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Volumn 287, Issue 4, 2012, Pages 2328-2341

ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease

Author keywords

[No Author keywords available]

Indexed keywords

ATP BINDING; ATP HYDROLYSIS; ENDONUCLEASES; EXONUCLEASE; EXONUCLEASE ACTIVITY; MOLECULAR SWITCHES; NUCLEASE ACTIVITY; OPEN-CLOSED TRANSITION; STRUCTURAL STATE;

EID: 84856074733     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.307041     Document Type: Article
Times cited : (33)

References (55)
  • 1
    • 78649445307 scopus 로고    scopus 로고
    • Mre11-Rad50- Nbs1 conformations and the control of sensing, signaling, and effector responses at DNA double-strand breaks
    • Williams, G. J., Lees-Miller, S. P., and Tainer, J. A. (2010) Mre11-Rad50- Nbs1 conformations and the control of sensing, signaling, and effector responses at DNA double-strand breaks. DNA Repair 9, 1299-1306
    • (2010) DNA Repair , vol.9 , pp. 1299-1306
    • Williams, G.J.1    Lees-Miller, S.P.2    Tainer, J.A.3
  • 2
    • 78649451417 scopus 로고    scopus 로고
    • Making the best of the loose ends. Mre11-Rad50 complexes and Sae2 promote DNA double-strand break resection
    • Paull, T. T. (2010) Making the best of the loose ends. Mre11-Rad50 complexes and Sae2 promote DNA double-strand break resection. DNA Repair 9, 1283-1291
    • (2010) DNA Repair , vol.9 , pp. 1283-1291
    • Paull, T.T.1
  • 4
    • 79951857925 scopus 로고    scopus 로고
    • DNA end resection. Unraveling the tail
    • Mimitou, E. P., and Symington, L. S. (2011) DNA end resection. Unraveling the tail. DNA Repair 10, 344-348
    • (2011) DNA Repair , vol.10 , pp. 344-348
    • Mimitou, E.P.1    Symington, L.S.2
  • 5
    • 79952235291 scopus 로고    scopus 로고
    • Dynamics of DNA damage response proteins at DNA breaks. A focus on protein modifications
    • Polo, S. E., and Jackson, S. P. (2011) Dynamics of DNA damage response proteins at DNA breaks. A focus on protein modifications. Genes Dev. 25, 409-433
    • (2011) Genes Dev. , vol.25 , pp. 409-433
    • Polo, S.E.1    Jackson, S.P.2
  • 6
    • 68249116573 scopus 로고    scopus 로고
    • DNA end resection. Many nucleases make light work
    • Mimitou, E. P., and Symington, L. S. (2009) DNA end resection. Many nucleases make light work. DNA Repair 8, 983-995
    • (2009) DNA Repair , vol.8 , pp. 983-995
    • Mimitou, E.P.1    Symington, L.S.2
  • 7
    • 0035930342 scopus 로고    scopus 로고
    • Promotion of Dnl4-Catalyzed DNA end-joining by the Rad50/Mre11/Xrs2 and Hdf1/Hdf2 complexes
    • DOI 10.1016/S1097-2765(01)00388-4
    • Chen, L., Trujillo, K., Ramos, W., Sung, P., and Tomkinson, A. E. (2001) Promotion of Dnl4-catalyzed DNA end-joining by the Rad50-Mre11- Xrs2 and Hdf1-Hdf2 complexes. Mol. Cell 8, 1105-1115 (Pubitemid 34031812)
    • (2001) Molecular Cell , vol.8 , Issue.5 , pp. 1105-1115
    • Chen, L.1    Trujillo, K.2    Ramos, W.3    Sung, P.4    Tomkinson, A.E.5
  • 8
    • 48649086824 scopus 로고    scopus 로고
    • The Yku70-Yku80 complex contributes to regulate double-strand break processing and checkpoint activation during the cell cycle
    • Clerici, M., Mantiero, D., Guerini, I., Lucchini, G., and Longhese, M. P. (2008) The Yku70-Yku80 complex contributes to regulate double-strand break processing and checkpoint activation during the cell cycle. EMBO Rep. 9, 810-818
    • (2008) EMBO Rep. , vol.9 , pp. 810-818
    • Clerici, M.1    Mantiero, D.2    Guerini, I.3    Lucchini, G.4    Longhese, M.P.5
  • 9
    • 0032493889 scopus 로고    scopus 로고
    • Saccharomyces Ku70, Mre11/Rad50, and RPA proteins regulate adaptation to G2/M arrest after DNA damage
    • DOI 10.1016/S0092-8674(00)81482-8
    • Lee, S. E., Moore, J. K., Holmes, A., Umezu, K., Kolodner, R. D., and Haber, J. E. (1998) Saccharomyces Ku70, mre11/rad50, and RPA proteins regulate adaptation to G2/M arrest after DNA damage. Cell 94, 399-409 (Pubitemid 28376083)
    • (1998) Cell , vol.94 , Issue.3 , pp. 399-409
    • Lee, S.E.1    Moore, J.K.2    Holmes, A.3    Umezu, K.4    Kolodner, R.D.5    Haber, J.E.6
  • 10
    • 2442463320 scopus 로고    scopus 로고
    • Role of the Nuclease Activity of Saccharomyces cerevisiae Mre11 in Repair of DNA Double-Strand Breaks in Mitotic Cells
    • DOI 10.1534/genetics.166.4.1701
    • Lewis, L. K., Storici, F., Van Komen, S., Calero, S., Sung, P., and Resnick, M. A. (2004) Role of the nuclease activity of Saccharomyces cerevisiae Mre11 in repair of DNA double-strand breaks in mitotic cells. Genetics 166, 1701-1713 (Pubitemid 38621053)
    • (2004) Genetics , vol.166 , Issue.4 , pp. 1701-1713
    • Lewis, L.K.1    Storici, F.2    Van Komen, S.3    Calero, S.4    Sung, P.5    Resnick, M.A.6
  • 11
    • 61849109768 scopus 로고    scopus 로고
    • Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2FHAdomain
    • Palmbos, P. L., Wu, D., Daley, J. M., and Wilson, T. E. (2008) Recruitment of Saccharomyces cerevisiae Dnl4-Lif1 complex to a double-strand break requires interactions with Yku80 and the Xrs2FHAdomain. Genetics 180, 1809-1819
    • (2008) Genetics , vol.180 , pp. 1809-1819
    • Palmbos, P.L.1    Wu, D.2    Daley, J.M.3    Wilson, T.E.4
  • 12
    • 4544281398 scopus 로고    scopus 로고
    • Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins
    • DOI 10.1016/j.cell.2004.08.015, PII S0092867404007974
    • Lisby, M., Barlow, J. H., Burgess, R. C., and Rothstein, R. (2004) Choreography of the DNA damage response. Spatiotemporal relationships among checkpoint and repair proteins. Cell 118, 699-713 (Pubitemid 39221730)
    • (2004) Cell , vol.118 , Issue.6 , pp. 699-713
    • Lisby, M.1    Barlow, J.H.2    Burgess, R.C.3    Rothstein, R.4
  • 13
    • 52949109260 scopus 로고    scopus 로고
    • Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation
    • Buis, J., Wu, Y., Deng, Y., Leddon, J., Westfield, G., Eckersdorff, M., Sekiguchi, J. M., Chang, S., and Ferguson, D. O. (2008) Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation. Cell 135, 85-96
    • (2008) Cell , vol.135 , pp. 85-96
    • Buis, J.1    Wu, Y.2    Deng, Y.3    Leddon, J.4    Westfield, G.5    Eckersdorff, M.6    Sekiguchi, J.M.7    Chang, S.8    Ferguson, D.O.9
  • 15
    • 0034892653 scopus 로고    scopus 로고
    • Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication
    • DOI 10.1016/S1097-2765(01)00294-5
    • Costanzo, V., Robertson, K., Bibikova, M., Kim, E., Grieco, D., Gottesman, M., Carroll, D., and Gautier, J. (2001) Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication. Mol. Cell 8, 137-147 (Pubitemid 32772912)
    • (2001) Molecular Cell , vol.8 , Issue.1 , pp. 137-147
    • Costanzo, V.1    Robertson, K.2    Bibikova, M.3    Kim, E.4    Grieco, D.5    Gottesman, M.6    Carroll, D.7    Gautier, J.8
  • 16
    • 33646122683 scopus 로고    scopus 로고
    • ATM and ATR promote Mre11-dependent restart of collapsed replication forks and prevent accumulation of DNA breaks
    • Trenz, K., Smith, E., Smith, S., and Costanzo, V. (2006) ATM and ATR promote Mre11-dependent restart of collapsed replication forks and prevent accumulation of DNA breaks. EMBO J. 25, 1764-1774
    • (2006) EMBO J. , vol.25 , pp. 1764-1774
    • Trenz, K.1    Smith, E.2    Smith, S.3    Costanzo, V.4
  • 17
    • 44949096478 scopus 로고    scopus 로고
    • A mutant allele of MRE11 found in mismatch repair-deficient tumor cells suppresses the cellular response to DNA replication fork stress in a dominant negative manner
    • DOI 10.1091/mbc.E07-09-0975
    • Wen, Q., Scorah, J., Phear, G., Rodgers, G., Rodgers, S., and Meuth, M. (2008) A mutant allele of MRE11 found in mismatch repair-deficient tumor cells suppresses the cellular response to DNA replication fork stress in a dominant negative manner. Mol. Biol. Cell 19, 1693-1705 (Pubitemid 351805121)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.4 , pp. 1693-1705
    • Wen, Q.1    Scorah, J.2    Phear, G.3    Rodgers, G.4    Rodgers, S.5    Meuth, M.6
  • 18
    • 0034749425 scopus 로고    scopus 로고
    • DNAdamage-dependent nuclear dynamics of the Mre11 complex
    • Mirzoeva, O. K., and Petrini, J. H. (2001)DNAdamage-dependent nuclear dynamics of the Mre11 complex. Mol. Cell Biol. 21, 281-288
    • (2001) Mol. Cell Biol. , vol.21 , pp. 281-288
    • Mirzoeva, O.K.1    Petrini, J.H.2
  • 19
    • 0041660970 scopus 로고    scopus 로고
    • ATM-related Tel1 associates with double-strand breaks through an Xrs2-dependent mechanism
    • DOI 10.1101/gad.1099003
    • Nakada, D., Matsumoto, K., and Sugimoto, K. (2003) ATM-related Tel1 associates with double-strand breaks through an Xrs2-dependent mechanism. Genes Dev. 17, 1957-1962 (Pubitemid 36999322)
    • (2003) Genes and Development , vol.17 , Issue.16 , pp. 1957-1962
    • Nakada, D.1    Matsumoto, K.2    Sugimoto, K.3
  • 20
    • 15844394846 scopus 로고    scopus 로고
    • Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage
    • DOI 10.1038/nature03442
    • Falck, J., Coates, J., and Jackson, S. P. (2005) Conserved modes of recruitment of ATM, ATR, and DNA-PKcs to sites of DNA damage. Nature 434, 605-611 (Pubitemid 40488547)
    • (2005) Nature , vol.434 , Issue.7033 , pp. 605-611
    • Falck, J.1    Coates, J.2    Jackson, S.P.3
  • 21
    • 34047102946 scopus 로고    scopus 로고
    • Dual role for Saccharomyces cerevisiae Tel1 in the checkpoint response to double-strand breaks
    • DOI 10.1038/sj.embor.7400911, PII 7400911
    • Mantiero, D., Clerici, M., Lucchini, G., and Longhese, M. P. (2007) Dual role for Saccharomyces cerevisiae Tel1 in the checkpoint response to double- strand breaks. EMBO Rep. 8, 380-387 (Pubitemid 46511039)
    • (2007) EMBO Reports , vol.8 , Issue.4 , pp. 380-387
    • Mantiero, D.1    Clerici, M.2    Lucchini, G.3    Longhese, M.P.4
  • 22
    • 34547950170 scopus 로고    scopus 로고
    • The Mre11-Rad50-Nbs1 complex acts both upstream and downstream of ataxia telangiectasia mutated and Rad3-related protein (ATR) to regulate the S-phase checkpoint following UV treatment
    • DOI 10.1074/jbc.M702162200
    • Olson, E., Nievera, C. J., Lee, A. Y., Chen, L., and Wu, X. (2007) The Mre11-Rad50-Nbs1 complex acts both upstream and downstream of ataxia telangiectasia mutated and Rad3-related protein (ATR) to regulate the S-phase checkpoint after UV treatment. J. Biol. Chem. 282, 22939-22952 (Pubitemid 47267303)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.31 , pp. 22939-22952
    • Olson, E.1    Nievera, C.J.2    Lee, A.Y.-L.3    Chen, L.4    Wu, X.5
  • 24
    • 77953495958 scopus 로고    scopus 로고
    • Tip60; connecting chromatin to DNA damage signaling
    • Sun, Y., Jiang, X., and Price, B. D. (2010) Tip60; connecting chromatin to DNA damage signaling. Cell Cycle 9, 930-936
    • (2010) Cell Cycle , vol.9 , pp. 930-936
    • Sun, Y.1    Jiang, X.2    Price, B.D.3
  • 25
    • 0033759543 scopus 로고    scopus 로고
    • Mre11 and Rad50 from Pyrococcus furiosus. Cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine
    • Hopfner, K. P., Karcher, A., Shin, D., Fairley, C., Tainer, J. A., and Carney, J. P. (2000) Mre11 and Rad50 from Pyrococcus furiosus. Cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine. J. Bacteriol. 182, 6036-6041
    • (2000) J. Bacteriol. , vol.182 , pp. 6036-6041
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.3    Fairley, C.4    Tainer, J.A.5    Carney, J.P.6
  • 26
    • 79956301873 scopus 로고    scopus 로고
    • Crystal structure of the Mre11-Rad50-ATPγS complex. Understanding the interplay between Mre11 and Rad50
    • Lim, H. S., Kim, J. S., Park, Y. B., Gwon, G. H., and Cho, Y. (2011) Crystal structure of the Mre11-Rad50-ATPγS complex. Understanding the interplay between Mre11 and Rad50. Genes Dev. 25, 1091-1104
    • (2011) Genes Dev. , vol.25 , pp. 1091-1104
    • Lim, H.S.1    Kim, J.S.2    Park, Y.B.3    Gwon, G.H.4    Cho, Y.5
  • 27
    • 0032085295 scopus 로고    scopus 로고
    • The 3′ to 5′ exonuclease activity of Mre11 facilitates repair of DNA double-strand breaks
    • Paull, T. T., and Gellert, M. (1998) The 3′ to 5′ exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. Mol. Cell 1, 969-979 (Pubitemid 128379258)
    • (1998) Molecular Cell , vol.1 , Issue.7 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 28
    • 0035929667 scopus 로고    scopus 로고
    • DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50-Mre11 complex
    • Trujillo, K. M., and Sung, P. (2001) DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50-Mre11 complex. J. Biol. Chem. 276, 35458-35464
    • (2001) J. Biol. Chem. , vol.276 , pp. 35458-35464
    • Trujillo, K.M.1    Sung, P.2
  • 29
    • 0033563229 scopus 로고    scopus 로고
    • Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex
    • Paull, T. T., and Gellert, M. (1999) Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11-Rad50 complex. Genes Dev. 13, 1276-1288 (Pubitemid 29250195)
    • (1999) Genes and Development , vol.13 , Issue.10 , pp. 1276-1288
    • Paull, T.T.1    Gellert, M.2
  • 30
    • 36248942617 scopus 로고    scopus 로고
    • Sae2 Is an Endonuclease that Processes Hairpin DNA Cooperatively with the Mre11/Rad50/Xrs2 Complex
    • DOI 10.1016/j.molcel.2007.11.001, PII S1097276507007332
    • Lengsfeld, B. M., Rattray, A. J., Bhaskara, V., Ghirlando, R., and Paull, T. T. (2007) Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11-Rad50-Xrs2 complex. Mol. Cell 28, 638-651 (Pubitemid 350137798)
    • (2007) Molecular Cell , vol.28 , Issue.4 , pp. 638-651
    • Lengsfeld, B.M.1    Rattray, A.J.2    Bhaskara, V.3    Ghirlando, R.4    Paull, T.T.5
  • 32
    • 66149114020 scopus 로고    scopus 로고
    • Human CtIP mediates cell cycle control of DNA end resection and double-strand break repair
    • Huertas, P., and Jackson, S. P. (2009) Human CtIP mediates cell cycle control of DNA end resection and double-strand break repair. J. Biol. Chem. 284, 9558-9565
    • (2009) J. Biol. Chem. , vol.284 , pp. 9558-9565
    • Huertas, P.1    Jackson, S.P.2
  • 35
    • 0024669753 scopus 로고
    • The yeast RAD50 gene encodes a predicted 153-kD protein containing a purine nucleotide binding domain and two large heptad-repeat regions
    • Alani, E., Subbiah, S., and Kleckner, N. (1989) The yeast RAD50 gene encodes a predicted 153-kD protein containing a purine nucleotide binding domain and two large heptad-repeat regions. Genetics 122, 47-57
    • (1989) Genetics , vol.122 , pp. 47-57
    • Alani, E.1    Subbiah, S.2    Kleckner, N.3
  • 36
    • 0028857690 scopus 로고
    • Structural and functional similarities between the SbcCD proteins of Escherichia coli and the RAD50 and MRE11 (RAD32) recombination and repair proteins of yeast
    • Sharples, G. J., and Leach, D. R. (1995) Structural and functional similarities between the SbcCD proteins of Escherichia coli and the RAD50 and MRE11 (RAD32) recombination and repair proteins of yeast. Mol. Microbiol. 17, 1215-1217
    • (1995) Mol. Microbiol. , vol.17 , pp. 1215-1217
    • Sharples, G.J.1    Leach, D.R.2
  • 37
    • 0035906860 scopus 로고    scopus 로고
    • Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase
    • DOI 10.1016/S0092-8674(01)00335-X
    • Hopfner, K. P., Karcher, A., Craig, L., Woo, T. T., Carney, J. P., and Tainer, J. A. (2001) Structural biochemistry and interaction architecture of the DNAdouble-strand break repair Mre11 nuclease and Rad50-ATPase. Cell 105, 473-485 (Pubitemid 32520853)
    • (2001) Cell , vol.105 , Issue.4 , pp. 473-485
    • Hopfner, K.-P.1    Karcher, A.2    Craig, L.3    Woo, T.T.4    Carney, J.P.5    Tainer, J.A.6
  • 38
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase. ATPdriven conformational control inDNAdouble-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P., Karcher, A., Shin, D. S., Craig, L., Arthur, L. M., Carney, J. P., and Tainer, J. A. (2000) Structural biology of Rad50 ATPase. ATPdriven conformational control inDNAdouble-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 39
    • 20544465434 scopus 로고    scopus 로고
    • SMC proteins and chromosome mechanics. From bacteria to humans
    • Hirano, T. (2005) SMC proteins and chromosome mechanics. From bacteria to humans. Philos. Trans. R. Soc. Lond B. Biol. Sci. 360, 507-514
    • (2005) Philos. Trans. R. Soc. Lond B. Biol. Sci. , vol.360 , pp. 507-514
    • Hirano, T.1
  • 43
    • 0025334351 scopus 로고
    • Analysis of wild-type and rad50 mutants of yeast suggests an intimate relationship between meiotic chromosome synapsis and recombination
    • Alani, E., Padmore, R., and Kleckner, N. (1990) Analysis of wild-type and rad50 mutants of yeast suggests an intimate relationship between meiotic chromosome synapsis and recombination. Cell 61, 419-436
    • (1990) Cell , vol.61 , pp. 419-436
    • Alani, E.1    Padmore, R.2    Kleckner, N.3
  • 44
    • 0030885998 scopus 로고    scopus 로고
    • mre11S - A yeast mutation that blocks double-strand-break processing and permits nonhomologous synapsis in meiosis
    • Nairz, K., and Klein, F. (1997) mre11S, a yeast mutation that blocks double- strand break processing and permits nonhomologous synapsis in meiosis. Genes Dev. 11, 2272-2290 (Pubitemid 27387977)
    • (1997) Genes and Development , vol.11 , Issue.17 , pp. 2272-2290
    • Nairz, K.1    Klein, F.2
  • 45
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • DOI 10.1017/S0033583507004635, PII S0033583507004635
    • Putnam, C. D., Hammel, M., Hura, G. L., and Tainer, J. A. (2007) X-ray solution scattering (SAXS) combined with crystallography and computation. Defining accurate macromolecular structures, conformations, and assemblies in solution. Q Rev. Biophys. 40, 191-285 (Pubitemid 350261954)
    • (2007) Quarterly Reviews of Biophysics , vol.40 , Issue.3 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 47
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 48
    • 8844265931 scopus 로고    scopus 로고
    • Sedimentation velocity analysis of highly heterogeneous systems
    • DOI 10.1016/j.ab.2004.08.039, PII S0003269704007225
    • Demeler, B., and van Holde, K. E. (2004) Sedimentation velocity analysis of highly heterogeneous systems. Anal. Biochem. 335, 279-288 (Pubitemid 39535193)
    • (2004) Analytical Biochemistry , vol.335 , Issue.2 , pp. 279-288
    • Demeler, B.1    Van Holde, K.E.2
  • 50
    • 66149115286 scopus 로고    scopus 로고
    • The nucleotide binding dynamics of human MSH2-MSH3 are lesion-dependent
    • Owen, B. A., H Lang, W., and McMurray, C. T. (2009) The nucleotide binding dynamics of human MSH2-MSH3 are lesion-dependent. Nat. Struct. Mol. Biol. 16, 550-557
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 550-557
    • Owen, B.A.1    H Lang, W.2    McMurray, C.T.3
  • 51
    • 24144485161 scopus 로고    scopus 로고
    • Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution of the Lamm equation
    • DOI 10.1529/biophysj.105.061135
    • Cao, W., and Demeler, B. (2005) Modeling analytical ultracentrifugation experiments with an adaptive space-time finite element solution of the Lamm equation. Biophys. J. 89, 1589-1602 (Pubitemid 41233516)
    • (2005) Biophysical Journal , vol.89 , Issue.3 , pp. 1589-1602
    • Cao, W.1    Demeler, B.2
  • 52
    • 77953002874 scopus 로고    scopus 로고
    • Diffusion in the reaction boundary of rapidly interacting macromolecules in sedimentation velocity
    • Shuck, P. (2010) Diffusion in the reaction boundary of rapidly interacting macromolecules in sedimentation velocity. Biophys. J. 98, 2741-2747
    • (2010) Biophys. J. , vol.98 , pp. 2741-2747
    • Shuck, P.1
  • 54
    • 63049099775 scopus 로고    scopus 로고
    • RAD50, an SMC family member with multiple roles in DNA break repair. How does ATP affect function?
    • Kinoshita, E., van der Linden, E., Sanchez, H., and Wyman, C. (2009) RAD50, an SMC family member with multiple roles in DNA break repair. How does ATP affect function? Chromosome Res. 17, 277-288
    • (2009) Chromosome Res. , vol.17 , pp. 277-288
    • Kinoshita, E.1    Van Der Linden, E.2    Sanchez, H.3    Wyman, C.4
  • 55
    • 38049155945 scopus 로고    scopus 로고
    • Regulation of DNA double-strand break repair pathway choice
    • Shrivastav, M., De Haro, L. P., and Nickoloff, J. A. (2008) Regulation of DNA double-strand break repair pathway choice. Cell Res. 18, 134-147
    • (2008) Cell Res. , vol.18 , pp. 134-147
    • Shrivastav, M.1    De Haro, L.P.2    Nickoloff, J.A.3


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