Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins. - Wikidata - awgldk - TriplyDB

Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.

Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.

http://www.wikidata.org/entity/Q37576606

about

Amino acid sequence of human plasma alpha 1B-glycoprotein: homology to the immunoglobulin supergene family Aceruloplasminemia: molecular characterization of this disorder of iron metabolism Complete cDNA and derived amino acid sequence of human factor V Complete cDNA sequence of human preceruloplasmin Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin Characterization, mapping, and expression of the human ceruloplasmin gene Analysis of the human hephaestin gene and protein: comparative modelling of the N-terminus ecto-domain based upon ceruloplasmin Shuffled domains in extracellular proteins Changes in the Factor VIII C2 domain upon membrane binding determined by hydrogen-deuterium exchange MS.Homocysteine inhibits inactivation of factor Va by activated protein C.Delayed translational silencing of ceruloplasmin transcript in gamma interferon-activated U937 monocytic cells: role of the 3' untranslated region Intact human ceruloplasmin oxidatively modifies low density lipoprotein.Isolation and study of an acquired inhibitor of human coagulation factor V.Human factor VIII procoagulant protein. Monoclonal antibodies define precursor-product relationships and functional epitopes A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins.Identification of the prooxidant site of human ceruloplasmin: a model for oxidative damage by copper bound to protein surfaces.Contribution of A1 subunit residue Q316 in thrombin-activated factor VIII to A2 subunit dissociation.Membrane-binding properties of the Factor VIII C2 domain.A large region (approximately equal to 95 kDa) of human factor VIII is dispensable for in vitro procoagulant activity.Localization of human factor FVIII inhibitor epitopes to two polypeptide fragments.Internal duplication and sequence homology in factors V and VIII.Significance of similarities in patterns: an application to beta interferon-related DNA on human chromosome 2.Factor VIII therapy for hemophilia A: current and future issues.Roles of phytanoyl-CoA alpha-hydroxylase in mediating the expression of human coagulation factor VIII.The sequence Glu1811-Lys1818 of human blood coagulation factor VIII comprises a binding site for activated factor IX.Identification of catalytically important amino acids in human ceruloplasmin by site-directed mutagenesis.Mass spectrometry-assisted study reveals that lysine residues 1967 and 1968 have opposite contribution to stability of activated factor VIII.Function of the activated protein C (APC) autolysis loop in activated FVIII inactivation.Coagulation factor Va Glu-96-Asp-111: a chelator-sensitive site involved in function and subunit association.Platelet binding sites for factor VIII in relation to fibrin and phosphatidylserine.Factor IXa:factor VIIIa interaction. helix 330-338 of factor ixa interacts with residues 558-565 and spatially adjacent regions of the a2 subunit of factor VIIIa.Four hydrophobic amino acids of the factor VIII C2 domain are constituents of both the membrane-binding and von Willebrand factor-binding motifs.Low density lipoprotein receptor-related protein and factor IXa share structural requirements for binding to the A3 domain of coagulation factor VIII.Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity.Identification of a factor Xa-interactive site within residues 337-372 of the factor VIII heavy chain.Functional characterization of a novel missense mutation identified in a Turkish patient affected by severe coagulation factor V deficiency.Exosite-interactive regions in the A1 and A2 domains of factor VIII facilitate thrombin-catalyzed cleavage of heavy chain.Characterization of five associations of F8 missense mutations containing FVIII B domain mutations.Monoclonal antibodies to factor VIII: their application in immunoblotting for the visualization of factor VIII in therapeutic concentrates and plasma.Identification of porcine coagulation factor VIII domains responsible for high level expression via enhanced secretion.

P2860

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P2860

Coagulation factors V and VIII and ceruloplasmin constitute a family of structurally related proteins.

http://www.wikidata.org/entity/Q37576606

description

1984 nî lūn-bûn

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1984年の論文

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1984年学术文章

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1984年学术文章

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1984年学术文章

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1984年学术文章

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1984年学术文章

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1984年學術文章

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1984年學術文章

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1984年學術文章

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name

Coagulation factors V and VIII ...... structurally related proteins.

@en

Coagulation factors V and VIII ...... structurally related proteins.

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type

label

Coagulation factors V and VIII ...... structurally related proteins.

@en

Coagulation factors V and VIII ...... structurally related proteins.

@nl

prefLabel

Coagulation factors V and VIII ...... structurally related proteins.

@en

Coagulation factors V and VIII ...... structurally related proteins.

@nl

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PNAS.81.22.6934

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Coagulation factors V and VIII ...... structurally related proteins.

@en

P2093

Church WR

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Fass DN

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Hewick RM

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Jernigan RL

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Knopf J

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Knutson GJ

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Mann KG

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Nesheim ME

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Toole J

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P2860

Internal triplication in the structure of human ceruloplasmin

A general method applicable to the search for similarities in the amino acid sequence of two proteins

Pattern recognition in nucleic acid sequences. I. A general method for finding local homologies and symmetries.

Ceruloplasmin: methods and clinical use.

Proteolysis of human ceruloplasmin. Some peptide bonds are particularly susceptible to proteolytic attack.

Characterization of Factor V activation intermediates.

Similar amino acid sequences: chance or common ancestry?

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6934-6937

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scholarly article

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10.1073/PNAS.81.22.6934

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22

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81

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16756931

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6438625

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392050

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