COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization.
about
Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregatesSerpin polymerization is prevented by a hydrogen bond network that is centered on his-334 and stabilized by glycerolC1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational diseaseCrystallographic and Cellular Characterisation of Two Mechanisms Stabilising the Native Fold of α1-Antitrypsin: Implications for Disease and Drug DesignFamilial dementia caused by polymerization of mutant neuroserpinThe role of strand 1 of the C beta-sheet in the structure and function of alpha(1)-antitrypsinPolymerization of plasminogen activator inhibitor-1.Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization.Presence of C1-inhibitor polymers in a subset of patients suffering from hereditary angioedemaAlpha1-antitrypsin deficiency. 4: Molecular pathophysiologyExhaustive mutation scanning by fluorescence-assisted mismatch analysis discloses new genotype-phenotype correlations in angiodemaSerpin alpha 1proteinase inhibitor probed by intrinsic tryptophan fluorescence spectroscopyalpha(1)-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1Polymers and inflammation: disease mechanisms of the serpinopathiesHepatic fibrosis and carcinogenesis in α1-antitrypsin deficiency: a prototype for chronic tissue damage in gain-of-function disorders.Unravelling the twists and turns of the serpinopathies.Twenty years of polymers: a personal perspective on alpha-1 antitrypsin deficiency.The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant.Genetics of Hereditary Angioedema Revisited.Heteropolymerization of S, I, and Z alpha1-antitrypsin and liver cirrhosis.The biostructural pathology of the serpins: critical function of sheet opening mechanism.Alpha-1-antitrypsin deficiency: biochemistry and clinical manifestations.Review: alpha 1-antitrypsin deficiency associated liver disease.Genetics and respiratory disease. 2. Alpha 1-antitrypsin deficiency, cirrhosis and emphysema.Structural factors affecting the choice between latency transition and polymerization in inhibitory serpins.6-mer peptide selectively anneals to a pathogenic serpin conformation and blocks polymerization. Implications for the prevention of Z alpha(1)-antitrypsin-related cirrhosis.Intermittent C1-Inhibitor Deficiency Associated with Recessive Inheritance: Functional and Structural Insight.alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization.Identification of a 4-mer Peptide Inhibitor that Effectively Blocks the Polymerization of Pathogenic Z α1-AntitrypsinA Kinetic Mechanism for the Polymerization of α1-Antitrypsin
P2860
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P2860
COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
COOH-terminal substitutions in ...... nd subsequent multimerization.
@en
type
label
COOH-terminal substitutions in ...... nd subsequent multimerization.
@en
prefLabel
COOH-terminal substitutions in ...... nd subsequent multimerization.
@en
P2093
P2860
P356
P1476
COOH-terminal substitutions in ...... nd subsequent multimerization.
@en
P2093
P2860
P304
P356
10.1074/JBC.270.6.2579
P407
P577
1995-02-01T00:00:00Z