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Volumn 12, Issue 5, 2003, Pages 973-981

Backbone 15N relaxation analysis of the N-terminal domain of the HTLV-I capsid protein and comparison with the capsid protein of HIV-1

Author keywords

Capsid protein; CyP A; HTLV I; Mutant; NMR spectroscopy; Relaxation; Retrovirus

Indexed keywords

CAPSID PROTEIN;

EID: 0242515819     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0235903     Document Type: Article
Times cited : (8)

References (31)
  • 1
    • 0031985780 scopus 로고    scopus 로고
    • Cells with high cyclophilin A content support replication of human immunodeficiency virus type-1 gag mutants with decreased ability to incorporate cyclophilin A
    • Ackerson, B., Rey, O., Canon, J., and Krogstard, P. 1998. Cells with high cyclophilin A content support replication of human immunodeficiency virus type-1 gag mutants with decreased ability to incorporate cyclophilin A. J. Virol. 72: 303-308.
    • (1998) J. Virol. , vol.72 , pp. 303-308
    • Ackerson, B.1    Rey, O.2    Canon, J.3    Krogstard, P.4
  • 2
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected 2-dimensional NMR spectroscopy - The central helix is flexible
    • 15N relaxation using inverse detected 2-dimensional NMR spectroscopy - The central helix is flexible. Biochemistry 31: 5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 3
    • 0001594959 scopus 로고
    • Optimized recording of heteronuclear multidimensional NMR-spectra using pulsed field gradients
    • Bax, A. and Pochapsky, S.S. 1992. Optimized recording of heteronuclear multidimensional NMR-spectra using pulsed field gradients. J. Magn. Reson. 99: 638-642.
    • (1992) J. Magn. Reson. , vol.99 , pp. 638-642
    • Bax, A.1    Pochapsky, S.S.2
  • 4
    • 0029949799 scopus 로고    scopus 로고
    • Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type-1 before the initiation of reverse transcription
    • Braaten, D., Franke, E.K., and Luban, J. 1996. Cyclophilin A is required for an early step in the life cycle of human immunodeficiency virus type-1 before the initiation of reverse transcription. J. Virol. 70: 3551-3560.
    • (1996) J. Virol. , vol.70 , pp. 3551-3560
    • Braaten, D.1    Franke, E.K.2    Luban, J.3
  • 5
    • 0019820314 scopus 로고
    • Theory for nuclear magnetic-relaxation of probes in anisotropic systems - Application to cholesterol in phospholipidvesicles
    • Brainard, J.R. and Szabo, A. 1981. Theory for nuclear magnetic-relaxation of probes in anisotropic systems - Application to cholesterol in phospholipidvesicles. Biochemistry 20: 4618-4628.
    • (1981) Biochemistry , vol.20 , pp. 4618-4628
    • Brainard, J.R.1    Szabo, A.2
  • 6
    • 0029103178 scopus 로고
    • Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1
    • Campbell, S. and Vogt, V.M. 1995. Self-assembly in vitro of purified CA-NC proteins from Rous sarcoma virus and human immunodeficiency virus type 1. J. Virol. 69: 6487-6497.
    • (1995) J. Virol. , vol.69 , pp. 6487-6497
    • Campbell, S.1    Vogt, V.M.2
  • 7
    • 0033543151 scopus 로고    scopus 로고
    • Backbone dynamics of the N-terminal domain of the HIV-1 capsid protein and comparison with the G94D mutant conferring cyclosporin resistance/dependence
    • Campos-Olivas, R. and Summers, M.F. 1999. Backbone dynamics of the N-terminal domain of the HIV-1 capsid protein and comparison with the G94D mutant conferring cyclosporin resistance/dependence. Biochemistry 38: 10262-10271.
    • (1999) Biochemistry , vol.38 , pp. 10262-10271
    • Campos-Olivas, R.1    Summers, M.F.2
  • 9
    • 0035793720 scopus 로고    scopus 로고
    • Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
    • Cornilescu, C.C., Bouamr, F., Yao, X., Carter, C., and Tjandra, N. 2001. Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein. J. Mol. Biol. 306: 783-797.
    • (2001) J. Mol. Biol. , vol.306 , pp. 783-797
    • Cornilescu, C.C.1    Bouamr, F.2    Yao, X.3    Carter, C.4    Tjandra, N.5
  • 10
    • 0029400480 scopus 로고
    • NMRPIPE - A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPIPE - A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6: 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 11
    • 0034328380 scopus 로고    scopus 로고
    • HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
    • de la Torre, J.G., Huertas, M.L., and Carrasco, B. 2000. HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. J. Magn. Reson. 147: 138-146.
    • (2000) J. Magn. Reson. , vol.147 , pp. 138-146
    • De la Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 12
    • 0000041361 scopus 로고
    • A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett, D.S., Powers, R., Gronenborn, A.M., and Clore, G.M. 1991. A common-sense approach to peak picking in 2-dimensional, 3-dimensional, and 4-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95: 214-220.
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 13
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti, R.K., Lee, B.M., Walker, J., Summers, M.F., Yoo, S., and Sundquist, W.I. 1996. Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 273: 231-235.
    • (1996) Science , vol.273 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5    Sundquist, W.I.6
  • 14
    • 0031954466 scopus 로고    scopus 로고
    • N-Terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles
    • Gross, I., Hohenberg, H., Huckagel, C., and Krausslich, H.G. 1998. N-Terminal extension of human immunodeficiency virus capsid protein converts the in vitro assembly phenotype from tubular to spherical particles. J. Virol. 72: 4798-4810.
    • (1998) J. Virol. , vol.72 , pp. 4798-4810
    • Gross, I.1    Hohenberg, H.2    Huckagel, C.3    Krausslich, H.G.4
  • 17
    • 0027787894 scopus 로고
    • 2O in protein NMR - Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR - Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115: 12593-12594.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
  • 18
    • 0032781006 scopus 로고    scopus 로고
    • Solution structure of the capsid protein from the human T-cell leukemia virus type-1
    • Khorasanizadeh, S., Campos-Olivas, R., and Summers, M.F. 1999. Solution structure of the capsid protein from the human T-cell leukemia virus type-1. J. Mol. Biol. 291: 491-505.
    • (1999) J. Mol. Biol. , vol.291 , pp. 491-505
    • Khorasanizadeh, S.1    Campos-Olivas, R.2    Summers, M.F.3
  • 19
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wuthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14: 51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 20
    • 0033577288 scopus 로고    scopus 로고
    • A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy
    • Loria, J.P., Rance, M., and Palmer III, A.G. 1999. A relaxation-compensated Carr-Purcell-Meiboom-Gill sequence for characterizing chemical exchange by NMR spectroscopy. J. Am. Chem. Soc. 121: 2331-2332.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2331-2332
    • Loria, J.P.1    Rance, M.2    Palmer A.G. III3
  • 21
    • 0027207885 scopus 로고
    • Human-immunodeficiency-virus type-1 gag protein binds to cyclophilin-A and cyclophilin-B
    • Luban, J., Bossolt, K.L., Franke, E.K., Kalpana, G.V., and Goff, S. 1993, Human-immunodeficiency-virus type-1 gag protein binds to cyclophilin-A and cyclophilin-B. Cell 73: 1067-1078.
    • (1993) Cell , vol.73 , pp. 1067-1078
    • Luban, J.1    Bossolt, K.L.2    Franke, E.K.3    Kalpana, G.V.4    Goff, S.5
  • 22
    • 0001475618 scopus 로고
    • Improved accuracy of heteronuclear transverse relaxation-time measurements in macromolecules - Elimination of antiphase contributions
    • Peng, J.W., Thanabal, V., and Wagner, G. 1991. Improved accuracy of heteronuclear transverse relaxation-time measurements in macromolecules - Elimination of antiphase contributions. J. Magn. Reson. 95: 421-427.
    • (1991) J. Magn. Reson. , vol.95 , pp. 421-427
    • Peng, J.W.1    Thanabal, V.2    Wagner, G.3
  • 23
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous-solutions
    • Piotto, M., Saudek, V., and Sklenar, V. 1992. Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous-solutions. J. Biomol. NMR 2: 661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 24
    • 0023041382 scopus 로고
    • Enzymatic recycling of clathrin from coated vesicles
    • Rothman, J.E. and Schmid, S.L. 1986. Enzymatic recycling of clathrin from coated vesicles. Cell 46: 5-9.
    • (1986) Cell , vol.46 , pp. 5-9
    • Rothman, J.E.1    Schmid, S.L.2
  • 25
    • 0036294666 scopus 로고    scopus 로고
    • Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein
    • Tang, C., Ndassa, Y., and Summers, M.F. 2002. Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein. Nat. Struct. Biol. 9: 537-543.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 537-543
    • Tang, C.1    Ndassa, Y.2    Summers, M.F.3
  • 31
    • 33644625296 scopus 로고
    • Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion
    • Woessner, D.E. 1962. Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion. J. Chem. Phys. 36: 647-654.
    • (1962) J. Chem. Phys. , vol.36 , pp. 647-654
    • Woessner, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.