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Volumn 47, Issue 37, 2008, Pages 9866-9879

Kinetic analysis of interaction of BRCA1 tandem breast cancer C-terminal domains with phosphorylated peptides reveals two binding conformations

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; CHLORINE COMPOUNDS; CONFORMATIONS; CRYSTALLOGRAPHY; DATA FLOW ANALYSIS; DISSOCIATION; ENZYMES; EQUILIBRIUM CONSTANTS; FLOW INTERACTIONS; MECHANISMS; MINERALOGY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEIC ACIDS; ORGANIC ACIDS; PEPTIDES; PHOSPHORYLATION; PORT TERMINALS; PROTEINS; SURFACE PLASMON RESONANCE;

EID: 51849105183     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi702247d     Document Type: Article
Times cited : (14)

References (60)
  • 1
    • 0028034348 scopus 로고
    • Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families
    • Friedman, L. S., Ostermeyer, E. A., Szabo, C. I., Dowd, P., Lynch, E. D., Rowell, S. E., and King, M. C. (1994) Confirmation of BRCA1 by analysis of germline mutations linked to breast and ovarian cancer in ten families. Nat. Genet. 8, 399-404.
    • (1994) Nat. Genet , vol.8 , pp. 399-404
    • Friedman, L.S.1    Ostermeyer, E.A.2    Szabo, C.I.3    Dowd, P.4    Lynch, E.D.5    Rowell, S.E.6    King, M.C.7
  • 2
    • 33749023326 scopus 로고    scopus 로고
    • The roles of BRCA1 and BRCA2 and associated proteins in the maintenance of genomic stability
    • Gudmundsdottir, K., and Ashworth, A. (2006) The roles of BRCA1 and BRCA2 and associated proteins in the maintenance of genomic stability. Oncogene 25, 5864-5874.
    • (2006) Oncogene , vol.25 , pp. 5864-5874
    • Gudmundsdottir, K.1    Ashworth, A.2
  • 3
    • 33749000596 scopus 로고    scopus 로고
    • The role of BRCA1 in transcriptional regulation and cell cycle control
    • Mullan, P. B., Quinn, J. E., and Harkin, D. P. (2006) The role of BRCA1 in transcriptional regulation and cell cycle control. Oncogene 25, 5854-5863.
    • (2006) Oncogene , vol.25 , pp. 5854-5863
    • Mullan, P.B.1    Quinn, J.E.2    Harkin, D.P.3
  • 6
    • 34347256776 scopus 로고    scopus 로고
    • Estrogen receptor α is a putative substrate for the BRCA1 ubiquitin ligase
    • Eakin, C. M., Maccoss, M. J., Finney, G. L., and Klevit, R. E. (2007) Estrogen receptor α is a putative substrate for the BRCA1 ubiquitin ligase. Proc. Natl. Acad. Sci. U.S.A. 104, 5794-5799.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 5794-5799
    • Eakin, C.M.1    Maccoss, M.J.2    Finney, G.L.3    Klevit, R.E.4
  • 7
    • 0034809456 scopus 로고    scopus 로고
    • Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1
    • Williams, R. S., Green, R., and Glover, J. N. (2001) Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1. Nat. Struct. Biol. 8, 838-842.
    • (2001) Nat. Struct. Biol , vol.8 , pp. 838-842
    • Williams, R.S.1    Green, R.2    Glover, J.N.3
  • 8
    • 9644252804 scopus 로고    scopus 로고
    • Characterization of segments from the central region of BRCA1: An intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions?
    • Mark, W. Y., Liao, J. C., Lu, Y., Ayed, A., Laister, R., Szymczyna, B., Chakrabartty, A., and Arrowsmith, C. H. (2005) Characterization of segments from the central region of BRCA1: An intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions? J. Mol. Biol. 345, 275-287.
    • (2005) J. Mol. Biol , vol.345 , pp. 275-287
    • Mark, W.Y.1    Liao, J.C.2    Lu, Y.3    Ayed, A.4    Laister, R.5    Szymczyna, B.6    Chakrabartty, A.7    Arrowsmith, C.H.8
  • 11
    • 0142147272 scopus 로고    scopus 로고
    • The BRCT domain is a phospho-protein binding domain
    • Yu, X., Chini, C. C., He, M., Mer, G., and Chen, J. (2003) The BRCT domain is a phospho-protein binding domain. Science 302, 639-642.
    • (2003) Science , vol.302 , pp. 639-642
    • Yu, X.1    Chini, C.C.2    He, M.3    Mer, G.4    Chen, J.5
  • 12
    • 3142608985 scopus 로고    scopus 로고
    • Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains
    • Botuyan, M. V., Nomine, Y., Yu, X., Juranic, N., Macura, S., Chen, J., and Mer, G. (2004) Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains. Structure 12, 1137-1146.
    • (2004) Structure , vol.12 , pp. 1137-1146
    • Botuyan, M.V.1    Nomine, Y.2    Yu, X.3    Juranic, N.4    Macura, S.5    Chen, J.6    Mer, G.7
  • 13
    • 0142240342 scopus 로고    scopus 로고
    • BRCT repeats as phosphopeptide-binding modules involved in protein targeting
    • Manke, I. A., Lowery, D. M., Nguyen, A., and Yaffe, M. B. (2003) BRCT repeats as phosphopeptide-binding modules involved in protein targeting. Science 302, 636-639.
    • (2003) Science , vol.302 , pp. 636-639
    • Manke, I.A.1    Lowery, D.M.2    Nguyen, A.3    Yaffe, M.B.4
  • 14
    • 6344264992 scopus 로고    scopus 로고
    • DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains
    • Yu, X., and Chen, J. (2004) DNA damage-induced cell cycle checkpoint control requires CtIP, a phosphorylation-dependent binding partner of BRCA1 C-terminal domains. Mol. Cell. Biol. 24, 9478-9486.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 9478-9486
    • Yu, X.1    Chen, J.2
  • 15
    • 33745614048 scopus 로고    scopus 로고
    • BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP
    • Yu, X., Fu, S., Lai, M., Baer, R., and Chen, J. (2006) BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP. Genes Dev. 20, 1721-1726.
    • (2006) Genes Dev , vol.20 , pp. 1721-1726
    • Yu, X.1    Fu, S.2    Lai, M.3    Baer, R.4    Chen, J.5
  • 16
    • 2542489188 scopus 로고    scopus 로고
    • Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer
    • Clapperton, J. A., Manke, I. A., Lowery, D. M., Ho, T., Haire, L. F., Yaffe, M. B., and Smerdon, S. J. (2004) Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer. Nat. Struct. Mol. Biol. 11, 512-518.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 512-518
    • Clapperton, J.A.1    Manke, I.A.2    Lowery, D.M.3    Ho, T.4    Haire, L.F.5    Yaffe, M.B.6    Smerdon, S.J.7
  • 17
    • 2342484423 scopus 로고    scopus 로고
    • Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: Implications for signaling
    • Shiozaki, E. N., Gu, L., Yan, N., and Shi, Y. (2004) Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: Implications for signaling. Mol. Cell 14, 405-412.
    • (2004) Mol. Cell , vol.14 , pp. 405-412
    • Shiozaki, E.N.1    Gu, L.2    Yan, N.3    Shi, Y.4
  • 18
    • 2542490186 scopus 로고    scopus 로고
    • Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1
    • Williams, R. S., Lee, M. S., Hau, D. D., and Glover, J. N. (2004) Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1. Nat. Struct. Mol. Biol. 11, 519-525.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 519-525
    • Williams, R.S.1    Lee, M.S.2    Hau, D.D.3    Glover, J.N.4
  • 19
    • 23944510641 scopus 로고    scopus 로고
    • Structural basis for cell cycle checkpoint control by the BRCA1-CtIP complex
    • Varma, A. K., Brown, R. S., Birrane, G., and Ladias, J. A. (2005) Structural basis for cell cycle checkpoint control by the BRCA1-CtIP complex. Biochemistry 44, 10941-10946.
    • (2005) Biochemistry , vol.44 , pp. 10941-10946
    • Varma, A.K.1    Brown, R.S.2    Birrane, G.3    Ladias, J.A.4
  • 20
    • 51849099704 scopus 로고    scopus 로고
    • Karlsson, R., Roos, H., Bruno, J., and Stolz, L. (1997) Practical aspects concerning direct detection of low molecular weight analytes using BIACORE 2000. B1A J., 18-21.
    • Karlsson, R., Roos, H., Bruno, J., and Stolz, L. (1997) Practical aspects concerning direct detection of low molecular weight analytes using BIACORE 2000. B1A J., 18-21.
  • 21
    • 0027198367 scopus 로고
    • Antigen-antibody binding and mass transport by convection and diffusion to a surface: A two-dimensional computer model of binding and dissociation kinetics
    • Glaser, R. W. (1993) Antigen-antibody binding and mass transport by convection and diffusion to a surface: A two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 213, 152-161.
    • (1993) Anal. Biochem , vol.213 , pp. 152-161
    • Glaser, R.W.1
  • 22
    • 0035863930 scopus 로고    scopus 로고
    • Use of optical biosensors for the study of mechanistically concerted surface adsorption processes
    • Hall, D. (2001) Use of optical biosensors for the study of mechanistically concerted surface adsorption processes. Anal. Biochem. 288, 109-125.
    • (2001) Anal. Biochem , vol.288 , pp. 109-125
    • Hall, D.1
  • 23
    • 0032701484 scopus 로고    scopus 로고
    • Improving biosensor analysis
    • Myszka, D. (1999) Improving biosensor analysis. J. Mol. Recognit. 12, 279-284.
    • (1999) J. Mol. Recognit , vol.12 , pp. 279-284
    • Myszka, D.1
  • 24
    • 0029939283 scopus 로고    scopus 로고
    • Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology
    • O'Shannessy, D. J., and Winzor, D. J. (1996) Interpretation of deviations from pseudo-first-order kinetic behavior in the characterization of ligand binding by biosensor technology. Anal. Biochem. 236, 275-283.
    • (1996) Anal. Biochem , vol.236 , pp. 275-283
    • O'Shannessy, D.J.1    Winzor, D.J.2
  • 25
    • 0032321401 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • Morton, T. A., and Myszka, D. G. (1998) Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors. Methods Enzymol. 295, 268-294.
    • (1998) Methods Enzymol , vol.295 , pp. 268-294
    • Morton, T.A.1    Myszka, D.G.2
  • 26
    • 0031958764 scopus 로고    scopus 로고
    • CLAMP: A biosensor kinetic data analysis program
    • Myszka, D., and Morton, T. (1998) CLAMP: A biosensor kinetic data analysis program. Trends Biochem. Sci. 23, 149-150.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 149-150
    • Myszka, D.1    Morton, T.2
  • 27
    • 23044525847 scopus 로고    scopus 로고
    • A hybrid global optimization algorithm involving simplex and inductive search
    • Offord, C., and Bajzer, Z. (2001) A hybrid global optimization algorithm involving simplex and inductive search. Computational Science 194 Iccs 2001, Proceedings Part 2, Vol. 2074, 680-688.
    • (2001) Computational Science 194 Iccs 2001, Proceedings Part 2 , vol.2074 , pp. 680-688
    • Offord, C.1    Bajzer, Z.2
  • 28
    • 0000536084 scopus 로고
    • Automatic selection of methods for solving stiff and non-stiff systems of ordinary differential equations
    • Petzold, L. (1983) Automatic selection of methods for solving stiff and non-stiff systems of ordinary differential equations. J. Sci. Stat. Comput. 4, 136-148.
    • (1983) J. Sci. Stat. Comput , vol.4 , pp. 136-148
    • Petzold, L.1
  • 31
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J., and Lin, L. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137.
    • (1989) Anal. Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.3    Lin, L.4
  • 32
    • 0027537127 scopus 로고
    • Structural energetics of peptide recognition: Angiotensin II/antibody binding
    • Murphy, K., Xie, D., Garcia, K., Amzel, L., and Freire, E. (1993) Structural energetics of peptide recognition: Angiotensin II/antibody binding. Proteins 15, 113-120.
    • (1993) Proteins , vol.15 , pp. 113-120
    • Murphy, K.1    Xie, D.2    Garcia, K.3    Amzel, L.4    Freire, E.5
  • 33
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • Gomez, J., and Freire, E. (1995) Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252, 337-350.
    • (1995) J. Mol. Biol , vol.252 , pp. 337-350
    • Gomez, J.1    Freire, E.2
  • 34
    • 0015222647 scopus 로고
    • The interpretation of protein structures: Estimation of static accessibility
    • Lee, B., and Richards, F. (1971) The interpretation of protein structures: Estimation of static accessibility. J. Mol. Biol 55, 379-400.
    • (1971) J. Mol. Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.2
  • 35
    • 0000372879 scopus 로고    scopus 로고
    • Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis
    • Stites, W. (1997) Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis. Chem. Rev. 97, 1233-1250.
    • (1997) Chem. Rev , vol.97 , pp. 1233-1250
    • Stites, W.1
  • 36
    • 0030036162 scopus 로고    scopus 로고
    • Large heat capacity change in a protein-monovalent cation interaction
    • Guinto, E., and Di Cera, E. (1996) Large heat capacity change in a protein-monovalent cation interaction. Biochemistry 35, 8800-8804.
    • (1996) Biochemistry , vol.35 , pp. 8800-8804
    • Guinto, E.1    Di Cera, E.2
  • 37
    • 0030948651 scopus 로고    scopus 로고
    • Energetics of thrombin-thrombomodulin interaction
    • Vindigni, A., White, C., Komives, E., and Di Cera, E. (1997) Energetics of thrombin-thrombomodulin interaction. Biochemistry 36, 6674-6681.
    • (1997) Biochemistry , vol.36 , pp. 6674-6681
    • Vindigni, A.1    White, C.2    Komives, E.3    Di Cera, E.4
  • 38
    • 0001988153 scopus 로고
    • The choice of approximative models in nonlinear regression
    • Zwanzig, S. (1980) The choice of approximative models in nonlinear regression. Statistics 11, 23-47.
    • (1980) Statistics , vol.11 , pp. 23-47
    • Zwanzig, S.1
  • 39
    • 0345079575 scopus 로고
    • A new method to discriminate between enzyme-kinetic models
    • Buckwitz, D., and Holzhutter, H.-G. (1990) A new method to discriminate between enzyme-kinetic models. Comp. Math. Appl. 20, 117-126.
    • (1990) Comp. Math. Appl , vol.20 , pp. 117-126
    • Buckwitz, D.1    Holzhutter, H.-G.2
  • 42
    • 0028861437 scopus 로고
    • Elusive affinities
    • Janin, J. (1995) Elusive affinities. Proteins 21, 30-39.
    • (1995) Proteins , vol.21 , pp. 30-39
    • Janin, J.1
  • 43
    • 0032311808 scopus 로고    scopus 로고
    • Prediction of binding energetics from structure using empirical parameterization
    • Baker, B. M., and Murphy, K. P. (1998) Prediction of binding energetics from structure using empirical parameterization. Methods Enzymol. 295, 294-315.
    • (1998) Methods Enzymol , vol.295 , pp. 294-315
    • Baker, B.M.1    Murphy, K.P.2
  • 44
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker, B. M., and Murphy, K. P. (1996) Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys. J. 71, 2049-2055.
    • (1996) Biophys. J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 45
    • 0030892423 scopus 로고    scopus 로고
    • Heat capacities of protein functional groups
    • Makhatadze, G. I., Lopez, M. M., and Privalov, P. L. (1997) Heat capacities of protein functional groups. Biophys. Chem. 64, 93-101.
    • (1997) Biophys. Chem , vol.64 , pp. 93-101
    • Makhatadze, G.I.1    Lopez, M.M.2    Privalov, P.L.3
  • 46
    • 33645768556 scopus 로고    scopus 로고
    • Binding-linked protonation of a DNA minor-groove agent
    • Nguyen, B., Stanek, J., and Wilson, W. D. (2006) Binding-linked protonation of a DNA minor-groove agent. Biophys. J. 90, 1319-1328.
    • (2006) Biophys. J , vol.90 , pp. 1319-1328
    • Nguyen, B.1    Stanek, J.2    Wilson, W.D.3
  • 47
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods
    • Day, Y. S., Baird, C. L., Rich, R. L., and Myszka, D. G. (2002) Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods. Protein Sci. 11, 1017-1025.
    • (2002) Protein Sci , vol.11 , pp. 1017-1025
    • Day, Y.S.1    Baird, C.L.2    Rich, R.L.3    Myszka, D.G.4
  • 48
    • 11144310680 scopus 로고    scopus 로고
    • Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1
    • Gaiser, O. J., Ball, L. J., Schmieder, P., Leitner, D., Strauss, H., Wahl, M., Kuhne, R., Oschkinat, H., and Heinemann, U. (2004) Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1. Biochemistry 43, 15983-15995.
    • (2004) Biochemistry , vol.43 , pp. 15983-15995
    • Gaiser, O.J.1    Ball, L.J.2    Schmieder, P.3    Leitner, D.4    Strauss, H.5    Wahl, M.6    Kuhne, R.7    Oschkinat, H.8    Heinemann, U.9
  • 49
    • 33748953157 scopus 로고    scopus 로고
    • Interpretation of the temperature dependence of equilibrium and rate constants
    • Winzor, D. J., and Jackson, C. M. (2006) Interpretation of the temperature dependence of equilibrium and rate constants. J. Mol. Recognit. 19, 389-407.
    • (2006) J. Mol. Recognit , vol.19 , pp. 389-407
    • Winzor, D.J.1    Jackson, C.M.2
  • 50
    • 34249946686 scopus 로고    scopus 로고
    • Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response
    • Wang, B., Matsuoka, S., Ballif, B. A., Zhang, D., Smogorzewska, A., Gygi, S. P., and Elledge, S. J. (2007) Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response. Science 316, 1194-1198.
    • (2007) Science , vol.316 , pp. 1194-1198
    • Wang, B.1    Matsuoka, S.2    Ballif, B.A.3    Zhang, D.4    Smogorzewska, A.5    Gygi, S.P.6    Elledge, S.J.7
  • 51
    • 34547662882 scopus 로고    scopus 로고
    • CCDC98 targets BRCA1 to DNA damage sites
    • Liu, Z., Wu, J., and Yu, X. (2007) CCDC98 targets BRCA1 to DNA damage sites. Nat. Struct. Mol. Biol. 14, 716-720.
    • (2007) Nat. Struct. Mol. Biol , vol.14 , pp. 716-720
    • Liu, Z.1    Wu, J.2    Yu, X.3
  • 52
    • 33744822528 scopus 로고    scopus 로고
    • ACCA phosphopeptide recognition by the BRCT repeats of BRCA1
    • Ray, H., Moreau, K., Dizin, E., Callebaut, I., and Venezia, N. D. (2006) ACCA phosphopeptide recognition by the BRCT repeats of BRCA1. J. Mol. Biol. 359, 973-982.
    • (2006) J. Mol. Biol , vol.359 , pp. 973-982
    • Ray, H.1    Moreau, K.2    Dizin, E.3    Callebaut, I.4    Venezia, N.D.5
  • 53
    • 34548441314 scopus 로고    scopus 로고
    • Thermodynamics of phosphopeptide tethering to BRCT: The structural minima for inhibitor design
    • Lokesh, G. L., Muralidhara, B. K., Negi, S. S., and Natarajan, A. (2007) Thermodynamics of phosphopeptide tethering to BRCT: The structural minima for inhibitor design. J. Am. Chem. Soc. 129, 10658-10659.
    • (2007) J. Am. Chem. Soc , vol.129 , pp. 10658-10659
    • Lokesh, G.L.1    Muralidhara, B.K.2    Negi, S.S.3    Natarajan, A.4
  • 54
    • 0034674706 scopus 로고    scopus 로고
    • Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor
    • Yu, X., and Baer, R. (2000) Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor. J. Biol. Chem. 275, 18541-18549.
    • (2000) J. Biol. Chem , vol.275 , pp. 18541-18549
    • Yu, X.1    Baer, R.2
  • 56
    • 0037462647 scopus 로고    scopus 로고
    • Structural consequences of a cancer-causing BRCA1-BRCT missense mutation
    • Williams, R. S., and Glover, J. N. (2003) Structural consequences of a cancer-causing BRCA1-BRCT missense mutation. J. Biol. Chem. 278, 2630-2635.
    • (2003) J. Biol. Chem , vol.278 , pp. 2630-2635
    • Williams, R.S.1    Glover, J.N.2
  • 57
    • 0346101739 scopus 로고    scopus 로고
    • Detection of protein folding defects caused by BRCA1-BRCT truncation and missense mutations
    • Williams, R. S., Chasman, D. I., Hau, D. D., Hui, B., Lau, A. Y., and Glover, J. N. (2003) Detection of protein folding defects caused by BRCA1-BRCT truncation and missense mutations. J. Biol. Chem. 278, 53007-53016.
    • (2003) J. Biol. Chem , vol.278 , pp. 53007-53016
    • Williams, R.S.1    Chasman, D.I.2    Hau, D.D.3    Hui, B.4    Lau, A.Y.5    Glover, J.N.6
  • 60
    • 0027942020 scopus 로고
    • + reductase and the role of water at the complex interface
    • + reductase and the role of water at the complex interface. Biochemistry 33, 13321-13328.
    • (1994) Biochemistry , vol.33 , pp. 13321-13328
    • Jelesarov, I.1    Bosshard, H.R.2


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