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Volumn 7, Issue 9, 1998, Pages 1851-1856

Class-directed structure determination: Foundation for a protein structure initiative

Author keywords

Biotechnology; Class directed structures; Genome projects; Microorganisms; Protein structure determination

Indexed keywords

PROTEIN; VEGETABLE PROTEIN;

EID: 0031665755     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560070901     Document Type: Review
Times cited : (75)

References (21)
  • 1
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known 3-dimensional structure
    • Bowie JU, Luthy R, Eisenberg D. 1991. A method to identify protein sequences that fold into a known 3-dimensional structure. Science 253:164-170.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 3
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, Lesk AM. 1986. The relation between the divergence of sequence and structure in proteins. EMBO J 5:823-826.
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 4
    • 0030688004 scopus 로고    scopus 로고
    • Variations on a theme: Cataloging human dna-sequence variation
    • Collins FS, Guyer MS, Chakravarti A. 1997. Variations on a theme: Cataloging human dna-sequence variation. Science 278:1580-1581.
    • (1997) Science , vol.278 , pp. 1580-1581
    • Collins, F.S.1    Guyer, M.S.2    Chakravarti, A.3
  • 5
    • 0030623575 scopus 로고    scopus 로고
    • All-in-one: A highly detailed rotamer library improves both accuracy speed in the modeling of side-chains by dead-end elimination
    • Demaeyer M, Desmet J, Lasters I. 1997. All-in-one: A highly detailed rotamer library improves both accuracy speed in the modeling of side-chains by dead-end elimination. Folding & Design 2:53-66.
    • (1997) Folding & Design , vol.2 , pp. 53-66
    • Demaeyer, M.1    Desmet, J.2    Lasters, I.3
  • 9
    • 0030764671 scopus 로고    scopus 로고
    • Protein structural classes in 5 complete genomes
    • Frishman D, Mewes HW. 1997. Protein structural classes in 5 complete genomes. Nature Struct Biol 4:626-268.
    • (1997) Nature Struct Biol , vol.4 , pp. 626-1268
    • Frishman, D.1    Mewes, H.W.2
  • 10
    • 0026420952 scopus 로고
    • Towards a paradigm shift in biology
    • Gilbert W. 1991. Towards a paradigm shift in biology. Nature 349:99.
    • (1991) Nature , vol.349 , pp. 99
    • Gilbert, W.1
  • 11
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • Hendrickson WA, Ogata C. 1997. Phase determination from multiwavelength anomalous diffraction measurements. Methods Enzymol 276:494-523.
    • (1997) Methods Enzymol , vol.276 , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.2
  • 12
    • 0030725715 scopus 로고    scopus 로고
    • Functional genomics: It's all how you read it
    • Hieter P, Boguski M. 1997. Functional genomics: It's all how you read it. Science 278:601-602.
    • (1997) Science , vol.278 , pp. 601-602
    • Hieter, P.1    Boguski, M.2
  • 13
    • 0028593509 scopus 로고
    • Protein superfamilies and domain superfolds
    • Orengo CA, Jones DT, Thornton JM. 1994. Protein superfamilies and domain superfolds. Nature 372:631-634.
    • (1994) Nature , vol.372 , pp. 631-634
    • Orengo, C.A.1    Jones, D.T.2    Thornton, J.M.3
  • 14
    • 0030978103 scopus 로고    scopus 로고
    • Construction of a catalytically active iron superoxide-dismutase rational protein design
    • Pinto AL, Hellinga HW, Caradonna JP. 1997. Construction of a catalytically active iron superoxide-dismutase rational protein design. Proc Natl Acad Sci USA 94:5562-5567.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5562-5567
    • Pinto, A.L.1    Hellinga, H.W.2    Caradonna, J.P.3
  • 15
    • 0029283962 scopus 로고
    • The biotechnology and applications of antibody engineering
    • Rapley R. 1995. The biotechnology and applications of antibody engineering. Molecular Biotechnology 3:139-154.
    • (1995) Molecular Biotechnology , vol.3 , pp. 139-154
    • Rapley, R.1
  • 16
    • 0028783819 scopus 로고
    • Progress of 1d protein-structure prediction at last
    • Rost B, Sander C. 1995. Progress of 1d protein-structure prediction at last. Proteins Struct Funct Genet 23:295-300.
    • (1995) Proteins Struct Funct Genet , vol.23 , pp. 295-300
    • Rost, B.1    Sander, C.2
  • 17
    • 0030708567 scopus 로고    scopus 로고
    • Sequencing the human genome
    • Rowen L, Mahairas G, Hood L. 1997. Sequencing the human genome. Science 278:605-607.
    • (1997) Science , vol.278 , pp. 605-607
    • Rowen, L.1    Mahairas, G.2    Hood, L.3
  • 20
    • 0028773887 scopus 로고
    • Structure-based drug design: Progress, results and challenges
    • Velinde CLMJ, Hol WGJ. 1994. Structure-based drug design: Progress, results and challenges. Structure 2:577-587.
    • (1994) Structure , vol.2 , pp. 577-587
    • Velinde, C.L.M.J.1    Hol, W.G.J.2
  • 21
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal-stability, hydrogen-bonds, and ion-pairs
    • Vogt G, Woell S, Argos P. 1997. Protein thermal-stability, hydrogen-bonds, and ion-pairs. J Mol Biol 269:631-643.
    • (1997) J Mol Biol , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.