Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins.
about
Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant.Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin.Characterization of a human alpha1-antitrypsin variant that is as stable as ovalbumin.
P2860
Proteolytically cleaved mutant antithrombin-Hamilton has high stability to denaturation characteristic of wild type inhibitor serpins.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh-hant
name
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@en
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@nl
type
label
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@en
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@nl
prefLabel
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@en
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@nl
P2860
P1433
P1476
Proteolytically cleaved mutant ...... f wild type inhibitor serpins.
@en
P2093
Blajchman MA
P2860
P356
10.1016/0014-5793(94)00568-0
P407
P577
1994-07-01T00:00:00Z