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Serine proteases and cardiac function
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2005The serine proteases of the trypsin superfamily are versatile enzymes involved in a variety of biological processes. In the cardiovascular system, the importance of these enzymes in blood coagulation, platelet activation, fibrinolysis, and thrombosis has been well established.
Qingyu, Wu +2 more
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Serine proteases regulating synaptic plasticity
Anatomical Science International, 2004A number of molecules have been postulated to be involved in long-term potentiation, an experimental model for learning and short-term memory. Although the molecular mechanisms of the long-term potentiation have been considerably well understood, it is not yet known why and how real memory can last very long with outstanding stability.
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Small, noncovalent serine protease inhibitors
Medicinal Research Reviews, 1999Thrombin and factor Xa (fXa) are the only serine proteases for which small, potent, selective, noncovalent inhibitors have been developed, which are ultimately intended as drug development candidates (in this case as anticoagulants). Noncovalent inhibitors may be more selective and chemically and metabolically less reactive than covalent inhibitors. In
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Intracellular serine protease-4, a new intracellular serine protease activity from Bacillus subtilis
Archives of Microbiology, 1991A previously undiscovered intracellular serine protease activity, which we have called intracellular serine protease-4, was identified in extracts of stationary Bacillus subtilis cells, purified 260 fold from the cytoplasmic fraction, and characterized.
S M, Sheehan, R L, Switzer
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Biochemical and Biophysical Research Communications, 1977
Summary Intracellular serine protease was isolated in a pure state from sporulating Bacillus subtilis A-50. The enzyme has the molecular weight about 30.000 daltons and pI 4.3, is completely inhibited with phenylmethylsulfonyl fluoride and EDTA, and possesses a rather low activity against protein substrates, but high specific activity with ...
V M, Stepanov +7 more
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Summary Intracellular serine protease was isolated in a pure state from sporulating Bacillus subtilis A-50. The enzyme has the molecular weight about 30.000 daltons and pI 4.3, is completely inhibited with phenylmethylsulfonyl fluoride and EDTA, and possesses a rather low activity against protein substrates, but high specific activity with ...
V M, Stepanov +7 more
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An Overview of Serine Proteases
Current Protocols in Protein Science, 2001AbstractThis unit summarizes the families of serine proteases and their mechanism of catalysis. Methods for assays and determining substrate specificity are briefly described. The mode of action of commonly available inhibitors is also included.
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Serine Protease Mechanism and Specificity
ChemInform, 2002AbstractFor Abstract see ChemInform Abstract in Full Text.
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Subtilases: Subtilisin-Like Serine Proteases
1996Subtilases are members of the family of subtilisin-like serine proteases. Over 70 subtilases are presently known, more than 60 of which with their complete amino acid sequence. In this update, details of more than 20 new subtilases discovered recently are summarized, and their sequences included in a multiple sequence alignment table.
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Neutral serine proteases of neutrophils
Immunological Reviews, 2016SummaryNeutrophil serine proteases (NSPs) exercise tissue‐degrading and microbial‐killing effects. The spectrum of NSP‐mediated functions grows continuously, not least because of methodological progress. Sensitive and specific FRET substrates were developed to study the proteolytic activity of each NSP member. Advanced biochemical methods are beginning
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