메뉴 건너뛰기




Volumn 98, Issue 12, 2010, Pages 2933-2942

Crystal structure and trimer-monomer transition of N-terminal domain of EhCaBP1 from entamoeba histolytica

Author keywords

[No Author keywords available]

Indexed keywords

ENTAMOEBA HISTOLYTICA;

EID: 77953602224     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.03.048     Document Type: Article
Times cited : (11)

References (31)
  • 1
    • 0031087498 scopus 로고    scopus 로고
    • WHO/PAHO/UNESCO. 1997. WHO/PAHO/UNESCO report. A consultation with experts on amoebiasis. Mexico City, Mexico 28-29 January
    • WHO/PAHO/UNESCO. 1997. WHO/PAHO/UNESCO report. A consultation with experts on amoebiasis. Mexico City, Mexico 28-29 January, 1997. Epidemiol. Bull. 18: 13-14.
    • (1997) Epidemiol. Bull. , vol.18 , pp. 13-14
  • 2
    • 0031087498 scopus 로고    scopus 로고
    • A consultation with experts on Amoebiasis
    • WHO/PAHO/UNESCO report (WHO, Mexico)
    • WHO/PAHO/UNESCO report (WHO, Mexico). 1997. A consultation with experts on Amoebiasis. Epidemiol. Bull. 18: 13-14.
    • (1997) Epidemiol. Bull. , vol.18 , pp. 13-14
  • 3
    • 0037460789 scopus 로고    scopus 로고
    • Amoebiasis
    • Stanley, Jr., S. L. 2003. Amoebiasis. Lancet. 361: 1025-1034.
    • (2003) Lancet. , vol.361 , pp. 1025-1034
    • Stanley Jr., S.L.1
  • 6
    • 4444262526 scopus 로고    scopus 로고
    • Calcium binding protein 1 of the protozoan parasite Entamoeba histolytica interacts with actin and is involved in cytoskeleton dynamics
    • DOI 10.1242/jcs.01198
    • Sahoo, N., E. Labruyère, ..., A. Bhattacharya. 2004. Calcium binding protein 1 of the protozoan parasite Entamoeba histolytica interacts with actin and is involved in cytoskeleton dynamics. J. Cell Sci. 117: 3625-3634. (Pubitemid 39206402)
    • (2004) Journal of Cell Science , vol.117 , Issue.16 , pp. 3625-3634
    • Sahoo, N.1    Labruyere, E.2    Bhattacharya, S.3    Sen, P.4    Guillen, N.5    Bhattacharya, A.6
  • 7
    • 34548775107 scopus 로고    scopus 로고
    • Crystal structure of calcium binding protein-1 from Entamoeba histolytica: A novel arrangement of EF hand motifs
    • DOI 10.1002/prot.21455
    • Kumar, S., N. Padhan,...., S. Gourinath. 2007. Crystal structure of calcium binding protein-1 from Entamoeba histolytica: a novel arrangement of EF hand motifs. Proteins. 68: 990-998. (Pubitemid 47434720)
    • (2007) Proteins: Structure, Function and Genetics , vol.68 , Issue.4 , pp. 990-998
    • Kumar, S.1    Padhan, N.2    Alam, N.3    Gourinath, S.4
  • 8
    • 0035807933 scopus 로고    scopus 로고
    • NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica
    • Atreya, H. S., S. C. Sahu,...,G. Govil. 2001. NMR derived solution structure of an EF-hand calcium-binding protein from Entamoeba Histolytica. Biochemistry. 40: 14392-14403.
    • (2001) Biochemistry. , vol.40 , pp. 14392-14403
    • Atreya, H.S.1    Sahu, S.C.2    Govil, G.3
  • 9
    • 0021881565 scopus 로고
    • Three-dimensional structure of calmodulin
    • Babu, Y. S., J. S. Sack,..., W. J. Cook. 1985. Three-dimensional structure of calmodulin. Nature. 315: 37-40.
    • (1985) Nature. , vol.315 , pp. 37-40
    • Babu, Y.S.1    Sack, J.S.2    Cook, W.J.3
  • 10
    • 67649171021 scopus 로고    scopus 로고
    • N- And C-terminal domains of the calcium binding protein EhCaBP1 of the parasite Entamoeba histolytica display distinct functions
    • Jain, R., S. Kumar, ..., A. Bhattacharya. 2009. N- and C-terminal domains of the calcium binding protein EhCaBP1 of the parasite Entamoeba histolytica display distinct functions. PLoS One. 4: e5269.
    • (2009) PLoS One. , vol.4
    • Jain, R.1    Kumar, S.2    Bhattacharya, A.3
  • 12
    • 0027236831 scopus 로고
    • The calcium binding protein of Entamoeba histolytica: Expression in Escherichia coli and immunochemical characterization
    • Prasad, J., S. Bhattacharya, and A. Bhattacharya. 1993. The calcium binding protein of Entamoeba histolytica: expression in Escherichia coli and immunochemical characterization. Cell. Mol. Biol. Res. 39: 167-175. (Pubitemid 23267353)
    • (1993) Cellular and Molecular Biology Research , vol.39 , Issue.2 , pp. 167-175
    • Prasad, J.1    Bhatracharya, S.2    Bhattacharya, A.3
  • 13
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, Jr., W. C. 1990. Protein secondary structure and circular dichroism: a practical guide. Proteins. 7: 205-214.
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 19
    • 0036153595 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of stem bromelain at low pH
    • Haq, S. K., S. Rasheedi, and R. H. Khan. 2002. Characterization of a partially folded intermediate of stem bromelain at low pH. Eur. J. Biochem. 269: 47-52.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 47-52
    • Haq, S.K.1    Rasheedi, S.2    Khan, R.H.3
  • 20
    • 1842424800 scopus 로고    scopus 로고
    • Identification and characterization of EhCaBP2: A second member of the calcium-binding protein family of the protozoan parasite Entamoeba histolytica
    • DOI 10.1074/jbc.M304716200
    • Chakrabarty, P., D. K. Sethi,..., A. Bhattacharya. 2004. Identification and characterization of EhCaBP1. A second member of the calciumbinding protein family of the protozoan parasite Entamoeba histolytica. J. Biol. Chem. 279: 12898-12908. (Pubitemid 38445865)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12898-12908
    • Chakrabarty, P.1    Sethi, D.K.2    Padhan, N.3    Kaur, K.J.4    Salunke, D.M.5    Bhattacharya, S.6    Bhattacharya, A.7
  • 21
    • 0030586823 scopus 로고    scopus 로고
    • Checking your imagination: Applications of the free R value
    • Kleywegt, G. J., and A. T. Brünger. 1996. Checking your imagination: applications of the free R value. Structure, 4: 897-904.
    • (1996) Structure , vol.4 , pp. 897-904
    • Kleywegt, G.J.1    Brünger, A.T.2
  • 22
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular diehroism spectra using an unsupervised learning neural network
    • Andrade, M. A., P. Chacón,...., F. Morán. 1993. Evaluation of secondary structure of proteins from UV circular diehroism spectra using an unsupervised learning neural network. Protein Eng. 6: 383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Morán, F.3
  • 24
    • 0013800421 scopus 로고
    • The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites
    • Stryer, L. 1965. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescent probe of non-polar binding sites. J. Mol. Biol. 13: 482-495.
    • (1965) J. Mol. Biol. , vol.13 , pp. 482-495
    • Stryer, L.1
  • 25
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., C. N. Pace, and J. M. Scholtz. 1995. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4: 2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 26
    • 43449100343 scopus 로고    scopus 로고
    • Calcium-binding protein 1 of Entamoeba histolytica transiently associates with phagocytic cups in a calcium-independent manner
    • DOI 10.1111/j.1462-5822.2008.01134.x
    • Jain, R., J. Santi-Rocca,..., A. Bhattacharya. 2008. Calcium-binding protein 1 of Entamoeba histolytica transiently associates with phagocytic cups in a calcium-independent manner. Cell. Microbiol. 10: 1373-1389. (Pubitemid 351663927)
    • (2008) Cellular Microbiology , vol.10 , Issue.6 , pp. 1373-1389
    • Jain, R.1    Santi-Rocca, J.2    Padhan, N.3    Bhattacharya, S.4    Guillen, N.5    Bhattacharya, A.6
  • 27
    • 0018110116 scopus 로고
    • Prediction of the secondary structure of proteins from their amino acid sequence
    • Chou, P. Y., and G. D. Fasman. 1978. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol. Relat. Areas Mol. Biol. 47: 45-148.
    • (1978) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.47 , pp. 45-148
    • Chou, P.Y.1    Fasman, G.D.2
  • 28
    • 0025681523 scopus 로고
    • α-helix to random coil transitions of two-chain coiled coils: Experiments on the thermal denaturation of isolated segments of α α-tropomyosin
    • Holtzer, M. E., and A. Holtzer. 1990. α-helix to random coil transitions of two-chain coiled coils: experiments on the thermal denaturation of isolated segments of α α-tropomyosin. Biopolymers. 30: 985-993.
    • (1990) Biopolymers. , vol.30 , pp. 985-993
    • Holtzer, M.E.1    Holtzer, A.2
  • 29
    • 33646761687 scopus 로고    scopus 로고
    • Structural basis for diversity of the EF-hand calcium-binding proteins
    • DOI 10.1016/j.jmb.2006.03.066, PII S0022283606004475
    • Grabarek, Z. 2006. Structural basis for diversity of the EF-hand calcium-binding proteins. J. Mol. Biol. 359: 509-525. (Pubitemid 43767271)
    • (2006) Journal of Molecular Biology , vol.359 , Issue.3 , pp. 509-525
    • Grabarek, Z.1
  • 31
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Petersen, E. F., T. D. Goddard,..., T. E. Ferrin. 2004. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25: 1605-1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Petersen, E.F.1    Goddard, T.D.2    Ferrin, T.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.