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Volumn 38, Issue 5, 2005, Pages 550-554

Solution structure of YKR049C, a putative redox protein from Saccharomyces cerevisiae

Author keywords

NMR spectroscopy; Saccharomyces cerevisiae; Structural proteomics; Thioredoxin fold

Indexed keywords

CANDIDA ALBICANS; SACCHAROMYCES CEREVISIAE;

EID: 32644432511     PISSN: 12258687     EISSN: 12258687     Source Type: Journal    
DOI: 10.5483/bmbrep.2005.38.5.550     Document Type: Article
Times cited : (18)

References (22)
  • 2
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • Baker, N. A., Sept, D., Joseph, S., Holst, M. J. and McCammon, J. A. (2001) Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98, 10037-10041.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 5
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., Delaglio, F. and Bax, A. (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 6
    • 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
  • 7
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard, T. D. and Kneller, D. G. SPARKY 3, University of California, San Francisco.
    • SPARKY , vol.3
    • Goddard, T.D.1    Kneller, D.G.2
  • 8
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Hermann, T., Guntert, P. and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Hermann, T.1    Guntert, P.2    Wüthrich, K.3
  • 9
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. and Sander, C. (1993) Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 10
    • 0029644246 scopus 로고
    • Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide
    • Holmgren, A. (1995) Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide. Structure 3, 239-243.
    • (1995) Structure , vol.3 , pp. 239-243
    • Holmgren, A.1
  • 12
    • 0030624544 scopus 로고    scopus 로고
    • NMR methods for the study of protein structure and dynamics
    • Kay, L. E. (1997) NMR methods for the study of protein structure and dynamics. Biochem. Cell. Biol. 75, 1-15.
    • (1997) Biochem. Cell. Biol. , vol.75 , pp. 1-15
    • Kay, L.E.1
  • 13
    • 0031928367 scopus 로고    scopus 로고
    • Shining a light on structural genomics
    • Kim, S. H. (1998) Shining a light on structural genomics. Nat. Struct. Biol. 5, 643.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 643
    • Kim, S.H.1
  • 14
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M. and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 15
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A., MacArthur, M. W., Kaptein, R. and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 17
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J. L. (1995) Thioredoxin - a fold for all reasons. Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 18
    • 0035190119 scopus 로고    scopus 로고
    • Insights into the structure, salvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme
    • Martin, P., DeMel, S., Shi, J., Gladysheva, T., Gatti, D. L., Rosen, B. P. and Edwards, B. F. P. (2001) Insights into the structure, salvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure 9, 1071-1081.
    • (2001) Structure , vol.9 , pp. 1071-1081
    • Martin, P.1    DeMel, S.2    Shi, J.3    Gladysheva, T.4    Gatti, D.L.5    Rosen, B.P.6    Edwards, B.F.P.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.