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Volumn 1804, Issue 11, 2010, Pages 2102-2110

Conformational and biochemical characterization of a rat epididymis-specific lipocalin 12 expressed in Escherichia coli

Author keywords

Barrel; Cysteine; Disulfide bond; Epididymis; Lipocalin 12 (Lcn12); Retinoic acid

Indexed keywords

CYSTEINE; EPIDIDYMIS SPECIFIC LIPOCALIN 12; LIPOCALIN; RETINOIC ACID; UNCLASSIFIED DRUG;

EID: 77956648214     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.07.020     Document Type: Article
Times cited : (9)

References (39)
  • 1
    • 0034684237 scopus 로고    scopus 로고
    • Evolution of the lipocalin family as inferred from a protein sequence phylogeny
    • Gutierrez G., Ganfornina M.D., Sanchez D. Evolution of the lipocalin family as inferred from a protein sequence phylogeny. Biochim. Biophys. Acta 2000, 1482:35-45.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 35-45
    • Gutierrez, G.1    Ganfornina, M.D.2    Sanchez, D.3
  • 2
    • 0034684194 scopus 로고    scopus 로고
    • Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses
    • Logdberg L., Wester L. Immunocalins: a lipocalin subfamily that modulates immune and inflammatory responses. Biochim. Biophys. Acta 2000, 1482:284-297.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 284-297
    • Logdberg, L.1    Wester, L.2
  • 3
    • 0034684228 scopus 로고    scopus 로고
    • Plasma retinol binding protein: structure and function of the prototypic lipocalin
    • Newcomer M.E., Ong D.E. Plasma retinol binding protein: structure and function of the prototypic lipocalin. Biochim. Biophys. Acta 2000, 1482:57-64.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 57-64
    • Newcomer, M.E.1    Ong, D.E.2
  • 4
    • 0024588899 scopus 로고
    • Primary structure of rat brain prostaglandin D synthetase deduced from cDNA sequence
    • Urade Y., Nagata A., Suzuki Y., Fujii Y., Hayaishi O. Primary structure of rat brain prostaglandin D synthetase deduced from cDNA sequence. J. Biol. Chem. 1989, 264:1041-1045.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1041-1045
    • Urade, Y.1    Nagata, A.2    Suzuki, Y.3    Fujii, Y.4    Hayaishi, O.5
  • 5
    • 0028102760 scopus 로고
    • The lipocalin protein family: a role in cell regulation
    • Flower D.R. The lipocalin protein family: a role in cell regulation. FEBS Lett. 1994, 354:7-11.
    • (1994) FEBS Lett. , vol.354 , pp. 7-11
    • Flower, D.R.1
  • 6
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin protein family: structure and function
    • Flower D.R. The lipocalin protein family: structure and function. Biochem. J. 1996, 318(Pt 1):1-14.
    • (1996) Biochem. J. , vol.318 , Issue.PART 1 , pp. 1-14
    • Flower, D.R.1
  • 7
    • 33644506112 scopus 로고    scopus 로고
    • Comparative ligand-binding analysis of ten human lipocalins
    • Breustedt D.A., Schonfeld D.L., Skerra A. Comparative ligand-binding analysis of ten human lipocalins. Biochim. Biophys. Acta 2006, 1764:161-173.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 161-173
    • Breustedt, D.A.1    Schonfeld, D.L.2    Skerra, A.3
  • 12
    • 0032860933 scopus 로고    scopus 로고
    • Protein and ligand adaptation in a retinoic acid binding protein
    • Pattanayek R., Newcomer M.E. Protein and ligand adaptation in a retinoic acid binding protein. Protein Sci. 1999, 8:2027-2032.
    • (1999) Protein Sci. , vol.8 , pp. 2027-2032
    • Pattanayek, R.1    Newcomer, M.E.2
  • 14
    • 70350784052 scopus 로고    scopus 로고
    • Soluble expression and characterization of a mouse epididymis-specific protein lipocalin6
    • Guo C., Lian Y., Liu Q., Liu J., Zhang Y., Lin D. Soluble expression and characterization of a mouse epididymis-specific protein lipocalin6. Protein Expr Purif 2010, 69:64-67.
    • (2010) Protein Expr Purif , vol.69 , pp. 64-67
    • Guo, C.1    Lian, Y.2    Liu, Q.3    Liu, J.4    Zhang, Y.5    Lin, D.6
  • 15
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N., Strong R.K. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 2002, 10:1033-1043.
    • (2002) Mol. Cell , vol.10 , 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
  • 17
    • 73649135741 scopus 로고    scopus 로고
    • Neutrophil gelatinase-associated lipocalin (NGAL) in human neoplasias: a new protein enters the scene
    • Bolignano D., Donato V., Lacquaniti A., Fazio M.R., Bono C., Coppolino G., Buemi M. Neutrophil gelatinase-associated lipocalin (NGAL) in human neoplasias: a new protein enters the scene. Cancer Lett 2010, 288:10-16.
    • (2010) Cancer Lett , vol.288 , pp. 10-16
    • Bolignano, D.1    Donato, V.2    Lacquaniti, A.3    Fazio, M.R.4    Bono, C.5    Coppolino, G.6    Buemi, M.7
  • 19
    • 0034684216 scopus 로고    scopus 로고
    • Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase
    • Urade Y., Hayaishi O. Biochemical, structural, genetic, physiological, and pathophysiological features of lipocalin-type prostaglandin D synthase. Bba-Protein Struct M. 2000, 1482:259-271.
    • (2000) Bba-Protein Struct M. , vol.1482 , pp. 259-271
    • Urade, Y.1    Hayaishi, O.2
  • 20
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 1997, 25:4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 21
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R., Billeter M., Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph 1996, 14:51-55. 29-32.
    • (1996) J. Mol. Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 22
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 1996, 8:477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 24
    • 4544297801 scopus 로고
    • UCSF Sparky-an NMR display, annotation and assignment tool
    • Kneller D.G., Kuntz I.D. UCSF Sparky-an NMR display, annotation and assignment tool. J. Cell. Biochem. 1993, 53:254-254.
    • (1993) J. Cell. Biochem. , vol.53 , pp. 254-254
    • Kneller, D.G.1    Kuntz, I.D.2
  • 25
    • 34548149278 scopus 로고    scopus 로고
    • Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M
    • Ahnstrom J., Faber K., Axler O., Dahlback B. Hydrophobic ligand binding properties of the human lipocalin apolipoprotein M. J. Lipid Res. 2007, 48:1754-1762.
    • (2007) J. Lipid Res. , vol.48 , pp. 1754-1762
    • Ahnstrom, J.1    Faber, K.2    Axler, O.3    Dahlback, B.4
  • 27
    • 0035093398 scopus 로고    scopus 로고
    • Bacterially produced apolipoprotein D binds progesterone and arachidonic acid, but not bilirubin or E-3M2H
    • Vogt M., Skerra A. Bacterially produced apolipoprotein D binds progesterone and arachidonic acid, but not bilirubin or E-3M2H. J. Mol. Recognit. 2001, 14:79-86.
    • (2001) J. Mol. Recognit. , vol.14 , pp. 79-86
    • Vogt, M.1    Skerra, A.2
  • 28
    • 20444424624 scopus 로고    scopus 로고
    • Role of the disulphide bridge in folding, stability and function of porcine odorant binding protein: spectroscopic equilibrium studies on C63A/C155A double mutant
    • Parisi M., Mazzini A., Tibor Sorbi R., Ramoni R., Grolli S., Favilla R. Role of the disulphide bridge in folding, stability and function of porcine odorant binding protein: spectroscopic equilibrium studies on C63A/C155A double mutant. Biochim. Biophys. Acta 2005, 1750:30-39.
    • (2005) Biochim. Biophys. Acta , vol.1750 , pp. 30-39
    • Parisi, M.1    Mazzini, A.2    Tibor Sorbi, R.3    Ramoni, R.4    Grolli, S.5    Favilla, R.6
  • 29
    • 33646054876 scopus 로고    scopus 로고
    • Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin
    • Yamada Y., Nakagawa K., Yajima T., Saito K., Tokushima A., Fujiwara K., Ikeguchi M. Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin. Proteins 2006, 63:595-602.
    • (2006) Proteins , vol.63 , pp. 595-602
    • Yamada, Y.1    Nakagawa, K.2    Yajima, T.3    Saito, K.4    Tokushima, A.5    Fujiwara, K.6    Ikeguchi, M.7
  • 30
    • 55349087538 scopus 로고    scopus 로고
    • Effects of removing a conserved disulfide bond on the biological characteristics of rat lipocalin-type prostaglandin D synthase
    • Liu J., Guo C., Yao Y., Lin D. Effects of removing a conserved disulfide bond on the biological characteristics of rat lipocalin-type prostaglandin D synthase. Biochimie 2008, 90:1637-1646.
    • (2008) Biochimie , vol.90 , pp. 1637-1646
    • Liu, J.1    Guo, C.2    Yao, Y.3    Lin, D.4
  • 31
    • 46449107710 scopus 로고    scopus 로고
    • Mutant bovine odorant-binding protein: temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations
    • Marabotti A., Lefevre T., Staiano M., Crescenzo R., Varriale A., Rossi M., Pezolet M., D'Auria S. Mutant bovine odorant-binding protein: temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations. Proteins 2008, 72:769-778.
    • (2008) Proteins , vol.72 , pp. 769-778
    • Marabotti, A.1    Lefevre, T.2    Staiano, M.3    Crescenzo, R.4    Varriale, A.5    Rossi, M.6    Pezolet, M.7    D'Auria, S.8
  • 33
    • 0029562554 scopus 로고
    • The Rxr heterodimers and orphan receptors
    • Mangelsdorf D.J., Evans R.M. The Rxr heterodimers and orphan receptors. Cell 1995, 83:841-850.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 34
    • 0027441333 scopus 로고
    • Endogenous retinoids in rat epididymal tissue and rat and human spermatozoa
    • Pappas R.S., Newcomer M.E., Ong D.E. Endogenous retinoids in rat epididymal tissue and rat and human spermatozoa. Biol. Reprod. 1993, 48:235-247.
    • (1993) Biol. Reprod. , vol.48 , pp. 235-247
    • Pappas, R.S.1    Newcomer, M.E.2    Ong, D.E.3
  • 35
    • 0027081489 scopus 로고
    • Physiological and clinical aspects of vitamin-A and its metabolites
    • Goss G.D., Mcburney M.W. Physiological and clinical aspects of vitamin-A and its metabolites. Crit. Rev. Cl Lab. Sci. 1992, 29:185-215.
    • (1992) Crit. Rev. Cl Lab. Sci. , vol.29 , pp. 185-215
    • Goss, G.D.1    Mcburney, M.W.2
  • 36
    • 0030978644 scopus 로고    scopus 로고
    • Male infertility caused by epididymal dysfunction in transgenic mice expressing a dominant negative mutation of retinoic acid receptor alpha
    • Costa S.L., Boekelheide K., Vanderhyden B.C., Seth R., McBurney M.W. Male infertility caused by epididymal dysfunction in transgenic mice expressing a dominant negative mutation of retinoic acid receptor alpha. Biol. Reprod. 1997, 56:985-990.
    • (1997) Biol. Reprod. , vol.56 , pp. 985-990
    • Costa, S.L.1    Boekelheide, K.2    Vanderhyden, B.C.3    Seth, R.4    McBurney, M.W.5
  • 38
    • 0032529154 scopus 로고    scopus 로고
    • Expression, characterization and engineered specificity of rat epididymal retinoic acid-binding protein
    • Sundaram M., Sivaprasadarao A., Van Aalten D.M.F., Findlay J.B.C. Expression, characterization and engineered specificity of rat epididymal retinoic acid-binding protein. Biochem. J. 1998, 334:155-160.
    • (1998) Biochem. J. , vol.334 , pp. 155-160
    • Sundaram, M.1    Sivaprasadarao, A.2    Van Aalten, D.M.F.3    Findlay, J.B.C.4
  • 39
    • 0030048046 scopus 로고    scopus 로고
    • A simple assay for intracellular lipid-binding proteins using displacement of 1-anilinonaphthalene 8-sulfonic acid
    • Kane C.D., Bernlohr D.A. A simple assay for intracellular lipid-binding proteins using displacement of 1-anilinonaphthalene 8-sulfonic acid. Anal. Biochem. 1996, 233:197-204.
    • (1996) Anal. Biochem. , vol.233 , pp. 197-204
    • Kane, C.D.1    Bernlohr, D.A.2


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