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Volumn 19, Issue 12, 2011, Pages 1796-1806

Galline Ex-FABP is an antibacterial siderocalin and a lysophosphatidic acid sensor functioning through dual ligand specificities

Author keywords

[No Author keywords available]

Indexed keywords

GALLINE EXTRACELLULAR FATTY ACID BINDING PROTEIN; LYSOPHOSPHATIDIC ACID; SIDEROPHORE; UNCLASSIFIED DRUG;

EID: 82955193818     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.09.019     Document Type: Article
Times cited : (31)

References (49)
  • 4
    • 49949098676 scopus 로고    scopus 로고
    • Two pathways for lysophosphatidic acid production
    • J. Aoki, A. Inoue, and S. Okudaira Two pathways for lysophosphatidic acid production Biochim. Biophys. Acta 1781 2008 513 518
    • (2008) Biochim. Biophys. Acta , vol.1781 , pp. 513-518
    • Aoki, J.1    Inoue, A.2    Okudaira, S.3
  • 6
    • 0011956652 scopus 로고
    • Miscellaneous bacterial diseases
    • B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald, Y.M. Saif, Iowa State University Press Ames, IA
    • H.J. Barnes Miscellaneous bacterial diseases B.W. Calnek, H.J. Barnes, C.W. Beard, L.R. McDougald, Y.M. Saif, Diseases of Poultry 1991 Iowa State University Press Ames, IA 289 293
    • (1991) Diseases of Poultry , pp. 289-293
    • Barnes, H.J.1
  • 8
    • 0025011945 scopus 로고
    • The Ch21 protein, developmentally regulated in chick embryo, belongs to the superfamily of lipophilic molecule carrier proteins
    • F.D. Cancedda, B. Dozin, F. Rossi, F. Molina, R. Cancedda, A. Negri, and S. Ronchi The Ch21 protein, developmentally regulated in chick embryo, belongs to the superfamily of lipophilic molecule carrier proteins J. Biol. Chem. 265 1990 19060 19064
    • (1990) J. Biol. Chem. , vol.265 , pp. 19060-19064
    • Cancedda, F.D.1    Dozin, B.2    Rossi, F.3    Molina, F.4    Cancedda, R.5    Negri, A.6    Ronchi, S.7
  • 11
    • 67651244131 scopus 로고    scopus 로고
    • Siderocalins: Siderophore-binding proteins of the innate immune system
    • M.C. Clifton, C. Corrent, and R.K. Strong Siderocalins: siderophore-binding proteins of the innate immune system Biometals 22 2009 557 564
    • (2009) Biometals , vol.22 , pp. 557-564
    • Clifton, M.C.1    Corrent, C.2    Strong, R.K.3
  • 14
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • DOI 10.1016/j.str.2004.03.008, PII S0969212604000887
    • Z.S. Derewenda Rational protein crystallization by mutational surface engineering Structure 12 2004 529 535 (Pubitemid 38447156)
    • (2004) Structure , vol.12 , Issue.4 , pp. 529-535
    • Derewenda, Z.S.1
  • 17
    • 0036812926 scopus 로고    scopus 로고
    • Ex-FABP, extracellular fatty acid binding protein, is a stress lipocalin expressed during chicken embryo development
    • DOI 10.1023/A:1020548118241
    • F. Descalzi Cancedda, B. Dozin, B. Zerega, S. Cermelli, C. Gentili, and R. Cancedda Ex-FABP, extracellular fatty acid binding protein, is a stress lipocalin expressed during chicken embryo development Mol. Cell. Biochem. 239 2002 221 225 (Pubitemid 35385813)
    • (2002) Molecular and Cellular Biochemistry , vol.239 , Issue.1-2 , pp. 221-225
    • Descalzi Cancedda, F.1    Dozin, B.2    Zerega, B.3    Cermelli, S.4    Gentili, C.5    Cancedda, R.6
  • 18
    • 0043270446 scopus 로고    scopus 로고
    • Inhibition of cell proliferation and induction of apoptosis by ExFABP gene targeting
    • DOI 10.1002/jcp.10310
    • E. Di Marco, N. Sessarego, B. Zerega, R. Cancedda, and F.D. Cancedda Inhibition of cell proliferation and induction of apoptosis by ExFABP gene targeting J. Cell. Physiol. 196 2003 464 473 (Pubitemid 36927741)
    • (2003) Journal of Cellular Physiology , vol.196 , Issue.3 , pp. 464-473
    • Di Marco, E.1    Sessarego, N.2    Zerega, B.3    Cancedda, R.4    Cancedda, F.D.5
  • 21
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • W116-8
    • J. Dundas, Z. Ouyang, J. Tseng, A. Binkowski, Y. Turpaz, and J. Liang CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues Nucleic Acids Res. 34 Web Server issue 2006 W116-8
    • (2006) Nucleic Acids Res. , vol.34 , Issue.WEB SERVER ISSUE
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 23
    • 33646593180 scopus 로고    scopus 로고
    • How pathogenic bacteria evade mammalian sabotage in the battle for iron
    • DOI 10.1038/nchembio771, PII NCHEMBIO771
    • M.A. Fischbach, H. Lin, D.R. Liu, and C.T. Walsh How pathogenic bacteria evade mammalian sabotage in the battle for iron Nat. Chem. Biol. 2 2006 132 138 (Pubitemid 44323863)
    • (2006) Nature Chemical Biology , vol.2 , Issue.3 , pp. 132-138
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 25
    • 0028102760 scopus 로고
    • The lipocalin protein family: A role in cell regulation
    • DOI 10.1016/0014-5793(94)01078-1
    • D.R. Flower The lipocalin protein family: a role in cell regulation FEBS Lett. 354 1994 7 11 (Pubitemid 24331695)
    • (1994) FEBS Letters , vol.354 , Issue.1 , pp. 7-11
    • Flower, D.R.1
  • 28
    • 0034728351 scopus 로고    scopus 로고
    • Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin
    • DOI 10.1021/bi992215v
    • D.H. Goetz, S.T. Willie, R.S. Armen, T. Bratt, N. Borregaard, and R.K. Strong Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin Biochemistry 39 2000 1935 1941 (Pubitemid 30124000)
    • (2000) Biochemistry , vol.39 , Issue.8 , pp. 1935-1941
    • Goetz, D.H.1    Willie, S.T.2    Armen, R.S.3    Bratt, T.4    Borregaard, N.5    Strong, R.K.6
  • 29
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • DOI 10.1016/S1097-2765(02)00708-6
    • D.H. Goetz, M.A. Holmes, N. Borregaard, M.E. Bluhm, K.N. Raymond, and R.K. Strong The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition Mol. Cell 10 2002 1033 1043 (Pubitemid 36001971)
    • (2002) Molecular Cell , vol.10 , Issue.5 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 31
    • 0141792417 scopus 로고    scopus 로고
    • Cell transformation by the v-myc oncogene abrogates c-Myc/Max-mediated suppression of a C/EBPβ-dependent lipocalin gene
    • DOI 10.1016/j.jmb.2003.08.018
    • M. Hartl, T. Matt, W. Schüler, G. Siemeister, G. Kontaxis, K. Kloiber, R. Konrat, and K. Bister Cell transformation by the v-myc oncogene abrogates c-Myc/Max-mediated suppression of a C/EBP beta-dependent lipocalin gene J. Mol. Biol. 333 2003 33 46 (Pubitemid 37153263)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.1 , pp. 33-46
    • Hartl, M.1    Matt, T.2    Schuler, W.3    Siemeister, G.4    Kontaxis, G.5    Kloiber, K.6    Konrat, R.7    Bister, K.8
  • 32
    • 67749095021 scopus 로고    scopus 로고
    • The role of electrostatics in siderophore recognition by the immunoprotein Siderocalin
    • T.M. Hoette, R.J. Abergel, J. Xu, R.K. Strong, and K.N. Raymond The role of electrostatics in siderophore recognition by the immunoprotein Siderocalin J. Am. Chem. Soc. 130 2008 17584 17592
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 17584-17592
    • Hoette, T.M.1    Abergel, R.J.2    Xu, J.3    Strong, R.K.4    Raymond, K.N.5
  • 33
    • 11844301598 scopus 로고    scopus 로고
    • Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration
    • DOI 10.1016/j.str.2004.10.009, PII S0969212604003831
    • M.A. Holmes, W. Paulsene, X. Jide, C. Ratledge, and R.K. Strong Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration Structure 13 2005 29 41 (Pubitemid 40092472)
    • (2005) Structure , vol.13 , Issue.1 , pp. 29-41
    • Holmes, M.A.1    Paulsene, W.2    Jide, X.3    Ratledge, C.4    Strong, R.K.5
  • 34
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • DOI 10.1006/abio.1996.0238
    • P. Kuzmic Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase Anal. Biochem. 237 1996 260 273 (Pubitemid 26177089)
    • (1996) Analytical Biochemistry , vol.237 , Issue.2 , pp. 260-273
    • Kuzmic, P.1
  • 39
    • 0023231674 scopus 로고
    • Cluster of genes controlling synthesis and activation of 2,3-dihydroxybenzoic acid in production of enterobactin in Escherichia coli
    • M.S. Nahlik, T.P. Fleming, and M.A. McIntosh Cluster of genes controlling synthesis and activation of 2,3-dihydroxybenzoic acid in production of enterobactin in Escherichia coli J. Bacteriol. 169 1987 4163 4170 (Pubitemid 17145736)
    • (1987) Journal of Bacteriology , vol.169 , Issue.9 , pp. 4163-4170
    • Nahlik, M.S.1    Fleming, T.P.2    McIntosh, M.A.3
  • 40
    • 0035036305 scopus 로고    scopus 로고
    • Hen egg yolk and white contain high amounts of lysophosphatidic acids, growth factor-like lipids: Distinct molecular species compositions
    • S. Nakane, A. Tokumura, K. Waku, and T. Sugiura Hen egg yolk and white contain high amounts of lysophosphatidic acids, growth factor-like lipids: distinct molecular species compositions Lipids 36 2001 413 419 (Pubitemid 32433878)
    • (2001) Lipids , vol.36 , Issue.4 , pp. 413-419
    • Nakane, S.1    Tokumura, A.2    Waku, K.3    Sugiura, T.4
  • 42
    • 0033040796 scopus 로고    scopus 로고
    • Tick histamine-binding proteins: Isolation, cloning, and three-dimensional structure
    • G.C. Paesen, P.L. Adams, K. Harlos, P.A. Nuttall, and D.I. Stuart Tick histamine-binding proteins: isolation, cloning, and three-dimensional structure Mol. Cell 3 1999 661 671
    • (1999) Mol. Cell , vol.3 , pp. 661-671
    • Paesen, G.C.1    Adams, P.L.2    Harlos, K.3    Nuttall, P.A.4    Stuart, D.I.5
  • 47
    • 0023067325 scopus 로고
    • Biophysical aspects of antigen recognition by T cells
    • T.H. Watts, and H. McConnell Biophysical aspects of antigen recognition by T cells Annu. Rev. Immunol. 5 1987 461 475
    • (1987) Annu. Rev. Immunol. , vol.5 , pp. 461-475
    • Watts, T.H.1    McConnell, H.2
  • 49
    • 0036634367 scopus 로고    scopus 로고
    • New insights into the structure and function of fatty acid-binding proteins
    • A.W. Zimmerman, and J.H. Veerkamp New insights into the structure and function of fatty acid-binding proteins Cell. Mol. Life Sci. 59 2002 1096 1116
    • (2002) Cell. Mol. Life Sci. , vol.59 , pp. 1096-1116
    • Zimmerman, A.W.1    Veerkamp, J.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.