Results 1 to 10 of about 50 (50)
Non‐peptide inhibitors of HCV serine proteinase [PDF]
FEBS Letters, 1998 We screened a chemical library of 2000 compounds for inhibitors of hepatitis C virus (HCV) serine proteinase using an in vitro screening method measuring the hydrolysis of the peptide substrate. Three compounds were found to be the most potent inhibitors (IC50<10−5 M).
Yasumasa Komoda +6 more
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The synthesis of peptidylfluoromethanes and their properties as inhibitors of serine proteinases and cysteine proteinases [PDF]
Biochemical Journal, 1986 A synthesis of peptidylfluoromethanes is described that utilizes the conversion of phthaloyl amino acids into their fluoromethane derivatives. These can be deblocked and elongated. The inactivation of chymotrypsin by Cbz-Phe-CH2F (benzyloxycarbonylphenylalanylfluoromethane) was found to be considerably slower than that of the analogous chloromethane ...
Brian Walker +3 more
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Protein inhibitors of serine proteinases.
Acta Biochimica Polonica, 1999 Serine proteinases and their natural protein inhibitors belong to the most intensively studied models of protein-protein recognition. Protein inhibitors do not form a single group but can be divided into about 20 different families. Global structures of proteins representing different inhibitor families are completely different and comprise alpha ...
Daniel Krowarsch +2 more
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Serine proteinases and their inhibitors in Phycomyces blakesleeanus.
Journal of Biological Chemistry, 1979 Three serine proteinases of Phycomyces blakesleeanus were isolated and characterized. The molecular weights were determined to be 18,000, 22,000, and 60,000. The proteinases were solubilized by detergent or salt treatment. Two soluble proteins that specifically inhibit these proteinases were also isolated and characterized. Both these proteins formed 1:
E.P. Fischer, K.S. Thomson
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Squash inhibitor family of serine proteinases.
Acta Biochimica Polonica, 1996 Squash inhibitors of serine proteinases form an uniform family of small proteins. They are built of 27-33 amino-acid residues and cross-linked with three disulfide bridges. The reactive site peptide bond (P1-P1') is between residue 5 (Lys, Arg or Leu) and 6 (always Ile). High resolution X-ray structures are available for two squash inhibitors complexed
Daniel Krowarsch, Jacek Otlewski
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Identification and purification of a novel serine proteinase inhibitor
Journal of Biological Chemistry, 1993 We report the identification, purification, and partial amino acid sequence of a novel serine proteinase inhibitor which is present in extracts from human placentas and in the cytosolic fraction of the leukemic cell line K562. Extracts from these tissues exhibited time-dependent inhibition of the serine proteinase thrombin.
Tim Tetaz +2 more
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Analysis of serine proteinase–inhibitor interaction by alanine shaving [PDF]
Protein Science, 2002 AbstractWe analyzed the energetic importance of residues surrounding the hot spot (the P1 position) of bovine pancreatic trypsin inhibitor (BPTI) in interaction with two proteinases, trypsin and chymotrypsin, by a procedure called molecular shaving.
Michal Dadlez +4 more
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The effects of serine proteinase inhibitors on bone resorption in vitro [PDF]
Journal of Endocrinology, 2003 The aims of this study were to identify the role and sites of action of serine proteinases (SPs) in bone resorption, a process which involves a cascade of events, the central step of which is the removal of bone matrix by osteoclasts (OCs). This resorbing activity, however, is also determined by recruitment of new OCs to future resorption sites and ...
Tumber, A +5 more
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Serine proteinase inhibitors from insect hemolymph.
Acta Biochimica Polonica, 1996 Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a relatively few species.
Antoni Polanowski, Tadeusz Wilusz
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Dietary regulation of serine proteinases that are resistant to serine proteinase inhibitors
Journal of Insect Physiology, 1997 Ingestion of Kunitz soybean trypsin inhibitor (STI) by larval Helicoverpa zea, Agrotis ipsilon, and Trichoplusia ni extended the retention time of food in the digestive tract and increased the level of activity of proteolytic enzymes that were not susceptible to inhibition by STI.
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