Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444----His) mutation.
about
Identification of a new P1 residue mutation (444Arg----Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasmaDysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition of an N-glycosylation siteClusters of intragenic Alu repeats predispose the human C1 inhibitor locus to deleterious rearrangementsType II hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor geneNonsense mutations affect C1 inhibitor messenger RNA levels in patients with type I hereditary angioneurotic edemaAn overview of the serpin superfamilyWhat do dysfunctional serpins tell us about molecular mobility and disease?Synthesis of C1 inhibitor in fibroblasts from patients with type I and type II hereditary angioneurotic edemaCrucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function.C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.Plasma levels of C1- inhibitor complexes and cleaved C1- inhibitor in patients with hereditary angioneurotic edema.A dysfunctional C1 inhibitor protein with a new reactive center mutation (Arg-444-->Leu).Identification of tissue-type plasminogen activator-specific plasminogen activator inhibitor-1 mutants. Evidence that second sites of interaction contribute to target specificity.HAE Pathophysiology and Underlying Mechanisms.Unique C1 inhibitor dysfunction in a kindred without angioedema. II. Identification of an Ala443-->Val substitution and functional analysis of the recombinant mutant protein.A hydrophobic patch surrounding Trp154 in human neuroserpin controls the helix F dynamics with implications in inhibition and aggregation.C1 inhibitor-C1s complexes are internalized and degraded by the low density lipoprotein receptor-related protein.Rapid and sensitive techniques for identification and analysis of 'reactive-centre' mutants of C1-inhibitor proteins contained in type II hereditary angio-oedema plasmas.Chymotrypsin inhibitory activity of normal C1-inhibitor and a P1 Arg to His mutant: evidence for the presence of overlapping reactive centers
P2860
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P2860
Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444----His) mutation.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@en
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@nl
type
label
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@en
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@nl
prefLabel
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@en
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@nl
P2093
P2860
P356
P1433
P1476
Dysfunctional C1-inhibitor(At) ...... tre' (Arg444----His) mutation.
@en
P2093
P A Pemberton
P J Lachmann
R A Harrison
R W Carrell
P2860
P304
P356
10.1042/BJ2530615
P407
P577
1988-07-01T00:00:00Z