메뉴 건너뛰기




Volumn 43, Issue 26, 2004, Pages 8568-8578

Sml1p is a dimer in solution: Characterization of denaturation and renaturation of recombinant Sml1p

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DNA; MASS SPECTROMETRY; SEDIMENTATION;

EID: 3142615305     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0361721     Document Type: Article
Times cited : (13)

References (53)
  • 2
    • 0027338038 scopus 로고
    • RAD9-dependent G1 arrest defines a second checkpoint for damaged DNA in the cell cycle of Saccharomyces cerevisiae
    • Siede, W., Friedberg, A. S., and Friedberg, E. C. (1993) RAD9-dependent G1 arrest defines a second checkpoint for damaged DNA in the cell cycle of Saccharomyces cerevisiae, Proc. Natl. Acad. Sci. U.S.A. 90, 7985-7989.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7985-7989
    • Siede, W.1    Friedberg, A.S.2    Friedberg, E.C.3
  • 3
    • 0034100565 scopus 로고    scopus 로고
    • Involvement of the checkpoint protein Mec1p in silencing of gene expression at telomeres in Saccharomyces cerevisiae
    • Craven, R. J., and Petes, T. D. (2000) Involvement of the checkpoint protein Mec1p in silencing of gene expression at telomeres in Saccharomyces cerevisiae, Mol. Cell. Biol. 20, 2378-2384.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2378-2384
    • Craven, R.J.1    Petes, T.D.2
  • 4
    • 0028932603 scopus 로고
    • Cell cycle regulation in response to DNA damage in mammalian cells: A historical perspective
    • Murnane, J. P. (1995) Cell cycle regulation in response to DNA damage in mammalian cells: a historical perspective, Cancer Metastasis Rev 14, 17-29.
    • (1995) Cancer Metastasis Rev. , vol.14 , pp. 17-29
    • Murnane, J.P.1
  • 5
    • 0032780113 scopus 로고    scopus 로고
    • Radiosensitive and mitotic recombination phenotypes of the Saccharomyces cerevisiae dun1 mutant defective in DNA damage-inducible gene expression
    • Fasullo, M., Koudelik, J., AhChing, P., Giallanza, P., and Cera, C. (1999) Radiosensitive and mitotic recombination phenotypes of the Saccharomyces cerevisiae dun1 mutant defective in DNA damage-inducible gene expression, Genetics 152, 909-919.
    • (1999) Genetics , vol.152 , pp. 909-919
    • Fasullo, M.1    Koudelik, J.2    AhChing, P.3    Giallanza, P.4    Cera, C.5
  • 6
    • 0030841865 scopus 로고    scopus 로고
    • Thioredoxin reductase-dependent inhibition of MCB cell cycle box activity in Saccharomyces cerevisiae
    • Machado, A. K., Morgan, B. A., and Merrill, G. F. (1997) Thioredoxin reductase-dependent inhibition of MCB cell cycle box activity in Saccharomyces cerevisiae, J. Biol. Chem. 272, 17045-17054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17045-17054
    • Machado, A.K.1    Morgan, B.A.2    Merrill, G.F.3
  • 7
    • 0030596311 scopus 로고    scopus 로고
    • Assessing p53 status in breast cancer prognosis: Where should you put the thermometer if you think your p53 is sick?
    • Elledge, R. M. (1996) Assessing p53 status in breast cancer prognosis: where should you put the thermometer if you think your p53 is sick? J. Natl. Cancer Inst. 88, 141-143.
    • (1996) J. Natl. Cancer Inst. , vol.88 , pp. 141-143
    • Elledge, R.M.1
  • 8
    • 0037133566 scopus 로고    scopus 로고
    • The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1
    • Zhao, X., and Rothstein, R. (2002) The Dun1 checkpoint kinase phosphorylates and regulates the ribonucleotide reductase inhibitor Sml1, Proc. Natl. Acad. Sci. U.S.A. 99, 3746-3751.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 3746-3751
    • Zhao, X.1    Rothstein, R.2
  • 10
    • 0014694297 scopus 로고
    • Role of effector binding in allosteric control of ribonucleoside diphosphate reductase
    • Brown, N. C. a. R. P. (1969) Role of effector binding in allosteric control of ribonucleoside diphosphate reductase, J. Mol. Biol. 46, 39-55.
    • (1969) J. Mol. Biol. , vol.46 , pp. 39-55
    • Brown, N.C.A.R.P.1
  • 11
    • 0030813561 scopus 로고    scopus 로고
    • Identification of RNR4, encoding a second essential small subunit of ribonucleotide reductase in Saccharomyces cerevisiae
    • Huang, M., and Elledge, S. J. (1997) Identification of RNR4, encoding a second essential small subunit of ribonucleotide reductase in Saccharomyces cerevisiae, Mol. Cell. Biol. 17, 6105-6113.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6105-6113
    • Huang, M.1    Elledge, S.J.2
  • 12
    • 0027605113 scopus 로고
    • DNA damage and cell cycle regulation of ribonucleotide reductase
    • Elledge, S. J., Zhou, Z., Allen, J. B., and Navas, T. A. (1993) DNA damage and cell cycle regulation of ribonucleotide reductase, Bioessays 15, 333-339.
    • (1993) Bioessays , vol.15 , pp. 333-339
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3    Navas, T.A.4
  • 13
    • 0025350420 scopus 로고
    • Two genes differentially regulated in the cell cycle and by DNA-damaging agents encode alternative regulatory subunits of ribonucleotide reductase
    • Elledge, S. J., and Davis, R. W. (1990) Two genes differentially regulated in the cell cycle and by DNA-damaging agents encode alternative regulatory subunits of ribonucleotide reductase, Genes Dev. 4, 740-751.
    • (1990) Genes Dev , vol.4 , pp. 740-751
    • Elledge, S.J.1    Davis, R.W.2
  • 14
    • 0025366033 scopus 로고
    • S-phase-specific expression of mammalian ribonucleotide reductase R1 and R2 subunit mRNAs
    • Bjorklund, S., Skog, S., Tribukait, B., and Thelander, L. (1990) S-phase-specific expression of mammalian ribonucleotide reductase R1 and R2 subunit mRNAs, Biochemistry 29, 5452-5458.
    • (1990) Biochemistry , vol.29 , pp. 5452-5458
    • Bjorklund, S.1    Skog, S.2    Tribukait, B.3    Thelander, L.4
  • 15
    • 0022260274 scopus 로고
    • Cell cycle-dependent expression of mammalian ribonucleotide reductase. Differential regulation of the two subunits
    • Engstrom, Y., Eriksson, S., Jildevik, I., Skog, S., Thelander, L., and Tribukait, B. (1985) Cell cycle-dependent expression of mammalian ribonucleotide reductase. Differential regulation of the two subunits, J. Biol. Chem. 260, 9114-9116.
    • (1985) J. Biol. Chem. , vol.260 , pp. 9114-9116
    • Engstrom, Y.1    Eriksson, S.2    Jildevik, I.3    Skog, S.4    Thelander, L.5    Tribukait, B.6
  • 16
    • 0038312250 scopus 로고    scopus 로고
    • Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways
    • Yao, R., Zhang, Z., An, X., Bucci, B., Perlstein, D. L., Stubbe, J., and Huang, M. (2003) Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways, Proc. Natl. Acad. Sci. U.S.A. 100, 6628-6633.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 6628-6633
    • Yao, R.1    Zhang, Z.2    An, X.3    Bucci, B.4    Perlstein, D.L.5    Stubbe, J.6    Huang, M.7
  • 17
    • 0033579443 scopus 로고    scopus 로고
    • Yeast Sml1, a protein inhibitor of ribonucleotide reductase
    • Chabes, A., Domkin, V., and Thelander, L. (1999) Yeast Sml1, a protein inhibitor of ribonucleotide reductase, J. Biol. Chem. 274, 36679-36683.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36679-36683
    • Chabes, A.1    Domkin, V.2    Thelander, L.3
  • 18
    • 0032956282 scopus 로고    scopus 로고
    • Interaction between the MEC1-dependent DNA synthesis checkpoint and G1 cyclin function in Saccharomyces cerevisiae
    • Vallen, E. A., and Cross, F. R. (1999) Interaction between the MEC1-dependent DNA synthesis checkpoint and G1 cyclin function in Saccharomyces cerevisiae, Genetics 151, 459-471.
    • (1999) Genetics , vol.151 , pp. 459-471
    • Vallen, E.A.1    Cross, F.R.2
  • 19
    • 0032215053 scopus 로고    scopus 로고
    • Molecular characterization of tobacco ribonucleotide reductase RNR1 and RNR2 cDNAs and cell cycle-regulated expression in synchronized plant cells
    • Chaboute, M. E., Combettes, B., Clement, B., Gigot, C., and Philipps, G. (1998) Molecular characterization of tobacco ribonucleotide reductase RNR1 and RNR2 cDNAs and cell cycle-regulated expression in synchronized plant cells, Plant Mol. Biol. 38, 797-806.
    • (1998) Plant Mol. Biol. , vol.38 , pp. 797-806
    • Chaboute, M.E.1    Combettes, B.2    Clement, B.3    Gigot, C.4    Philipps, G.5
  • 20
    • 0026582672 scopus 로고
    • Ribonucleotide reductase: Regulation, regulation, regulation
    • Elledge, S. J., Zhou, Z., and Allen, J. B. (1992) Ribonucleotide reductase: regulation, regulation, regulation, Trends Biochem. Sci. 17, 119-123.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 119-123
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3
  • 21
    • 0035796505 scopus 로고    scopus 로고
    • The ribonucleotide reductase inhibitor Sml1 is a new target of the Mec1/Rad53 kinase cascade during growth and in response to DNA damage
    • Zhao, X., Chabes, A., Domkin, V., Thelander, L., and Rothstein, R. (2001) The ribonucleotide reductase inhibitor Sml1 is a new target of the Mec1/Rad53 kinase cascade during growth and in response to DNA damage, EMBO J. 20, 3544-3553.
    • (2001) EMBO J. , vol.20 , pp. 3544-3553
    • Zhao, X.1    Chabes, A.2    Domkin, V.3    Thelander, L.4    Rothstein, R.5
  • 22
    • 1642442486 scopus 로고    scopus 로고
    • Identification of phosphorylation sites on the yeast ribonucleotide reductase inhibitor Sml1
    • Uchiki, T., Dice, L. T., Hettich, R. L., and Dealwis, C. (2004) Identification of phosphorylation sites on the yeast ribonucleotide reductase inhibitor Sml1, J. Biol. Chem. 279, 11293-11303.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11293-11303
    • Uchiki, T.1    Dice, L.T.2    Hettich, R.L.3    Dealwis, C.4
  • 23
    • 0034460153 scopus 로고    scopus 로고
    • Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality
    • Zhao, X., Georgieva, B., Chabes, A., Domkin, V., Ippel, J. H., Schleucher, J., Wijmenga, S., Thelander, L., and Rothstein, R. (2000) Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality, Mol. Cell. Biol. 20, 9076-9083.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 9076-9083
    • Zhao, X.1    Georgieva, B.2    Chabes, A.3    Domkin, V.4    Ippel, J.H.5    Schleucher, J.6    Wijmenga, S.7    Thelander, L.8    Rothstein, R.9
  • 24
    • 0036467707 scopus 로고    scopus 로고
    • Characterization of monomeric and dimeric forms of recombinant Sml1p-histag protein by electrospray mass spectrometry
    • Uchiki, T., Hettich, R., Gupta, V., and Dealwis, C. (2002) Characterization of monomeric and dimeric forms of recombinant Sml1p-histag protein by electrospray mass spectrometry, Anal. Biochem. 301, 35-48.
    • (2002) Anal. Biochem. , vol.301 , pp. 35-48
    • Uchiki, T.1    Hettich, R.2    Gupta, V.3    Dealwis, C.4
  • 26
    • 0037155822 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor type 1 promotes the self-association of vitronectin into complexes exhibiting altered incorporation into the extracellular matrix
    • Minor, K. H., and Peterson, C. B. (2002) Plasminogen activator inhibitor type 1 promotes the self-association of vitronectin into complexes exhibiting altered incorporation into the extracellular matrix, J. Biol. Chem. 277, 10337-10345.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10337-10345
    • Minor, K.H.1    Peterson, C.B.2
  • 27
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidine hydrochloride
    • Kawahara, K., and Tanford, C. (1966) Viscosity and density of aqueous solutions of urea and guanidine hydrochloride, J. Biol. Chem. 241, 3228-3232.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 28
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • in press
    • Vistica, J., Dam, J., Balbo, A., Yikilmaz, E., Mariuzza, R. A., Rouault, T. A., and Schuck, P. (2004) Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition, Anal. Biochem., in press.
    • (2004) Anal. Biochem.
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5    Rouault, T.A.6    Schuck, P.7
  • 29
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server, Bioinformatics 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 30
    • 0034663738 scopus 로고    scopus 로고
    • Protein threading using PROSPECT: Design and evaluation
    • Xu, Y., and Xu, D. (2000) Protein threading using PROSPECT: design and evaluation, Proteins 40, 343-354.
    • (2000) Proteins , vol.40 , pp. 343-354
    • Xu, Y.1    Xu, D.2
  • 31
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones, D. T. (1999) GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences, J. Mol. Biol. 287, 797-815.
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 32
    • 0034821220 scopus 로고    scopus 로고
    • High-frequency (140-GHz) time domain EPR and ENDOR spectroscopy: The tyrosyl radical-diiron cofactor in ribonucleotide reductase from yeast
    • Bar, G., Bennati, M., Nguyen, H. H., Ge, J., Stubbe, J. A., and Griffin, R. G. (2001) High-frequency (140-GHz) time domain EPR and ENDOR spectroscopy: the tyrosyl radical-diiron cofactor in ribonucleotide reductase from yeast, J. Am. Chem. Soc. 123, 3569-3576.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3569-3576
    • Bar, G.1    Bennati, M.2    Nguyen, H.H.3    Ge, J.4    Stubbe, J.A.5    Griffin, R.G.6
  • 33
    • 0034604368 scopus 로고    scopus 로고
    • HMMSTR: A hidden Markov model for local sequence-structure correlations in proteins
    • Bystroff, C., Thorsson, V., and Baker, D. (2000) HMMSTR: a hidden Markov model for local sequence-structure correlations in proteins, J. Mol. Biol. 301, 173-190.
    • (2000) J. Mol. Biol. , vol.301 , pp. 173-190
    • Bystroff, C.1    Thorsson, V.2    Baker, D.3
  • 34
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Sali, A., and Overington, J. P. (1994) Derivation of rules for comparative protein modeling from a database of protein structure alignments, Protein Sci. 3, 1582-1596.
    • (1994) Protein Sci. , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. M., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, Appl. Crystallogr. 26, 283-290.
    • (1993) Appl. Crystallogr. , vol.26 , pp. 283-290
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.M.3    Thornton, J.M.4
  • 38
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera, O. D., Kay, C. M., and Hodges, R. S. (1994) Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions, Protein Sci. 3, 1984-1991.
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 39
  • 40
    • 0035801540 scopus 로고    scopus 로고
    • Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily
    • Staniforth, R. A., Giannini, S., Higgins, L. D., Conroy, M. J., Hounslow, A. M., Jerala, R., Craven, C. J., and Waltho, J. P. (2001) Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily, EMBO J. 20, 4774-4781.
    • (2001) EMBO J. , vol.20 , pp. 4774-4781
    • Staniforth, R.A.1    Giannini, S.2    Higgins, L.D.3    Conroy, M.J.4    Hounslow, A.M.5    Jerala, R.6    Craven, C.J.7    Waltho, J.P.8
  • 41
    • 0242353812 scopus 로고    scopus 로고
    • Predissociated dimers and molten globule monomers in the equilibrium unfolding of yeast glutathione reductase
    • Louzada, P. R., Sebollela, A., Scaramello, M. E., and Ferreira, S. T. (2003) Predissociated dimers and molten globule monomers in the equilibrium unfolding of yeast glutathione reductase. Biophys. J. 85, 3255-3261.
    • (2003) Biophys. J. , vol.85 , pp. 3255-3261
    • Louzada, P.R.1    Sebollela, A.2    Scaramello, M.E.3    Ferreira, S.T.4
  • 42
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of nativelike topology in a denatured protein in 8 M urea
    • Shortle, D., and Ackerman, M. S. (2001) Persistence of nativelike topology in a denatured protein in 8 M urea, Science 293, 487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 43
    • 0035836687 scopus 로고    scopus 로고
    • Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
    • Kazmirski, S. L., Wong, K. B., Freund, S. M., Tan, Y. J., Fersht, A. R., and Daggett, V. (2001) Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution, Proc. Natl. Acad. Sci. U.S.A. 98, 4349-4354.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4349-4354
    • Kazmirski, S.L.1    Wong, K.B.2    Freund, S.M.3    Tan, Y.J.4    Fersht, A.R.5    Daggett, V.6
  • 44
    • 0345304461 scopus 로고    scopus 로고
    • Origin of Unusual f-values in protein folding: Evidence against specific nucleation sites
    • Sanchez, I. E. a. K. T. (2003) Origin of Unusual f-values in protein folding: evidence against specific nucleation sites, J. Mol. Biol. 334, 1077-1085.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1077-1085
    • Sanchez, I.E.A.K.T.1
  • 45
    • 0032161269 scopus 로고    scopus 로고
    • A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools
    • Zhao, X., Muller, E. G. D., and Rothstein, R. (1998) A suppressor of two essential checkpoint genes identifies a novel protein that negatively affects dNTP pools, Mol. Cell 2, 329-340.
    • (1998) Mol. Cell , vol.2 , pp. 329-340
    • Zhao, X.1    Muller, E.G.D.2    Rothstein, R.3
  • 46
    • 0031793928 scopus 로고    scopus 로고
    • Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases
    • Altschul, S. F., and Koonin, E. V. (1998) Iterated profile searches with PSI-BLAST-a tool for discovery in protein databases, Trends Biochem. Sci. 23, 444-447.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 444-447
    • Altschul, S.F.1    Koonin, E.V.2
  • 47
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M., and Rodgers, S. W. (1996) PEST sequences and regulation by proteolysis, Trends Biochem. Sci. 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rodgers, S.W.2
  • 48
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation, Annu. Rev. Genet. 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 49
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho
    • Cicchetti, P., Mayer, B. J., Thiel, G., and Baltimore, D. (1992) Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho, Science 257, 803-806.
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 51
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein and Sos nucleotide exchange factor
    • Buday, L., and Downward, J. (1993) Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adaptor protein and Sos nucleotide exchange factor, Cell 73, 610-620.
    • (1993) Cell , vol.73 , pp. 610-620
    • Buday, L.1    Downward, J.2
  • 52
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren, R., Mayer, B. J., Cicchetti, P., and Baltimore, D. (1993) Identification of a ten-amino acid proline-rich SH3 binding site, Science 259, 1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 53
    • 0043222570 scopus 로고    scopus 로고
    • Fully automated ab initio protein structure prediction using I-SITES, HMMSTR, and ROSETTA
    • Bystroff, C., and Shao, Y. (2002) Fully automated ab initio protein structure prediction using I-SITES, HMMSTR, and ROSETTA, Bioinformatics 18, S54-S61.
    • (2002) Bioinformatics , vol.18
    • Bystroff, C.1    Shao, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.