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  1. Book: Hematology

    Babior, Bernard M. / Stossel, Thomas P.

    a pathophysiological approach

    1990  

    Author's details Bernard M. Babior ; Thomas P. Stossel
    Keywords Hematologic Diseases / physiopathology
    Language English
    Size VIII, 448 S. : Ill., graph. Darst.
    Edition 2. ed.
    Publisher Churchill Livingstone
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT003472421
    ISBN 0-443-08608-7 ; 978-0-443-08608-3
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1990 A 1535 order for loan Magazin

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  2. Book: Cobalamin

    Babior, Bernard M.

    biochemistry and pathophysiology

    1975  

    Author's details ed. by Bernard M. Babior
    Keywords Vitamin B12
    Subject APF ; Cyanocobalamin
    Language English
    Size XII, 477 S.
    Publisher Wiley
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT000464114
    ISBN 0-471-03970-5 ; 978-0-471-03970-9
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1977 A 1480 order for loan Magazin

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  3. Book: Hematology

    Babior, Bernard M. / Stossel, Thomas P.

    a pathophysiological approach

    1984  

    Author's details Bernard M. Babior ; Thomas B. Stossel
    Keywords HEMATOLOGIC DISEASES / PHYSIOPATHOLOGY ; Hämatologie
    Size VIII, 396 S. : Ill.
    Publisher Churchill Livingstone
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT002573106
    ISBN 0-443-08170-0 ; 978-0-443-08170-5
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1985 A 228 order for loan Magazin

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  4. Article ; Online: Pillars article: Biological defense mechanisms. The production by leukocytes of superoxide, a potential bactericidal agent. J. Clin. Invest. 1973. 52: 741-744.

    Babior, Bernard M / Kipnes, Ruby S / Curnutte, John T

    Journal of immunology (Baltimore, Md. : 1950)

    2014  Volume 193, Issue 11, Page(s) 5359–5362

    MeSH term(s) Allergy and Immunology/history ; Animals ; Anti-Infective Agents/immunology ; Anti-Infective Agents/therapeutic use ; Bacterial Infections/immunology ; Bacterial Infections/therapy ; History, 20th Century ; Humans ; Leukocytes/immunology ; Oxidative Stress/immunology ; Superoxides/immunology ; Superoxides/therapeutic use
    Chemical Substances Anti-Infective Agents ; Superoxides (11062-77-4)
    Language English
    Publishing date 2014-12-01
    Publishing country United States
    Document type Biography ; Classical Article ; Historical Article ; Journal Article
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: NADPH oxidase.

    Babior, Bernard M

    Current opinion in immunology

    2004  Volume 16, Issue 1, Page(s) 42–47

    Abstract: NADPH oxidase is an enzyme that catalyzes the production of superoxide from oxygen and NADPH. It is a complex enzyme consisting of two membrane-bound components and three components in the cytosol, plus rac 1 or rac 2. Activation of the oxidase involves ... ...

    Abstract NADPH oxidase is an enzyme that catalyzes the production of superoxide from oxygen and NADPH. It is a complex enzyme consisting of two membrane-bound components and three components in the cytosol, plus rac 1 or rac 2. Activation of the oxidase involves the phosphorylation of one of the cytosolic components. Recent crystallography data indicate that the tail of this cytosolic component lies in a groove between two Src homology 3 domains and, when phosphorylated, the tail leaves the groove and is replaced by the tail of one of the membrane-bound components. Chronic granulomatous disease is an inherited immune deficiency caused by the absence of one of the components of the oxidase. The most important recent advances in the field have been the crystallographic analysis of the oxidase and the use of antifungal agents in the prophylaxis of chronic granulomatous disease.
    MeSH term(s) Crystallography, X-Ray ; Granulomatous Disease, Chronic/genetics ; Granulomatous Disease, Chronic/therapy ; Humans ; Models, Molecular ; NADPH Oxidases/chemistry ; NADPH Oxidases/genetics ; Protein Subunits/chemistry ; Protein Subunits/genetics ; src Homology Domains
    Chemical Substances Protein Subunits ; NADPH Oxidases (EC 1.6.3.-)
    Language English
    Publishing date 2004-02
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 1035767-1
    ISSN 1879-0372 ; 0952-7915
    ISSN (online) 1879-0372
    ISSN 0952-7915
    DOI 10.1016/j.coi.2003.12.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.MG 13: Show issues

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  6. Article: My life in Konrad's Lab.

    Babior, Bernard M

    Biochemical and biophysical research communications

    2002  Volume 292, Issue 5, Page(s) 1237–1238

    MeSH term(s) Anecdotes as Topic ; Biochemistry/history ; Coenzyme A/history ; Coenzyme A/metabolism ; Fatty Acids/chemistry ; Fatty Acids/history ; Fatty Acids/metabolism ; History, 20th Century ; Lipid Metabolism ; Lipids/history ; United States
    Chemical Substances Fatty Acids ; Lipids ; Coenzyme A (SAA04E81UX)
    Language English
    Publishing date 2002-04-19
    Publishing country United States
    Document type Autobiography ; Biography ; Historical Article ; Journal Article
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1006/bbrc.2002.2001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article: The activity of leukocyte NADPH oxidase: regulation by p47PHOX cysteine and serine residues.

    Babior, Bernard M

    Antioxidants & redox signaling

    2002  Volume 4, Issue 1, Page(s) 35–38

    Abstract: The leukocyte NADPH oxidase is regulated chiefly by phosphorylation of the serines of p47(PHOX), one of its cytosolic subunits. Its activity is also regulated, however, by the four cysteines of the same subunit, as indicated by the replacement of those ... ...

    Abstract The leukocyte NADPH oxidase is regulated chiefly by phosphorylation of the serines of p47(PHOX), one of its cytosolic subunits. Its activity is also regulated, however, by the four cysteines of the same subunit, as indicated by the replacement of those cysteines by alanines.
    MeSH term(s) Alanine/metabolism ; Cell-Free System ; Cysteine/metabolism ; Cytosol/enzymology ; Gene Expression Regulation, Enzymologic ; Humans ; Leukocytes/enzymology ; Lymphocytes/metabolism ; Mutation ; NADPH Oxidases/metabolism ; Oxidation-Reduction ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Phosphorylation ; Serine/metabolism
    Chemical Substances Phosphoproteins ; Serine (452VLY9402) ; NADPH Oxidases (EC 1.6.3.-) ; neutrophil cytosolic factor 1 (EC 1.6.3.1) ; Cysteine (K848JZ4886) ; Alanine (OF5P57N2ZX)
    Language English
    Publishing date 2002-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1483836-9
    ISSN 1557-7716 ; 1523-0864
    ISSN (online) 1557-7716
    ISSN 1523-0864
    DOI 10.1089/152308602753625834
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 5488: Show issues Location:
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  8. Article: The leukocyte NADPH oxidase.

    Babior, Bernard M

    The Israel Medical Association journal : IMAJ

    2002  Volume 4, Issue 11, Page(s) 1023–1024

    Abstract: The leukocyte NADPH oxidase catalyzes the reduction of oxygen to O2- (superoxide) at the expense of NADPH. The O2- then dismutes to H2O2, which serves to oxidize Cl- to HOCl, a potent microbicidal agent that is used by leukocytes to kill invading ... ...

    Abstract The leukocyte NADPH oxidase catalyzes the reduction of oxygen to O2- (superoxide) at the expense of NADPH. The O2- then dismutes to H2O2, which serves to oxidize Cl- to HOCl, a potent microbicidal agent that is used by leukocytes to kill invading microorganisms. This oxidation is catalyzed by myeloperoxidase. O2 is also used to make other microbicidal oxidants, some in reactions with nitric oxide. The oxidase itself is highly complex, consisting of four unique subunits and Rac2. In the resting cell, two of the subunits, p22PHOX and gp91PHOX, are located in the membrane, and the other two, p47PHOX and p67PHOX, are in the cytosol. The electron-carrying components of the oxidase are located in gp91PHOX; the NADPH binding site is generally regarded to be in gp91PHOX as well, but there is some evidence that it may be in p67PHOX. When the oxidase is activated, p47PHOX is phosphorylated at specific sites, and the cytosolic components plus Rac2 migrate to the membrane to assemble the active oxidase.
    MeSH term(s) Humans ; Leukocytes/enzymology ; NADPH Oxidases/physiology ; Nitric Oxide/physiology ; Oxidation-Reduction
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; NADPH Oxidases (EC 1.6.3.-)
    Language English
    Publishing date 2002-11
    Publishing country Israel
    Document type Journal Article ; Review
    ZDB-ID 2008291-5
    ISSN 1565-1088 ; 0021-2180
    ISSN 1565-1088 ; 0021-2180
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: The C2A domain of JFC1 binds to 3'-phosphorylated phosphoinositides and directs plasma membrane association in living cells.

    Catz, Sergio D / Johnson, Jennifer L / Babior, Bernard M

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

    2002  Volume 99, Issue 18, Page(s) 11652–11657

    Abstract: Phosphatidylinositol 3-kinase products play a central role in the regulation of several intracellular pathways via adaptor proteins that share the ability to bind to 3'-phosphoinositides with high affinity and specificity. JFC1 is a C2 domain-containing ... ...

    Abstract Phosphatidylinositol 3-kinase products play a central role in the regulation of several intracellular pathways via adaptor proteins that share the ability to bind to 3'-phosphoinositides with high affinity and specificity. JFC1 is a C2 domain-containing protein involved in cellular trafficking that has been shown to bind 3'-phosphoinositides in vitro. In this work, we demonstrate that the C2A domain of JFC1 is the module responsible for its binding to the plasma membrane via 3'-phosphoinositides in vivo. We show that the C2A domain of JFC1 is the only domain present in this protein that localizes to the plasma membrane in living cells. Moreover, the C2A domain of JFC1 binds 3'-phosphoinositides in vitro with similar specificity as that described for full-length JFC1, suggesting that the domain mediates the specific membrane localization of the full-length protein. Furthermore, the C2A domain of JFC1 colocalized with the pleckstrin homology domain of Akt in vivo, and both the JFC1 C2A domain and the full-length JFC1 dissociated from the membrane in the presence of PI 3-kinase specific inhibitors. We also show that the association of the C2A domain to the membrane is modulated by calcium. From these results we analyze possible mechanisms for the role of JFC1 in cellular trafficking.
    MeSH term(s) 3T3 Cells ; Animals ; Base Sequence ; Binding Sites ; Calcium/metabolism ; Cell Membrane/metabolism ; DNA Primers ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mice ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositols/metabolism ; Phosphorylation
    Chemical Substances DNA Primers ; Membrane Proteins ; Phosphatidylinositols ; SYTL1 protein, human ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2002-08-20
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.172382799
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article: JFC1 is transcriptionally activated by nuclear factor-kappaB and up-regulated by tumour necrosis factor alpha in prostate carcinoma cells.

    Catz, Sergio D / Babior, Bernard M / Johnson, Jennifer L

    The Biochemical journal

    2001  Volume 367, Issue Pt 3, Page(s) 791–799

    Abstract: The human promoter region of JFC1, a phosphatidylinositol 3,4,5-trisphosphate binding ATPase, was isolated by amplification of a 549 bp region upstream of the jfc1 gene by the use of a double-PCR system. By primer extension analysis we mapped the ... ...

    Abstract The human promoter region of JFC1, a phosphatidylinositol 3,4,5-trisphosphate binding ATPase, was isolated by amplification of a 549 bp region upstream of the jfc1 gene by the use of a double-PCR system. By primer extension analysis we mapped the transcription initiation site at nucleotide -321 relative to the translation start site. Putative regulatory elements were identified in the jfc1 TATA-less promoter, including three consensus sites for nuclear factor-kappaB (NF-kappaB). We analysed the three putative NF-kappaB binding sites by gel retardation and supershift assays. Each of the putative NF-kappaB sites interacted specifically with recombinant NF-kappaB p50, and the complexes co-migrated with those formed by the NF-kappaB consensus sequence and p50. An antibody to p50 generated a supershifted complex for these NF-kappaB sites. These sites formed specific complexes with nuclear proteins from tumour necrosis factor alpha (TNFalpha)-treated WEHI 231 cells, which were supershifted with antibodies against p50 and p65. The jfc1 promoter was transcriptionally active in various cell lines, as determined by luciferase reporter assays following transfection with a jfc1 promoter luciferase vector. Co-transfection with NF-kappaB expression vectors or stimulation with TNFalpha resulted in significant transactivation of the jfc1 promoter construct, although transactivation of a mutated jfc1 promoter was negligible. The expression of a dominant negative IkappaB (inhibitor kappaB) decreased basal jfc1 promoter activity. The cell lines PC-3, LNCaP and DU-145, but not Epstein-Barr virus-transformed lymphocytes, showed a dramatic increase in the expression of JFC1 after treatment with TNFalpha, suggesting that transcriptional activation of JFC1 by the TNFalpha/NF-kappaB pathway is significant in prostate carcinoma cell lines.
    MeSH term(s) Base Sequence ; Blotting, Western ; Cloning, Molecular ; DNA ; Humans ; Male ; Membrane Proteins/genetics ; Molecular Sequence Data ; NF-kappa B/physiology ; Promoter Regions, Genetic ; Prostatic Neoplasms/metabolism ; Prostatic Neoplasms/pathology ; Recombinant Proteins/metabolism ; Transcriptional Activation/physiology ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/physiology ; Up-Regulation/physiology
    Chemical Substances Membrane Proteins ; NF-kappa B ; Recombinant Proteins ; SYTL1 protein, human ; Tumor Necrosis Factor-alpha ; DNA (9007-49-2)
    Language English
    Publishing date 2001-12-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0264-6021 ; 0006-2936 ; 0306-3275
    ISSN (online) 1470-8728
    ISSN 0264-6021 ; 0006-2936 ; 0306-3275
    DOI 10.1042/BJ20020345
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