Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition.
about
An overview of the serpin superfamilyThe role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsinThe molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment.Determining serpin conformational distributions with single molecule fluorescenceThe human serpin proteinase inhibitor-9 self-associates at physiological temperatures.Kinetic intermediates en route to the final serpin-protease complex: studies of complexes of α1-protease inhibitor with trypsinInhibitory serpins. New insights into their folding, polymerization, regulation and clearance.Short-lived protease serpin complexes: partial disruption of the rat trypsin active site.Revisiting antithrombotic therapeutics; sculptin, a novel specific, competitive, reversible, scissile and tight binding inhibitor of thrombin.Conformational change in elastase following complexation with alpha1-proteinase inhibitor: a CD investigation.Comparative trajectories of active and S195A inactive trypsin upon binding to serpins.Mapping of the epitope of a monoclonal antibody protecting plasminogen activator inhibitor-1 against inactivating agents.Distortion of the catalytic domain of tissue-type plasminogen activator by plasminogen activator inhibitor-1 coincides with the formation of stable serpin-proteinase complexes.The loss of tryptophan 194 in antichymotrypsin lowers the kinetic barrier to misfolding
P2860
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P2860
Intrinsic fluorescence changes and rapid kinetics of proteinase deformation during serpin inhibition.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@en
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@nl
type
label
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@en
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@nl
prefLabel
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@en
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@nl
P2860
P1433
P1476
Intrinsic fluorescence changes ...... tion during serpin inhibition.
@en
P2093
P2860
P356
10.1016/S0014-5793(01)02305-5
P407
P577
2001-04-01T00:00:00Z