Results 251 to 260 of about 28,039,605 (307)
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2013
Protein S (PS) is a vitamin K-dependent plasma glycoprotein. Around 60-70% of PS in plasma is noncovalently bound to C4-binding protein (C4BP). Free PS functions as a cofactor that enhances the activity of activated protein C (APC) in the proteolytic degradation of activated factors V and VIII.
Mirta, Hepner, Vasiliki, Karlaftis
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Protein S (PS) is a vitamin K-dependent plasma glycoprotein. Around 60-70% of PS in plasma is noncovalently bound to C4-binding protein (C4BP). Free PS functions as a cofactor that enhances the activity of activated protein C (APC) in the proteolytic degradation of activated factors V and VIII.
Mirta, Hepner, Vasiliki, Karlaftis
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Thrombosis and Haemostasis, 1997
The protein C (PC) pathway, with its cofactor protein S (PS), is an important natural antithrombotic mechanism. Patients with phenotypic PS deficiency may develop recurrent thrombosis during adulthood, with a probability of remaining free of thrombosis of about 50% at age 45.
D, Borgel, S, Gandrille, M, Aiach
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The protein C (PC) pathway, with its cofactor protein S (PS), is an important natural antithrombotic mechanism. Patients with phenotypic PS deficiency may develop recurrent thrombosis during adulthood, with a probability of remaining free of thrombosis of about 50% at age 45.
D, Borgel, S, Gandrille, M, Aiach
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Analysis of the Protein S Gene in Protein S Deficiency
2003Protein S (PS) is a 71-kDa vitamin K-dependent glycoprotein first identified in human plasma by DiScipio and colleagues in 1977 (1), a year after the discovery of the anticoagulant protein C (PC) (2,3). A few years later, Walker demonstrated that PS acts as a cofactor for activated protein C (APC) in the proteolytic inactivation of the procoagulant ...
N, Sala, Y, Espinosa-Parrilla
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Protein-S-S-Glutathione Mixed Disulfides as Models of Unfolded Proteins
Biochemistry, 1994Mixed disulfides between glutathione and the reduced forms of disulfide-bonded proteins were generated and characterized to explore their suitability as models of the unfolded state of newly-synthesized secretory proteins. RNase T1 and alpha-lactalbumin were reduced and converted to mixed disulfide derivatives, named GS-RNase T1 and GS-alpha ...
RUOPPOLO, MARGHERITA, R. B. Freedman
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Inhibition of Protein S by Autoantibodies in Patients with Acquired Protein S Deficiency
Thrombosis and Haemostasis, 1996SummaryThis study was undertaken to analyze antibodies to protein S (PS) in patients with an acquired PS deficiency. Plasma from symptomatic patients with acquired (n = 14) or congenital (n = 10) PS deficiency and 10 healthy donors was screened for PS antibodies by immunoblotting and for anti-phospholipid antibodies.
SORICE, Maurizio +7 more
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2019
Palmitoylation or S-acylation is the posttranslational attachment of fatty acids to cysteine residues and is common among integral and peripheral membrane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells.
Larisa, Kordyukova +3 more
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Palmitoylation or S-acylation is the posttranslational attachment of fatty acids to cysteine residues and is common among integral and peripheral membrane proteins. Palmitoylated proteins have been found in every eukaryotic cell type examined (yeast, insect, and vertebrate cells), as well as in viruses grown in these cells.
Larisa, Kordyukova +3 more
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Cell Calcium, 1986
S-100 is a group of closely related, small, acidic Ca2+-binding proteins (S-100a0, S-100a and S-100b, which are alpha alpha, alpha beta, and beta beta in composition, respectively). S-100 is structurally related to calmodulin and other Ca2+-binding proteins.
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S-100 is a group of closely related, small, acidic Ca2+-binding proteins (S-100a0, S-100a and S-100b, which are alpha alpha, alpha beta, and beta beta in composition, respectively). S-100 is structurally related to calmodulin and other Ca2+-binding proteins.
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Nanotechnology with S-Layer Proteins
2013Nanosciences are distinguished by the cross-fertilization of biology, chemistry, material sciences, and solid-state physics and hence open up a great variety of new opportunities for innovation. The technological utilization of self-assembly systems, wherein molecules spontaneously associate under equilibrium conditions into reproducible supramolecular
Bernhard, Schuster, Uwe B, Sleytr
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Cellular and Molecular Life Sciences, 1999
The transfer of a nitric oxide group to cysteine sulfhydryls on proteins, known as S-nitrosylation, is increasingly becoming recognized as a ubiquitous regulatory reaction comparable to phosphorylation. It represents a form of redox modulation in diverse tissues, including the brain.
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The transfer of a nitric oxide group to cysteine sulfhydryls on proteins, known as S-nitrosylation, is increasingly becoming recognized as a ubiquitous regulatory reaction comparable to phosphorylation. It represents a form of redox modulation in diverse tissues, including the brain.
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Oral contraceptives reduce total protein S, but not free protein S.
Thrombosis Research, 1987This study is an attempt to isolate the mechanism by which oral contraceptives (OCs) despite reduced estrogen content increase the risk of thromboembolitic disease. The subjects were 10 women athletes who had used OCs containing a combination of ethinylestradiol and levonorgestrel for more than a year.
Huisveld, I. A. +5 more
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