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Kininogenase

Known as: Kallikreins, KLK, Kallikreins [Chemical/Ingredient] 
Proteolytic enzymes from the serine endopeptidase family found in normal blood and urine. Specifically, Kallikreins are potent vasodilators and… 
National Institutes of Health

Related topics

Related topics

44 relations

Broader (3)

CoagulantsSerine EndopeptidasesSerine Proteases

Narrower (25)

DilminalKLK10 protein, humanKLK14 protein, humanKLK15 protein, human
Enzyme GeneHydrolysisIn BloodKallikrein.tissue type:ACnc:Pt:Plas:Qn

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2011
Highly Cited
2011
First-line therapy with coagulation factor concentrates combined with point-of-care coagulation testing is associated with decreased allogeneic blood transfusion in cardiovascular surgery: a…
INTRODUCTION Blood transfusion is associated with increased morbidity and mortality. We developed and implemented an algorithm… 
Highly Cited
2009
Highly Cited
2009
Kallikrein 5 induces atopic dermatitis–like lesions through PAR2-mediated thymic stromal lymphopoietin expression in Netherton syndrome
Netherton syndrome (NS) is a severe genetic skin disease with constant atopic manifestations that is caused by mutations in the… 
Review
2005
Review
2005
International Union of Pharmacology. XLV. Classification of the Kinin Receptor Family: from Molecular Mechanisms to Pathophysiological Consequences
Kinins are proinflammatory peptides that mediate numerous vascular and pain responses to tissue injury. Two pharmacologically… 
Review
1997
Review
1997
Contact system: a vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes.
THE KALLIKREIN-KININ system was first recognized as a plasma and tissue proteolytic system responsible for the liberation of the… 
Highly Cited
1997
Highly Cited
1997
Interactions of Mast Cell Tryptase with Thrombin Receptors and PAR-2*
Tryptase is a serine protease secreted by mast cells that is able to activate other cells. In the present studies we have tested… 
Highly Cited
1992
Highly Cited
1992
Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties.
Highly Cited
1990
Highly Cited
1990
Purification and NH2-terminal amino acid sequence of guinea pig tumor-secreted vascular permeability factor.
Rodent and human tumor cell lines secrete a potent vascular permeability factor (VPF) which causes a rapid and substantial… 
Highly Cited
1990
Highly Cited
1990
Matrix metalloproteinase 2 from human rheumatoid synovial fibroblasts. Purification and activation of the precursor and enzymic properties.
Human rheumatoid synovial cells in culture secrete at least three related metalloproteinases that digest extracellular matrix… 
Highly Cited
1985
Highly Cited
1985
A kallikrein-like serine protease in prostatic fluid cleaves the predominant seminal vesicle protein.
A 33-kD glycoprotein, known as the "prostate-specific antigen," was purified to homogeneity from human seminal plasma. The… 
Review
1982
Review
1982
Urinary enzymes, nephrotoxicity and renal disease.
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