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Volumn 9, Issue 7, 2014, Pages

Flexibility of PCNA-protein interface accommodates differential binding partners

Author keywords

[No Author keywords available]

Indexed keywords

CYCLINE; AKT1 PROTEIN, HUMAN; HYBRID PROTEIN; LIGAND; PEPTIDE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE 3 KINASE; PROTEIN BINDING; PROTEIN KINASE B;

EID: 84904490612     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0102481     Document Type: Article
Times cited : (15)

References (60)
  • 1
    • 0041885325 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen (PCNA): A dancer with many partners
    • DOI 10.1242/jcs.00653
    • Maga G, Hübscher U (2003) Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J Cell Sci 116: 3051-3060. doi:10.1242/jcs.00653. (Pubitemid 37038954)
    • (2003) Journal of Cell Science , vol.116 , Issue.15 , pp. 3051-3060
    • Maga, G.1    Hubscher, U.2
  • 2
    • 34249066085 scopus 로고    scopus 로고
    • PCNA, the Maestro of the Replication Fork
    • DOI 10.1016/j.cell.2007.05.003, PII S0092867407005946
    • Moldovan G-L, Pfander B, Jentsch S (2007) PCNA, the Maestro of the Replication Fork. Cell 129: 665-679. doi:10.1016/j.cell.2007.05.003. (Pubitemid 46802385)
    • (2007) Cell , vol.129 , Issue.4 , pp. 665-679
    • Moldovan, G.-L.1    Pfander, B.2    Jentsch, S.3
  • 3
    • 67749127822 scopus 로고    scopus 로고
    • PCNA on the crossroad of cancer
    • doi:10.1042/BST0370605
    • Stoimenov I, Helleday T (2009) PCNA on the crossroad of cancer. Biochem Soc Trans 37: 605. doi:10.1042/BST0370605.
    • (2009) Biochem Soc Trans , vol.37 , pp. 605
    • Stoimenov, I.1    Helleday, T.2
  • 4
    • 84876786426 scopus 로고    scopus 로고
    • Regulation of PCNA-protein interactions for genome stability
    • doi:10.1038/nrm3562
    • Mailand N, Gibbs-Seymour I, Bekker-Jensen S (2013) Regulation of PCNA-protein interactions for genome stability. Nat Rev Mol Cell Biol 14: 269-282. doi:10.1038/nrm3562.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 269-282
    • Mailand, N.1    Gibbs-Seymour, I.2    Bekker-Jensen, S.3
  • 5
    • 0039710446 scopus 로고    scopus 로고
    • Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen
    • doi:10.1093/emboj/17.8.2412
    • Jónsson ZO, Hindges R, Hübscher U (1998) Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen. EMBO J 17: 2412-2425. doi:10.1093/emboj/17. 8.2412.
    • (1998) EMBO J , vol.17 , pp. 2412-2425
    • Jónsson, Z.O.1    Hindges, R.2    Hübscher, U.3
  • 6
    • 57349184695 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen: A proteomics view
    • doi:10.1007/s00018-008-8305-x
    • Naryzhny SN (2008) Proliferating cell nuclear antigen: a proteomics view. Cell Mol Life Sci CMLS 65: 3789-3808. doi:10.1007/s00018-008-8305-x.
    • (2008) Cell Mol Life Sci CMLS , vol.65 , pp. 3789-3808
    • Naryzhny, S.N.1
  • 7
    • 0034720729 scopus 로고    scopus 로고
    • A quantitative study of the in vitro binding of the C-terminal domain of p21 to PCNA: Affinity, stoichiometry, and thermodynamics
    • DOI 10.1021/bi992498r
    • Zheleva DI, Zhelev NZ, Fischer PM, Duff SV, Warbrick E, et al. (2000) A quantitative study of the in vitro binding of the C-terminal domain of p21 to PCNA: affinity, stoichiometry, and thermodynamics. Biochemistry 39: 7388-7397. (Pubitemid 30422055)
    • (2000) Biochemistry , vol.39 , Issue.25 , pp. 7388-7397
    • Zheleva, D.I.1    Zhelev, N.Z.2    Fischer, P.M.3    Duff, S.V.4    Warbrick, E.5    Blake, D.G.6    Lane, D.P.7
  • 8
    • 40649100251 scopus 로고    scopus 로고
    • Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathways
    • doi:10.1016/j.jmb.2007.10.074
    • Guo Z, Chavez V, Singh P, Finger LD, Hang H, et al. (2008) Comprehensive mapping of the C-terminus of flap endonuclease-1 reveals distinct interaction sites for five proteins that represent different DNA replication and repair pathways. J Mol Biol 377: 679-690. doi:10.1016/j.jmb.2007.10.074.
    • (2008) J Mol Biol , vol.377 , pp. 679-690
    • Guo, Z.1    Chavez, V.2    Singh, P.3    Finger, L.D.4    Hang, H.5
  • 9
    • 0030913166 scopus 로고    scopus 로고
    • Homologous regions of Fen1 and p21(Cip1) compete for binding to the same site on PCNA: A potential mechanism to co-ordinate DNA replication and repair
    • Warbrick E, Lane DP, Glover DM, Cox LS (1997) Homologous regions of Fen1 and p21Cip1 compete for binding to the same site on PCNA: a potential mechanism to co-ordinate DNA replication and repair. Oncogene 14: 2313-2321. doi:10.1038/sj.onc.1201072. (Pubitemid 27260723)
    • (1997) Oncogene , vol.14 , Issue.19 , pp. 2313-2321
    • Warbrick, E.1    Lane, D.P.2    Glover, D.M.3    Cox, L.S.4
  • 10
    • 9944227232 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-δ p66 subunit and flap endonuclease-1
    • DOI 10.1016/j.str.2004.09.018, PII S0969212604003533
    • Bruning JB, Shamoo Y (2004) Structural and Thermodynamic Analysis of Human PCNA with Peptides Derived from DNA Polymerase-δ p66 Subunit and Flap Endonuclease-1. Structure 12: 2209-2219. doi:10.1016/j.str.2004.09.018. (Pubitemid 39593198)
    • (2004) Structure , vol.12 , Issue.12 , pp. 2209-2219
    • Bruning, J.B.1    Shamoo, Y.2
  • 11
    • 79955993911 scopus 로고    scopus 로고
    • PCNA directs type 2 RNase H activity on DNA replication and repair substrates
    • doi:10.1093/nar/gkq980
    • Bubeck D, Reijns MAM, Graham SC, Astell KR, Jones EY, et al. (2011) PCNA directs type 2 RNase H activity on DNA replication and repair substrates. Nucleic Acids Res 39: 3652-3666. doi:10.1093/nar/gkq980.
    • (2011) Nucleic Acids Res , vol.39 , pp. 3652-3666
    • Bubeck, D.1    Reijns, M.A.M.2    Graham, S.C.3    Astell, K.R.4    Jones, E.Y.5
  • 12
    • 0030592544 scopus 로고    scopus 로고
    • Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA
    • DOI 10.1016/S0092-8674(00)81347-1
    • Gulbis JM, Kelman Z, Hurwitz J, O'Donnell M, Kuriyan J (1996) Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNA. Cell 87: 297-306. doi:10.1016/S0092-8674(00)81347-1. (Pubitemid 26359007)
    • (1996) Cell , vol.87 , Issue.2 , pp. 297-306
    • Gulbis, J.M.1    Kelman, Z.2    Hurwitz, J.3    O'Donnell, M.4    Kuriyan, J.5
  • 14
    • 70350340728 scopus 로고    scopus 로고
    • The role of dynamic conformational ensembles in biomolecular recognition
    • doi:10.1038/nchembio.232
    • Boehr DD, Nussinov R, Wright PE (2009) The role of dynamic conformational ensembles in biomolecular recognition. Nat Chem Biol 5: 789-796. doi:10.1038/nchembio.232.
    • (2009) Nat Chem Biol , vol.5 , pp. 789-796
    • Boehr, D.D.1    Nussinov, R.2    Wright, P.E.3
  • 15
    • 61349196789 scopus 로고    scopus 로고
    • Differential Responses of the Backbone and Side-Chain Conformational Dynamics in FKBP12 upon Binding the Transition-State Analog FK506: Implications for Transition-State Stabilization and Target Protein Recognition
    • doi:10.1016/j.jmb.2009.01.047
    • Brath U, Akke M (2009) Differential Responses of the Backbone and Side-Chain Conformational Dynamics in FKBP12 upon Binding the Transition-State Analog FK506: Implications for Transition-State Stabilization and Target Protein Recognition. J Mol Biol 387: 233-244. doi:10.1016/j.jmb.2009.01.047.
    • (2009) J Mol Biol , vol.387 , pp. 233-244
    • Brath, U.1    Akke, M.2
  • 16
    • 64349107039 scopus 로고    scopus 로고
    • Solution Structure and Dynamics of the Small GTPase RalB in Its Active Conformation: Significance for Effector Protein Binding
    • doi:10.1021/bi802129d
    • Fenwick RB, Prasannan S, Campbell LJ, Nietlispach D, Evetts KA, et al. (2009) Solution Structure and Dynamics of the Small GTPase RalB in Its Active Conformation: Significance for Effector Protein Binding. Biochemistry 48: 2192-2206. doi:10.1021/bi802129d.
    • (2009) Biochemistry , vol.48 , pp. 2192-2206
    • Fenwick, R.B.1    Prasannan, S.2    Campbell, L.J.3    Nietlispach, D.4    Evetts, K.A.5
  • 17
    • 34547096510 scopus 로고    scopus 로고
    • Structural determinants for ligand-receptor conformational selection in a peptide G protein-coupled receptor
    • DOI 10.1074/jbc.M610413200
    • Lu Z-L, Coetsee M, White CD, Millar RP (2007) Structural Determinants for Ligand-Receptor Conformational Selection in a Peptide G Protein-coupled Receptor. J Biol Chem 282: 17921-17929. doi:10.1074/jbc.M610413200. (Pubitemid 47100331)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17921-17929
    • Lu, Z.-L.1    Coetsee, M.2    White, C.D.3    Millar, R.P.4
  • 18
    • 84877863454 scopus 로고    scopus 로고
    • In silico discovery of small-molecule Ras inhibitors that display antitumor activity by blocking the Ras-effector interaction
    • doi:10.1073/pnas.1217730110
    • Shima F, Yoshikawa Y, Ye M, Araki M, Matsumoto S, et al. (2013) In silico discovery of small-molecule Ras inhibitors that display antitumor activity by blocking the Ras-effector interaction. Proc Natl Acad Sci 110: 8182-8187. doi:10.1073/pnas.1217730110.
    • (2013) Proc Natl Acad Sci , vol.110 , pp. 8182-8187
    • Shima, F.1    Yoshikawa, Y.2    Ye, M.3    Araki, M.4    Matsumoto, S.5
  • 19
    • 84855347756 scopus 로고    scopus 로고
    • Interfacial inhibitors: Targeting macromolecular complexes
    • doi:10.1038/nrd3404
    • Pommier Y, Marchand C (2012) Interfacial inhibitors: targeting macromolecular complexes. Nat Rev Drug Discov 11: 25-36. doi:10.1038/nrd3404.
    • (2012) Nat Rev Drug Discov , vol.11 , pp. 25-36
    • Pommier, Y.1    Marchand, C.2
  • 20
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells JA, McClendon CL (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature 450: 1001-1009. doi:10.1038/nature06526. (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2
  • 22
    • 84876427538 scopus 로고    scopus 로고
    • Proliferating Cell Nuclear Antigen (PCNA) Interactions in Solution Studied by NMR
    • doi:10.1371/journal.pone.0048390
    • De Biasio A, Campos-Olivas R, Sánchez R, López-Alonso JP, Pantoja-Uceda D, et al. (2012) Proliferating Cell Nuclear Antigen (PCNA) Interactions in Solution Studied by NMR. PLOS ONE 7: e48390. doi:10.1371/journal.pone.0048390.
    • (2012) PLOS ONE , vol.7
    • De Biasio, A.1    Campos-Olivas, R.2    Sánchez, R.3    López-Alonso, J.P.4    Pantoja-Uceda, D.5
  • 24
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • DOI 10.1177/108705719900400206
    • Zhang J-H, Chung TDY, Oldenburg KR (1999) A Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J Biomol Screen 4: 67-73. doi:10.1177/108705719900400206. (Pubitemid 29278954)
    • (1999) Journal of Biomolecular Screening , vol.4 , Issue.2 , pp. 67-73
    • Zhang, J.-H.1    Chung, T.D.Y.2    Oldenburg, K.R.3
  • 26
    • 11144265736 scopus 로고    scopus 로고
    • A general framework for development and data analysis of competitive high-throughput screens for small-molecule inhibitors of protein-protein interactions by fluorescence polarization
    • DOI 10.1021/bi048233g
    • Roehrl MHA, Wang JY, Wagner G (2004) A General Framework for Development and Data Analysis of Competitive High-Throughput Screens for Small-Molecule Inhibitors of Protein2Protein Interactions by Fluorescence Polarization. Biochemistry 43: 16056-16066. doi:10.1021/bi048233g. (Pubitemid 40041019)
    • (2004) Biochemistry , vol.43 , Issue.51 , pp. 16056-16066
    • Roehrl, M.H.A.1    Wang, J.Y.2    Wagner, G.3
  • 29
    • 33750398103 scopus 로고    scopus 로고
    • Bio3d: An R package for the comparative analysis of protein structures
    • DOI 10.1093/bioinformatics/btl461
    • Grant BJ, Rodrigues APC, ElSawy KM, McCammon JA, Caves LSD (2006) Bio3d: an R package for the comparative analysis of protein structures. Bioinformatics 22: 2695-2696. doi:10.1093/bioinformatics/btl461. (Pubitemid 44642612)
    • (2006) Bioinformatics , vol.22 , Issue.21 , pp. 2695-2696
    • Grant, B.J.1    Rodrigues, A.P.C.2    ElSawy, K.M.3    McCammon, J.A.4    Caves, L.S.D.5
  • 31
    • 77954260900 scopus 로고    scopus 로고
    • ANCHOR: A web server and database for analysis of protein-protein interaction binding pockets for drug discovery
    • doi:10.1093/nar/gkq502
    • Meireles LMC, Dömling AS, Camacho CJ (2010) ANCHOR: a web server and database for analysis of protein-protein interaction binding pockets for drug discovery. Nucleic Acids Res 38: W407-W411. doi:10.1093/nar/gkq502.
    • (2010) Nucleic Acids Res , vol.38
    • Meireles, L.M.C.1    Dömling, A.S.2    Camacho, C.J.3
  • 32
    • 84859965553 scopus 로고    scopus 로고
    • Identification of Small Molecule Proliferating Cell Nuclear Antigen (PCNA) Inhibitor That Disrupts Interactions with PIP-box Proteins and Inhibits DNA Replication
    • doi:10.1074/jbc.M112.353201
    • Punchihewa C, Inoue A, Hishiki A, Fujikawa Y, Connelly M, et al. (2012) Identification of Small Molecule Proliferating Cell Nuclear Antigen (PCNA) Inhibitor That Disrupts Interactions with PIP-box Proteins and Inhibits DNA Replication. J Biol Chem 287: 14289-14300. doi:10.1074/jbc.M112.353201.
    • (2012) J Biol Chem , vol.287 , pp. 14289-14300
    • Punchihewa, C.1    Inoue, A.2    Hishiki, A.3    Fujikawa, Y.4    Connelly, M.5
  • 33
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng Y, Prusoff WH (1973) Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem Pharmacol 22: 3099-3108.
    • (1973) Biochem Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 34
    • 60649098779 scopus 로고    scopus 로고
    • Proliferating cell nuclear antigen destabilizes c-Abl tyrosine kinase and regulates cell apoptosis in response to DNA damage
    • doi:10.1007/s10495-009-0313-2
    • He X, Wei C, Song T, Yuan J, Zhang Y, et al. (2009) Proliferating cell nuclear antigen destabilizes c-Abl tyrosine kinase and regulates cell apoptosis in response to DNA damage. Apoptosis Int J Program Cell Death 14: 268-275. doi:10.1007/s10495-009-0313-2.
    • (2009) Apoptosis Int J Program Cell Death , vol.14 , pp. 268-275
    • He, X.1    Wei, C.2    Song, T.3    Yuan, J.4    Zhang, Y.5
  • 35
    • 49749129283 scopus 로고    scopus 로고
    • Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening
    • doi:10.1107/S0907444908021665
    • Hlinkova V, Xing G, Bauer J, Shin YJ, Dionne I, et al. (2008) Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening. Acta Crystallogr D 64: 941-949. doi:10.1107/S0907444908021665.
    • (2008) Acta Crystallogr D , vol.64 , pp. 941-949
    • Hlinkova, V.1    Xing, G.2    Bauer, J.3    Shin, Y.J.4    Dionne, I.5
  • 36
    • 0029121622 scopus 로고
    • Expression and Physicochemical Characterization of Human Proliferating Cell Nuclear Antigen
    • doi:10.1021/bi00034a002
    • Zhang P, Zhang S-J, Zhang Z, Woessner JF, Lee MYWT (1995) Expression and Physicochemical Characterization of Human Proliferating Cell Nuclear Antigen. Biochemistry 34: 10703-10712. doi:10.1021/bi00034a002.
    • (1995) Biochemistry , vol.34 , pp. 10703-10712
    • Zhang, P.1    Zhang, S.-J.2    Zhang, Z.3    Woessner, J.F.4    Lee, M.Y.W.T.5
  • 37
    • 0029678248 scopus 로고    scopus 로고
    • Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases
    • Yao N, Turner J, Kelman Z, Stukenberg PT, Dean F, et al. (1996) Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases. Genes Cells Devoted Mol Cell Mech 1: 101-113. (Pubitemid 126673110)
    • (1996) Genes to Cells , vol.1 , Issue.1 , pp. 101-113
    • Yao, N.1    Turner, J.2    Kelman, Z.3    Todd, S.P.4    Dean, F.5    Shechter, D.6    Pan, Z.-Q.7    Hurwitz, J.8    O'Donnell, M.9
  • 38
    • 76649142732 scopus 로고    scopus 로고
    • Hill coefficients, dose-response curves and allosteric mechanisms
    • doi:10.1007/s12154-009-0029-3
    • Prinz H (2010) Hill coefficients, dose-response curves and allosteric mechanisms. J Chem Biol 3: 37-44. doi:10.1007/s12154-009-0029-3.
    • (2010) J Chem Biol , vol.3 , pp. 37-44
    • Prinz, H.1
  • 39
    • 66149112970 scopus 로고    scopus 로고
    • Specific function of phosphoinositide 3-kinase beta in the control of DNA replication
    • doi:10.1073/pnas.0812000106
    • Marqués M, Kumar A, Poveda AM, Zuluaga S, Hernández C, et al. (2009) Specific function of phosphoinositide 3-kinase beta in the control of DNA replication. Proc Natl Acad Sci 106: 7525-7530. doi:10.1073/pnas. 0812000106.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 7525-7530
    • Marqués, M.1    Kumar, A.2    Poveda, A.M.3    Zuluaga, S.4    Hernández, C.5
  • 40
    • 13844280351 scopus 로고    scopus 로고
    • Human 3-methyladenine-DNA glycosylase: Effect of sequence context on excision, association with PCNA, and stimulation by AP endonuclease
    • DOI 10.1016/j.jmb.2005.01.014
    • Xia L, Zheng L, Lee H-W, Bates SE, Federico L, et al. (2005) Human 3-Methyladenine-DNA Glycosylase: Effect of Sequence Context on Excision, Association with PCNA, and Stimulation by AP Endonuclease. J Mol Biol 346: 1259-1274. doi:10.1016/j.jmb.2005.01.014. (Pubitemid 40248827)
    • (2005) Journal of Molecular Biology , vol.346 , Issue.5 , pp. 1259-1274
    • Xia, L.1    Zheng, L.2    Lee, H.-W.3    Bates, S.E.4    Federico, L.5    Shen, B.6    O'Connor, T.R.7
  • 42
    • 84875223664 scopus 로고    scopus 로고
    • Small molecule inhibitors of PCNA/PIP-box interaction suppress translesion DNA synthesis
    • doi:10.1016/j.bmc.2013.01.022
    • Actis M, Inoue A, Evison B, Perry S, Punchihewa C, et al. (2013) Small molecule inhibitors of PCNA/PIP-box interaction suppress translesion DNA synthesis. Bioorg Med Chem 21: 1972-1977. doi:10.1016/j.bmc.2013.01.022.
    • (2013) Bioorg Med Chem , vol.21 , pp. 1972-1977
    • Actis, M.1    Inoue, A.2    Evison, B.3    Perry, S.4    Punchihewa, C.5
  • 43
    • 0000372879 scopus 로고    scopus 로고
    • Protein2Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis
    • doi:10.1021/cr960387h
    • Stites WE (1997) Protein2Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational Analysis. Chem Rev 97: 1233-1250. doi:10.1021/cr960387h.
    • (1997) Chem Rev , vol.97 , pp. 1233-1250
    • Stites, W.E.1
  • 44
    • 0036805481 scopus 로고    scopus 로고
    • Intramolecular interactions at protein surfaces and their impact on protein function
    • doi:10.1016/S0968-0004(02)02184-9
    • Robertson AD (2002) Intramolecular interactions at protein surfaces and their impact on protein function. Trends Biochem Sci 27: 521-526. doi:10.1016/S0968-0004(02)02184-9.
    • (2002) Trends Biochem Sci , vol.27 , pp. 521-526
    • Robertson, A.D.1
  • 45
    • 33846925964 scopus 로고    scopus 로고
    • The molecular architecture of protein-protein binding sites
    • DOI 10.1016/j.sbi.2007.01.004, PII S0959440X0700005X, Foldinf and Binding / Protein-Nucleic Interactions
    • Reichmann D, Rahat O, Cohen M, Neuvirth H, Schreiber G (2007) The molecular architecture of protein-protein binding sites. Curr Opin Struct Biol 17: 67-76. doi:10.1016/j.sbi.2007.01.004. (Pubitemid 46240815)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 67-76
    • Reichmann, D.1    Rahat, O.2    Cohen, M.3    Neuvirth, H.4    Schreiber, G.5
  • 46
    • 0035836496 scopus 로고    scopus 로고
    • A novel PCNA-binding motif identified by the panning of a random peptide display library
    • DOI 10.1021/bi010103+
    • Xu H, Zhang P, Liu L, Lee MYWT (2001) A Novel PCNA-Binding Motif Identified by the Panning of a Random Peptide Display Library. Biochemistry 40: 4512-4520. doi:10.1021/bi010103+. (Pubitemid 32319597)
    • (2001) Biochemistry , vol.40 , Issue.14 , pp. 4512-4520
    • Xu, H.1    Zhang, P.2    Liu, L.3    Lee, M.Y.W.T.4
  • 47
    • 69949163202 scopus 로고    scopus 로고
    • Identification of a Novel, Widespread, and Functionally Important PCNA-Binding Motif
    • doi:10.1083/jcb.200903138
    • Gilljam KM, Feyzi E, Aas PA, Sousa MML, Müller R, et al. (2009) Identification of a Novel, Widespread, and Functionally Important PCNA-Binding Motif. J Cell Biol 186: 645-654. doi:10.1083/jcb.200903138.
    • (2009) J Cell Biol , vol.186 , pp. 645-654
    • Gilljam, K.M.1    Feyzi, E.2    Aas, P.A.3    Sousa, M.M.L.4    Müller, R.5
  • 48
    • 78650630819 scopus 로고    scopus 로고
    • Fluorescence Polarization Assays in Small Molecule Screening
    • doi:10.1517/17460441.2011.537322
    • Lea WA, Simeonov A (2011) Fluorescence Polarization Assays in Small Molecule Screening. Expert Opin Drug Discov 6: 17-32. doi:10.1517/17460441.2011. 537322.
    • (2011) Expert Opin Drug Discov , vol.6 , pp. 17-32
    • Lea, W.A.1    Simeonov, A.2
  • 49
    • 0030474049 scopus 로고    scopus 로고
    • What can we learn from molecular recognition in protein-ligand complexes for the design of new drugs?
    • Böhm H-J, Klebe G (1996) What Can We Learn from Molecular Recognition in Protein-Ligand Complexes for the Design of New Drugs? Angew Chem Int Ed Engl 35: 2588-2614. doi:10.1002/anie.199625881. (Pubitemid 27025001)
    • (1996) Angewandte Chemie - International Edition in English , vol.35 , Issue.22 , pp. 2588-2614
    • Bohm, H.-J.1    Klebe, G.2
  • 50
    • 0034663710 scopus 로고    scopus 로고
    • Dynamics of proteins predicted by molecular simulations and analytical approaches: Application to alpha-amylase inhibitor
    • DOI 10.1002/1097-0134(20000815)40:3<512::AID-PROT1
    • Doruker P, Atilgan AR, Bahar I (2000) Dynamics of proteins predicted by molecular dynamics simulations and analytical approaches: application to alpha-amylase inhibitor. Proteins 40: 512-524. (Pubitemid 30624460)
    • (2000) Proteins: Structure, Function and Genetics , vol.40 , Issue.3 , pp. 512-524
    • Doruker, P.1    Atilgan, A.R.2    Bahar, I.3
  • 51
    • 54549098184 scopus 로고    scopus 로고
    • Target Flexibility: An Emerging Consideration in Drug Discovery and Design
    • doi:10.1021/jm800562d
    • Cozzini P, Kellogg GE, Spyrakis F, Abraham DJ, Costantino G, et al. (2008) Target Flexibility: An Emerging Consideration in Drug Discovery and Design. J Med Chem 51: 6237-6255. doi:10.1021/jm800562d.
    • (2008) J Med Chem , vol.51 , pp. 6237-6255
    • Cozzini, P.1    Kellogg, G.E.2    Spyrakis, F.3    Abraham, D.J.4    Costantino, G.5
  • 52
    • 0030587930 scopus 로고    scopus 로고
    • p21Cip1/Waf1 disrupts the recruitment of human Fen1 by proliferating-cell nuclear antigen into the DNA replication complex
    • Chen U, Chen S, Saha P, Dutta A (1996) p21Cip1/Waf1 disrupts the recruitment of human Fen1 by proliferating-cell nuclear antigen into the DNA replication complex. Proc Natl Acad Sci 93: 11597-11602.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 11597-11602
    • Chen, U.1    Chen, S.2    Saha, P.3    Dutta, A.4
  • 53
    • 84861949244 scopus 로고    scopus 로고
    • Developing peptide-based multivalent antagonists of proliferating cell nuclear antigen and a fluorescence-based PCNA binding assay
    • doi:10.1016/j.ab.2012.04.018
    • Bozza WP, Yang K, Wang J, Zhuang Z (2012) Developing peptide-based multivalent antagonists of proliferating cell nuclear antigen and a fluorescence-based PCNA binding assay. Anal Biochem 427: 69-78. doi:10.1016/j.ab.2012.04.018.
    • (2012) Anal Biochem , vol.427 , pp. 69-78
    • Bozza, W.P.1    Yang, K.2    Wang, J.3    Zhuang, Z.4
  • 54
    • 77952146825 scopus 로고    scopus 로고
    • Nuclear phosphoinositide 3-kinase β controls double-strand break DNA repair
    • doi:10.1073/pnas.0914242107
    • Kumar A, Fernandez-Capetillo O, Carrera AC (2010) Nuclear phosphoinositide 3-kinase β controls double-strand break DNA repair. Proc Natl Acad Sci USA 107: 7491-7496. doi:10.1073/pnas.0914242107.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 7491-7496
    • Kumar, A.1    Fernandez-Capetillo, O.2    Carrera, A.C.3
  • 55
    • 1042275583 scopus 로고    scopus 로고
    • A Dissection of Specific and Non-specific Protein-Protein Interfaces
    • DOI 10.1016/j.jmb.2003.12.073
    • Bahadur RP, Chakrabarti P, Rodier F, Janin J (2004) A Dissection of Specific and Non-specific Protein-Protein Interfaces. J Mol Biol 336: 943-955. doi:10.1016/j.jmb.2003.12.073. (Pubitemid 38201541)
    • (2004) Journal of Molecular Biology , vol.336 , Issue.4 , pp. 943-955
    • Bahadur, R.P.1    Chakrabarti, P.2    Rodier, F.3    Janin, J.4
  • 56
    • 78149392991 scopus 로고    scopus 로고
    • Subtle Alterations in PCNA-Partner Interactions Severely Impair DNA Replication and Repair
    • doi:10.1371/journal.pbio.1000507
    • Fridman Y, Palgi N, Dovrat D, Ben-Aroya S, Hieter P, et al. (2010) Subtle Alterations in PCNA-Partner Interactions Severely Impair DNA Replication and Repair. PLOS Biol 8: e1000507. doi:10.1371/journal.pbio.1000507.
    • (2010) PLOS Biol , vol.8
    • Fridman, Y.1    Palgi, N.2    Dovrat, D.3    Ben-Aroya, S.4    Hieter, P.5
  • 57
    • 84872620083 scopus 로고    scopus 로고
    • Computational protein design suggests that human PCNA-partner interactions are not optimized for affinity
    • doi:10.1002/prot.24190
    • Fridman Y, Gur E, Fleishman SJ, Aharoni A (2012) Computational protein design suggests that human PCNA-partner interactions are not optimized for affinity. Proteins Struct Funct Bioinforma 81: 341-348. doi:10.1002/prot.24190.
    • (2012) Proteins Struct Funct Bioinforma , vol.81 , pp. 341-348
    • Fridman, Y.1    Gur, E.2    Fleishman, S.J.3    Aharoni, A.4
  • 58
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • DOI 10.1038/nature03665
    • Pfander B, Moldovan G-L, Sacher M, Hoege C, Jentsch S (2005) SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436: 428-433. doi:10.1038/nature03665. (Pubitemid 41059056)
    • (2005) Nature , vol.436 , Issue.7049 , pp. 428-433
    • Pfander, B.1    Moldovan, G.-L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 59
    • 84896760723 scopus 로고    scopus 로고
    • A Small Molecule Inhibitor of Monoubiquitinated Proliferating Cell Nuclear Antigen (PCNA) inhibits Repair of Interstrand DNA Crosslink, enhances DNA Double-strand Break, and sensitizes Cancer Cells to Cisplatin
    • jbc.M113.520429. doi:10.1074/jbc.M113.520429
    • Inoue A, Kikuchi S, Hishiki A, Shao Y, Heath R, et al. (2014) A Small Molecule Inhibitor of Monoubiquitinated Proliferating Cell Nuclear Antigen (PCNA) inhibits Repair of Interstrand DNA Crosslink, enhances DNA Double-strand Break, and sensitizes Cancer Cells to Cisplatin. J Biol Chem: jbc.M113.520429. doi:10.1074/jbc.M113.520429.
    • (2014) J Biol Chem
    • Inoue, A.1    Kikuchi, S.2    Hishiki, A.3    Shao, Y.4    Heath, R.5
  • 60
    • 79959593991 scopus 로고    scopus 로고
    • Characterization of Protein-Protein Interaction Interfaces from a Single Species
    • doi:10.1371/journal.pone.0021053
    • Talavera D, Robertson DL, Lovell SC (2011) Characterization of Protein-Protein Interaction Interfaces from a Single Species. PLOS ONE 6: e21053. doi:10.1371/journal.pone.0021053.
    • (2011) PLOS ONE , vol.6
    • Talavera, D.1    Robertson, D.L.2    Lovell, S.C.3


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