메뉴 건너뛰기




Volumn 425, Issue 13, 2013, Pages 2359-2371

The disordered C-terminal domain of human DNA glycosylase NEIL1 contributes to its stability via intramolecular interactions

Author keywords

DNA repair; electrostatic interactions; intrinsically unstructured region; oxidative DNA damage; protein stability

Indexed keywords

DNA GLYCOSYLTRANSFERASE; NEI ENDONUCLEASE VIII LIKE PROTEIN 1; UNCLASSIFIED DRUG;

EID: 84879097056     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.03.030     Document Type: Article
Times cited : (41)

References (58)
  • 1
    • 38049112778 scopus 로고    scopus 로고
    • Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells
    • M.L. Hegde, T.K. Hazra, and S. Mitra Early steps in the DNA base excision/single-strand interruption repair pathway in mammalian cells Cell Res. 18 2008 27 47
    • (2008) Cell Res. , vol.18 , pp. 27-47
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 3
    • 0037133684 scopus 로고    scopus 로고
    • Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA
    • T.K. Hazra, T. Izumi, I. Boldogh, B. Imhoff, Y.W. Kow, and P. Jaruga Identification and characterization of a human DNA glycosylase for repair of modified bases in oxidatively damaged DNA Proc. Natl Acad. Sci. USA 99 2002 3523 3528
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3523-3528
    • Hazra, T.K.1    Izumi, T.2    Boldogh, I.3    Imhoff, B.4    Kow, Y.W.5    Jaruga, P.6
  • 4
    • 0037125133 scopus 로고    scopus 로고
    • A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII
    • V. Bandaru, S. Sunkara, S.S. Wallace, and J.P. Bond A novel human DNA glycosylase that removes oxidative DNA damage and is homologous to Escherichia coli endonuclease VIII DNA Repair (Amst.) 1 2002 517 529
    • (2002) DNA Repair (Amst.) , vol.1 , pp. 517-529
    • Bandaru, V.1    Sunkara, S.2    Wallace, S.S.3    Bond, J.P.4
  • 5
    • 0037162995 scopus 로고    scopus 로고
    • Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions
    • T.K. Hazra, Y.W. Kow, Z. Hatahet, B. Imhoff, I. Boldogh, and S.K. Mokkapati Identification and characterization of a novel human DNA glycosylase for repair of cytosine-derived lesions J. Biol. Chem. 277 2002 30417 30420
    • (2002) J. Biol. Chem. , vol.277 , pp. 30417-30420
    • Hazra, T.K.1    Kow, Y.W.2    Hatahet, Z.3    Imhoff, B.4    Boldogh, I.5    Mokkapati, S.K.6
  • 8
    • 0347379928 scopus 로고    scopus 로고
    • Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2
    • H. Dou, S. Mitra, and T.K. Hazra Repair of oxidized bases in DNA bubble structures by human DNA glycosylases NEIL1 and NEIL2 J. Biol. Chem. 278 2003 49679 49684
    • (2003) J. Biol. Chem. , vol.278 , pp. 49679-49684
    • Dou, H.1    Mitra, S.2    Hazra, T.K.3
  • 9
    • 55249083320 scopus 로고    scopus 로고
    • Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1
    • M.L. Hegde, C.A. Theriot, A. Das, P.M. Hegde, Z. Guo, and R.K. Gary Physical and functional interaction between human oxidized base-specific DNA glycosylase NEIL1 and flap endonuclease 1 J. Biol. Chem. 283 2008 27028 27037
    • (2008) J. Biol. Chem. , vol.283 , pp. 27028-27037
    • Hegde, M.L.1    Theriot, C.A.2    Das, A.3    Hegde, P.M.4    Guo, Z.5    Gary, R.K.6
  • 10
    • 41249094475 scopus 로고    scopus 로고
    • Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes
    • H. Dou, C.A. Theriot, A. Das, M.L. Hegde, Y. Matsumoto, and I. Boldogh Interaction of the human DNA glycosylase NEIL1 with proliferating cell nuclear antigen. The potential for replication-associated repair of oxidized bases in mammalian genomes J. Biol. Chem. 283 2008 3130 3140
    • (2008) J. Biol. Chem. , vol.283 , pp. 3130-3140
    • Dou, H.1    Theriot, C.A.2    Das, A.3    Hegde, M.L.4    Matsumoto, Y.5    Boldogh, I.6
  • 11
    • 77952580830 scopus 로고    scopus 로고
    • RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures
    • C.A. Theriot, M.L. Hegde, T.K. Hazra, and S. Mitra RPA physically interacts with the human DNA glycosylase NEIL1 to regulate excision of oxidative DNA base damage in primer-template structures DNA Repair (Amst.) 9 2010 643 652
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 643-652
    • Theriot, C.A.1    Hegde, M.L.2    Hazra, T.K.3    Mitra, S.4
  • 12
    • 34548824343 scopus 로고    scopus 로고
    • The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1
    • A. Das, I. Boldogh, J.W. Lee, J.A. Harrigan, M.L. Hegde, and J. Piotrowski The human Werner syndrome protein stimulates repair of oxidative DNA base damage by the DNA glycosylase NEIL1 J. Biol. Chem. 282 2007 26591 26602
    • (2007) J. Biol. Chem. , vol.282 , pp. 26591-26602
    • Das, A.1    Boldogh, I.2    Lee, J.W.3    Harrigan, J.A.4    Hegde, M.L.5    Piotrowski, J.6
  • 13
    • 85016372853 scopus 로고    scopus 로고
    • Human DNA glycosylase NEIL1's interactions with downstream repair proteins is critical for efficient repair of oxidized DNA base damage and enhanced cell survival
    • M.L. Hegde, P.M. Hegde, D. Arijit, I. Boldogh, and S. Mitra Human DNA glycosylase NEIL1's interactions with downstream repair proteins is critical for efficient repair of oxidized DNA base damage and enhanced cell survival Biomolecules 2 2012 564 578
    • (2012) Biomolecules , vol.2 , pp. 564-578
    • Hegde, M.L.1    Hegde, P.M.2    Arijit, D.3    Boldogh, I.4    Mitra, S.5
  • 14
    • 78149469033 scopus 로고    scopus 로고
    • Functions of disordered regions in mammalian early base excision repair proteins
    • M.L. Hegde, T.K. Hazra, and S. Mitra Functions of disordered regions in mammalian early base excision repair proteins Cell. Mol. Life Sci. 67 2010 3573 3587
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 3573-3587
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 15
    • 3142702720 scopus 로고    scopus 로고
    • The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity
    • S. Doublie, V. Bandaru, J.P. Bond, and S.S. Wallace The crystal structure of human endonuclease VIII-like 1 (NEIL1) reveals a zincless finger motif required for glycosylase activity Proc. Natl Acad. Sci. USA 101 2004 10284 10289
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10284-10289
    • Doublie, S.1    Bandaru, V.2    Bond, J.P.3    Wallace, S.S.4
  • 16
    • 84867261398 scopus 로고    scopus 로고
    • Enhancement of NEIL1-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction
    • M.L. Hegde, S. Banerjee, P.M. Hegde, L.A. Bellot, T.K. Hazra, I. Boldogh, and S. Mitra Enhancement of NEIL1-initiated oxidized DNA base excision repair by heterogeneous nuclear ribonucleoprotein U (hnRNP-U) via direct interaction J. Biol. Chem. 287 2012 34202 34211
    • (2012) J. Biol. Chem. , vol.287 , pp. 34202-34211
    • Hegde, M.L.1    Banerjee, S.2    Hegde, P.M.3    Bellot, L.A.4    Hazra, T.K.5    Boldogh, I.6    Mitra, S.7
  • 17
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Y. Liu, and D.W. Bolen The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes Biochemistry 34 1995 12884 12891
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 18
    • 34447618598 scopus 로고    scopus 로고
    • DNA induces folding in alpha-synuclein: Understanding the mechanism using chaperone property of osmolytes
    • M.L. Hegde, and K.S. Rao DNA induces folding in alpha-synuclein: understanding the mechanism using chaperone property of osmolytes Arch. Biochem. Biophys. 464 2007 57 69
    • (2007) Arch. Biochem. Biophys. , vol.464 , pp. 57-69
    • Hegde, M.L.1    Rao, K.S.2
  • 20
    • 0013943915 scopus 로고
    • Validity of the "two-state" hypothesis for conformational transitions of proteins
    • R. Lumry, and R. Biltonen Validity of the "two-state" hypothesis for conformational transitions of proteins Biopolymers 4 1966 917 944
    • (1966) Biopolymers , vol.4 , pp. 917-944
    • Lumry, R.1    Biltonen, R.2
  • 22
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • R.P. Rambo, and J.A. Tainer Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law Biopolymers 95 2011 559 571
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 23
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: Comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • R.P. Rambo, and J.A. Tainer Bridging the solution divide: comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering Curr. Opin. Struct. Biol. 20 2010 128 137
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 24
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • C.D. Putnam, M. Hammel, G.L. Hura, and J.A. Tainer X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution Q. Rev. Biophys. 40 2007 191 285
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 25
    • 34248363563 scopus 로고    scopus 로고
    • Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography
    • S.E. Tsutakawa, G.L. Hura, K.A. Frankel, P.K. Cooper, and J.A. Tainer Structural analysis of flexible proteins in solution by small angle X-ray scattering combined with crystallography J. Struct. Biol. 158 2007 214 223
    • (2007) J. Struct. Biol. , vol.158 , pp. 214-223
    • Tsutakawa, S.E.1    Hura, G.L.2    Frankel, K.A.3    Cooper, P.K.4    Tainer, J.A.5
  • 26
    • 68349097394 scopus 로고    scopus 로고
    • Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)
    • G.L. Hura, A.L. Menon, M. Hammel, R.P. Rambo, F.L. Poole 2nd, and S.E. Tsutakawa Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS) Nat. Methods 6 2009 606 612
    • (2009) Nat. Methods , vol.6 , pp. 606-612
    • Hura, G.L.1    Menon, A.L.2    Hammel, M.3    Rambo, R.P.4    Poole II, F.L.5    Tsutakawa, S.E.6
  • 27
    • 67650992092 scopus 로고    scopus 로고
    • Structure and flexibility within proteins as identified through small angle X-ray scattering
    • M. Pelikan, G.L. Hura, and M. Hammel Structure and flexibility within proteins as identified through small angle X-ray scattering Gen. Physiol. Biophys. 28 2009 174 189
    • (2009) Gen. Physiol. Biophys. , vol.28 , pp. 174-189
    • Pelikan, M.1    Hura, G.L.2    Hammel, M.3
  • 28
    • 74049134920 scopus 로고    scopus 로고
    • Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex
    • M. Hammel, Y. Yu, B.L. Mahaney, B. Cai, R. Ye, and B.M. Phipps Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex J. Biol. Chem. 285 2012 1414 1423
    • (2012) J. Biol. Chem. , vol.285 , pp. 1414-1423
    • Hammel, M.1    Yu, Y.2    Mahaney, B.L.3    Cai, B.4    Ye, R.5    Phipps, B.M.6
  • 29
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • D. Schneidman-Duhovny, M. Hammel, and A. Sali FoXS: a web server for rapid computation and fitting of SAXS profiles Nucleic Acids Res. 38 2010 W540 W544
    • (2010) Nucleic Acids Res. , vol.38
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 30
    • 76249122268 scopus 로고    scopus 로고
    • Biochemistry. An ensemble view of allostery
    • V.J. Hilser Biochemistry. An ensemble view of allostery Science 327 2010 653 654
    • (2010) Science , vol.327 , pp. 653-654
    • Hilser, V.J.1
  • 31
    • 33847673237 scopus 로고    scopus 로고
    • The intricate structural chemistry of base excision repair machinery: Implications for DNA damage recognition, removal, and repair
    • K. Hitomi, S. Iwai, and J.A. Tainer The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair DNA Repair (Amst.) 6 2007 410 428
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 410-428
    • Hitomi, K.1    Iwai, S.2    Tainer, J.A.3
  • 32
    • 24044460415 scopus 로고    scopus 로고
    • DNA base damage recognition and removal: New twists and grooves
    • J.L. Huffman, O. Sundheim, and J.A. Tainer DNA base damage recognition and removal: new twists and grooves Mutat. Res. 577 2005 55 76
    • (2005) Mutat. Res. , vol.577 , pp. 55-76
    • Huffman, J.L.1    Sundheim, O.2    Tainer, J.A.3
  • 35
    • 70349472553 scopus 로고    scopus 로고
    • Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair
    • R.S. Williams, G.E. Dodson, O. Limbo, Y. Yamada, J.S. Williams, and G. Guenther Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair Cell 139 2009 87 99
    • (2009) Cell , vol.139 , pp. 87-99
    • Williams, R.S.1    Dodson, G.E.2    Limbo, O.3    Yamada, Y.4    Williams, J.S.5    Guenther, G.6
  • 36
    • 79953894934 scopus 로고    scopus 로고
    • Human flap endonuclease structures, DNA double-base flipping, and a unified understanding of the FEN1 superfamily
    • S.E. Tsutakawa, S. Classen, B.R. Chapados, A.S. Arvai, L.D. Finger, and G. Guenther Human flap endonuclease structures, DNA double-base flipping, and a unified understanding of the FEN1 superfamily Cell 145 2011 198 211
    • (2011) Cell , vol.145 , pp. 198-211
    • Tsutakawa, S.E.1    Classen, S.2    Chapados, B.R.3    Arvai, A.S.4    Finger, L.D.5    Guenther, G.6
  • 37
    • 82655181911 scopus 로고    scopus 로고
    • Intrinsic disorder in cell signaling and gene transcription
    • A. Tantos, K.H. Han, and P. Tompa Intrinsic disorder in cell signaling and gene transcription Mol. Cell. Endocrinol. 348 2012 457 465
    • (2012) Mol. Cell. Endocrinol. , vol.348 , pp. 457-465
    • Tantos, A.1    Han, K.H.2    Tompa, P.3
  • 39
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa Intrinsically unstructured proteins Trends Biochem. Sci. 27 2002 527 533
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 40
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat. Rev. Mol. Cell Biol. 6 2005 197 208
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 41
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins from A to Z
    • V.N. Uversky Intrinsically disordered proteins from A to Z Int. J. Biochem. Cell Biol. 43 2011 1090 1103
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1090-1103
    • Uversky, V.N.1
  • 43
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • V.J. Hilser, and E.B. Thompson Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins Proc. Natl Acad. Sci. USA 104 2007 8311 8315
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 44
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • H.J. Dyson, and P.E. Wright Coupling of folding and binding for unstructured proteins Curr. Opin. Struct. Biol. 12 2002 54 60
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 45
    • 70350131719 scopus 로고    scopus 로고
    • Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins
    • T.P. Schrank, D.W. Bolen, and V.J. Hilser Rational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins Proc. Natl Acad. Sci. USA 106 2009 16984 16989
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16984-16989
    • Schrank, T.P.1    Bolen, D.W.2    Hilser, V.J.3
  • 46
    • 84864545860 scopus 로고    scopus 로고
    • Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor
    • J. Li, H.N. Motlagh, C. Chakuroff, E.B. Thompson, and V.J. Hilser Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor J. Biol. Chem. 287 2012 26777 26787
    • (2012) J. Biol. Chem. , vol.287 , pp. 26777-26787
    • Li, J.1    Motlagh, H.N.2    Chakuroff, C.3    Thompson, E.B.4    Hilser, V.J.5
  • 47
    • 33751086423 scopus 로고    scopus 로고
    • Visualization of transient encounter complexes in protein-protein association
    • C. Tang, J. Iwahara, and G.M. Clore Visualization of transient encounter complexes in protein-protein association Nature 444 2006 383 386
    • (2006) Nature , vol.444 , pp. 383-386
    • Tang, C.1    Iwahara, J.2    Clore, G.M.3
  • 49
    • 0032475933 scopus 로고    scopus 로고
    • Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: Coupling DNA and PCNA binding to FEN-1 activity
    • D.J. Hosfield, C.D. Mol, B. Shen, and J.A. Tainer Structure of the DNA repair and replication endonuclease and exonuclease FEN-1: coupling DNA and PCNA binding to FEN-1 activity Cell 95 1998 135 146
    • (1998) Cell , vol.95 , pp. 135-146
    • Hosfield, D.J.1    Mol, C.D.2    Shen, B.3    Tainer, J.A.4
  • 50
    • 33749668010 scopus 로고    scopus 로고
    • A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA
    • J.M. Pascal, O.V. Tsodikov, G.L. Hura, W. Song, E.A. Cotner, and S. Classen A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA Mol. Cell 24 2006 279 291
    • (2006) Mol. Cell , vol.24 , pp. 279-291
    • Pascal, J.M.1    Tsodikov, O.V.2    Hura, G.L.3    Song, W.4    Cotner, E.A.5    Classen, S.6
  • 51
    • 0042738069 scopus 로고    scopus 로고
    • Full-length archaeal Rad51 structure and mutants: Mechanisms for RAD51 assembly and control by BRCA2
    • D.S. Shin, L. Pellegrini, D.S. Daniels, B. Yelent, L. Craig, and D. Bates Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2 EMBO J. 22 2003 4566 4576
    • (2003) EMBO J. , vol.22 , pp. 4566-4576
    • Shin, D.S.1    Pellegrini, L.2    Daniels, D.S.3    Yelent, B.4    Craig, L.5    Bates, D.6
  • 53
    • 0025861597 scopus 로고
    • Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c
    • V.A. Roberts, H.C. Freeman, A.J. Olson, J.A. Tainer, and E.D. Getzoff Electrostatic orientation of the electron-transfer complex between plastocyanin and cytochrome c J. Biol. Chem. 266 1991 13431 13441
    • (1991) J. Biol. Chem. , vol.266 , pp. 13431-13441
    • Roberts, V.A.1    Freeman, H.C.2    Olson, A.J.3    Tainer, J.A.4    Getzoff, E.D.5
  • 54
    • 0033605817 scopus 로고    scopus 로고
    • Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase
    • C.D. Putnam, M.J. Shroyer, A.J. Lundquist, C.D. Mol, A.S. Arvai, D.W. Mosbaugh, and J.A. Tainer Protein mimicry of DNA from crystal structures of the uracil-DNA glycosylase inhibitor protein and its complex with Escherichia coli uracil-DNA glycosylase J. Mol. Biol. 287 1999 331 346
    • (1999) J. Mol. Biol. , vol.287 , pp. 331-346
    • Putnam, C.D.1    Shroyer, M.J.2    Lundquist, A.J.3    Mol, C.D.4    Arvai, A.S.5    Mosbaugh, D.W.6    Tainer, J.A.7
  • 55
    • 77956545422 scopus 로고    scopus 로고
    • Specific inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: Potential etiological linkage to neurodegenerative diseases
    • M.L. Hegde, P.M. Hegde, L.M. Holthauzen, T.K. Hazra, K.S. Rao, and S. Mitra Specific inhibition of NEIL-initiated repair of oxidized base damage in human genome by copper and iron: potential etiological linkage to neurodegenerative diseases J. Biol. Chem. 285 2010 28812 28825
    • (2010) J. Biol. Chem. , vol.285 , pp. 28812-28825
    • Hegde, M.L.1    Hegde, P.M.2    Holthauzen, L.M.3    Hazra, T.K.4    Rao, K.S.5    Mitra, S.6
  • 56
    • 77958554597 scopus 로고    scopus 로고
    • Software for the high-throughput collection of SAXS data using an enhanced Blu-Ice/DCS control system
    • S. Classen, I. Rodic, J. Holton, G.L. Hura, M. Hammel, and J.A. Tainer Software for the high-throughput collection of SAXS data using an enhanced Blu-Ice/DCS control system J. Synchrotron Radiat. 17 2010 774 781
    • (2010) J. Synchrotron Radiat. , vol.17 , pp. 774-781
    • Classen, S.1    Rodic, I.2    Holton, J.3    Hura, G.L.4    Hammel, M.5    Tainer, J.A.6
  • 57
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS 2.1 - Towards automated and web-supported small-angle scattering data analysis
    • M.V. Petoukhov, P.V. Konarev, A.G. Kikhney, and D.I. Svergun ATSAS 2.1 - towards automated and web-supported small-angle scattering data analysis J. Appl. Crystallogr. 40 2007 s223 s228
    • (2007) J. Appl. Crystallogr. , vol.40
    • Petoukhov, M.V.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.