Výsledky vyhledávání - "J J Birktoft"

Identification of a calcium binding site in the protease domain of human blood coagulation factor VII: evidence for its role in factor VII - tissue factor interaction

Autor: Lars Christian Petersen, D Foster, J Schiødt, J J Birktoft, F C Wiberg, P Wildgoose

Publikováno v: Biochemistry. 32:114-119

Previous studies have identified a putative calcium binding site involving two glutamic acid residues located in the protease domain of coagulation factor IX. Amino acid sequence homology considerations suggest that factor VII (FVII) possesses a simi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16b74d7351d1be5d5685c8f82cf4715b
https://doi.org/10.1021/bi00052a016

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Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX

Autor: S P Bajaj, Klaus Olek, Kenneth J. Smith, J J Birktoft, A K Sabharwal, Hans-Hermann Brackmann, Michael Ludwig

Publikováno v: Blood. 79:1225-1232

Factor IX is a multidomain protein and is the proenzyme of a serine protease, factor IXa, essential for hemostasis. In this report, we describe the molecular basis of hemophilia B (deficiency of factor IX activity) in five patients who have neither d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b2ce45e54ab7f117a0c331a28a92804c
https://doi.org/10.1182/blood.v79.5.1225.1225

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Antibody-probed conformational transitions in the protease domain of human factor IX upon calcium binding and zymogen activation: putative high-affinity Ca(2+)-binding site in the protease domain

Autor: S P Bajaj, J Gorka, J J Birktoft, A K Sabharwal

Publikováno v: Proceedings of the National Academy of Sciences. 89:152-156

The Fab fragment of a monoclonal antibody (mAb) reactive to the N-terminal half (residues 180-310) of the protease domain of human factor IX has been previously shown to inhibit the binding of factor IXa to its cofactor, factor VIIIa. These data sugg

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89f5b81b75257e2e50090e1f39e1b67a
https://doi.org/10.1073/pnas.89.1.152

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Factor IXHollywood: substitution of Pro55 by Ala in the first epidermal growth factor-like domain

Autor: S G, Spitzer, M N, Kuppuswamy, R, Saini, C K, Kasper, J J, Birktoft, S P, Bajaj

Publikováno v: Blood. 76:1530-1537

Factor IX is a multidomain protein essential for hemostasis. We describe a mutation in a patient affecting the first epidermal growth factor (EGF)-like domain of the protein. All exons and the promoter region of the gene were amplified by the polymer

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f2a46d6d8a1fe4effa0553362d3f5e2
https://doi.org/10.1182/blood.v76.8.1530.bloodjournal7681530

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Structure and biology of tissue factor pathway inhibitor

Autor: M S, Bajaj, J J, Birktoft, S A, Steer, S P, Bajaj

Publikováno v: Thrombosis and haemostasis. 86(4)

Human tissue factor pathway inhibitor (TFPI) is a modular protein comprised of three Kunitz type domains flanked by peptide segments that are less structured. The sequential order of the elements are: an N-terminal acidic region followed by the first

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1267412ddb46784706c7531e06e2765d
https://pubmed.ncbi.nlm.nih.gov/11686353

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Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus

Autor: Klaus Breddam, J J Birktoft, Henning R. Stennicke

The glutamic acid-specific protease from Streptomyces griseus (SGPE) is an 18.4-kDa serine protease with a distinct preference for Glu in the P1 position. Other enzymes characterized by a strong preference for negatively charged residues in the P1 po

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02d4e3efcf9283a3a7efa66f47fa822f
https://europepmc.org/articles/PMC2143298/

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First epidermal growth factor-like domain of human blood coagulation factor IX is required for its activation by factor VIIa/tissue factor but not by factor XIa

Autor: Kenneth J. Smith, J J Birktoft, S P Bajaj, D Zhong

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 91(9)

Factor IX consists of a gamma-carboxyglutamic acid-rich domain followed by two epidermal growth factor (EGF)-like domains and the C-terminal protease domain. To delineate the function of EGF1 domain in factor IX, we constructed three mutants: an EGF1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8621c060a25b967d7ae7a9251cc6452a
https://pubmed.ncbi.nlm.nih.gov/8170949

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Alteration of coenzyme specificity of malate dehydrogenase from Thermus flavus by site-directed mutagenesis

Autor: Teruhiko Beppu, Makoto Nishiyama, J J Birktoft

Publikováno v: Scopus-Elsevier

On the basis of the crystal structure of the NAD-dependent cytoplasmic malate dehydrogenase (MDH) and its alignment with NADP-dependent counterparts, the loop region between beta-strand B and alpha-helix C in the dinucleotide-binding fold was predict

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff609eee894bf18a1696eb73c89d52aa
https://pubmed.ncbi.nlm.nih.gov/8444839

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[6] Human factor IX and factor IXa

Autor: S P Bajaj, J J Birktoft

Publisher Summary This chapter provides methods for factor IX and factor IXa isolation from human plasma and recombinant cultures and discusses the preparation of [ 3 H]sialyl and of 125 I-labeled tyrosyl factor IX and their use in investigations of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::aad9ca22971599b8f4944669ca03724e
https://doi.org/10.1016/0076-6879(93)22009-5

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