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Volumn 3, Issue 7, 2004, Pages 729-742

Mutations in the nucleotide-binding domain of MutS homologs uncouple cell death from cell survival

Author keywords

Cell death; Cell survival; MutS homologs

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CISPLATIN; PROTEIN MSH2; PROTEIN MSH6; PROTEIN MUTS; PROTEIN SUBUNIT;

EID: 2642554558     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2004.02.011     Document Type: Article
Times cited : (38)

References (67)
  • 1
    • 0035161816 scopus 로고    scopus 로고
    • Functional interactions and signaling properties of mammalian DNA mismatch repair proteins
    • Bellacosa A. Functional interactions and signaling properties of mammalian DNA mismatch repair proteins. Cell Death Differ. 8:2001;1076-1092
    • (2001) Cell Death Differ. , vol.8 , pp. 1076-1092
    • Bellacosa, A.1
  • 2
    • 0036252540 scopus 로고    scopus 로고
    • DNA mismatch repair defects: Role in colorectal carcinogenesis
    • Jacob S., Praz F. DNA mismatch repair defects: role in colorectal carcinogenesis. Biochimie. 84:2002;27-47
    • (2002) Biochimie , vol.84 , pp. 27-47
    • Jacob, S.1    Praz, F.2
  • 3
    • 0032907596 scopus 로고    scopus 로고
    • Involvement of the DNA MMR system in antineoplastic drug resistance
    • Lage H., Dietel M. Involvement of the DNA MMR system in antineoplastic drug resistance. J. Cancer Res. Clin. Oncol. 125:1999;156-165
    • (1999) J. Cancer Res. Clin. Oncol. , vol.125 , pp. 156-165
    • Lage, H.1    Dietel, M.2
  • 4
    • 0035558723 scopus 로고    scopus 로고
    • Mismatch repair defects as a cause of resistance to cytotoxic drugs
    • Irving J.A., Hall A.G. Mismatch repair defects as a cause of resistance to cytotoxic drugs. Expert. Rev. Anticancer Ther. 1:2001;149-158
    • (2001) Expert. Rev. Anticancer Ther. , vol.1 , pp. 149-158
    • Irving, J.A.1    Hall, A.G.2
  • 5
    • 0142123326 scopus 로고    scopus 로고
    • Mismatch repair and response to DNA-damaging antitumour therapies
    • Bignami M., Casorelli I., Karran P. Mismatch repair and response to DNA-damaging antitumour therapies. Eur. J. Cancer. 39:2003;2142-2149
    • (2003) Eur. J. Cancer , vol.39 , pp. 2142-2149
    • Bignami, M.1    Casorelli, I.2    Karran, P.3
  • 6
    • 0642345198 scopus 로고    scopus 로고
    • DNA damage-triggered apoptosis: Critical role of DNA repair, double-strand breaks, cell proliferation and signaling
    • Kaina B. DNA damage-triggered apoptosis: critical role of DNA repair, double-strand breaks, cell proliferation and signaling. Biochem. Pharmacol. 66:2003;1547-1554
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1547-1554
    • Kaina, B.1
  • 7
    • 0042377252 scopus 로고    scopus 로고
    • Recognition and repair of DNA-cisplatin adducts
    • Wozniak K., Blasiak J. Recognition and repair of DNA-cisplatin adducts. Acta Biochim. Polym. 49:2002;583-596
    • (2002) Acta Biochim. Polym. , vol.49 , pp. 583-596
    • Wozniak, K.1    Blasiak, J.2
  • 8
    • 0033841622 scopus 로고    scopus 로고
    • Molecular mechanisms involved in cisplatin cytotoxicity
    • Jordan P., Carmo-Fonseca M. Molecular mechanisms involved in cisplatin cytotoxicity. Cell Mol. Life Sci. 57:2000;1229-1235
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 1229-1235
    • Jordan, P.1    Carmo-Fonseca, M.2
  • 9
    • 0141452189 scopus 로고    scopus 로고
    • Role of mismatch repair in the induction of chromosomal aberrations and sister chromatid exchanges in cells treated with different chemotherapeutic agents
    • Vernole P., Pepponi R., D'Atri S. Role of mismatch repair in the induction of chromosomal aberrations and sister chromatid exchanges in cells treated with different chemotherapeutic agents. Cancer Chemother. Pharmacol. 52:2003;185-192
    • (2003) Cancer Chemother. Pharmacol. , vol.52 , pp. 185-192
    • Vernole, P.1    Pepponi, R.2    D'Atri, S.3
  • 10
    • 0035687887 scopus 로고    scopus 로고
    • Mechanisms of tolerance to DNA damaging therapeutic drugs
    • Karran P. Mechanisms of tolerance to DNA damaging therapeutic drugs. Carcinogenesis. 22:2001;1931-1937
    • (2001) Carcinogenesis , vol.22 , pp. 1931-1937
    • Karran, P.1
  • 11
    • 0034622670 scopus 로고    scopus 로고
    • The effect of O6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3
    • Berardini M., Mazurek A., Fishel R. The effect of O6-methylguanine DNA adducts on the adenosine nucleotide switch functions of hMSH2-hMSH6 and hMSH2-hMSH3. J. Biol. Chem. 275:2000;27851-27857
    • (2000) J. Biol. Chem. , vol.275 , pp. 27851-27857
    • Berardini, M.1    Mazurek, A.2    Fishel, R.3
  • 12
    • 0344284564 scopus 로고    scopus 로고
    • Interaction of mismatch repair protein PMS2 and the p53-related transcription factor p73 in apoptosis response to cisplatin
    • Shimodaira H., Yoshioka-Yamashita A., Kolodner R.D., Wang J.Y.J. Interaction of mismatch repair protein PMS2 and the p53-related transcription factor p73 in apoptosis response to cisplatin. Proc. Natl. Acad. Sci. U.S.A. 100:2003;2420-2425
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 2420-2425
    • Shimodaira, H.1    Yoshioka-Yamashita, A.2    Kolodner, R.D.3    Wang, J.Y.J.4
  • 13
    • 0033290537 scopus 로고    scopus 로고
    • The role of MMR in DNA damage-induced apoptosis
    • Li G.-M. The role of MMR in DNA damage-induced apoptosis. Oncol. Res. 11:1999;393-400
    • (1999) Oncol. Res. , vol.11 , pp. 393-400
    • Li, G.-M.1
  • 15
    • 0032529467 scopus 로고    scopus 로고
    • The role of hMLH1, hMSH3, and hMSH6 defects in cisplatin and oxaliplatin resistance: Correlation with replicative bypass of platinum-DNA adducts
    • Vaisman A., Varchenko M., Umar A., Kunkel T.A., Risinger J.I., Barrett J.C., Hamilton T.C., Chaney S.G. The role of hMLH1, hMSH3, and hMSH6 defects in cisplatin and oxaliplatin resistance: correlation with replicative bypass of platinum-DNA adducts. Cancer Res. 58:1998;3579-3585
    • (1998) Cancer Res. , vol.58 , pp. 3579-3585
    • Vaisman, A.1    Varchenko, M.2    Umar, A.3    Kunkel, T.A.4    Risinger, J.I.5    Barrett, J.C.6    Hamilton, T.C.7    Chaney, S.G.8
  • 16
    • 0033389390 scopus 로고    scopus 로고
    • The role of DNA mismatch repair in cisplatin mutagenicity
    • Lin X., Kim H.-K., Howell S.B. The role of DNA mismatch repair in cisplatin mutagenicity. J. Inorg. Biochem. 77:1999;89-93
    • (1999) J. Inorg. Biochem. , vol.77 , pp. 89-93
    • Lin, X.1    Kim, H.-K.2    Howell, S.B.3
  • 18
    • 0037742273 scopus 로고    scopus 로고
    • Binding discrimination of MutS to a set of lesions and compound lesions (base damage and mismatch) reveals its potential role as a cisplatin-damaged DNA sensing protein
    • Fourrier L., Brooks P., Malinge J.-M. Binding discrimination of MutS to a set of lesions and compound lesions (base damage and mismatch) reveals its potential role as a cisplatin-damaged DNA sensing protein. J. Biol. Chem. 278:2003;21267-21275
    • (2003) J. Biol. Chem. , vol.278 , pp. 21267-21275
    • Fourrier, L.1    Brooks, P.2    Malinge, J.-M.3
  • 21
    • 0030811508 scopus 로고    scopus 로고
    • Selective recognition of a cisplatin-DNA adduct by human MMR proteins
    • Yamada M., O'Regan E., Brown R., Karran P. Selective recognition of a cisplatin-DNA adduct by human MMR proteins. Nucl. Acids Res. 25:1997;491-496
    • (1997) Nucl. Acids Res. , vol.25 , pp. 491-496
    • Yamada, M.1    O'Regan, E.2    Brown, R.3    Karran, P.4
  • 22
    • 0031053575 scopus 로고    scopus 로고
    • Recognition and repair of compound DNA lesions (base damage and mismatch) by human MMR and excision repair systems
    • Mu D., Tursun M., Duckett D.R., Drummond J.T., Modrich P., Sancar A. Recognition and repair of compound DNA lesions (base damage and mismatch) by human MMR and excision repair systems. Mol. Cell. Biol. 17:1997;760-769
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 760-769
    • Mu, D.1    Tursun, M.2    Duckett, D.R.3    Drummond, J.T.4    Modrich, P.5    Sancar, A.6
  • 23
    • 0030198880 scopus 로고    scopus 로고
    • The mismatch-repair protein hMSH2 binds selectively to DNA adducts of the anticancer drug cisplatin
    • Mello J.A., Acharya S., Fishel R., Essigmann J.M. The mismatch-repair protein hMSH2 binds selectively to DNA adducts of the anticancer drug cisplatin. Chem. Biol. 3:1996;579-589
    • (1996) Chem. Biol. , vol.3 , pp. 579-589
    • Mello, J.A.1    Acharya, S.2    Fishel, R.3    Essigmann, J.M.4
  • 24
    • 0029783348 scopus 로고    scopus 로고
    • Repair of cisplatin-DNA adducts by the mammalian excision nuclease
    • Zamble D.B., Mu D., Reardon J.T., Sancar A., Lippard S.J. Repair of cisplatin-DNA adducts by the mammalian excision nuclease. Biochemistry. 35:1996;10004-10013
    • (1996) Biochemistry , vol.35 , pp. 10004-10013
    • Zamble, D.B.1    Mu, D.2    Reardon, J.T.3    Sancar, A.4    Lippard, S.J.5
  • 25
    • 0030751955 scopus 로고    scopus 로고
    • Differential human nucleotide excision repair of paired and mispaired cisplatin-DNA adducts
    • Moggs J.G., Szymkowski D.E., Yamada M., Karran P., Wood R.D. Differential human nucleotide excision repair of paired and mispaired cisplatin-DNA adducts. Nucl. Acids Res. 25:1997;480-491
    • (1997) Nucl. Acids Res. , vol.25 , pp. 480-491
    • Moggs, J.G.1    Szymkowski, D.E.2    Yamada, M.3    Karran, P.4    Wood, R.D.5
  • 26
    • 0030877559 scopus 로고    scopus 로고
    • Differential induction of c-Jun NH2-terminal kinase and c-Abl kinase in DNA mismatch repair-proficient and -deficient cells exposed to cisplatin
    • Nehme A., Baskaran R., Aebi S., Fink D., Nebel S., Cenni B., Wang J.Y., Howell S.B., Christen R.D. Differential induction of c-Jun NH2-terminal kinase and c-Abl kinase in DNA mismatch repair-proficient and -deficient cells exposed to cisplatin. Cancer Res. 57:1997;3253-3257
    • (1997) Cancer Res. , vol.57 , pp. 3253-3257
    • Nehme, A.1    Baskaran, R.2    Aebi, S.3    Fink, D.4    Nebel, S.5    Cenni, B.6    Wang, J.Y.7    Howell, S.B.8    Christen, R.D.9
  • 27
    • 0033600234 scopus 로고    scopus 로고
    • The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage
    • Gong J., Costanzo A., Yang H.-Q., Melino G., Kaelin W.G. Jr., Levrero M., Wang J.Y. The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage. Nature. 399:1999;806-809
    • (1999) Nature , vol.399 , pp. 806-809
    • Gong, J.1    Costanzo, A.2    Yang, H.-Q.3    Melino, G.4    Kaelin Jr., W.G.5    Levrero, M.6    Wang, J.Y.7
  • 29
    • 0030962035 scopus 로고    scopus 로고
    • Hypermutability of homonucleotide runs in mismatch repair and DNA polymerase proofreading yeast mutants
    • Tran H.T., Keen J.T., Kricker M., Resnick M.A., Gordenin D.A. Hypermutability of homonucleotide runs in mismatch repair and DNA polymerase proofreading yeast mutants. Mol. Cell. Biol. 17:1997;2859-2865
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2859-2865
    • Tran, H.T.1    Keen, J.T.2    Kricker, M.3    Resnick, M.A.4    Gordenin, D.A.5
  • 30
    • 0033607008 scopus 로고    scopus 로고
    • Mutator phenotypes of common polymorphisms and missense mutations in MSH2
    • Drotschmann K., Clark A.B., Kunkel T.A. Mutator phenotypes of common polymorphisms and missense mutations in MSH2. Curr. Biol. 9:1999;907-910
    • (1999) Curr. Biol. , vol.9 , pp. 907-910
    • Drotschmann, K.1    Clark, A.B.2    Kunkel, T.A.3
  • 31
    • 0037019605 scopus 로고    scopus 로고
    • Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6
    • Drotschmann K., Yang W., Kunkel T.A. Evidence for sequential action of two ATPase active sites in yeast Msh2-Msh6. DNA Repair. 1:2002;743-753
    • (2002) DNA Repair , vol.1 , pp. 743-753
    • Drotschmann, K.1    Yang, W.2    Kunkel, T.A.3
  • 33
    • 0035824554 scopus 로고    scopus 로고
    • Asymmetric recognition of DNA local distortion: Structure-based functional studies of eukaryotic Msh2-Msh6
    • Drotschmann K., Yang W., Brownewell F.E., Kool E.T., Kunkel T.A. Asymmetric recognition of DNA local distortion: structure-based functional studies of eukaryotic Msh2-Msh6. J. Biol. Chem. 276:2001;46225-46339
    • (2001) J. Biol. Chem. , vol.276 , pp. 46225-46339
    • Drotschmann, K.1    Yang, W.2    Brownewell, F.E.3    Kool, E.T.4    Kunkel, T.A.5
  • 36
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., McCammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125:1998;185-195
    • (1998) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 37
    • 0035102126 scopus 로고    scopus 로고
    • Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair
    • Junop M.S., Obmolova G., Rausch K., Hsieh P., Yang W. Composite active site of an ABC ATPase: MutS uses ATP to verify mismatch recognition and authorize DNA repair. Mol. Cell. 7:2001;1-12
    • (2001) Mol. Cell , vol.7 , pp. 1-12
    • Junop, M.S.1    Obmolova, G.2    Rausch, K.3    Hsieh, P.4    Yang, W.5
  • 38
    • 0037415693 scopus 로고    scopus 로고
    • The alternating ATPase domains of MutS control DNA mismatch repair
    • Lamers M.H., Winterwerp H.H.K., Sixma T.K. The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J. 22:2003;746-756
    • (2003) EMBO J. , vol.22 , pp. 746-756
    • Lamers, M.H.1    Winterwerp, H.H.K.2    Sixma, T.K.3
  • 39
    • 0030962031 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of Msh2p-Msh6p: Role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition
    • Alani E., Sokolsky T., Studamire B., Miret J.J., Lahue R.S. Genetic and biochemical analysis of Msh2p-Msh6p: role of ATP hydrolysis and Msh2p-Msh6p subunit interactions in mismatch base pair recognition. Mol. Cell. Biol. 17:1997;2436-2447
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2436-2447
    • Alani, E.1    Sokolsky, T.2    Studamire, B.3    Miret, J.J.4    Lahue, R.S.5
  • 40
    • 0031784272 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair
    • Studamire B., Quach T., Alani E. Saccharomyces cerevisiae Msh2p and Msh6p ATPase activities are both required during mismatch repair. Mol. Cell. Biol. 18:1998;7590-7601
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7590-7601
    • Studamire, B.1    Quach, T.2    Alani, E.3
  • 42
    • 0034641938 scopus 로고    scopus 로고
    • Crystal structures of MMR protein MutS and its complex with a substrate DNA
    • Obmolova G., Bam C., Hsieh P., Yang W. Crystal structures of MMR protein MutS and its complex with a substrate DNA. Nature. 407:2000;703-710
    • (2000) Nature , vol.407 , pp. 703-710
    • Obmolova, G.1    Bam, C.2    Hsieh, P.3    Yang, W.4
  • 43
    • 0034737442 scopus 로고    scopus 로고
    • The MutL ATPase is required for mismatch repair
    • Spampinato C., Modrich P. The MutL ATPase is required for mismatch repair. J. Biol. Chem. 275:2000;9863-9869
    • (2000) J. Biol. Chem. , vol.275 , pp. 9863-9869
    • Spampinato, C.1    Modrich, P.2
  • 44
    • 0035830953 scopus 로고    scopus 로고
    • MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp
    • Bowers J., Tran P.T., Joshi A., Liskay R.M., Alani E. MSH-MLH complexes formed at a DNA mismatch are disrupted by the PCNA sliding clamp. J. Mol. Biol. 306:2001;957-968
    • (2001) J. Mol. Biol. , vol.306 , pp. 957-968
    • Bowers, J.1    Tran, P.T.2    Joshi, A.3    Liskay, R.M.4    Alani, E.5
  • 47
    • 0032913389 scopus 로고    scopus 로고
    • MSH3 deficiency is not sufficient for a mutator phenotype in Chinese hamster ovary cells
    • Hinz J.M., Meuth M. MSH3 deficiency is not sufficient for a mutator phenotype in Chinese hamster ovary cells. Carcinogenesis. 20:1999;215-220
    • (1999) Carcinogenesis , vol.20 , pp. 215-220
    • Hinz, J.M.1    Meuth, M.2
  • 49
    • 0031577279 scopus 로고    scopus 로고
    • Frequent somatic mutations of hMSH3 with reference to microsatellite instability in hereditary non-polyposis colorectal cancers
    • Akiyama Y., Tsubouchi N., Yuasa Y. Frequent somatic mutations of hMSH3 with reference to microsatellite instability in hereditary non-polyposis colorectal cancers. Biochem. Biophys. Res. Commun. 236:1997;248-252
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 248-252
    • Akiyama, Y.1    Tsubouchi, N.2    Yuasa, Y.3
  • 51
    • 0033946516 scopus 로고    scopus 로고
    • Genetic progression in microsatellite instability high (MSI-H) colon cancers correlates with clinico-pathological parameters: A study of the TGFbetaRII, BAX, hMSH3, hMSH6, IGFIIR and BLM genes
    • Calin G.A., Gafa R., Tibiletti M.G., Herlea V., Becheanu G., Cavazzini L., Barbanti-Brodano G., Nenci I., Negrini M., Lanza G. Genetic progression in microsatellite instability high (MSI-H) colon cancers correlates with clinico-pathological parameters: a study of the TGFbetaRII, BAX, hMSH3, hMSH6, IGFIIR and BLM genes. Int. J. Cancer. 89:2000;230-235
    • (2000) Int. J. Cancer , vol.89 , pp. 230-235
    • Calin, G.A.1    Gafa, R.2    Tibiletti, M.G.3    Herlea, V.4    Becheanu, G.5    Cavazzini, L.6    Barbanti-Brodano, G.7    Nenci, I.8    Negrini, M.9    Lanza, G.10
  • 52
    • 0035844994 scopus 로고    scopus 로고
    • Germline and somatic mutations in hMSH6 and hMSH3 in gastrointestinal cancers of the microsatellite mutator phenotype
    • Ohmiya N., Matsumoto S., Yamamoto H., Baranovskaya S., Malkhosyan S.R., Perucho M. Germline and somatic mutations in hMSH6 and hMSH3 in gastrointestinal cancers of the microsatellite mutator phenotype. Gene. 272:2001;301-313
    • (2001) Gene , vol.272 , pp. 301-313
    • Ohmiya, N.1    Matsumoto, S.2    Yamamoto, H.3    Baranovskaya, S.4    Malkhosyan, S.R.5    Perucho, M.6
  • 54
    • 0037414642 scopus 로고    scopus 로고
    • Transfer of the MSH2-MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA
    • Lau P.J., Kolodner R.D. Transfer of the MSH2-MSH6 complex from proliferating cell nuclear antigen to mispaired bases in DNA. J. Biol. Chem. 278:2003;14-17
    • (2003) J. Biol. Chem. , vol.278 , pp. 14-17
    • Lau, P.J.1    Kolodner, R.D.2
  • 55
    • 0036597521 scopus 로고    scopus 로고
    • HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions
    • Heinen C.D., Wilson T., Mazurek A., Berardini M., Butz C. HNPCC mutations in hMSH2 result in reduced hMSH2-hMSH6 molecular switch functions. Cancer Cell. 1:2002;469-478
    • (2002) Cancer Cell , vol.1 , pp. 469-478
    • Heinen, C.D.1    Wilson, T.2    Mazurek, A.3    Berardini, M.4    Butz, C.5
  • 57
    • 0034695488 scopus 로고    scopus 로고
    • Mutation in the magnesium binding site of hMSH6 disables the hMutS-alpha sliding clamp from translocating along DNA
    • Iaccarino I., Marra G., Dufner P., Jiricny J. Mutation in the magnesium binding site of hMSH6 disables the hMutS-alpha sliding clamp from translocating along DNA. J. Biol. Chem. 275:2000;2080-2086
    • (2000) J. Biol. Chem. , vol.275 , pp. 2080-2086
    • Iaccarino, I.1    Marra, G.2    Dufner, P.3    Jiricny, J.4
  • 58
    • 1542782362 scopus 로고    scopus 로고
    • Hydrolytically deficient MutS E694A is defective in the MutL-dependent activation of MutH and in the mismatch-dependent assembly of the MutS-MutL-heteroduplex complex
    • Baitinger C., Burdett V., Modrich P. Hydrolytically deficient MutS E694A is defective in the MutL-dependent activation of MutH and in the mismatch-dependent assembly of the MutS-MutL-heteroduplex complex. J. Biol. Chem. 278:2003;49505-49511
    • (2003) J. Biol. Chem. , vol.278 , pp. 49505-49511
    • Baitinger, C.1    Burdett, V.2    Modrich, P.3
  • 59
  • 61
    • 0025734115 scopus 로고
    • Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities
    • Haber L.T., Walker G.C. Altering the conserved nucleotide binding motif in the Salmonella typhimurium MutS mismatch repair protein affects both its ATPase and mismatch binding activities. EMBO J. 10:1991;2707-2715
    • (1991) EMBO J. , vol.10 , pp. 2707-2715
    • Haber, L.T.1    Walker, G.C.2
  • 62
    • 0033610878 scopus 로고    scopus 로고
    • Nucleotide-promoted release of hMutS alpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism
    • Blackwell L.J., Martik D., Bjornson K.P., Bjornson E.S., Modrich P. Nucleotide-promoted release of hMutS alpha from heteroduplex DNA is consistent with an ATP-dependent translocation mechanism. J. Biol. Chem. 273:1998;32055-32062
    • (1998) J. Biol. Chem. , vol.273 , pp. 32055-32062
    • Blackwell, L.J.1    Martik, D.2    Bjornson, K.P.3    Bjornson, E.S.4    Modrich, P.5
  • 63
    • 0041669372 scopus 로고    scopus 로고
    • The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair
    • Acharya S., Foster P.L., Brooks P., Fishel R. The coordinated functions of the E. coli MutS and MutL proteins in mismatch repair. Mol. Cell. 12:2003;233-246
    • (2003) Mol. Cell , vol.12 , pp. 233-246
    • Acharya, S.1    Foster, P.L.2    Brooks, P.3    Fishel, R.4
  • 64
    • 0029868110 scopus 로고    scopus 로고
    • Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair
    • Marsischky G.T., Filosi N., Kane M.F., Kolodner R. Redundancy of Saccharomyces cerevisiae MSH3 and MSH6 in MSH2-dependent mismatch repair. Genes Dev. 10:1996;407-420
    • (1996) Genes Dev. , vol.10 , pp. 407-420
    • Marsischky, G.T.1    Filosi, N.2    Kane, M.F.3    Kolodner, R.4
  • 65
    • 0029659046 scopus 로고    scopus 로고
    • HMutS-beta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA
    • Palombo F., Iaccarino I., Nakajima E., Ikejima M., Shimada T., Jiricny J. hMutS-beta, a heterodimer of hMSH2 and hMSH3, binds to insertion/deletion loops in DNA. Curr. Biol. 6:1996;1181-1184
    • (1996) Curr. Biol. , vol.6 , pp. 1181-1184
    • Palombo, F.1    Iaccarino, I.2    Nakajima, E.3    Ikejima, M.4    Shimada, T.5    Jiricny, J.6
  • 66
    • 0030897578 scopus 로고    scopus 로고
    • Microsatellite instability in yeast: Dependence on repeat unit size and DNA mismatch repair genes
    • Sia E.A., Kokoska R.J., Dominska M., Greenwell P., Petes T.D. Microsatellite instability in yeast: dependence on repeat unit size and DNA mismatch repair genes. Mol. Cell Biol. 17:1997;2851-2858
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2851-2858
    • Sia, E.A.1    Kokoska, R.J.2    Dominska, M.3    Greenwell, P.4    Petes, T.D.5
  • 67
    • 0038797998 scopus 로고    scopus 로고
    • Crystal structure and biochemical analysis of the MutS-ADP-beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair
    • Alani E., Lee J.Y., Schofield M.J., Kijas A.W., Hsieh P., Yang W. Crystal structure and biochemical analysis of the MutS-ADP-beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair. J. Biol. Chem. 278:2003;16088-16094
    • (2003) J. Biol. Chem. , vol.278 , pp. 16088-16094
    • Alani, E.1    Lee, J.Y.2    Schofield, M.J.3    Kijas, A.W.4    Hsieh, P.5    Yang, W.6


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