Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
about
The 1.8-A crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognitionCalcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion.The proteolytic environment of chronic wounds.Similarity of binding sites of human matrix metalloproteinases.Effect of species differences on stromelysin-1 (MMP-3) inhibitor potency. An explanation of inhibitor selectivity using homology modeling and chimeric proteins.
P2860
Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data.
description
1998 nî lūn-bûn
@nan
1998 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Structure of malonic acid-base ...... ins apparently anomalous data.
@ast
Structure of malonic acid-base ...... ins apparently anomalous data.
@en
type
label
Structure of malonic acid-base ...... ins apparently anomalous data.
@ast
Structure of malonic acid-base ...... ins apparently anomalous data.
@en
prefLabel
Structure of malonic acid-base ...... ins apparently anomalous data.
@ast
Structure of malonic acid-base ...... ins apparently anomalous data.
@en
P2093
P2860
P356
P1433
P1476
Structure of malonic acid-base ...... ins apparently anomalous data.
@en
P2093
Brandstetter H
Von Roedern EG
P2860
P304
P356
10.1002/PRO.5560070605
P577
1998-06-01T00:00:00Z