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  1. Book ; Conference proceedings: Blood coagulation, fibrinolysis, and platelets

    Davie, Earl W.

    1996  

    Event/congress Japanese Chinese Symposium on Coagulation, Fibrinolysis, and Platelets (3, 1994, Kōbe)
    Author's details [Third Japanese-Chinese Symposium on Coagulation, Fibrinolysis, and Platelets ... Kobe, Japan, from October 4 through 6, 1994] E. W. Davie ... (eds.)
    Keywords Blood Coagulation / congresses ; Blood Platelets / congresses ; Fibrinolysis / congresses ; Blutgerinnung ; Koagulopathie ; Fibrinolyse ; Thrombozyt ; Thrombose
    Subject Blutplättchen ; Platelet ; Thrombozyten ; Fibrinolysesystem ; Thrombolyse ; Gerinnung ; Blutkoagulation ; Blood coagulation ; Thrombosen ; Blutgerinnungsstörung ; Coagulopathy ; Gerinnungsstörung
    Language English
    Size 228 S. : Ill., graph. Darst.
    Publisher Springer
    Publishing place Tokyo u.a.
    Publishing country Japan
    Document type Book ; Conference proceedings
    HBZ-ID HT007226686
    ISBN 4-431-70165-6 ; 978-4-431-70165-1
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1996 A 3675 order for loan Magazin

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  2. Book ; Conference proceedings: Thrombin biology in the 21st century: implications in hemostasis, inflammation, coagulopathies, and cancer

    Roberts, Harold R. / Davie, Earl W.

    [symposium in September of 2005]

    (Seminars in thrombosis and hemostasis ; 32, Suppl. 1)

    2006  

    Author's details Harold R. Roberts and Earl W. Davie
    Series title Seminars in thrombosis and hemostasis ; 32, Suppl. 1
    Collection
    Language English
    Size 110 S. : Ill., graph. Darst.
    Publisher Thieme Med. Publ
    Publishing place New York u.a.
    Publishing country United States
    Document type Book ; Conference proceedings
    HBZ-ID HT014738629
    Database Catalogue ZB MED Medicine, Health

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    Zs A 1259 -32,Suppl.1- not available for loan Zeitschriften-Lesesaal

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  3. Book ; Online: Recent Advances in Thrombosis and Hemostasis 2008

    Tanaka, Kenzo / Davie, Earl W. / Ikeda, Yasuo / Iwanaga, Sadaaki / Saito, Hidehiko / Sueishi, Katsuo

    2008  

    Author's details edited by Kenzo Tanaka, Earl W. Davie, Yasuo Ikeda, Sadaaki Iwanaga, Hidehiko Saito, Katsuo Sueishi
    Keywords Cytology ; Hematology ; Internal medicine ; Medicine
    Language English
    Publisher Springer Japan
    Publishing place Tokyo
    Document type Book ; Online
    HBZ-ID TT050387888
    ISBN 978-4-431-78846-1 ; 978-4-431-78847-8 ; 4-431-78846-8 ; 4-431-78847-6
    DOI 10.1007/978-4-431-78847-8
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

    Full text online

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  4. Article: A brief historical review of the waterfall/cascade of blood coagulation.

    Davie, Earl W

    The Journal of biological chemistry

    2003  Volume 278, Issue 51, Page(s) 50819–50832

    MeSH term(s) Animals ; Blood Coagulation ; Blood Proteins ; Hematology/history ; History, 20th Century ; History, 21st Century ; Humans ; Research/history
    Chemical Substances Blood Proteins
    Language English
    Publishing date 2003-10-21
    Publishing country United States
    Document type Historical Article ; Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.X300009200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: An overview of the structure and function of thrombin.

    Davie, Earl W / Kulman, John D

    Seminars in thrombosis and hemostasis

    2006  Volume 32 Suppl 1, Page(s) 3–15

    Abstract: The fundamental importance of thrombin in biology and medicine has made it one of the most extensively studied of all proteases. Thrombin performs essential functions in vertebrate biology as the central enzyme involved in blood coagulation and platelet ... ...

    Abstract The fundamental importance of thrombin in biology and medicine has made it one of the most extensively studied of all proteases. Thrombin performs essential functions in vertebrate biology as the central enzyme involved in blood coagulation and platelet aggregation, and as a mitogen and secretagogue for a variety of cell types. Thrombin is synthesized in the liver and secreted into the general circulation in an inactive zymogen form (prothrombin), a complex multidomain glycoprotein that is activated to yield thrombin at sites of vascular injury by limited proteolysis following upstream activation of the coagulation cascade. Thrombin shares its general architecture and catalytic mechanism with those of pancreatic trypsin, the prototypical digestive serine protease. However, the specificity of thrombin toward substrates and cofactors, as well as its spatiotemporal regulation by effectors and inhibitors, is directed by features of the molecule that distinguish it from relatively nonspecific serine proteases like trypsin. Structural and functional studies have demonstrated the presence of surface loops that partially occlude the active site and make specific contacts with residues adjacent to the scissile bond of substrates. Specificity toward macromolecular substrates and cofactors is additionally enhanced by anion-binding exosites that are spatially distinct from the active site. More than five decades of multidisciplinary research on thrombin have produced an abundance of functional and structural information and provided a robust framework for understanding the role of thrombin in vertebrate biology.
    MeSH term(s) Animals ; Binding Sites ; Hemostasis ; Humans ; Sequence Alignment ; Serine Endopeptidases/chemistry ; Thrombin/biosynthesis ; Thrombin/chemistry ; Thrombin/physiology
    Chemical Substances Serine Endopeptidases (EC 3.4.21.-) ; Thrombin (EC 3.4.21.5)
    Language English
    Publishing date 2006-04
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 196901-8
    ISSN 1098-9064 ; 0094-6176
    ISSN (online) 1098-9064
    ISSN 0094-6176
    DOI 10.1055/s-2006-939550
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1259: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  6. Article: Thrombin Biology in the 21st Century

    Roberts, Harold R / Davie, Earl W

    Seminars in Thrombosis and Hemostasis

    (Thrombin Biology in the 21st Century: Implications in Hemostasis, Inflammation, Coagulopathies, and Cancer)

    2006  Volume 32, Issue S 1, Page(s) 1–2

    Series title Thrombin Biology in the 21st Century: Implications in Hemostasis, Inflammation, Coagulopathies, and Cancer
    Language English
    Publishing date 2006-02-01
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 196901-8
    ISSN 1098-9064 ; 0094-6176
    ISSN (online) 1098-9064
    ISSN 0094-6176
    DOI 10.1055/s-2006-939549
    Database Thieme publisher's database

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    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  7. Article: Biochemical and Molecular Aspects of the Coagulation Cascade

    Davie, Earl W

    Thrombosis and Haemostasis

    1995  Volume 74, Issue 01, Page(s) 1–6

    Language English
    Publishing date 1995-01-01
    Publisher Schattauer GmbH
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 518294-3
    ISSN 2567-689X ; 0340-6245
    ISSN (online) 2567-689X
    ISSN 0340-6245
    DOI 10.1055/s-0038-1642645
    Database Thieme publisher's database

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    Uh III Zs.192: Show issues Location:
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    Zs.MO 433: Show issues

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  8. Article: An Overview of the Structure and Function of Thrombin

    Davie, Earl W / Kulman, John D

    Seminars in Thrombosis and Hemostasis

    2006  Volume 32, Issue S 1, Page(s) 3–15

    Abstract: The fundamental importance of thrombin in biology and medicine has made it one of the most extensively studied of all proteases. Thrombin performs essential functions in vertebrate biology as the central enzyme involved in blood coagulation and platelet ... ...

    Abstract The fundamental importance of thrombin in biology and medicine has made it one of the most extensively studied of all proteases. Thrombin performs essential functions in vertebrate biology as the central enzyme involved in blood coagulation and platelet aggregation, and as a mitogen and secretagogue for a variety of cell types. Thrombin is synthesized in the liver and secreted into the general circulation in an inactive zymogen form (prothrombin), a complex multidomain glycoprotein that is activated to yield thrombin at sites of vascular injury by limited proteolysis following upstream activation of the coagulation cascade. Thrombin shares its general architecture and catalytic mechanism with those of pancreatic trypsin, the prototypical digestive serine protease. However, the specificity of thrombin toward substrates and cofactors, as well as its spatiotemporal regulation by effectors and inhibitors, is directed by features of the molecule that distinguish it from relatively nonspecific serine proteases like trypsin. Structural and functional studies have demonstrated the presence of surface loops that partially occlude the active site and make specific contacts with residues adjacent to the scissile bond of substrates. Specificity toward macromolecular substrates and cofactors is additionally enhanced by anion-binding exosites that are spatially distinct from the active site. More than five decades of multidisciplinary research on thrombin have produced an abundance of functional and structural information and provided a robust framework for understanding the role of thrombin in vertebrate biology.
    Keywords Thrombin ; antithrombin ; prothrombin ; blood coagulation ; serine protease
    Language English
    Publishing date 2006-02-01
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 196901-8
    ISSN 1098-9064 ; 0094-6176
    ISSN (online) 1098-9064
    ISSN 0094-6176
    DOI 10.1055/s-2006-939550
    Database Thieme publisher's database

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  9. Article: Proline-rich Gla protein 2 is a cell-surface vitamin K-dependent protein that binds to the transcriptional coactivator Yes-associated protein.

    Kulman, John D / Harris, Jeff E / Xie, Ling / Davie, Earl W

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

    2007  Volume 104, Issue 21, Page(s) 8767–8772

    Abstract: Proline-rich Gla protein 2 (PRGP2) is one of four known vertebrate transmembrane gamma-carboxyglutamic acid (Gla) proteins. Members of this protein family are broadly expressed in fetal and adult human tissues and share a common architecture consisting ... ...

    Abstract Proline-rich Gla protein 2 (PRGP2) is one of four known vertebrate transmembrane gamma-carboxyglutamic acid (Gla) proteins. Members of this protein family are broadly expressed in fetal and adult human tissues and share a common architecture consisting of a predicted propeptide and Gla domain, a single-pass transmembrane segment, and tandem Pro/Leu-Pro-Xaa-Tyr (PY) motifs near their C termini. Using a methodology developed for the regulated expression of enzymatically biotinylated proteins in mammalian cells, we demonstrate that PRGP2 undergoes gamma-glutamyl carboxylation in a manner that is both dependent upon the presence of a proteolytically cleavable propeptide and sensitive to warfarin, a vitamin K antagonist that is widely used as an antithrombotic agent. When expressed at physiologically relevant levels, the majority of PRGP2 is present in the gamma-glutamyl carboxylated, propeptide-cleaved (mature) form. We additionally demonstrate, by Western blotting and flow cytometry, that mature PRGP2 is predominantly located on the cell surface with the Gla domain exposed extracellularly. In a yeast two-hybrid screen that used the C-terminal cytoplasmic region of PRGP2 as bait, we identified the WW domain-containing transcriptional coactivator Yes-associated protein (YAP) as a binding partner for PRGP2. In GST pull-down experiments, both PRGP2 PY motifs and both YAP WW domains were essential for complex formation, as were residues proximal to the core sequence of the first PY motif. These findings suggest that PRGP2 may be involved in a signal transduction pathway, the impairment of which may be an unintended consequence of warfarin therapy.
    MeSH term(s) Adaptor Proteins, Signal Transducing/chemistry ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Sequence ; Animals ; CHO Cells ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cricetinae ; Cricetulus ; Humans ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Molecular Sequence Data ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Binding ; Protein Processing, Post-Translational ; Trans-Activators/genetics ; Trans-Activators/metabolism ; Transcription Factors ; Vitamin K/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Membrane Proteins ; PRRG2 protein, human ; Phosphoproteins ; Trans-Activators ; Transcription Factors ; YAP1 protein, human ; Vitamin K (12001-79-5)
    Language English
    Publishing date 2007-05-14
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.0703195104
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1148: Show issues Location:
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  10. Article ; Online: Comparative analysis and supragenome modeling of twelve Moraxella catarrhalis clinical isolates.

    Davie, Jeremiah J / Earl, Josh / de Vries, Stefan P W / Ahmed, Azad / Hu, Fen Z / Bootsma, Hester J / Stol, Kim / Hermans, Peter W M / Wadowsky, Robert M / Ehrlich, Garth D / Hays, John P / Campagnari, Anthony A

    BMC genomics

    2011  Volume 12, Page(s) 70

    Abstract: Background: M. catarrhalis is a gram-negative, gamma-proteobacterium and an opportunistic human pathogen associated with otitis media (OM) and exacerbations of chronic obstructive pulmonary disease (COPD). With direct and indirect costs for treating ... ...

    Abstract Background: M. catarrhalis is a gram-negative, gamma-proteobacterium and an opportunistic human pathogen associated with otitis media (OM) and exacerbations of chronic obstructive pulmonary disease (COPD). With direct and indirect costs for treating these conditions annually exceeding $33 billion in the United States alone, and nearly ubiquitous resistance to beta-lactam antibiotics among M. catarrhalis clinical isolates, a greater understanding of this pathogen's genome and its variability among isolates is needed.
    Results: The genomic sequences of ten geographically and phenotypically diverse clinical isolates of M. catarrhalis were determined and analyzed together with two publicly available genomes. These twelve genomes were subjected to detailed comparative and predictive analyses aimed at characterizing the supragenome and understanding the metabolic and pathogenic potential of this species. A total of 2383 gene clusters were identified, of which 1755 are core with the remaining 628 clusters unevenly distributed among the twelve isolates. These findings are consistent with the distributed genome hypothesis (DGH), which posits that the species genome possesses a far greater number of genes than any single isolate. Multiple and pair-wise whole genome alignments highlight limited chromosomal re-arrangement.
    Conclusions: M. catarrhalis gene content and chromosomal organization data, although supportive of the DGH, show modest overall genic diversity. These findings are in stark contrast with the reported heterogeneity of the species as a whole, as wells as to other bacterial pathogens mediating OM and COPD, providing important insight into M. catarrhalis pathogenesis that will aid in the development of novel therapeutic regimens.
    MeSH term(s) Bacterial Typing Techniques ; Codon ; DNA, Bacterial/genetics ; Genome, Bacterial ; Interspersed Repetitive Sequences ; Models, Genetic ; Moraxella catarrhalis/genetics ; Moraxella catarrhalis/isolation & purification ; Multigene Family ; Multilocus Sequence Typing ; Sequence Alignment ; Sequence Analysis, DNA ; Virulence Factors/genetics
    Chemical Substances Codon ; DNA, Bacterial ; Virulence Factors
    Language English
    Publishing date 2011-01-26
    Publishing country England
    Document type Comparative Study ; Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1471-2164
    ISSN (online) 1471-2164
    DOI 10.1186/1471-2164-12-70
    Database MEDical Literature Analysis and Retrieval System OnLINE

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