Results 131 to 140 of about 149 (148)
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Serine Proteinase Inhibitors in the Skin: Role in Homeostasis and Disease
Current Protein & Peptide Science, 2005Serine proteinases fulfill and facilitate a broad spectrum of biological processes. They are held in check by different specific inhibitors. This delicate balance can be disturbed by genetic defects or exogenous influences and has been shown as the underlying or promoting cause for a large number of different diseases.
Hans-Jürgen Mägert +2 more
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Peptidic Inhibitors of Serine Proteinases of Plant Origin
2013Serine proteinases play important roles in many physiological processes and in consequence, when unbalanced, are responsible for numerous severe diseases. The most predominant mechanism of their control is the ubiquitous presence of their inhibitors.
Anna Łęgowska +3 more
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The Role of Scaffolding in Standard Mechanism Serine Proteinase Inhibitors
Protein & Peptide Letters, 2005In single domain, "standard mechanism" protein inhibitors of serine proteinases, about a dozen residues make contact with the cognate enzyme. The remainder of the molecule, the scaffolding, holds the reactive site region of the inhibitor in a canonical conformation, improves the binding by about six orders of magnitude and protects it from proteolysis.
Clyde A. Kelly +2 more
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Detection of serine proteinase inhibitors in human cornified cells
Biochemical and Biophysical Research Communications, 1981Abstract A screening test for serine proteinase inhibitors revealed trypsin and urokinase inhibitors in the extract of human cornified cells. No inhibition for α-chymotrypsin, thrombin or plasmin was detected. Characterization of the inhibitors separated with a Sephacryl S-200 gel column demonstrated that: 1) trypsin inhibitor with a molecular weight
Seiichi Izaki +2 more
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The Effect of a Serine Proteinase Inhibitor on DIC in Septic Abortion
Asia-Oceania Journal of Obstetrics and Gynaecology, 1987AbstractA 21‐year‐old woman developed septic shock complicated by acute renal insufficiency after D & C to terminate early pregnancy.Although immediate and aggressive treatment improved the profound cardiovascular collapse, DIC became manifest.
Masahiko Mizuno +7 more
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Molecular Reproduction and Development, 2007
AbstractWe have recently identified and characterized twoimplantationserineproteinase genes, ISP1 and ISP2, which give rise to a dimeric proteinase, ISP that facilitates embryo invasion during peri‐implantation period. As many proteinases have cognate serpins that regulate their proteolytic activity, we have been investigating anti‐tryptases, expressed
Navneet Sharma +4 more
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AbstractWe have recently identified and characterized twoimplantationserineproteinase genes, ISP1 and ISP2, which give rise to a dimeric proteinase, ISP that facilitates embryo invasion during peri‐implantation period. As many proteinases have cognate serpins that regulate their proteolytic activity, we have been investigating anti‐tryptases, expressed
Navneet Sharma +4 more
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Pathology - Research and Practice, 1994
Heparin and heparan sulfate, exhibiting wide biological interactions, are constituted of block structures. A defined pentasaccharide motif was found responsible for the enhancement of the rate of inactivation of factor Xa by antithrombin III. Heparin also interacts with other serine proteinase inhibitors as protease nexin I, and thus possibly modulates
Ladislas Robert +4 more
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Heparin and heparan sulfate, exhibiting wide biological interactions, are constituted of block structures. A defined pentasaccharide motif was found responsible for the enhancement of the rate of inactivation of factor Xa by antithrombin III. Heparin also interacts with other serine proteinase inhibitors as protease nexin I, and thus possibly modulates
Ladislas Robert +4 more
openaire +3 more sources
Journal of Biochemistry, 2008
The 20S proteasome (20S) is an intracellular threonine proteinase (Mr 750,000) that plays important roles in many cellular regulations. Several synthetic peptide inhibitors and bacteria-derived inhibitors such as lactacystin and epoxomicin have been identified as potent proteasome inhibitors.
Takehiko Koide, Kimihiko Yabe
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The 20S proteasome (20S) is an intracellular threonine proteinase (Mr 750,000) that plays important roles in many cellular regulations. Several synthetic peptide inhibitors and bacteria-derived inhibitors such as lactacystin and epoxomicin have been identified as potent proteasome inhibitors.
Takehiko Koide, Kimihiko Yabe
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Enzyme and Microbial Technology, 1992
Peptidyl chloromethyl ketones were used for the specific labeling of proteinases by attaching a biotin group to the N-terminal end of the peptide. Such labeled peptide inhibitors allowed the detection and quantitation of proteolytic enzymes immobilized on the plastic surface of a microtiter plate, as well as on nitrocellulose.
Breton-Maintier, C. +2 more
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Peptidyl chloromethyl ketones were used for the specific labeling of proteinases by attaching a biotin group to the N-terminal end of the peptide. Such labeled peptide inhibitors allowed the detection and quantitation of proteolytic enzymes immobilized on the plastic surface of a microtiter plate, as well as on nitrocellulose.
Breton-Maintier, C. +2 more
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Serine proteinase inhibitor proteins: Exogenous and endogenous functions
In Vitro Cellular & Developmental Biology - Plant, 2006Summary Proteinase inhibitor II (PIN2) proteins from the Solanaceae family have been previously used in plant transformation to acquire protection against caterpillars. Some of these PIN2 proteins have been shown to exhibit exogenous activities against trypsin and/or chymotrypsin in vitro.
Xu, ZF, Yeung, EC, Chye, ML, Sin, SF
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