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Volumn 20, Issue 8, 2012, Pages 1374-1383

Tangled up in knots: Structures of inactivated forms of E. coli class Ia ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

CATENANE; DEOXYADENOSINE TRIPHOSPHATE; GEMCITABINE; GEMCITABINE DIPHOSPHATE; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG; VIRUS ENZYME;

EID: 84864834779     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.05.009     Document Type: Article
Times cited : (56)

References (55)
  • 1
    • 38349152753 scopus 로고    scopus 로고
    • High hydrostatic pressure small-angle X-ray scattering cell for protein solution studies featuring diamond windows and disposable sample cells
    • N. Ando, P. Chenevier, M. Novak, M.W. Tate, and S.M. Gruner High hydrostatic pressure small-angle X-ray scattering cell for protein solution studies featuring diamond windows and disposable sample cells J. Appl. Crystallogr. 41 2008 167 175
    • (2008) J. Appl. Crystallogr. , vol.41 , pp. 167-175
    • Ando, N.1    Chenevier, P.2    Novak, M.3    Tate, M.W.4    Gruner, S.M.5
  • 3
    • 71549129302 scopus 로고    scopus 로고
    • Insight into the mechanism of inactivation of ribonucleotide reductase by gemcitabine 5′-diphosphate in the presence or absence of reductant
    • E. Artin, J. Wang, G.J. Lohman, K. Yokoyama, G. Yu, R.G. Griffin, G. Bar, and J. Stubbe Insight into the mechanism of inactivation of ribonucleotide reductase by gemcitabine 5′-diphosphate in the presence or absence of reductant Biochemistry 48 2009 11622 11629
    • (2009) Biochemistry , vol.48 , pp. 11622-11629
    • Artin, E.1    Wang, J.2    Lohman, G.J.3    Yokoyama, K.4    Yu, G.5    Griffin, R.G.6    Bar, G.7    Stubbe, J.8
  • 4
    • 77952094752 scopus 로고    scopus 로고
    • Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering
    • P. Bernadó Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering Eur. Biophys. J. 39 2010 769 780
    • (2010) Eur. Biophys. J. , vol.39 , pp. 769-780
    • Bernadó, P.1
  • 6
    • 59649102440 scopus 로고    scopus 로고
    • Conformational flexibility of metazoan fatty acid synthase enables catalysis
    • E.J. Brignole, S. Smith, and F.J. Asturias Conformational flexibility of metazoan fatty acid synthase enables catalysis Nat. Struct. Mol. Biol. 16 2009 190 197
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 190-197
    • Brignole, E.J.1    Smith, S.2    Asturias, F.J.3
  • 7
    • 0014694297 scopus 로고
    • Role of effector binding in allosteric control of ribonucleoside diphosphate reductase
    • N.C. Brown, and P. Reichard Role of effector binding in allosteric control of ribonucleoside diphosphate reductase J. Mol. Biol. 46 1969 39 55
    • (1969) J. Mol. Biol. , vol.46 , pp. 39-55
    • Brown, N.C.1    Reichard, P.2
  • 9
    • 27644443951 scopus 로고    scopus 로고
    • Bovine mitochondrial peroxiredoxin III forms a two-ring catenane
    • DOI 10.1016/j.str.2005.07.021, PII S0969212605003126
    • Z. Cao, A.W. Roszak, L.J. Gourlay, J.G. Lindsay, and N.W. Isaacs Bovine mitochondrial peroxiredoxin III forms a two-ring catenane Structure 13 2005 1661 1664 (Pubitemid 41571829)
    • (2005) Structure , vol.13 , Issue.11 , pp. 1661-1664
    • Cao, Z.1    Roszak, A.W.2    Gourlay, L.J.3    Lindsay, J.G.4    Isaacs, N.W.5
  • 10
    • 29444439322 scopus 로고    scopus 로고
    • Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques
    • DOI 10.1016/j.jmb.2005.11.021, PII S0022283605014075
    • Y. Cheng, E. Wolf, M. Larvie, O. Zak, P. Aisen, N. Grigorieff, S.C. Harrison, and T. Walz Single particle reconstructions of the transferrin-transferrin receptor complex obtained with different specimen preparation techniques J. Mol. Biol. 355 2006 1048 1065 (Pubitemid 43012147)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 1048-1065
    • Cheng, Y.1    Wolf, E.2    Larvie, M.3    Zak, O.4    Aisen, P.5    Grigorieff, N.6    Harrison, S.C.7    Walz, T.8
  • 11
    • 0027605113 scopus 로고
    • DNA damage and cell cycle regulation of ribonucleotide reductase
    • S.J. Elledge, Z. Zhou, J.B. Allen, and T.A. Navas DNA damage and cell cycle regulation of ribonucleotide reductase Bioessays 15 1993 333 339
    • (1993) Bioessays , vol.15 , pp. 333-339
    • Elledge, S.J.1    Zhou, Z.2    Allen, J.B.3    Navas, T.A.4
  • 12
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • DOI 10.1016/S0968-0004(01)01938-7, PII S0968000401019387
    • R.J. Ellis Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 2001 597 604 (Pubitemid 32925190)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.10 , pp. 597-604
    • Ellis R.John1
  • 14
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
    • M. Eriksson, U. Uhlin, S. Ramaswamy, M. Ekberg, K. Regnström, B.M. Sjöberg, and H. Eklund Binding of allosteric effectors to ribonucleotide reductase protein R1: reduction of active-site cysteines promotes substrate binding Structure 5 1997 1077 1092 (Pubitemid 27393092)
    • (1997) Structure , vol.5 , Issue.8 , pp. 1077-1092
    • Eriksson, M.1    Uhlin, U.2    Ramaswamy, S.3    Ekberg, M.4    Regnstrom, K.5    Sjoberg, B.-M.6    Eklund, H.7
  • 16
    • 75649147383 scopus 로고    scopus 로고
    • Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale
    • H. Fischer, M. de Oliverira Neto, H.B. Napolitano, I. Polikarpov, and A.F. Craievich Determination of the molecular weight of proteins in solution from a single small-angle X-ray scattering measurement on a relative scale J. Appl. Crystallogr. 43 2010 101 109
    • (2010) J. Appl. Crystallogr. , vol.43 , pp. 101-109
    • Fischer, H.1    De Oliverira Neto, M.2    Napolitano, H.B.3    Polikarpov, I.4    Craievich, A.F.5
  • 19
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • DOI 10.1016/j.jsb.2006.06.010, PII S1047847706001948, Software Tools for Macromolecular Microscopy
    • T.D. Goddard, C.C. Huang, and T.E. Ferrin Visualizing density maps with UCSF Chimera J. Struct. Biol. 157 2007 281 287 (Pubitemid 44880787)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 20
    • 0034737315 scopus 로고    scopus 로고
    • The BPTI decamer observed in acidic pH crystal forms pre-exists as a stable species in solution
    • C. Hamiaux, J. Pérez, T. Prangé, S. Veesler, M. Riès-Kautt, and P. Vachette The BPTI decamer observed in acidic pH crystal forms pre-exists as a stable species in solution J. Mol. Biol. 297 2000 697 712
    • (2000) J. Mol. Biol. , vol.297 , pp. 697-712
    • Hamiaux, C.1    Pérez, J.2    Prangé, T.3    Veesler, S.4    Riès-Kautt, M.5    Vachette, P.6
  • 21
    • 0025325071 scopus 로고
    • Evaluation of the antitumor activity of Gemcitabine (2',2'-difluoro-2'- deoxycytidine)
    • L.W. Hertel, G.B. Boder, J.S. Kroin, S.M. Rinzel, G.A. Poore, G.C. Todd, and G.B. Grindey Evaluation of the antitumor activity of gemcitabine (2′,2′-difluoro-2′-deoxycytidine) Cancer Res. 50 1990 4417 4422 (Pubitemid 20225688)
    • (1990) Cancer Research , vol.50 , Issue.14 , pp. 4417-4422
    • Hertel, L.W.1    Boder, G.B.2    Kroin, J.S.3    Rinzel, S.M.4    Poore, G.A.5    Todd, G.C.6    Grindey, G.B.7
  • 23
    • 0020336098 scopus 로고
    • The wrapping phenomenon in air-dried and negatively stained preparations
    • E. Kellenberger, M. Häner, and M. Wurtz The wrapping phenomenon in air-dried and negatively stained preparations Ultramicroscopy 9 1982 139 150
    • (1982) Ultramicroscopy , vol.9 , pp. 139-150
    • Kellenberger, E.1    Häner, M.2    Wurtz, M.3
  • 24
    • 0014010713 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli
    • A. Larsson, and P. Reichard Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli J. Biol. Chem. 241 1966 2533 2539
    • (1966) J. Biol. Chem. , vol.241 , pp. 2533-2539
    • Larsson, A.1    Reichard, P.2
  • 25
    • 0014010709 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; Allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B
    • A. Larsson, and P. Reichard Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B J. Biol. Chem. 241 1966 2540 2549
    • (1966) J. Biol. Chem. , vol.241 , pp. 2540-2549
    • Larsson, A.1    Reichard, P.2
  • 26
    • 2942563756 scopus 로고    scopus 로고
    • Ring-shaped architecture of RecR: Implications for its role in homologous recombinational DNA repair
    • DOI 10.1038/sj.emboj.7600222
    • B.I. Lee, K.H. Kim, S.J. Park, S.H. Eom, H.K. Song, and S.W. Suh Ring-shaped architecture of RecR: implications for its role in homologous recombinational DNA repair EMBO J. 23 2004 2029 2038 (Pubitemid 38737730)
    • (2004) EMBO Journal , vol.23 , Issue.10 , pp. 2029-2038
    • Lee II, B.1    Kim, K.H.2    Park, S.J.3    Eom, S.H.4    Song, H.K.5    Suh, S.W.6
  • 27
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • S. Licht, G.J. Gerfen, and J. Stubbe Thiyl radicals in ribonucleotide reductases Science 271 1996 477 481 (Pubitemid 26044465)
    • (1996) Science , vol.271 , Issue.5248 , pp. 477-481
    • Licht, S.1    Gerfen, G.J.2    Stubbe, J.3
  • 28
    • 0030587599 scopus 로고    scopus 로고
    • Crystal structure of reduced protein R2 of ribonucleotide reductase: The structural basis for oxygen activation at a dinuclear iron site
    • DOI 10.1016/S0969-2126(96)00112-8
    • D.T. Logan, X.D. Su, A. Aberg, K. Regnström, J. Hajdu, H. Eklund, and P. Nordlund Crystal structure of reduced protein R2 of ribonucleotide reductase: the structural basis for oxygen activation at a dinuclear iron site Structure 4 1996 1053 1064 (Pubitemid 26369771)
    • (1996) Structure , vol.4 , Issue.9 , pp. 1053-1064
    • Logan, D.T.1    Su, X.-D.2    Aberg, A.3    Regnstrom, K.4    Hajdu, J.5    Eklund, H.6    Nordlund, P.7
  • 30
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • DOI 10.1016/S0959-440X(99)00045-7
    • A.P. Minton Implications of macromolecular crowding for protein assembly Curr. Opin. Struct. Biol. 10 2000 34 39 (Pubitemid 30099324)
    • (2000) Current Opinion in Structural Biology , vol.10 , Issue.1 , pp. 34-39
    • Minton, A.P.1
  • 31
    • 0027283896 scopus 로고
    • Structure and function of the Escherichia coli ribonucleotide reductase protein R2
    • DOI 10.1006/jmbi.1993.1374
    • P. Nordlund, and H. Eklund Structure and function of the Escherichia coli ribonucleotide reductase protein R2 J. Mol. Biol. 232 1993 123 164 (Pubitemid 23245406)
    • (1993) Journal of Molecular Biology , vol.232 , Issue.1 , pp. 123-164
    • Nordlund, P.1    Eklund, H.2
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0030832990 scopus 로고    scopus 로고
    • Gemcitabine: Actions and interactions
    • W. Plunkett, P. Huang, and V. Gandhi Gemcitabine: actions and interactions Nucleosides Nucleotides Nucleic Acids 16 1997 1261 1270 (Pubitemid 27494460)
    • (1997) Nucleosides and Nucleotides , vol.16 , Issue.7-9 , pp. 1261-1270
    • Plunkett, W.1    Huang, P.2    Gandhi, V.3
  • 34
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • M. Radermacher, T. Wagenknecht, A. Verschoor, and J. Frank Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli J. Microsc. 146 1987 113 136
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 35
    • 0035782681 scopus 로고    scopus 로고
    • The structure of the V(1)-ATPase determined by three-dimensional electron microscopy of single particles
    • M. Radermacher, T. Ruiz, H. Wieczorek, and G. Grüber The structure of the V(1)-ATPase determined by three-dimensional electron microscopy of single particles J. Struct. Biol. 135 2001 26 37
    • (2001) J. Struct. Biol. , vol.135 , pp. 26-37
    • Radermacher, M.1    Ruiz, T.2    Wieczorek, H.3    Grüber, G.4
  • 36
    • 0023925454 scopus 로고
    • Interactions between deoxyribonucleotide and DNA synthesis
    • P. Reichard Interactions between deoxyribonucleotide and DNA synthesis Annu. Rev. Biochem. 57 1988 349 374
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 349-374
    • Reichard, P.1
  • 37
    • 58149091633 scopus 로고    scopus 로고
    • Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase
    • R. Rofougaran, M. Crona, M. Vodnala, B.M. Sjöberg, and A. Hofer Oligomerization status directs overall activity regulation of the Escherichia coli class Ia ribonucleotide reductase J. Biol. Chem. 283 2008 35310 35318
    • (2008) J. Biol. Chem. , vol.283 , pp. 35310-35318
    • Rofougaran, R.1    Crona, M.2    Vodnala, M.3    Sjöberg, B.M.4    Hofer, A.5
  • 38
    • 0022532243 scopus 로고
    • Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase
    • S.P. Salowe, and J. Stubbe Cloning, overproduction, and purification of the B2 subunit of ribonucleoside-diphosphate reductase J. Bacteriol. 165 1986 363 366 (Pubitemid 16060500)
    • (1986) Journal of Bacteriology , vol.165 , Issue.2 , pp. 363-366
    • Salowe, S.P.1    Stubbe, J.2
  • 39
    • 0023657750 scopus 로고
    • Products of the inactivation of ribonucleoside diphosphate reductase from Escherichia coli with 2′-azido-2′-deoxyuridine 5′-diphosphate
    • S.P. Salowe, M.A. Ator, and J. Stubbe Products of the inactivation of ribonucleoside diphosphate reductase from Escherichia coli with 2′-azido-2′-deoxyuridine 5′-diphosphate Biochemistry 26 1987 3408 3416
    • (1987) Biochemistry , vol.26 , pp. 3408-3416
    • Salowe, S.P.1    Ator, M.A.2    Stubbe, J.3
  • 40
    • 77951623055 scopus 로고    scopus 로고
    • Super-resolution biomolecular crystallography with low-resolution data
    • G.F. Schröder, M. Levitt, and A.T. Brunger Super-resolution biomolecular crystallography with low-resolution data Nature 464 2010 1218 1222
    • (2010) Nature , vol.464 , pp. 1218-1222
    • Schröder, G.F.1    Levitt, M.2    Brunger, A.T.3
  • 41
    • 37549042071 scopus 로고    scopus 로고
    • 2s: Distance measurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase
    • 2s: distance measurements between residues involved in the radical propagation pathway of E. coli ribonucleotide reductase J. Am. Chem. Soc. 129 2007 15748 15749
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15748-15749
    • Seyedsayamdost, M.R.1    Chan, C.T.2    Mugnaini, V.3    Stubbe, J.4    Bennati, M.5
  • 43
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a Program to Evaluate X-ray Solution Scattering of Biological Macromolecules from Atomic Coordinates J. Appl. Crystallogr. 28 1995 768 773 (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 44
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • DOI 10.1016/j.jsb.2006.05.009, PII S1047847706001894, Software Tools for Macromolecular Microscopy
    • G. Tang, L. Peng, P.R. Baldwin, D.S. Mann, W. Jiang, I. Rees, and S.J. Ludtke EMAN2: an extensible image processing suite for electron microscopy J. Struct. Biol. 157 2007 38 46 (Pubitemid 44880785)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 45
    • 0001912129 scopus 로고
    • A Large-Format High-Resolution Area X-ray Detector Based on a Fiber-Optically Bonded Charge-Coupled Device (CCD)
    • M.W. Tate, E.F. Eikenberry, S.L. Barna, M.E. Wall, J.L. Lowrance, and S.M. Gruner A Large-Format High-Resolution Area X-ray Detector Based on a Fiber-Optically Bonded Charge-Coupled Device (CCD) J. Appl. Crystallogr. 28 1995 196 205
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 196-205
    • Tate, M.W.1    Eikenberry, E.F.2    Barna, S.L.3    Wall, M.E.4    Lowrance, J.L.5    Gruner, S.M.6
  • 46
    • 0016257826 scopus 로고
    • Reaction mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Oxidation-reduction-active disulfides in the B1 subunit
    • L. Thelander Reaction mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Oxidation-reduction-active disulfides in the B1 subunit J. Biol. Chem. 249 1974 4858 4862
    • (1974) J. Biol. Chem. , vol.249 , pp. 4858-4862
    • Thelander, L.1
  • 47
    • 0016310542 scopus 로고
    • Determination of the location of proteins L14, L17, L18, L19, L22, L23 on the surface of the 5oS ribosomal subunit of Escherichia coli by immune electron microscopy
    • G.W. Tischendorf, H. Zeichhardt, and G. Stöffler Determination of the location of proteins L14, L17, L18, L19, L22, L23 on the surface of the 5oS ribosomal subunit of Escherichia coli by immune electron microscopy Mol. Gen. Genet. 134 1974 187 208
    • (1974) Mol. Gen. Genet. , vol.134 , pp. 187-208
    • Tischendorf, G.W.1    Zeichhardt, H.2    Stöffler, G.3
  • 48
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • DOI 10.1038/370533a0
    • U. Uhlin, and H. Eklund Structure of ribonucleotide reductase protein R1 Nature 370 1994 533 539 (Pubitemid 24264919)
    • (1994) Nature , vol.370 , Issue.6490 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 49
    • 0032485857 scopus 로고    scopus 로고
    • Detection of a new substrate-derived radical during inactivation of ribonucleotide reductase from Escherichia coli by gemcitabine 5'-diphosphate
    • DOI 10.1021/bi9729357
    • W.A. van der Donk, G. Yu, L. Pérez, R.J. Sanchez, J. Stubbe, V. Samano, and M.J. Robins Detection of a new substrate-derived radical during inactivation of ribonucleotide reductase from Escherichia coli by gemcitabine 5′-diphosphate Biochemistry 37 1998 6419 6426 (Pubitemid 28213662)
    • (1998) Biochemistry , vol.37 , Issue.18 , pp. 6419-6426
    • Van Der Donk, W.A.1    Yu, G.2    Perez, L.3    Sanchez, R.J.4    Stubbe, J.5    Samano, V.6    Robins, M.J.7
  • 50
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
    • N.R. Voss, C.K. Yoshioka, M. Radermacher, C.S. Potter, and B. Carragher DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy J. Struct. Biol. 166 2009 205 213
    • (2009) J. Struct. Biol. , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 52
    • 27844495735 scopus 로고    scopus 로고
    • Stimulation of mutagenesis by proportional deoxyribonucleoside triphosphate accumulation in Escherichia coli
    • DOI 10.1016/j.dnarep.2005.09.003, PII S1568786405002545
    • L.J. Wheeler, I. Rajagopal, and C.K. Mathews Stimulation of mutagenesis by proportional deoxyribonucleoside triphosphate accumulation in Escherichia coli DNA Repair (Amst.) 4 2005 1450 1456 (Pubitemid 41653306)
    • (2005) DNA Repair , vol.4 , Issue.12 , pp. 1450-1456
    • Wheeler, L.J.1    Rajagopal, I.2    Mathews, C.K.3
  • 53
    • 33645239831 scopus 로고    scopus 로고
    • Structures of eukaryotic ribonucleotide reductase i provide insights into dNTP regulation
    • H. Xu, C. Faber, T. Uchiki, J.W. Fairman, J. Racca, and C. Dealwis Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation Proc. Natl. Acad. Sci. USA 103 2006 4022 4027
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 4022-4027
    • Xu, H.1    Faber, C.2    Uchiki, T.3    Fairman, J.W.4    Racca, J.5    Dealwis, C.6
  • 54
    • 70349771790 scopus 로고    scopus 로고
    • Mechanisms of anti-cancer action and pharmacology of clofarabine
    • A. Zhenchuk, K. Lotfi, G. Juliusson, and F. Albertioni Mechanisms of anti-cancer action and pharmacology of clofarabine Biochem. Pharmacol. 78 2009 1351 1359
    • (2009) Biochem. Pharmacol. , vol.78 , pp. 1351-1359
    • Zhenchuk, A.1    Lotfi, K.2    Juliusson, G.3    Albertioni, F.4
  • 55
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • H.X. Zhou, G. Rivas, and A.P. Minton Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences Annu Rev Biophys 37 2008 375 397
    • (2008) Annu Rev Biophys , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3


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