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protein c deficiency/protease
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A molecular model of the serine protease domain of activated protein C: application to the study of missense mutations causing protein C deficiency.
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A molecular model of the serine protease domain of protein C was constructed by standard comparative methods. Individual missense mutations were inserted into the model and plausible explanations for their interference with protein C structure/function were derived through consideration of location,
Cellular basis for protein C deficiency caused by a single amino acid substitution at Arg15 in the gamma-carboxyglutamic acid domain.
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Protein C is a zymogen of an anticoagulant vitamin K-dependent serine protease. Inherited protein C deficiency is often associated with a high risk for venous thromboembolism. It is characteristic of protein C deficiency that most single amino acid replacements result in type I (secretion defect)
Molecular dynamics and docking simulation of a natural variant of Activated Protein C with impaired protease activity: implications for integrin-mediated antiseptic function.
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Activated Protein C (APC) is a multifunctional serine protease, primarily known for its anticoagulant function in the coagulation system. Several studies have already elucidated its role in counteracting apoptosis and inflammation in cells, while significant effort is still ongoing for defining its
Purpura fulminans. A cutaneous manifestation of severe protein C deficiency.
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Protein C, when activated, is a vitamin K-dependent serine protease that has anticoagulant and profibrinolytic activities. An increased risk of thrombotic disease is associated with deficiency of this enzyme. A neonate developing purpura fulminans with internal thrombotic complications and
Protein C deficiency in liver disease.
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Protein C is a vitamin K-dependent zymogen of a serine protease that is found in blood plasma. The active form, activated protein C, can inhibit blood coagulation and stimulate fibrinolysis. Protein C is synthesized in the liver as a single chain protein. Its synthesis requires several
Symptomatic type 1 protein C deficiency caused by a de novo Ser270Leu mutation in the catalytic domain.
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Heterozygosity for a C8524T transition in the protein C gene converting Ser270(TCG) to Leu(TTG) in the protease domain was identified in a family with venous thrombosis. The mutation was associated with parallel reduction in plasma levels of protein C anticoagulant activity and protein C antigen,
Possible structural implications of 20 mutations in the protein C protease domain.
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Analysis of naturally occurring protein mutations yields valuable insights into functionally important sequences. Characterizing mutations responsible for protein C deficiency at the molecular level has been the subject of intensive investigation. In a previous study, a three-dimensional model of
HIV-associated thromboembolic phenomenon due to protein C deficiency.
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HIV-infected individuals are at a high risk of developing arterial and venous thromboembolism. Opportunistic infections, protease inhibitors, low CD4 count, antiphospholipid antibodies, protein S, and protein C deficiencies are some important risk factors associated with it. However, thromboembolic
Genetic characterization of protein C deficiency in Japanese subjects using a rapid and nonradioactive method for single-stand conformational polymorphism analysis and a model building.
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We studied the molecular basis of protein C deficiency in 28 Japanese families including 4 asymptomatic families. Two showed a decreased level of function with a normal antigen concentration consistent with type II protein C deficiency and the remaining 26 showed type I deficiency with decreases in
Two mutations in the promoter region of the human protein C gene both cause type I protein C deficiency by disruption of two HNF-3 binding sites.
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Protein C is a vitamin K-dependent zymogen of a serine protease that inhibits blood coagulation by the proteolytic inactivation of factors Va and VIIIa. Individuals affected with protein C deficiency are at risk for thrombosis. Genetic analyses of affected individuals, to determine the cause of the
A molecular model of a point mutation (Val297Met) in the serine protease domain of protein C.
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A heterozygous GTG to ATG (Val297Met) mutation was detected in a patient with inherited protein C deficiency and deep vein thrombosis. Cosegregation of the mutation with protein C deficiency was observed through a family pedigree study. Molecular models of the serine protease domains of wild type
Structural basis for type I and type II deficiencies of antithrombotic plasma protein C: patterns revealed by three-dimensional molecular modelling of mutations of the protease domain.
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Familial deficiency of protein C is associated with inherited thrombophilia. To explore how specific missense mutations might cause observed clinical phenotypes, know protein C missense mutations were mapped onto three-dimensional homology models of the protein C protease domain, and the
Type I protein C deficiency caused by disruption of a hepatocyte nuclear factor (HNF)-6/HNF-1 binding site in the human protein C gene promoter.
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Protein C is a vitamin K-dependent zymogen of a serine protease that inhibits blood coagulation by proteolytic inactivation of factors Va and VIIIa. Individuals affected by protein C deficiency are at risk for venous thrombosis. One such affected individual was shown earlier to carry a -14 T --> C
Persistent Fetal Vasculature and Severe Protein C Deficiency.
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Persistent fetal vasculature (PFV) is most often a condition of unknown cause. It represents persisting elements of fetal ocular vessels including the hyaloid arterial network. Protein C is a vitamin K-dependent serine protease, which regulates coagulation. Deficiency of protein C leads to a
Homozygous protein C deficiency: identification of a novel missense mutation that causes impaired secretion of the mutant protein C.
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We analyzed the promoter region and all the coding exons and exon-intron boundaries of the protein C gene in a Japanese patient with recurrent thromboembolism and complete protein C deficiency. By sequencing these fragments we identified a previously undescribed mutation. A guanine residue was
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