Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites.
about
Type II hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor geneRecombinant human pigment epithelium-derived factor (PEDF): characterization of PEDF overexpressed and secreted by eukaryotic cellsA structure-derived snap-trap mechanism of a multispecific serpin from the dysbiotic human oral microbiome.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Serpin Inhibition Mechanism: A Delicate Balance between Native Metastable State and Polymerization.Bypassing the kinetic trap of serpin protein folding by loop extension.Structural comparisons of the native and reactive-centre-cleaved forms of alpha 1-antitrypsin by neutron- and X-ray-scattering in solution.Serpins in arthropod biology.Polymerization of human angiotensinogen: insights into its structural mechanism and functional significanceThe conversion of active to latent plasminogen activator inhibitor-1 is an energetically silent event.Loop variants of the serpin thyroxine-binding globulin: implications for hormone release upon limited proteolysis.Structural factors affecting the choice between latency transition and polymerization in inhibitory serpins.Kinetic evidence for a two-step mechanism for the binding of chymotrypsin to alpha 1-proteinase inhibitor.Specific interactions of serpins in their native forms attenuate their conformational transitions.Retarded protein folding of deficient human alpha 1-antitrypsin D256V and L41P variants.Functional unfolding of alpha1-antitrypsin probed by hydrogen-deuterium exchange coupled with mass spectrometry.Ovalbumin and angiotensinogen lack serpin S-R conformational change.Probing the local conformational change of alpha1-antitrypsin.
P2860
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P2860
Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites.
description
1988 nî lūn-bûn
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1988年の論文
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1988年学术文章
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1988年学术文章
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1988年学术文章
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1988年学术文章
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1988年学术文章
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1988年学术文章
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1988年學術文章
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1988年學術文章
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name
Plasma serine proteinase inhib ...... avage at their reactive sites.
@en
Plasma serine proteinase inhibitors
@nl
type
label
Plasma serine proteinase inhib ...... avage at their reactive sites.
@en
Plasma serine proteinase inhibitors
@nl
prefLabel
Plasma serine proteinase inhib ...... avage at their reactive sites.
@en
Plasma serine proteinase inhibitors
@nl
P2093
P1476
Plasma serine proteinase inhib ...... avage at their reactive sites.
@en
P2093
P304
16626-16630
P407
P577
1988-11-01T00:00:00Z