메뉴 건너뛰기




Volumn 47, Issue 15, 2008, Pages 4427-4438

Structural features responsible for the biological stability of Histoplasma's virulence factor CBP

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOCHEMISTRY; CALCIUM; FUNGI; MACROPHAGES; MICROSTRUCTURE;

EID: 42049113174     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701495v     Document Type: Article
Times cited : (16)

References (44)
  • 1
    • 0024248054 scopus 로고
    • Fusion of lysosomes with phagosomes containing Histoplasma capsulatum: Use of fluoresceinated dextran
    • Eissenberg, L. G., and Goldman, W. E. (1988) Fusion of lysosomes with phagosomes containing Histoplasma capsulatum: Use of fluoresceinated dextran. Adv. Exp. Med. Biol. 239, 53-61.
    • (1988) Adv. Exp. Med. Biol , vol.239 , pp. 53-61
    • Eissenberg, L.G.1    Goldman, W.E.2
  • 2
    • 0027243781 scopus 로고
    • Histoplasma capsulatum modulates the acidification of phagolysosomes
    • Eissenberg, L. G., Goldman, W. E., and Schlesinger, P. H. (1993) Histoplasma capsulatum modulates the acidification of phagolysosomes. J. Exp. Med. 177, 1605-1611.
    • (1993) J. Exp. Med , vol.177 , pp. 1605-1611
    • Eissenberg, L.G.1    Goldman, W.E.2    Schlesinger, P.H.3
  • 3
    • 0034680884 scopus 로고    scopus 로고
    • Intracellular parasitism by Histoplasma capsulatum: Fungal virulence and calcium dependence
    • Sebghati, T. S., Engle, J. T., and Goldman, W. E. (2000) Intracellular parasitism by Histoplasma capsulatum: Fungal virulence and calcium dependence. Science 290, 1368-1372.
    • (2000) Science , vol.290 , pp. 1368-1372
    • Sebghati, T.S.1    Engle, J.T.2    Goldman, W.E.3
  • 4
    • 3142621221 scopus 로고    scopus 로고
    • RNA interference in Histoplasma capsulatum demonstrates a role for α-(1,3)-glucan in virulence
    • Rappleye, C. A., Engle, J. T., and Goldman, W. E. (2004) RNA interference in Histoplasma capsulatum demonstrates a role for α-(1,3)-glucan in virulence. Mol. Microbiol. 53, 153-165.
    • (2004) Mol. Microbiol , vol.53 , pp. 153-165
    • Rappleye, C.A.1    Engle, J.T.2    Goldman, W.E.3
  • 5
    • 0030731699 scopus 로고    scopus 로고
    • Calcium dependence and binding in cultures of Histoplasma capsulatum
    • Batanghari, J. W., and Goldman, W. E. (1997) Calcium dependence and binding in cultures of Histoplasma capsulatum. Infect. Immun. 65, 5257-5261.
    • (1997) Infect. Immun , vol.65 , pp. 5257-5261
    • Batanghari, J.W.1    Goldman, W.E.2
  • 7
    • 0029184233 scopus 로고
    • Determinants That Govern High-Affinity Calcium Binding
    • Means, A. R, Ed, pp, Raven Press, Ltd, New York
    • Linse, S., and Forsen, S. (1995) Determinants That Govern High-Affinity Calcium Binding, in Advances in Second Messenger and Phosphoprotein Research (Means, A. R., Ed.) pp 89-108, Raven Press, Ltd., New York.
    • (1995) Advances in Second Messenger and Phosphoprotein Research , pp. 89-108
    • Linse, S.1    Forsen, S.2
  • 8
    • 0026771336 scopus 로고
    • Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories
    • Nakayama, S., Moncrief, N. D., and Kretsinger, R. H. (1992) Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories. J. Mol. Evol. 34, 416-448.
    • (1992) J. Mol. Evol , vol.34 , pp. 416-448
    • Nakayama, S.1    Moncrief, N.D.2    Kretsinger, R.H.3
  • 9
    • 0030577844 scopus 로고    scopus 로고
    • 2+-binding proteins parvalbumin and oncomodulin and their genes: New structural and functional findings
    • 2+-binding proteins parvalbumin and oncomodulin and their genes: New structural and functional findings. Biochim. Biophys. Acta 1306, 39-54.
    • (1996) Biochim. Biophys. Acta , vol.1306 , pp. 39-54
    • Pauls, T.L.1    Cox, J.A.2    Berchtold, M.W.3
  • 10
    • 84907123709 scopus 로고
    • Quantitative plating of Histoplasma capsulatum without addition of conditioned medium or siderophores
    • Worsham, P. L., and Goldman, W. E. (1988) Quantitative plating of Histoplasma capsulatum without addition of conditioned medium or siderophores. J. Med. Vet. Mycol. 26, 137-143.
    • (1988) J. Med. Vet. Mycol , vol.26 , pp. 137-143
    • Worsham, P.L.1    Goldman, W.E.2
  • 11
    • 0036365845 scopus 로고    scopus 로고
    • Calcium Binding to Proteins Studied via Competition with Chromophoric Chelators
    • Vogel, H. J, Ed, pp, Humana Press, Totowa, NJ
    • Linse, S. (2002) Calcium Binding to Proteins Studied via Competition with Chromophoric Chelators, in Calcium-Binding Protein Protocols (Vogel, H. J., Ed.) pp 15-24, Humana Press, Totowa, NJ.
    • (2002) Calcium-Binding Protein Protocols , pp. 15-24
    • Linse, S.1
  • 14
  • 15
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • Harding, S. E, Rowe, A. J, and Horton, J. C, Eds, pp, Royal Society of Chemistry, Cambridge, U.K
    • Laue, T. M., Shah, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) Computer-aided interpretation of analytical sedimentation data for proteins, in Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.) pp 90-125, Royal Society of Chemistry, Cambridge, U.K.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 16
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro, M. M., and Bolen, D. W. (1992) A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range. Biochemistry 31, 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 18
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and comprehensive automatic analysis of large datasets
    • Chalkley, R. J., Baker, P. R., Huang, L., Hansen, K. C., Allen, N. P., Rexach, M., and Burlingame, A. L. (2005) Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and comprehensive automatic analysis of large datasets. Mol. Cell. Proteomics 4, 1194-204.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1194-1204
    • Chalkley, R.J.1    Baker, P.R.2    Huang, L.3    Hansen, K.C.4    Allen, N.P.5    Rexach, M.6    Burlingame, A.L.7
  • 19
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser, K. R., Baker, P., and Burlingame, A. L. (1999) Role of accurate mass measurement (±10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal. Chem. 71, 2871-2882.
    • (1999) Anal. Chem , vol.71 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 22
    • 0001689741 scopus 로고
    • Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity
    • Muhandiram, D. R., and Kay, L. E. (1994) Gradient-Enhanced Triple-Resonance Three-Dimensional NMR Experiments with Improved Sensitivity. J. Magn. Reson., Ser. B 103, 203-216.
    • (1994) J. Magn. Reson., Ser. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 25
    • 0001498267 scopus 로고
    • 1Hα chemical shifts in uniformly carbon-13-labeled proteins dissolved in water
    • 1Hα chemical shifts in uniformly carbon-13-labeled proteins dissolved in water. J. Am. Chem. Soc. 115, 2055-2057.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 2055-2057
    • Kay, L.E.1
  • 30
    • 0001038767 scopus 로고
    • Equilibrium Ultracentrifugation of Dilute Solutions
    • Yphantis, D. A. (1964) Equilibrium Ultracentrifugation of Dilute Solutions. Biochemistry 3, 297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 31
    • 0029055313 scopus 로고
    • LINUS: A hierarchic procedure to predict the fold of a protein
    • Srinivasan, R., and Rose, G. D. (1995) LINUS: A hierarchic procedure to predict the fold of a protein. Proteins 22, 81-99.
    • (1995) Proteins , vol.22 , pp. 81-99
    • Srinivasan, R.1    Rose, G.D.2
  • 33
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • 13C NMR chemical shifts can predict disulfide bond formation. J. Biomol. NMR 18, 165-171.
    • (2000) J. Biomol. NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 34
    • 0036882287 scopus 로고    scopus 로고
    • Protein disulfide bond determination by mass spectrometry
    • Gorman, J. J., Wallis, T. P., and Pitt, J. J. (2002) Protein disulfide bond determination by mass spectrometry. Mass Spectrom. Rev. 21, 183-216.
    • (2002) Mass Spectrom. Rev , vol.21 , pp. 183-216
    • Gorman, J.J.1    Wallis, T.P.2    Pitt, J.J.3
  • 37
    • 0028606077 scopus 로고
    • Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
    • Neet, K. E., and Timm, D. E. (1994) Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation. Protein Sci. 3, 2167-2174.
    • (1994) Protein Sci , vol.3 , pp. 2167-2174
    • Neet, K.E.1    Timm, D.E.2
  • 38
    • 0036472494 scopus 로고    scopus 로고
    • pH-dependent regulation of lysosomal calcium in macrophages
    • Christensen, K. A., Myers, J. T., and Swanson, J. A. (2002) pH-dependent regulation of lysosomal calcium in macrophages. J. Cell Sci. 115, 599-607.
    • (2002) J. Cell Sci , vol.115 , pp. 599-607
    • Christensen, K.A.1    Myers, J.T.2    Swanson, J.A.3
  • 39
    • 0028149245 scopus 로고
    • Analytical ultracentrifugation of complex macromolecular systems
    • Hansen, J. C., Lebowitz, J., and Demeler, B. (1994) Analytical ultracentrifugation of complex macromolecular systems. Biochemistry 33, 13155-13163.
    • (1994) Biochemistry , vol.33 , pp. 13155-13163
    • Hansen, J.C.1    Lebowitz, J.2    Demeler, B.3
  • 40
    • 0025212142 scopus 로고
    • Determination of size, molecular weight, and presence of subunits
    • Laue, T. M., and Rhodes, D. G. (1990) Determination of size, molecular weight, and presence of subunits. Methods Enzymol. 182, 566-587.
    • (1990) Methods Enzymol , vol.182 , pp. 566-587
    • Laue, T.M.1    Rhodes, D.G.2
  • 41
    • 15744384902 scopus 로고
    • The relationship of disulfide bonds and activity in ribonuclease
    • Resnick, H., Carter, J. R., and Kalnitsky, G. (1959) The relationship of disulfide bonds and activity in ribonuclease. J. Biol. Chem. 234, 1711-1713.
    • (1959) J. Biol. Chem , vol.234 , pp. 1711-1713
    • Resnick, H.1    Carter, J.R.2    Kalnitsky, G.3
  • 42
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace, C. N. (1990) Conformational stability of globular proteins. Trends Biochem. Sci. 15, 14-17.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 14-17
    • Pace, C.N.1
  • 43
    • 0032481105 scopus 로고    scopus 로고
    • Calcium uptake via endocytosis with rapid release from acidifying endosomes
    • Gerasimenko, J. V., Tepikin, A. V., Petersen, O. H., and Gerasimenko, O. V. (1998) Calcium uptake via endocytosis with rapid release from acidifying endosomes. Curr. Biol. 8, 1335-1338.
    • (1998) Curr. Biol , vol.8 , pp. 1335-1338
    • Gerasimenko, J.V.1    Tepikin, A.V.2    Petersen, O.H.3    Gerasimenko, O.V.4
  • 44
    • 0034522850 scopus 로고    scopus 로고
    • Monitoring phase-specific gene expression in Histoplasma capsulatum with telomeric GFP fusion plasmids
    • Kugler, S., Young, B., Miller, V. L., Goldman, W. E., Bhattacharya, A., Murthy, M. R., and Surolia, A. (2000) Monitoring phase-specific gene expression in Histoplasma capsulatum with telomeric GFP fusion plasmids. Cell Microbiol. 2, 537-547.
    • (2000) Cell Microbiol , vol.2 , pp. 537-547
    • Kugler, S.1    Young, B.2    Miller, V.L.3    Goldman, W.E.4    Bhattacharya, A.5    Murthy, M.R.6    Surolia, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.