Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
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Identification of a new P1 residue mutation (444Arg----Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasmaStructural and circular-dichroism studies on the interaction between human C1-esterase inhibitor and C1sAlpha-2-macroglobulin functions as an inhibitor of fibrinolytic, clotting, and neutrophilic proteinases in sepsis: studies using a baboon modelRecombinant human C1 esterase inhibitor in the management of hereditary angioedemaCombined treatment with C1 esterase inhibitor and antithrombin III improves survival in severe acute experimental pancreatitisN-linked glycosylation at Asn3 and the positively charged residues within the amino-terminal domain of the c1 inhibitor are required for interaction of the C1 Inhibitor with Salmonella enterica serovar typhimurium lipopolysaccharide and lipid A.Recombinant alpha 1-antitrypsin Pittsburgh (Met 358----Arg) is a potent inhibitor of plasma kallikrein and activated factor XII fragmentPlatelet C1- inhibitor. A secreted alpha-granule proteinDemonstration of modified inactive first component of complement (C1) inhibitor in the plasmas of C1 inhibitor-deficient patientsSurface-mediated defense reactions. The plasma contact activation systemEcallantide for the treatment of hereditary angiodema in adults.Inactivation of factor XII active fragment in normal plasma. Predominant role of C-1-inhibitor.Cinryze as the first approved C1 inhibitor in the USA for the treatment of hereditary angioedema: approval, efficacy and safety.Activation of the contact system in lethal hypotensive bacteremia in a baboon model.The glomerular polyanion (GPA) of the rat kidney. III. Further characterization of a vaso-active serum factor which reduces GPAProteolytic Systems in Milk: Perspectives on the Evolutionary Function within the Mammary Gland and the Infant.The therapeutic potential of a kallikrein inhibitor for treating hereditary angioedema.New treatments addressing the pathophysiology of hereditary angioedemaHuman plasma kallikrein-kinin system: physiological and biochemical parametersThe use of plasma-derived C1 inhibitor in the treatment of hereditary angioedema.Human plasma kallikrein and C1 inhibitor form a complex possessing an epitope that is not detectable on the parent molecules: demonstration using a monoclonal antibody.The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant.Mapping of the discontinuous kininogen binding site of prekallikrein. A distal binding segment is located in the heavy chain domain A4.C1-inhibitor and its genetic alterations in hereditary angioneurotic edema.Inactivation of kallikrein in human plasma.Endotoxin-induced pulmonary dysfunction is prevented by C1-esterase inhibitor.Proteolytic inactivation of plasma C1- inhibitor in sepsis.Polyphosphate is a novel cofactor for regulation of complement by a serpin, C1 inhibitor.Biochemical characterization of a novel high-affinity and specific plasma kallikrein inhibitor.Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157:H7.Rapid and sensitive techniques for identification and analysis of 'reactive-centre' mutants of C1-inhibitor proteins contained in type II hereditary angio-oedema plasmas.Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444----His) mutation.A novel human complement-related protein, C1r-like protease (C1r-LP), specifically cleaves pro-C1s.Correlation among complement activation, protease inhibitors, and clinical course in acute pancreatitis in man.Analysis of Milk from Mothers Who Delivered Prematurely Reveals Few Changes in Proteases and Protease Inhibitors across Gestational Age at Birth and Infant Postnatal Age.Plasma Prekallikrein: Its Role in Hereditary Angioedema and Health and Disease.C1 inhibitor function using contact-phase proteases as target: evaluation of an innovative assay.Well-Known and Less Well-Known Functions of Alpha-1 Antitrypsin. Its Role in Chronic Obstructive Pulmonary Disease and Other Disease Developments.Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore).Peptidoglycan induces disseminated intravascular coagulation in baboons through activation of both coagulation pathways
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Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on February 1982
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@en
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@nl
type
label
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@en
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@nl
prefLabel
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@en
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@nl
P2093
P2860
P356
P1476
Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma.
@en
P2093
P2860
P304
P356
10.1172/JCI110470
P407
P577
1982-02-01T00:00:00Z