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This study characterizes the CBP virulence factor biochemically and establishes the parameters for calcium binding as well as the folding and multimeric state of CBP. The CBP protein is surprisingly resistant to proteolysis and other harsh treatments that the authors suggest contribute to its function within the phagolysosome.
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Beck M.R., Dekoster G.T., Hambly D.M., Gross M.L., Cistola D.P., and Goldman W.E. Structural features responsible for the biological stability of Histoplasma's virulence factor CBP. Biochemistry 47 (2008) 4427-4438. This study characterizes the CBP virulence factor biochemically and establishes the parameters for calcium binding as well as the folding and multimeric state of CBP. The CBP protein is surprisingly resistant to proteolysis and other harsh treatments that the authors suggest contribute to its function within the phagolysosome.
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(2008)
Biochemistry
, vol.47
, pp. 4427-4438
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Beck, M.R.1
Dekoster, G.T.2
Hambly, D.M.3
Gross, M.L.4
Cistola, D.P.5
Goldman, W.E.6
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44
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48749126518
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Beck MR, DeKoster GT, Cistola DP, Goldman WE: NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. 2008, submitted for publication
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Beck MR, DeKoster GT, Cistola DP, Goldman WE: NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B. 2008, submitted for publication. This study describes the first high-resolution structure of a fungal virulence protein. The authors' use of structure-based comparisons instead of amino acid sequence identify CBP as a member of the saposin-like protein family, revealing an unsuspected role for CBP in lipid interactions.
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45
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34548563758
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Production of extracellular proteolytic activity by Histoplasma capsulatum grown in Histoplasma-macrophage medium is limited to restriction fragment length polymorphism class 1 isolates
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Zarnowski R., Connolly P.A., Wheat L.J., and Woods J.P. Production of extracellular proteolytic activity by Histoplasma capsulatum grown in Histoplasma-macrophage medium is limited to restriction fragment length polymorphism class 1 isolates. Diagn Microbiol Infect Dis 59 (2007) 39-47
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(2007)
Diagn Microbiol Infect Dis
, vol.59
, pp. 39-47
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Zarnowski, R.1
Connolly, P.A.2
Wheat, L.J.3
Woods, J.P.4
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46
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0032702583
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Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum
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Timmerman M.M., and Woods J.P. Ferric reduction is a potential iron acquisition mechanism for Histoplasma capsulatum. Infect Immun 67 (1999) 6403-6408
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(1999)
Infect Immun
, vol.67
, pp. 6403-6408
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Timmerman, M.M.1
Woods, J.P.2
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47
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0034059728
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Hydroxamate siderophores of Histoplasma capsulatum
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Howard D.H., Rafie R., Tiwari A., and Faull K.F. Hydroxamate siderophores of Histoplasma capsulatum. Infect Immun 68 (2000) 2338-2343
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(2000)
Infect Immun
, vol.68
, pp. 2338-2343
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Howard, D.H.1
Rafie, R.2
Tiwari, A.3
Faull, K.F.4
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48
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0035189288
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Potential role for extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum
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Timmerman M.M., and Woods J.P. Potential role for extracellular glutathione-dependent ferric reductase in utilization of environmental and host ferric compounds by Histoplasma capsulatum. Infect Immun 69 (2001) 7671-7678
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(2001)
Infect Immun
, vol.69
, pp. 7671-7678
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Timmerman, M.M.1
Woods, J.P.2
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49
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22144479376
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Glutathione-dependent extracellular ferric reductase activities in dimorphic zoopathogenic fungi
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Zarnowski R., and Woods J.P. Glutathione-dependent extracellular ferric reductase activities in dimorphic zoopathogenic fungi. Microbiology 151 (2005) 2233-2240
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(2005)
Microbiology
, vol.151
, pp. 2233-2240
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Zarnowski, R.1
Woods, J.P.2
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