Crystallographic study of the ...... or the mechanism of catalysis.
@nl
prefLabel
Crystallographic study of the ...... or the mechanism of catalysis.
@ast
Crystallographic study of the ...... or the mechanism of catalysis.
@en
Crystallographic study of the ...... or the mechanism of catalysis.
@nl
P356
P1433
P1476
Crystallographic study of the ...... or the mechanism of catalysis.
@en
P2093
Matthews BW
P304
P356
10.1021/BI00630A030
P407
P577
1977-05-01T00:00:00Z