Current PubMed listings for MM Cox Lab
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Publications
2023
ME Cherry, K Dubiel, C Henry, EA Wood, SA Revitt-Mills, JL Keck, MM Cox, AM van Oijen, H Ghodke, A Robinson. (2023) Spatiotemporal Dynamics of Single-stranded DNA Intermediates in Escherichia coli. bioRxiv. 05.08.539320. DOI: 10.1101/2023.05.08.539320. Preprint
Cox MM, MF Goodman, JL Keck, A van Oijen, ST Lovett, A Robinson. (2023) Generation and Repair of Postreplication Gaps in Escherichia coli. Microbiol Mol Biol Rev. e0007822. DOI: 10.1128/mmbr.00078-22. Online ahead of print.
Osorio Garcia MA, EA Wood, JL Keck, MM Cox. (2023) Interaction with single-stranded DNA-binding protein (SSB) modulates Escherichia coli RadD DNA repair activities. J Biol Chem. 299(6):104773. DOI: 10.1016/j.jbc.2023.104773. [PDF]
Henry C, G Kaur, ME Cherry, SS Henrikus, NJ Bonde, N Sharma, HA Beyer, EA Wood, S Chitteni-Pattu, AM van Oijen, A Robinson, MM Cox. (2023) RecF protein targeting to post-replication (daughter strand) gaps II: RecF interaction with replisomes. Nucleic Acids Res. DOI: 10.1093/nar/gkad310. Online ahead of print
Henry C, N Mbele, MM Cox. (2023) RecF protein targeting to postreplication (daughter strand) gaps I: DNA binding by RecF and RecFR. Nucleic Acids Res. DOI: 10.1093/nar/gkad311 Online ahead of print
Pham P, EA Wood, MM Cox, MF Goodman. (2023) RecA and SSB genome-wide distribution in ssDNA gaps and ends in Escherichia coli. Nucleic Acids Res. DOI: 10.1093/nar/gkad263. Online ahead of print
Bonde NJ, C Henry, EA Wood, MM Cox, JL Keck. (2023) Interaction with the carboxy-terminal tip of SSB is critical for RecG function in E. coli. Nucleic Acids Res. 8;51(8):3735-3753. DOI: 10.1093/nar/gkad162. [PDF]
2022
Ojha D, MM Jaszczur, A Sikand, JP McDonald, A Robinson, AM van Oije, CH Mak, F Pinaud, MM Cox, R Woodgate, MF Goodman. (2022) Host cell RecA activates a mobile element-encoded mutagenic DNA polymerase. Nucleic Acids Res. 50(12):6854-6869. DOI: 10.1093/nar/gkac515. [PDF]
Osorio Garcia MA, KA Satyshur, MM Cox, JL Keck. (2022) X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain. PLoS One. 17(4):e0266031. DOI: 10.1371/journal.pone.0266031 [PDF]
Jain K, TH Stanage, EA Wood, MM Cox. (2022) The Escherichia coli serS gene promoter region overlaps with the rarA gene. PLoS One. 17(4):e0260282. DOI: 10.1371/journal.pone.0260282. [PDF]
Bonde NJ, ZJ Romero, S Chitteni-Pattu, MM Cox. (2022) RadD is a RecA-dependent accessory protein that accelerates DNA strand exchange. Nucleic Acids Res, 50(4):2201-2210. DOI: 10.1093/nar/gkac041 [PDF]
Pham P, Y Shao, MM Cox, MF Goodman. (2022) Genomic landscape of single-stranded DNA gapped intermediates in Escherichia coli. Nucleic Acids Res, 50(2):937-951. DOI: 10.1093/nar/gkab1269 [PDF]
2021
Jain K, EA Wood, MM Cox. (2021) The rarA gene as part of an expanded RecFOR recombination pathway: Negative epistasis and synthetic lethality with ruvB, recG, and recQ. PLoS Genet, 17(12):e1009972. DOI: 10.1371/journal.pgen.1009972 [PDF]
Bruckbauer ST, and MM Cox. (2021) Experimental evolution of extremophile resistance to ionizing radiation. Trends Genet., 37(9):830-845. DOI: 10.1016/j.tig.2021.04.011 [PDF]
Sikand A, M Jaszczur, LB Bloom, R Woodgate, MM Cox, MF Goodman. (2021) The SOS Error-Prone DNA Polymerase V Mutasome and β-Sliding Clamp Acting in Concert on Undamaged DNA and during Translesion Synthesis. Cells, 10(5):1083. DOI: 10.3390/cells10051083 [PDF]
Bruckbauer, ST, BB Minkoff, MR Sussman, MM Cox. (2021) Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman. Cells, 10(4):1083. DOI: 10.3390/cells10040954 [PDF]
Henry, C, (from the lab of MM Cox) and S Henrikus. (2021) Elucidating Recombination Mediator Function Using Biophysical Tools. Biology, 10(4), 288. DOI: org/10.3390/biology10040288 [PDF]
Henry, C, L Loiseau, A Vergnes, D Vertommen, A Mérida-Floriano, S Chitteni-Pattu, EA Wood, J Casadesús, MM Cox, F Barras, B Ezraty. (2021) Redox controls RecA protein activity via reversible oxidation of its methionine residues. eLIFE, 10:e63747. DOI: 10.7554/eLife.63747 [eLIFE] [PDF]
Nelson, DL and Cox, MM (2021). Lehninger Principles of Biochemistry, Eighth Edition (W.H. Freeman Publishers), New York.
2020
Bruckbauer, ST, J Martin, BB Minkoff, MT Veling, I Lancaster, J Liu, JD Trimarco, B Bushnell, A Lipzen, EA Wood, MR Sussman, C Pennacchio, MM Cox. (2020) Physiology of Highly Radioresistant Escherichia coli After Experimental Evolution for 100 Cycles of Selection. Front Microbiol, 11:582590. DOI: 10.3389/fmicb.2020.582590 [PDF] Corrigendum DOI: 10.3389/fmicb.2020.617806 [PDF]
Henrikus, SS, C Henry, AE McGrath, S Jergic, JP McDonald, Y Hellmich, ST Bruckbauer, ML Ritger, ME Cherry, EA Wood, PT Pham, MF Goodman, R Woodgate, MM Cox, AM van Oijen, H Ghodke, A Robinson. (2020) Single-molecule live-cell imaging reveals RecB-dependent function of DNA polymerase IV in double strand break repair. Nucleic Acids Res, 48(15):8490-8508. DOI: 10.1093/nar/gkaa597 [PDF]
Bruckbauer, ST, BB Minkoff, D Yu, VL Cryns, MM Cox, MR Sussman. (2020) Ionizing Radiation-Induced Proteomic Oxidation in Escherichia coli. Mol Cell Proteomics, 19(8):1375-1395. DOI: 10.1074/mcp.RA120.002092. [PDF]
Dubiel, K, C Henry, LM Spenkelink, AG Kozlov, EA Wood, S Jergic, NE Dixon, AM van Oijen, MM Cox, TM Lohman, SJ Sandler, JL Keck. (2020) Development of a Single-Stranded DNA-binding Protein Fluorescent Fusion Toolbox. Nucleic Acids Res, 48(11):6053-6067. DOI: 10.1093/nar/gkaa320 [PDF]
Romero, ZJ, TJ Armstrong, SS Henrikus, SH Chen, DJ Glass, AE Ferrazzoli, EA Wood, S Chitteni-Pattu, AM van Oijen, ST Lovett, A Robinson, MM Cox. (2020) Frequent Template Switching in Postreplication Gaps: Suppression of Deleterious Consequences by the Escherichia Coli Uup and RadD Proteins. Nucleic Acids Research, 48, 212-230. DOI: 10.1093/nar/gkz960 [PDF]
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2015-2019
2019
Lin, YH, CC Chu, HF Fan, PY Wang, MM Cox and HW Li. (2019) A 5’-3’ strand exchange polarity is intrinsic to RecA nucleoprotein filaments in the absence of ATP hydrolysis. Nucleic Acids Research 47, 5126-5140. DOI: 10.1093/nar/gkz189 [PDF]
Minkoff, BB, ST Bruckbauer, G Sabat, MM Cox and MR Sussman. (2019) Covalent modification of amino acids and peptides induced by ionizing radiation from an electron beam linear accelerator used in radiotherapy. Radiation Research. 191, 447-459. DOI: 10.1667/RR15288.1 [PDF]
Ghodke, H, BP Paudel, JS Lewis, S Jergic, K Gopall, ZJ Romero, EA Wood, R Woodgate, MM Cox and AM van Oijen. (2019) Spatial and temporal organization of RecA in the Escherichia coli DNA-damage response. eLife. 8 pii: e42761. DOI: 10.7554/eLife.42761. [PDF]
Jaszczur, MM, DD Vo, R Stanciauskas, JG Bertram, MM Cox, R Woodgate, CH Mak, F Pinaud, and MF Goodman. (2019) Conformational regulation of DNA polymerase V by RecA and ATP. PLoS Genetics, 15(2):e1007956.
DOI: 10.1371/journal.pgen.1007956. [PDF]
Bruckbauer, ST, JD Trimarco, J Martin, B Bushnell, KA Senn, W Schackwitz, A Lipzen, M Blow, EA Wood, WS Culberson, C Pennacchio and MM Cox. (2019) Experimental evolution of extreme resistance to ionizing radiation in Escherichia coli after 50 cycles of selection. J Bacteriology. 201(8). pii: JB.00784-18. DOI: 10.1128/JB.00784-18. [PDF]
Bruckbauer, ST, JD Trimarco, C Henry, EA Wood, JR Battista, and MM Cox. (2019) A variant of the Escherichia coli anaerobic transcription factor FNR exhibiting diminished promoter activation function enhances ionizing radiation resistance. PLoS One, 14(1): e0199482. DOI: 10.1371/journal.pone.0199482. [PDF]
Henrikus, SS, C Henry, H Ghodke, EA Wood, N Mbele, R Saxena, U Basu, AM van Oijen, MM Cox, and A Robinson. (2019) RecFOR epistasis group: RecF and RecO have distinct localisations and functions in Escherichia coli. Nucleic Acids Research, 47, 2946-2965. DOI: 10.1093/nar/gkz003 [PDF]
2018
Henrikus SS, Wood EA, McDonald JP, Cox MM, Woodgate R, Goodman MF, van Oijen AM, Robinson A. (2018) DNA polymerase IV primarily operates outside of DNA replication forks in Escherichia coli. PLoS Genet. 14(1):e1007161. doi: 10.1371/journal.pgen.1007161. [PDF]
2017
Lewis, JS, LS Spenkelink, S Jergic, EA Wood, E Monachino, NP Horan, KE Duderstadt, MM Cox, A Robinson, NE Dixon and AM van Oijen. (2017) Single-molecule visualization of fast polymerase turnover in the bacterial replisome. eLife 2017;6:e23932 pii: e23932. doi: 10.7554/3Life.23932. [eLIFE] [PDF]
Nelson, D.L. and Cox, M.M. (2017). Lehninger Principles of Biochemistry, Seventh Edition (W.H. Freeman Publishers), New York.
2016
Stanage, TH, AN Page and Cox MM (2016) DNA Flap Creation by the RarA/MgsA protein of Escherichia coli. Nucleic Acids Res. 45, 2724-2735. [PDF]
Chen, SH, RT Byrne-Nash and MM Cox (2016) Escherichia coli RadD Protein Functionally Interacts with the Single-stranded DNA-binding Protein. J. Biol. Chem. 291, 20779-20786. [PDF]
Leite, WC, CW Galvão, SC Saab, J Lulek, RM Etto, ME Steffens, S Chitteni-Pattu, T Stanage, JL Keck and MM Cox (2016) Structural and Functional Studies of H. seropedicae RecA Protein – Insights into the Polymerization of RecA Protein as Nucleoprotein Filament. PLoS One. 11(7):e0159871. doi: 10.1371/journal.pone.0159871. [PDF]
Jaszczur, M, JG Bertram, A Robinson, AM van Oijen, R Woodgate, MM Cox and MF Goodman (2016) Mutations for worse or better: Low fidelity DNA synthesis by SOS DNA polymerase V is a tightly-regulated double-edged sword. Biochemistry. 55, 2309-2318. [PDF]
Bakhlanova, IV, AV Dudkina, EA Wood, V Lanzov, MM Cox and DM Baitin (2016) DNA metabolism in balance: rapid loss of a RecA-based hyperrec phenotype. PLoS One. 11(4):e0154137. doi: 10.1371/journal.pone.0154137. [PDF]
2015
Ronayne, EA, YC Serena Wan, BA Boudreau, R Landick and MM Cox. (2015) P1 Ref Endonuclease: a Molecular Mechanism for Phage-Enhanced Antibiotic Lethality. PLoS Genetics. 12(1):e1005797. doi: 10.1371/journal.pgen.1005797. [PDF]
Rajendram, M, L Zhang, BJ Reynolds, GK Auer, HH Tucson, KV Ngo, MM Cox, A. Yethiraj, Q Cui and DB Weibel (2015) Anionic Phospholipids Stabilize RecA Filament bundles in Escherichia coli. Mol Cell. 60, 374-384. [PDF]
Robinson, A, JP McDonald, VEA Caldas, M Patel, EA Wood, CM Punter, H Ghodke, MM Cox, R Woodgate, MF Goodman, AM van Oijen (2015) Regulation of Mutagenic DNA Polymerase V Activation in Space and Time. PLoS Genetics. 11(8):e1005482. doi: 10.1371/journal.pgen.1005482. [PDF]
Kim, T, S Chitteni-Pattu, BL Cox, EA Wood, SJ Sandler and MM Cox (2015) Directed evolution of RecA variants with enhanced capacity for conjugational recombination. PLoS Genetics. 11(6):e1005278. doi: 10.1371/journal.pgen.1005278 [PDF].
Petrova, V, S Chen, E Molzberger, E Tomko, S Chitteni-Pattu, H Jia, Y Ordabayev, T Lohman and MM Cox (2015) Active Displacement of RecA Filaments by UvrD Translocase Activity. Nucleic Acids Res. 43, 4133-4149. [PDF]
Gruber, AJ, AL Erdem, G Sabat, K Karata, MM Jaszczur, DD Vo, TM Olsen, R Woodgate, MF Goodman and MM Cox (2015) A RecA protein surface required for activation of DNA polymerase V. PLOS Genetics. 11(3):e1005066. doi: 10.1371/journal.pgen.1005066. [PDF]
Piechura, JR, T-L Tseng, H-F Hsu, RT Byrne, TA Windgassen, S Chitteni-Pattu, JR Battista, H-W Li and MM Cox (2015) Biochemical characterization of RecA variants that contribute to extreme resistance to ionizing radiation. DNA Repair (Amst). 26, 30-43. [PDF]
Gruber, A, T Olsen, R Dvorak and MM Cox (2015) Function of the N-terminal segment of the RecA-dependent nuclease Ref. Nucleic Acids Res. 43, 1795-1803. [PDF]
Chen, SH, RT Byrne, EA Wood and MM Cox (2015) Escherichia coli radD (yejH) gene: a novel function involved in radiation resistance and double-strand break repair. Mol Microbiol. 95, 754-768. [PDF]
2010-2014
2014
Byrne, RT, SH Chen, EA Wood, EL Cabot and MM Cox (2014) Escherichia coli Genes and Pathways Involved in Surviving Extreme Exposure to Ionizing Radiation. J Bact. 196, 3534-3545. [PDF]
Erdem, A, M Jaszczur, J Bertram, R Woodgate, M Cox and M Goodman (2014) DNA polymerase V activity is autoregulated by a novel intrinsic DNA-dependent ATPase. eLIFE. 3:e02384 [eLIFE] [PDF]
Ronayne, EA and Cox, MM (2014) RecA-dependent programmable endonuclease Ref cleaves DNA in two distinct steps. Nucleic Acids Research. 42, 3871-3883. [PDF]
Byrne, RT, AJ Klingele, EL Cabot, WS Schackwitz, JA Martin, J Martin, Z Wang, EA Wood, C Pennacchio, LA Pennacchio, NT Perna, JR Battista and MM Cox (2014) Evolution of Extreme Resistance to Ionizing Radiation via Genetic Adaptation of DNA Repair. eLIFE. 3:e01322 [eLIFE] [PDF]
2013
Cox, M.M. (2013). Proteins pinpoint double strand breaks. eLIFE. 2:e01561 [eLIFE] [PDF]
Tansey, J.T., T. Baird, Jr., M.M. Cox, K.M. Fox, J. Knight, D. Sears, and E. Bell. (2013). Foundational Concepts and Assessment Tools for Biochemistry and Molecular Biology Educators, Part 1: Essential Concepts and Skills. Biochem Mol Biol Educ. 41, 289-296. [PDF]
Tham, K.-C., N. Hermans, H. Winterwerp, M. Cox, C. Wyman, R. Kanaar, and J. Lebbink. (2013). Mismatch repair inhibits homeologous recombination by coordinated directional unwinding of trapped DNA structures. Molecular Cell. 51, 326-337. [PDF]
Ngo, K.V., E.T. Molzberger, S. Chitteni-Pattu, and M.M. Cox. (2013). Regulation of Deinococcus radiodurans RecA protein function via modulation of active and inactive nucleoprotein filament states. J Biol Chem. 288, 21351-21366. [PDF]
Norais, C., P. Servant, C. Bouthier-de-la-Tour, P.-D. Coureux, S. Ithurbide, F. Vannier, P.P. Guerin, C.L. Dulberger, K.A. Satyshur, J.L. Keck, J. Armengaud, M.M. Cox, and S. Sommer. (2013). The Deinococcus radiodurans DR1245 Protein, a DdrB Partner Homologous to YbjN Proteins and Reminiscent of Type III Secretion Systems Chaperones. PLoS One. 8: e56558. [PDF]
Nelson, D.L. and Cox, M.M. (2013). Lehninger Principles of Biochemistry, Sixth Edition (W.H. Freeman Publishers), New York.
2012
George, N.P., K.V. Ngo, S. Chitteni-Pattu, C.A. Norais, J.R. Battista, M.M. Cox and J.L. Keck. (2012). Structure and cellular dynamics of Deinococcus radiodurans SSB/DNA complexes. J. Biol. Chem. 287, 22123-22132. [PDF]
2011
Bouthier de la Tour, C., S. Boisnard, C. Norais, M. Toueille, E. Bentchikou, F. Vannier, M.M. Cox, S. Sommer, and P. Servant. (2011). The deinococcal DdrB protein is involved in an early stop of DNA double strand break repair and in plasmid transformation through its single-strand anealling activity. DNA Repair (Amst). 10, 1223-1231. [PDF]
Fan, H.-F., M.M. Cox, and H.-W. Li. (2011). Developing single-molecule TPM experiments for direct observation of successful RecA-mediated strand exchange reaction. PLoS One. 6(7): e21359. [PDF]
Hsu, H.-F., M.M. Cox, and H.-W. Li. (2011). Investigating Deinococcus radiodurans RecA Protein Filament Formation on Double-Stranded DNA by a Real-Time Single-Molecule Approach. Biochemistry, 50, 8270-8280. [PDF]
Galkin, V.E., R.L. Britt, L.B. Bane, X. Yu, M.M. Cox, and E.H. Egelman. (2011). Two modes of Binding of DinI to RecA Filament Provide a New Insight into the Regulation of SOS Response by DinI Protein. J. Mol. Biol. 408, 815-824. [PDF]
Cox, MM, Doudna, J.A., and M. O’Donnell. (2012). Molecular Biology: Principles and Practice, First Edition (W.H. Freeman Publishers), New York. (Printed February 2011)
Gruenig, M.C., D. Lu, S.J. Won, C.L. Dulberger, A.J. Manlick, J.L. Keck, and M.M. Cox. (2011). Creating directed double strand breaks with the Ref protein: a novel RecA-dependent nuclease from bacteriophage P1. J. Biol. Chem. 286, 8240-8251. [PDF]
Britt, R.L., S. Chitteni-Pattu, A.N. Page, and M.M. Cox. (2011). RecA K72R filament formation defects reveal an oligomeric RecA species involved in filament extension. J. Biol. Chem. 296, 7830-7840. [PDF]
Page, A.N., N.P. George, A.H. Marceau, M.M. Cox, and J.L. Keck. (2011). Structure and biochemical activities of Escherichia coli MgsA. J. Biol. Chem. 286, 12075-12085. [PDF]
Stohl, E.A., M.C. Gruenig, M.M. Cox, and H. Steven Seifert. (2011). Purification and characterization of the RecA protein from Neisseria gonorrhoeae. PLOS One. 6, e17101. [PDF]
2010
Bakhlanova, I.R., A.V. Dudkina, D.M. Baitin, K.L. Knight, M.M. Cox, and V.A. Lanzov. (2010). Modulating cellular recombination potential through alterations in RecA structure and regulation. Molecular Microbiology. 78, 1523-1538. [PDF]
Kozlov, A.G., J.M. Eggington, M.M. Cox, and T.M. Lohman. (2010). Binding of the Dimeric Deinococcus radiodurans Single-Stranded DNA Binding Protein to Single-Stranded DNA. Biochemistry. 49, 8266-8275. [PDF]
Gruenig, M.C., E.A. Stohl, S. Chitteni-Pattu, H.S. Seifert, and M.M. Cox. (2010). Less is More-Neisseria gonorrhoeae RecX Protein Stimulates Recombination by Inhibiting RecA. J. Biol. Chem. 285, 37188-37197. [PDF]
Petrova, V., K.A. Satyshur, N.P. George, D. McCaslin, M.M. Cox, and J.L. Keck. (2010). X-ray crystal structure of the bacterial conjugation factor PsiB, a negative regulator of RecA. J. Biol. Chem. 285, 30615-30621. [PDF]
Patel, M., Q. Jiang, R. Woodgate, M.M. Cox, and M.F. Goodman. (2010). A new model for SOS-induced mutagenesis: How RecA protein activates DNA polymerase V. Crit. Rev. Biochem. Mol Biol. 45, 171-184. [PDF]
Cox, M.M., J.L. Keck, and J.R. Battista. (2010). Rising from the Ashes: DNA repair in Deinococcus radiodurans. PLoS Genetics. 6, e1000815. [PDF]
Kozlov, A.G., M. M. Cox, and T.M. Lohman. (2010). Regulation of single stranded DNA binding by the C-termini of E. coli SSB protein. J. Biol. Chem. 285, 17246-17252. [PDF]
Britt, R.L., N. Haruta, S.L. Lusetti, S. Chitteni-Pattu, R.B. Inman, and M.M. Cox. (2010). Disassembly of Escherichia coli RecA E38K/ΔC17 nucleoprotein filaments is required to complete DNA strand exchange. J. Biol. Chem. 285, 3211-3226. [PDF]
2005-2009
2009
Petrova, V., S. Chitteni-Pattu, J.C. Drees, R.B. Inman, and M.M. Cox. (2009). An SOS Inhibitor that Binds to Free RecA protein: the PsiB protein. Molecular Cell, 36, 121-130. [PDF]
Cox, M.M. (2009). A new look at the human Rad51 protein. Proc. Natl. Acad. Sci. USA. Commentary. 106, 13147-13148. [PDF]
Harris, D.R, S.V. Pollock, E.A. Wood, R.J. Goiffon, A.J. Klingele, E.L. Cabot, W. Schackwitz, J. Martin, J. Eggington, T.J. Durfee, C.M. Middle, J.E. Norton, M.C. Popelars, H. Li, S.A. Klugman, L.L. Hamilton, L.B. Bane, L. Pennacchio, T.J. Albert, N.T. Perna, M.M. Cox, and J.R. Battista. (2009). Directed evolution of ionizing radiation resistance in Escherichia coli. J. Bact. 191, 5240-5252. [PDF]
Norais, C.A., S. Chitteni-Patu, E.A. Wood, R.B. Inman, and M.M. Cox. (2009). DdrB protein, an alternative Deinococcus radiodurans SSB induced by ionizing radiation. J. Biol. Chem. 284, 21402-21411. [PDF]
Jiang, Q., K. Karata, R. Woodgate, M.M. Cox, and M.F. Goodman. (2009). The active form of DNA polymerase V is UmuD’2C-RecA-ATP. Nature 460, 359-363. [PDF]
Sakai, A. and M.M. Cox. (2009). RecFOR and RecOR as distinct RecA loading pathways. J. Biol. Chem. 284, 3264-3272. [PDF]
Nelson, D.L. and Cox, M.M. (2009). Lehninger Principles of Biochemistry, Fifth Edition (W.H. Freeman Publishers), New York.
2008
Harris, D.R., K.V. Ngo, and M.M. Cox. (2008). The stable, functional core of DdrA from Deinococcus radiodurans R1 does not restore Radioresistance in vivo. J. Bact. 190, 6475-6482. [PDF]
Baitin, D.M., M.C. Gruenig, and M.M. Cox. (2008). SSB antagonizes RecX-RecA interaction. J. Biol. Chem. 283, 14198-14204. [PDF]
Gruenig, M.C., N. Renzette, E. Long, S. Chiteni-Pattu, R.B. Inman, M.M. Cox, and S.J. Sandler. (2008). RecA-mediated SOS induction requires an extended filament conformation but no ATP hydrolysis. Mol. Micro. 69, 1165-1179. [PDF]
Cox, J.M., H. Li, E.A. Wood, S. Chitteni-Pattu, R.B. Inman, and M.M. Cox. (2008). Defective dissociation of a “slow” RecA mutant protein imparts an Escherichia coli growth defect. J. Biol. Chem., 283, 24909-24921. [PDF]
Shereda, R.D., A.G.Kozlov, T.M. Lohman, M.M. Cox, and J.L. Keck. (2008). SSB as an organizer/mobilizer of genome maintenance complexes. Crit. Rev. Biochem. Mol. Biol. 43, 289-318. [PDF]
Baitin, D.M., I.V. Bakhlanova, D.V. Chervyakova, Y.V. Kil, V.A. Lanzov, and M.M. Cox. (2008). Two RecA protein types that mediate different modes of hyperrecombination. J. Bact. 190, 3036-3045. [PDF]
2007
Cox, M.M. and Phillips, G.N. (2007). Handbook of Proteins: Structure, Function and Methods. (John Wiley & Sons, Ltd.), Chichester, UK.
Cox, M.M. (2007). The bacterial RecA protein: structure, function, and regulation. In Topics in Current Genetics. Molecular Genetics of Recombination. (A. Aguilera and R. Rothstein, eds.) (Springer-Verlag GmbH, Heidelberg, Germany). Vol. 1, pp. 53-94. [PDF]
Hobbs, M.D., Sakai, A., and Cox, M.M. (2007). SSB limits RecOR binding onto single strand DNA. J. Biol. Chem. 282, 11058-11067. [PDF]
Cox, M.M. (2007). Motoring along with the bacterial RecA protein. Nature Rev Mol. Cell Biol. 8, 127-138. [PDF]
Cox, M.M. (2007). Regulation of bacterial RecA protein function. Crit Rev Biochem Mol Biol. 42, 41-63. [PDF]
2006
Eggington, J.M., Kozlov, A.G., Cox, M.M., and Lohman, T.M. (2006). Polar destabilization of DNA duplexes with single-stranded overhangs by the Deinococcus radiodurans SSB protein. Biochemistry. 45, 14490-14502. [PDF]
Schlacher, K., Cox, M.M., Woodgate, R., Goodman, M.F. (2006). RecA acts in trans to allow replication of damaged DNA by DNA polymerase V. Nature 442, 883-887. [PDF]
Baitin, D.M., Bakhlanova, I.V., Kil, Y.V., Cox, M.M., Lanzov, V.A. (2006). Distinguishing characteristics of hyperrecombinogenic RecA protein from Pseudomonas aeruginosa acting in Escherichia coli. J. Bact. 188, 5812-5820. [PDF]
Attie, A.D., Sober, E., Numbers, R.L., Amasino, R.M., Cox, , Berceau, T., Powell, T., and Cox, M.M. (2006). Defending science education against intelligent design: a call to action. Journal of Clinical Investigation. 116, 1134-1138. [PDF]
Cox, J.M., Abbott, S.A., Chtteni-Pattu, S., Inman, R.B., and Cox, M.M. (2006). Complementation of one RecA protein Point mutation by another. Evidence for trans catalysis of ATP hydrolysis. J. Biol. Chem. 281, 12968-12975. [PDF]
Battista, J. R., and Cox, M. M. (2006) Genome reconstitution in the extremely radiation-resistant bacterium Deinococcus radiodurans. In “Impact of Radiation Risk Estimates in Normal and Emergency Situations”. Proceedings of the NATO Advanced Research Workshop on Impact of Radiation Risk Estimates in Normal and Emergency Situations, Yerevan, Armenia, 8-11 September 2005. Editors: Arrigo A. Cigna & Marco Durante. Springer. Netherlands. Part 4.
Schlacher, K., Pham, P., Cox, M. M., and Goodman, M. F. (2006) Roles of DNA Polymerase V and RecA Protein in SOS Damage-induced Mutation. Chem. Rev., 106, 406-419. [PDF]
Drees, J. C., Chitteni-Pattu, S., McCaslin, D. R., Inman, R. B., and Cox, M. M. (2006) Inhibition of RecA protein function by the RdgC protein from Escherichia coli. J. Biol. Chem., 281, 4708-4717. [PDF]
Lusetti, S.L., Hobbs, M.D., Stohl, E.A., Chitteni-Pattu, S., Inman, R.B., Seifert, H.S., and Cox, M.M. (2006). The RecF protein antagonizes RecX function via direct interaction. Mol. Cell, 21, 41-50. [PDF]
Harris, D.R., M. Tanaka, S.V. Saveliev E. Jolivet, A.M. Earl, M.M. Cox, and J.R. Battista. (2006). Correction: Preserving Genome Integrity: The DdrA Protein of Deinococcus radiodurans R1. PloS Biology, 4(11), e305, 2165. [PDF]
2005
Cox, M.M., and Battista, J.R. (2005). Deinococcus radiodurans, the consummate survivor. Nature Rev. Microbiology 3, 882-892. [PDF]
Schlacher, K., Leslie, K., Wyman, C., Woodgate, R., Cox, M.M., and Goodman, M.F. (2005) DNA Polymerase V and RecA Protein, a Minimal Mutasome. Molecular Cell, Vol. 17, 561–572. [PDF]
Cox, M.M. (2005) The RecA protein. In The Bacterial Chromosome. (N. Patrick Higgins, ed.) (American Society of Microbiology Press, Washington, DC). pp. 369-388.[PDF]
Cox, J.M., Tsodikov, O.V., and Cox, M.M. (2005). Organized Unidirectional Waves of ATP Hydrolysis Within a RecA Filament. PloS Biology. 3(2), e52. [PDF]
2000-2004
2004
Lusetti, S.L., Voloshin, O.N., Inman, R.B., Camerini-Otero, R.D., and Cox, M.M. (2004). The DinI Protein Stabilizes RecA Protein Filaments. J. Biol. Chem. 279, 30037-30046. [PDF]
Harris, D.R., Tanaka, M., Saveliev, S.V., Jolivet, E., Earl, A.M., Cox, M.M., and Battista, J.R. (2004). Preserving Genome Integrity: The DdrA Protein of Deinococcus radiodurans R1. PloS Biology, 2(10), 1629-1639. [PDF] correction [PDF]
Robu, M.E., Inman, R.B., and Cox, M.M. (2004) Situational repair of replication forks: Roles of RecG and RecA proteins. J. Biol. Chem. 279. 10973-10981. [PDF]
Eggington, J.M., Haruta., N., Wood, E.A., and Cox, M.M. (2004). The single-stranded DNA-binding protein of Deinococcus radiodurans. BMC Microbiology, 4, Art. No. 2. [PDF]
Drees, J.C., Lusetti, S.L., and Cox, M.M. (2004). Inhibition of RecA protein by the Escherichia coli RecX protein: Modulation by the RecA C-terminus and filament functional state. J. Biol. Chem., 279, 52991-52997. [PDF]
Lusetti, S.L., Drees, J.C., Stohl, E.A., Seifert, H.S., and Cox, M.M. (2004) The DinI and RecX proteins are competing modulators of RecA function. J. Biol. Chem., 279, 55073 – 55079. [PDF]
Drees, J.C., Lusetti, S.L., Chitteni-Pattu, S., Inman, R.B., and Cox, M.M. (2004). A RecA filament capping mechanism for RecX protein. Mol. Cell. 15, 789-798. [PDF]
Bernstein, D.A., Eggington, J.M., Kolloran, M.P., Misic, A.M., Cox, M.M., and Keck, J.L. (2004). Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage. Proc. Natl. Acad. Sci. U.S.A. 101, 8575-8580. [PDF]
Nelson, D.L. and Cox, M.M. (2004). Principles of Biochemistry Fourth Edition (Freeman Publishers), New York.
2003
Haruta, N., Yu, Xiong, Yang, Shixin, Egelman, Edward H., and Cox, M.M. (2003) A DNA pairing-enhanced conformation of bacterial RecA proteins. J. Biol. Chem. 278, 52710-52723. [PDF]
Battista, J.R., Cox, M.M., Daly, M.J., Narumi, I., Radman, M. and Sommer, S. (2003). The structure of D. radiodurans. Science, 302, 567-568. [PDF]
Lusetti, S.L., Wood, E.A., Fleming, C.D., Modica, M.J., Korth, J., Abbott, L., Dwyer, D.W., Roca, A.I., Inman, R.B. and Cox, M.M. (2003) C terminal deletions of the Escherichia coli RecA protein: Characterization of in vivo and in vitro effects. J. Biol. Chem. 278, 16372-16380. [PDF]
Lusetti, S., Shaw, J. and Cox, M.M. (2003) Magnesium ion-dependent activation of the RecA protein involves the C terminus. J. Biol. Chem. 278, 16381-16388. [PDF]
Eggler, A.L, Lusetti, S. and Cox, M.M. (2003) The C Terminus of the Escherichia coli RecA protein modulates the DNA binding competition with single-stranded DNA-binding protein. J. Biol. Chem. 278, 16389-16396. [PDF]
Cox, M.M. (2003) Better chemistry for better survival, through regulation. Cell, 112, 286-287. [PDF]
2002
Lusetti, S.L., and Cox, M.M. (2002) The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. In Annual Review of Biochemistry (Charles Richardson, ed.) (Annual Reviews, Palo Alto, CA), Vol. 71, pp. 71-100. [PDF]
Cox, M.M. (2002). The nonmutagenic repair of broken replication forks via recombination. In Fundamental and Molecular Mechanisms of Mutagenesis. A section of Mutation Research. Special Issue: The bypass of DNA lesions by DNA and RNA polymerases (Guest eds. G. P. Holmquist, V. M. Maher). Vol. 510, Nos. 1,2, pp. 107-120. [PDF]
Mori, T., Saveliev, S.V., Xu, Y., Stafford, W.F., Cox, M.M., Inman, R.B., and Johnson, C.H. (2002). Circadian clock protein KaiC forms ATP-dependent hexameric rings and binds DNA. Proc. Natl. Acad. Sci. USA, 99, 17203-17208. [PDF]
Pham, P., Seitz, E.M., Saveliev, S., Shen, X., Woodgate, R., Cox, M.M., and Goodman, M.F. (2002). Two distinct modes of RecA action are required for DNA polymerase V-catalyzed translesion synthesis. Proc. Natl. Acad. Sci. USA, 99, 11061-11066. [PDF]
Eggler, A.L., Inman, R.B., and Cox, M.M. (2002). The Rad51-dependent pairing of long DNA substrates is stabilized by replication protein A. J. Biol. Chem., 277, 39280-39288. [PDF]
Kim, J.-I., and Cox, M. M. (2002). The RecA proteins of Deinococcus radiodurans and Escherichia coli promote DNA strand exchange via inverse pathways. Proc. Natl. Acad. Sci. USA, 99, 7917-7921. [PDF]
Kim, J.-I., Sharma, A.K., Abbott, S.N., Wood, E.A., Dwyer, D.W., Jambura, A., Minton, K.W., Inman, R.B., Daly, M.J., and Cox, M.M. (2002). RecA protein from the extremely radioresistant bacterium Deinococcus radiodurans: Expression, purification, and characterization. J. Bact., 184, 1649-1660. [PDF]
2001
Cox, M.M. (2001) Recombinational DNA repair of damaged replication forks in Escherichia coli: Questions. In Annual Review of Genetics (Allan Campbell, ed.) (Annual Reviews, Palo Alto, CA), Vol. 35, pp. 53-82. [PDF]
Rice, K. and Cox, M.M. (2001). Recombinational DNA repair in bacteria: Postreplication. In Embryonic Encyclopedia of Life Sciences, Nature Publishing Group, London. www.els.net. [PDF]
Bork, J.M., Cox, M.M., and Inman, R.B. (2001). The RecOR proteins modulate RecA protein function at 5′ ends of single-stranded DNA. EMBO J., 20, 7313-7322. [PDF]
Bork, J.M., Cox, M.M., and Inman, R.B. (2001). RecA protein filaments disassemble in the 5′ to 3′ direction on single-stranded DNA. J. Biol. Chem., 276, 45740-45743. [PDF]
Rice, K.P., Eggler, A.L., Sung, P., and Cox, M.M. (2001). DNA pairing and strand exchange by the Escherichia coli RecA and yeast Rad51 proteins without ATP hydrolysis: On the importance of not getting stuck. J. Biol. Chem., 276, 38570-38581. [PDF]
Saveliev, S.V. and Cox, M.M. (2001). Product analysis illuminates the final steps of IES deletion in Tetrahymena thermophila. EMBO J., 20, 3251-3261. [PDF]
Robu, M.E., Inman, R.B., and Cox, M.M. (2001). RecA protein promotes the regression of stalled replication forks in vitro. Proc. Natl. Acad. Sci. USA. 98, 8211-8218. [PDF]
Cox, M.M. (2001). Historical overview: Searching for replication help in all the rec places. Proc. Natl. Acad. Sci. USA. 98, 8173-8180. [PDF]
Cox, M.M. (2001). Synapsis in DNA transactions. In Encyclopedia of Genetics. (S. Brenner and J.H. Miller, eds.) (Academic Press, Inc., San Diego, CA), Vol. 4, pp. 1906-1909. [PDF]
2000
Cox, M.M. (2000). Recombinational DNA repair in bacteria and the RecA protein. In Progress in Nucleic Acid Research and Molecular Biology. (K. Moldave, editor) (Academic Press, Inc., San Diego, CA), Vol. 63, pp. 311-366. [PDF]
Lehninger, A. L., Nelson, D. L. and Cox, M. M. (2000). Principles of Biochemistry Third Edition (Freeman Publishers), New York
Cox, M. M., Goodman, M. F., Kreuzer, K. N., Sherratt, D. J., Sandler, S. J., and Marlans, K. J. (2000). The importance of repairing stalled replication forks. Nature 404, 37-41. [PDF]
Rice, K. P., Chaput, J. C., Cox, M. M., and Switzer, C. (2000). RecA protein promotes strand exchange with DNA substrates containing isoguanine and 5-Methyl Isocytosine. Biochemistry, 39, 10177-10188. [PDF]
Chen, Y., Narendra, U., Iype, E. I., Cox, M. M., and Rice, P. A. (2000). Crystal Structure of a Flp Recombinase-Holliday Junction Complex: Assembly of an Active Oligomer by Helix Swapping. Molecular Cell, 6, 885-897. [PDF]
1995-1999
1999
Webb, B.L., Cox, M.M. and Inman, R.B. (1999). ATP Hydrolysis and DNA binding by the Escherichia coli RecF Protein. J. Biol. Chem. 274, 15367-15374. [PDF]
Arenson, T.A., O.V. Tsodikov and M.M. Cox. (1999). Quantitative analysis of the kinetics of end-dependent disassembly of RecA filaments from ssDNA. J. Mol. Biol. 288, 391-401. [PDF]
1998
Shan, Q. and Cox, M.M. (1998). On the mechanism of RecA-mediated repair of double strand breaks: No role for four-strand DNA pairing intermediates. Molecular Cell 1, 309-317. [PDF]
Cox, M. M. (1998). A broadening view of recombinational DNA repair in bacteria. Genes Cells 3, 65-78. [PDF]
1997
Shan, Q., Bork, J. M., Webb, B. L., Inman, R. B. and Cox, M. M. (1997). RecA protein filaments: End-dependent dissociation from ssDNA and stabilization by RecO and RecR proteins. J. Mol. Biol. 265, 519-540. [PDF]
Shan, Q. and Cox, M.M. (1997). RecA filament dynamics during DNA strand exchange reactions. J. Biol. Chem. 272, 11063-11073. [PDF]
Cox, M.M. (1997). A path for coevolution of recombinational DNA repair, transposition, and the common nucleotides. Mutation Research 384, 15-22. [PDF]
Huang, L.-C., Wood, E.A. and Cox, M.M. (1997). Convenient and reversible site-specific targeting of exogenous DNA into a bacterial chromosome using the FLP recombinase: the FLIRT system. J. Bact. 179, 6076-6083. [PDF]
MacFarland, K. J., Shan, Q., Inman, R. B. and Cox, M. M. (1997). RecA as a motor protein: testing models for the role of ATP hydrolysis in DNA strand exchange. J. Biol. Chem. 272, 17675-17685. [PDF]
Webb, B. L., Cox, M. M. and Inman, R. B. (1997). Recombinational DNA Repair: The RecF and RecR proteins limit the extension of RecA filaments beyond single-strand DNA gaps. Cell 91, 347-356. [PDF]
Cox, M. M. (1997). Gene amplification. In McGraw-Hill Encyclopedia of Science and Technology. Sybil P. Parker, ed. (McGraw-Hill, Inc.), Vol. 7, pp. 749-751. [PDF]
Cox, M. M. (1997). Recombinational crossroads: eucaryotic enzymes and the limits of bacterial precedents. Proc. Natl. Acad. Sci. USA. 94, 11764-11766. [PDF]
Roca, A. L. and Cox, M. M. (1997). RecA protein: Structure, function, and role in recombinational DNA repair. In Progress in Nucleic Acid Research and Molecular Biology. W. E. Cohn and K. Moldave, eds. (Academic Press, Inc., San Diego, CA), Vol. 56, pp. 129-223. [PDF]
1996
Shan, Q., Cox, M. M. and Inman, R. B. (1996). DNA strand exchange promoted by RecA K72R: Two reaction phases with different Mg2+ requirements. J. Biol. Chem. 271, 5712-5724. [PDF]
Bedale, W. A. and Cox, M. M. (1996). Evidence for the coupling of ATP hydrolysis to the final (extension) phase of RecA protein-mediated DNA strand exchange. J. Biol. Chem. 271, 5725-5732. [PDF]
Shan, Q. and Cox, M. M. (1996). RecA protein dynamics in the interior of RecA nucleoprotein filaments. J. Mol. Biol. 257, 756-774. [PDF]
Saveliev, S. V. and Cox, M. M. (1996). Developmentally programmed DNA deletion in Tetrahymena thermophilia by a transposon-like reaction pathway. EMBO J. 15, 2858-2869. [PDF]
Marrione, P. A. and Cox, M. M. (1996). Allosteric effects of RuvA protein, ATP, and DNA on RuvB protein-mediated ATP hydrolysis. Biochemistry 35, 11228-11238. [PDF]
Ishimori, K., Sommer, S., Bailone, A., Takahashi, M., Cox, M. M. and Devoret, R. (1996). Characterization of a mutant RecA protein that facilitates homologous genetic recombination but not recombinational DNA repair: RecA423. J. Mol. Biol. 264, 696-712. [PDF]
Cox, M. M. (1996). RecA protein: Structure and function. In Encyclopedia of Molecular Biology and Molecular Medicine. R. A. Meyers, ed. (VCH Publishers, Inc.), Vol. 5, pp. 220-229. [PDF]
1995
Margraf, R. L., Roca, A. I. and Cox, M. M. (1995). The deduced Vibrio cholerae RecA amino acid sequence. Gene 152, 135-136. [PDF]
Jain, S. K., Cox, M. M. and Inman, R. B. (1995). Occurrence of three-stranded DNA within a RecA protein filament. J. Biol. Chem. 270, 4943-4949. [PDF]
Saveliev, S. V. and Cox, M. M. (1995). Transient DNA breaks associated with programmed genomic deletion events in conjugating cells of Tetrahymena thermophila. Genes Dev. 9, 248-255. [PDF]
Qian, X.-H. and Cox, M. M. (1995). Asymmetry in active complexes of FLP recombinase. Genes Dev. 9, 2053-2064. [PDF]
Ullsperger, C. J. and Cox, M. M. (1995). Quantitative RecA protein binding to the hybrid duplex product of DNA strand exchange. Biochemistry 34, 10859-10866. [PDF]
Iype, E. I., Inman, R. B. and Cox, M. M. (1995). Blocked RecA protein-mediated DNA strand exchange reactions are reversed by the RuvA and RuvB proteins. J. Biol. Chem. 270, 19473-19480. [PDF]
Marrione, P. E. and Cox, M. M. (1995). RuvB protein-mediated ATP hydrolysis: Functional asymmetry in the RuvB hexamer. Biochemistry 34, 9809-9818. [PDF]
Waite, L. L. and Cox, M. M. (1995). A protein dissociation step limits turnover in FLP recombinase-mediated site-specific recombination. J. Biol. Chem. 270, 23409-23414. [PDF]
Webb, B. L., Cox, M. M. and Inman, R. I. (1995). An interaction between the Escherichia coli RecF and RecR proteins dependent on ATP and double-stranded DNA. J. Biol. Chem. 270, 31397-31404. [PDF]
Cox, M. M. (1995). RecA protein: Structure and function. In Molecular Biology and Biotechnology: A Comprehensive Desk Reference. R. A. Meyers, ed. (VCH Publishers, Inc.), pp. 784-789. [PDF]
Cox, M. M. (1995). Alignment of 3 (but not 4) DNA strands within a RecA protein filament. J. Biol. Chem. 270, 26021-26024. [PDF]
1990-1994
1994
Saveliev, S. V. and Cox, M. M. (1994). The fate of deleted DNA produced during programmed genomic deletion events in Tetrahymena thermophila. Nucleic Acids Res. 22, 5695-5701. [PDF]
Jain, S. K., Cox, M. M. and Inman, R. B. (1994). On the role of ATP hydrolysis in RecA protein-mediated DNA strand exchange. III. Unidirectional branch migration and extensive hybrid DNA formation. J. Biol. Chem. 269, 20653-20661. [PDF]
Iype, L. E., Wood, E. A., Inman, R. B. and Cox, M. M. (1994). RuvA and RuvB proteins facilitate the bypass of heterologous DNA insertions during RecA protein-mediated DNA strand exchange. J. Biol. Chem. 269, 24967-24978. [PDF]
Cox, M. M. (1994). Why does RecA protein hydrolyze ATP? Trends Biochem. Sciences 19, 217-222. [PDF]
1993
Bedale, W. A., Inman, R. B. and Cox, M. M. (1993). A reverse DNA strand exchange mediated by RecA protein and exonuclease I. J. Biol. Chem. 268, 15004-15016. [PDF]
Cox, M. M. (1993). Relating biochemistry to biology: How the recombinational repair function of the recA system is manifested in its molecular properties. BioEssays 15, 617-623. [PDF]
Lehninger, A. L., Nelson, D. L. and Cox, M. M. (1993). Principles of Biochemistry Second Edition (Worth), New York
1992
Jain, S. K., Inman, R. B. and Cox, M. M. (1992). Putative three-stranded DNA pairing intermediate in recA protein-mediated DNA strand exchange: No role for guanine N-7. J. Biol. Chem. 267, 4215-4222. [PDF]
Qian, X.-H., Inman, R. B. and Cox, M. M. (1992). Reactions between half- and full-FLP recombination target sites. A model system for analyzing early steps in FLP protein-mediated site-specific recombination. J. Biol. Chem. 267, 7794-7805. [PDF]
Kim, J.-I., Cox, M. M. and Inman, R. B. (1992). On the role of ATP hydrolysis in recA protein-mediated DNA strand exchange: I. Bypassing a short heterologous insert in one DNA substrate. J. Biol. Chem. 267, 16438-16443. [PDF]
Kim, J.-I., Cox, M. M. and Inman, R. B. (1992). On the role of ATP hydrolysis in recA protein-mediated DNA strand exchange: II. Four-strand exchanges. J. Biol. Chem. 267,16444-16449. [PDF]
1991
Huang, L.-C., Wood, E. A. and Cox, M. M. (1991). A bacterial model system for chromosomal targeting. Nucleic Acids Res. 19, 443-448. [PDF] Corrigenda [PDF]
Bedale, W. A., Inman, R. B. and Cox, M. M. (1991). RecA protein-facilitated DNA strand breaks. A mechanism for bypassing DNA structural barriers during strand exchange. J. Biol. Chem. 266, 6499-6510. [PDF]
Cox, M. M. (1991). The recA protein as a recombinational repair system. Mol. Microbiol. 5, 1295-1299. [PDF]
1990
Morrical, S. W. and Cox, M. M. (1990). Stabilization of recA protein-ssDNA complexes by the single-stranded DNA binding protein of Escherichia coli. Biochemistry 29, 837-843. [PDF]
Meyer-Leon, L., Inman, R. B. and Cox, M. M. (1990). Characterization of Holliday structures in FLP protein-promoted site-specific recombination. Mol. Cell. Biol. 10, 235-242. [PDF]
Lindsley, J. E. and Cox, M. M. (1990). Assembly and disassembly of recA protein filaments occur at opposite filament ends. Relationship to DNA strand exchange. J. Biol. Chem. 265, 9043-9054. [PDF]
Lindsley, J. E. and Cox, M. M. (1990). On recA protein-mediated homologous alignment of two DNA molecules. Three strands versus four strands. J. Biol. Chem. 265, 10164-10171. [PDF]
Lee, J. W. and Cox, M. M. (1990). Inhibition of recA protein promoted ATP hydrolysis. 1. ATPgS and ADP are antagonistic inhibitors. Biochemistry 29, 7666-7676. [PDF]
Lee, J. W. and Cox, M. M. (1990). Inhibition of recA protein promoted ATP hydrolysis. 2. Longitudinal assembly and disassembly of recA protein filaments mediated by ATP and ADP. Biochemistry 29, 7677-7683. [PDF]
Umlauf, S. W., Cox, M. M. and Inman, R. B. (1990). Triple-helical DNA pairing intermediates formed by recA protein. J. Biol. Chem. 265, 16898-16912. [PDF]
Qian, X.-H., Inman, R. B. and Cox, M. M. (1990). Protein-based asymmetry and protein-protein interactions in FLP recombinase-mediated site-specific recombination. J. Biol. Chem. 265, 21779-21788. [PDF]
Cox, M. M. (1990). Binding two DNA molecules at once: The recA protein. In The Biology of Nonspecific DNA-Protein Interactions, A. Revzin, ed. (CRC Press), pp. 171-196. [PDF]
Cox, M. M., Lindsley, J. E., Umlauf, S. W. and Inman, R. B. (1990). Towards an understanding of recA protein-mediated DNA strand exchange. In Molecular Mechanisms in DNA Replication and Recombination, C. C. Richardson and I. R. Lehman, eds. (Alan R. Liss), UCLA Symp. Mol. Cell. Biol., New Ser., 127, 375-386. [PDF]
Roca, A. I. and Cox, M. M. (1990). The recA protein: Structure and function. Crit. Rev. Biochem. Mol. Biol. 25, 415-456. [PDF]
1985-1989
1989
Lindsley, J. E. and Cox, M. M. (1989). Dissociation pathway for recA nucleoprotein filaments formed on linear duplex DNA. J. Mol. Biol. 205, 695-711. [PDF]
Pugh, B. F., Schutte, B. C. and Cox, M. M. (1989). Extent of duplex DNA underwinding induced by recA protein binding in the presence of ATP. J. Mol. Biol. 205, 487-492. [PDF]
Bruckner, R. C. and Cox, M. M. (1989). The histone-like H protein of Escherichia coli is ribosomal protein S3. Nucleic Acids Res. 17, 3145-3161. [PDF]
Kim, J.-I., Heuser, J. and Cox, M. M. (1989). Enhanced recA protein binding to Z DNA represents a kinetic perturbation of a general duplex DNA binding pathway. J. Biol. Chem. 264, 21848-21856. [PDF]
Cox, M. M. (1989). DNA inversion in the 2μm plasmid of Saccharomyces cerevisiae. In Mobile DNA, D. E. Berg and M. M. Howe, eds. (American Society for Microbiology), pp. 661-670. [PDF]
Cox, M. M. (1989). The role of recA protein in homologous genetic recombination. In Molecular Biology of Chromosome Function, K. W. Adolph, ed. (Springer-Verlag), pp. 43-70. [PDF]
1988
Pugh, B. F. and Cox, M. M. (1988). High salt activation of recA protein ATPase in the absence of DNA. J. Biol. Chem. 263, 76-83. [PDF]
Senecoff, J. F., Rossmeissl, P. J. and Cox, M. M. (1988). DNA recognition by the FLP recombinase of the yeast 2μ plasmid. A mutational analysis of the FLP binding site. J. Mol. Biol. 201, 405-421. [PDF]
Gates, C. A. and Cox, M. M. (1988). FLP recombinase is an enzyme. Proc. Natl. Acad. Sci. USA 85, 4628-4632. [PDF]
Umlauf, S. W. and Cox, M. M. (1988). The functional significance of DNA sequence structure in a site-specific genetic recombination reaction. EMBO J. 7, 1845-1852. [PDF]
Schutte, B. C. and Cox, M. M. (1988). Homology-dependent underwinding of duplex DNA in recA protein generated paranemic complexes. Biochemistry 27, 7886-7894. [PDF]
Pugh, B. F. and Cox, M. M. (1988). General mechanism for RecA protein binding to duplex DNA. J. Mol. Biol. 203, 479-493. [PDF]
Meyer-Leon, L., Huang, L.-C., Umlauf, S. W., Cox, M. M. and Inman, R. B. (1988). Holliday intermediates and reaction by-products in FLP protein-promoted site-specific recombination. Mol. Cell. Biol. 8, 3784-3796. [PDF]
Cox, M. M. (1988). FLP site-specific recombination system of Saccharomyces cerevisiae. In Genetic Recombination, R. Kucherlapati and G. R. Smith, eds. (American Society for Microbiology), pp. 429-443. [PDF]
1987
Pugh, B. F. and Cox, M. M. (1987). Stable binding of recA protein to duplex DNA: Unraveling a paradox. J. Biol. Chem. 262, 1326-1336. [PDF]
Pugh, B. F. and Cox, M. M. (1987). RecA protein binding to the heteroduplex product of DNA strand exchange. J. Biol. Chem. 262, 1337-1343. [PDF]
Brenner, S. L., Mitchell, R. S., Morrical, S. W., Neuendorf, S. K., Schutte, B. C. and Cox, M. M. (1987). RecA protein-promoted ATP hydrolysis occurs throughout recA nucleoprotein filaments. J. Biol. Chem. 262, 4011-4016. [PDF]
Schutte, B. C. and Cox, M. M. (1987). Homology-dependent changes in adenosine 5′-triphosphate hydrolysis during recA protein promoted DNA strand exchange: Evidence for long paranemic complexes. Biochemistry 26, 5616-5625. [PDF]
Meyer-Leon, L., Gates, C. A., Attwood, J. M., Wood, E. A. and Cox, M. M. (1987). Purification of the FLP site-specific recombinase by affinity chromatography and re-examination of basic properties of the system. Nucleic Acids Res. 15, 6469-6488. [PDF]
Fishbein, J. C., Baum, H., Cox M. M. and Jencks, W. P. (1987). Concerted general base and bifunctional general acid catalysis of the aminolysis of phenyl acetate by pyrazole. J. Am. Chem. Soc. 109, 5790-5800. [PDF]
Cox, M. M. and Lehman, I. R. (1987). Enzymes of general recombination. Annu. Rev. Biochem. 56, 229-262. [PDF]
Cox, M. M., Pugh, B. F., Schutte, B. C., Lindsley, J. E., Lee, J. and Morrical, S. W. (1987). On the mechanism of recA protein-promoted DNA branch migration. In DNA Replication and Recombination, T. Kelly and R. McMacken, eds. (Alan R. Liss), UCLA Symp. Mol. Cell. Biol., New Ser., 47, 597-607. [PDF]
Gates, C. A., Meyer-Leon, L., Attwood, J. M., Wood, E. A. and Cox, M. M. (1987). Purification of FLP recombinase using sequence-specific DNA affinity chromatography. In Protein Purification: Micro to Macro, R. Burgess, ed. (Alan R. Liss), UCLA Symp. Mol. Cell. Biol., New Ser., 68, 197-206. [PDF]
Pugh, B. F. and Cox, M. M. (1987). Salt can functionally mimick DNA in activating the recA protein ATPase. In Protein Structure, Folding, and Design 2, D. Oxender, ed. (Alan R. Liss), UCLA Symp. Mol. Cell. Biol., New Ser., 69, 275-282. [PDF]
1986
Morrical, S. W., Lee, J. and Cox, M. M. (1986). Continuous association of Escherichia coli single-stranded DNA binding protein with stable complexes of recA protein and single-stranded DNA. Biochemistry 25, 1482-1494. [PDF]
Neuendorf, S. K. and Cox, M. M. (1986). Exchange of recA protein between adjacent recA protein-single-stranded DNA complexes. J. Biol. Chem. 261, 8276-8282. [PDF]
Senecoff, J. F. and Cox, M. M. (1986). Directionality in FLP protein-promoted site-specific recombination is mediated by DNA-DNA pairing. J. Biol. Chem. 261, 7380-7386. [PDF]
Bruckner, R. C. and Cox, M. M. (1986). Specific contacts between the FLP protein of the yeast 2-micron plasmid and its recombination site. J. Biol. Chem. 261, 11798-11807. [PDF]
Senecoff, J. F., Bruckner, R C., Meyer-Leon, L., Gates, C. A., Wood, E., Umlauf, S. W., Attwood, J. M. and Cox, M. M. (1986). Site-specific recombination promoted in vitro by the FLP protein of the yeast two-micron plasmid. In Extrachromosomal Elements in Lower Eukaryotes, R. B.Wickner et al., eds. (Plenum Press), pp. 397-405. [PDF]
1985
Morrical, S. W. and Cox, M. M. (1985). Light scattering studies of the recA protein of Escherichia coli: Relationship between free recA filaments and the recAossDNA complex. Biochemistry 24, 760-767. [PDF]
Senecoff, J. F., Bruckner, R. C. and Cox, M. M. (1985). The FLP recombinase of the yeast 2-μm plasmid: Characterization of its recombination site. Proc. Natl. Acad. Sci. USA 82, 7270-7274. [PDF]
1978, 1981-1984
1984
Meyer-Leon, L., Senecoff, J. F., Bruckner, R. C. and Cox, M. M. (1984). Site-specific genetic recombination promoted by the FLP protein of the yeast 2-micron plasmid in vitro. Cold Spring Harbor Symp. Quant. Biol. 49, 797-804. [PDF]
Cox, M. M., Morrical, S. W. and Neuendorf, S. K. (1984). Unidirectional branch migration promoted by nucleoprotein filaments of RecA protein and DNA. Cold Spring Harbor Symp. Quant. Biol. 49, 525-533. [PDF]
1983
Cox, M. M., Soltis, D. A., Livneh, Z. and Lehman, I. R. (1983). On the role of single-stranded DNA binding protein in recA protein-promoted DNA strand exchange. J. Biol. Chem. 258, 2577-2585. [PDF]
Cox, M. M., Soltis, D. A., Lehman, I. R., DeBrosse, C. and Benkovic, S. J. (1983). ADP-mediated dissociation of stable complexes of recA protein and single-stranded DNA. J. Biol. Chem. 258, 2586-2592. [PDF]
Cox, M. M. (1983). The FLP protein of the yeast 2-mm plasmid: Expression of a eukaryotic genetic recombination system in Escherichia coli. Proc. Natl. Acad. Sci. USA 80, 4223-4227. [PDF]
Cox, M. M., Soltis, D. A., Livneh, Z. and Lehman, I. R. (1983). DNA strand exchange promoted by recA protein and single-stranded DNA-binding protein of Escherichia coli. Cold Spring Harbor Symp. Quant. Biol. 47, 803-810. [PDF]
Soltis, D. A., Cox, M. M., Livneh, Z. and Lehman, I. R. (1983). A stable recA protein-single-stranded DNA complex: An intermediate in DNA strand exchange. In Mechanisms of DNA Replication and Recombination, N. R. Cozzarelli, ed. (Alan R. Liss), pp. 709-721. [PDF]
1982
Cox, M. M. and Lehman, I. R. (1982). RecA protein-promoted DNA strand exchange: Stable complexes of recA protein and single-stranded DNA formed in the presence of ATP and single-stranded DNA binding protein. J. Biol. Chem. 257, 8523-8532. [PDF]
1981
Cox, M. M. and Jencks, W. P. (1981). Catalysis of the methoxyaminolysis of phenyl acetate by a preassociation mechanism with a solvent isotope effect maximum. J. Am. Chem. Soc. 103, 572-580. [PDF]
Cox, M. M. and Jencks, W. P. (1981). Concerted bifunctional proton transfer and general base catalysis in the methoxyaminolysis of phenyl acetate. J. Am. Chem. Soc. 103, 580-587. [PDF]
Cox, M. M. and Lehman, I. R. (1981). Renaturation of DNA: A novel reaction of histones. Nucleic Acids Res. 9, 389-400. [PDF]
Cox, M. M., McEntee, K. and Lehman, I. R. (1981). A simple and rapid procedure for the large scale purification of the recA protein of Escherichia coli. J. Biol. Chem. 256, 4676-4678. [PDF]
Cox, M. M. and Lehman, I. R. (1981). RecA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange. Proc. Natl. Acad. Sci. USA 78, 3433-3437. [PDF]
Cox, M. M. and Lehman, I. R. (1981). Directionality and polarity in recA protein-promoted branch migration. Proc. Natl. Acad. Sci. USA 78, 6018-6022. [PDF]
1978
Cox, M. M. and Jencks, W. P. (1978). General acid catalysis of the aminolysis of phenyl acetate by a preassociation mechanism. J. Am. Chem. Soc. 100, 5956-5957. [PDF]