| Year |
Citation |
Score |
| 2016 |
Yuan Q, Dohrmann PR, Sutton MD, McHenry CS. DNA Polymerase III, but not Polymerase IV, Must be Bound to τ-Containing DnaX Complex to Enable Exchange into Replication Forks. The Journal of Biological Chemistry. PMID 27056333 DOI: 10.1074/Jbc.M116.725358 |
0.555 |
|
| 2016 |
Dohrmann PR, Correa R, Frisch RL, Rosenberg SM, McHenry CS. The DNA polymerase III holoenzyme contains γ and is not a trimeric polymerase. Nucleic Acids Research. PMID 26786318 DOI: 10.1093/Nar/Gkv1510 |
0.565 |
|
| 2015 |
Lindow JC, Dohrmann PR, McHenry CS. DNA Polymerase α Subunit Residues and Interactions Required for Efficient Initiation Complex Formation Identified by a Genetic Selection. The Journal of Biological Chemistry. 290: 16851-60. PMID 25987558 DOI: 10.1074/Jbc.M115.661090 |
0.548 |
|
| 2015 |
Manhart CM, McHenry CS. Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome. The Journal of Biological Chemistry. 290: 10828-39. PMID 25745110 DOI: 10.1074/Jbc.M115.642066 |
0.545 |
|
| 2014 |
Yuan Q, McHenry CS. Cycling of the E. coli lagging strand polymerase is triggered exclusively by the availability of a new primer at the replication fork. Nucleic Acids Research. 42: 1747-56. PMID 24234450 DOI: 10.1093/Nar/Gkt1098 |
0.374 |
|
| 2013 |
Antony E, Weiland E, Yuan Q, Manhart CM, Nguyen B, Kozlov AG, McHenry CS, Lohman TM. Multiple C-terminal tails within a single E. coli SSB homotetramer coordinate DNA replication and repair. Journal of Molecular Biology. 425: 4802-19. PMID 24021816 DOI: 10.1016/J.Jmb.2013.08.021 |
0.538 |
|
| 2013 |
Manhart CM, McHenry CS. The PriA replication restart protein blocks replicase access prior to helicase assembly and directs template specificity through its ATPase activity. The Journal of Biological Chemistry. 288: 3989-99. PMID 23264623 DOI: 10.1074/Jbc.M112.435966 |
0.523 |
|
| 2011 |
Dohrmann PR, Manhart CM, Downey CD, McHenry CS. The rate of polymerase release upon filling the gap between Okazaki fragments is inadequate to support cycling during lagging strand synthesis Journal of Molecular Biology. 414: 15-27. PMID 21986197 DOI: 10.1016/J.Jmb.2011.09.039 |
0.464 |
|
| 2011 |
McHenry CS. Bacterial replicases and related polymerases. Current Opinion in Chemical Biology. 15: 587-94. PMID 21855395 DOI: 10.1016/J.Cbpa.2011.07.018 |
0.528 |
|
| 2011 |
Downey CD, Crooke E, McHenry CS. Polymerase chaperoning and multiple ATPase sites enable the E. coli DNA polymerase III holoenzyme to rapidly form initiation complexes Journal of Molecular Biology. 412: 340-353. PMID 21820444 DOI: 10.1016/J.Jmb.2011.07.051 |
0.544 |
|
| 2011 |
McHenry CS. DNA replicases from a bacterial perspective. Annual Review of Biochemistry. 80: 403-36. PMID 21675919 DOI: 10.1146/Annurev-Biochem-061208-091655 |
0.588 |
|
| 2011 |
McHenry CS. Breaking the rules: bacteria that use several DNA polymerase IIIs. Embo Reports. 12: 408-14. PMID 21475246 DOI: 10.1038/Embor.2011.51 |
0.549 |
|
| 2010 |
Wieczorek A, Downey CD, Dallmann HG, McHenry CS. Only one ATP-binding DnaX subunit is required for initiation complex formation by the Escherichia coli DNA polymerase III holoenzyme Journal of Biological Chemistry. 285: 29049-29053. PMID 20675375 DOI: 10.1074/Jbc.C110.165076 |
0.622 |
|
| 2010 |
Downey CD, McHenry CS. Chaperoning of a Replicative Polymerase onto a Newly Assembled DNA-Bound Sliding Clamp by the Clamp Loader Molecular Cell. 37: 481-491. PMID 20188667 DOI: 10.1016/J.Molcel.2010.01.013 |
0.635 |
|
| 2010 |
Dallmann HG, Fackelmayer OJ, Tomer G, Chen J, Wiktor-Becker A, Ferrara T, Pope C, Oliveira MT, Burgers PM, Kaguni LS, McHenry CS. Parallel multiplicative target screening against divergent bacterial replicases: identification of specific inhibitors with broad spectrum potential. Biochemistry. 49: 2551-62. PMID 20184361 DOI: 10.1021/Bi9020764 |
0.352 |
|
| 2010 |
Sanders GM, Dallmann HG, McHenry CS. Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases. Molecular Cell. 37: 273-81. PMID 20122408 DOI: 10.1016/J.Molcel.2009.12.025 |
0.525 |
|
| 2009 |
Yuan Q, McHenry CS. Strand displacement by DNA polymerase III occurs through a tau-psi-chi link to single-stranded DNA-binding protein coating the lagging strand template. The Journal of Biological Chemistry. 284: 31672-9. PMID 19749191 DOI: 10.1074/Jbc.M109.050740 |
0.624 |
|
| 2009 |
Guiles J, Sun X, Critchley IA, Ochsner U, Tregay M, Stone K, Bertino J, Green L, Sabin R, Dean F, Dallmann HG, McHenry CS, Janjic N. Quinazolin-2-ylamino-quinazolin-4-ols as novel non-nucleoside inhibitors of bacterial DNA polymerase III. Bioorganic & Medicinal Chemistry Letters. 19: 800-2. PMID 19109016 DOI: 10.1016/J.Bmcl.2008.12.038 |
0.461 |
|
| 2006 |
Stano NM, Chen J, McHenry CS. A coproofreading Zn(2+)-dependent exonuclease within a bacterial replicase. Nature Structural & Molecular Biology. 13: 458-9. PMID 16604084 DOI: 10.1038/Nsmb1078 |
0.515 |
|
| 2006 |
Wieczorek A, McHenry CS. The NH2-terminal php domain of the alpha subunit of the Escherichia coli replicase binds the epsilon proofreading subunit. The Journal of Biological Chemistry. 281: 12561-7. PMID 16517598 DOI: 10.1074/Jbc.M513844200 |
0.461 |
|
| 2005 |
Jarvis TC, Beaudry AA, Bullard JM, Ochsner U, Dallmann HG, McHenry CS. Discovery and characterization of the cryptic psi subunit of the pseudomonad DNA replicase. The Journal of Biological Chemistry. 280: 40465-73. PMID 16210315 DOI: 10.1074/Jbc.M508310200 |
0.548 |
|
| 2005 |
Dohrmann PR, McHenry CS. A bipartite polymerase-processivity factor interaction: only the internal beta binding site of the alpha subunit is required for processive replication by the DNA polymerase III holoenzyme. Journal of Molecular Biology. 350: 228-39. PMID 15923012 DOI: 10.1016/J.Jmb.2005.04.065 |
0.449 |
|
| 2005 |
Jarvis TC, Beaudry AA, Bullard JM, Janjic N, McHenry CS. Reconstitution of a minimal DNA replicase from Pseudomonas aeruginosa and stimulation by non-cognate auxiliary factors. The Journal of Biological Chemistry. 280: 7890-900. PMID 15611049 DOI: 10.1074/Jbc.M412263200 |
0.574 |
|
| 2003 |
McHenry CS. Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences. Molecular Microbiology. 49: 1157-65. PMID 12940977 DOI: 10.1046/J.1365-2958.2003.03645.X |
0.58 |
|
| 2002 |
Bullard JM, Williams JC, Acker WK, Jacobi C, Janjic N, McHenry CS. DNA polymerase III holoenzyme from Thermus thermophilus identification, expression, purification of components, and use to reconstitute a processive replicase. The Journal of Biological Chemistry. 277: 13401-8. PMID 11823461 DOI: 10.1074/Jbc.M110833200 |
0.635 |
|
| 2002 |
Bullard JM, Pritchard AE, Song MS, Glover BP, Wieczorek A, Chen J, Janjic N, McHenry CS. A three-domain structure for the delta subunit of the DNA polymerase III holoenzyme delta domain III binds delta' and assembles into the DnaX complex. The Journal of Biological Chemistry. 277: 13246-56. PMID 11809766 DOI: 10.1074/Jbc.M108708200 |
0.789 |
|
| 2002 |
Muthuswami R, Chen J, Burnett BP, Thimmig RL, Janjic N, McHenry CS. The HIV plus-strand transfer reaction: determination of replication-competent intermediates and identification of a novel lentiviral element, the primer over-extension sequence. Journal of Molecular Biology. 315: 311-23. PMID 11786014 DOI: 10.1006/Jmbi.2001.5205 |
0.44 |
|
| 2001 |
Song MS, McHenry CS. Carboxyl-terminal domain III of the delta' subunit of DNA polymerase III holoenzyme binds DnaX and supports cooperative DnaX complex assembly. The Journal of Biological Chemistry. 276: 48709-15. PMID 11606586 DOI: 10.1074/Jbc.M107936200 |
0.739 |
|
| 2001 |
Song MS, Dallmann HG, McHenry CS. Carboxyl-terminal domain III of the delta' subunit of the DNA polymerase III holoenzyme binds delta. The Journal of Biological Chemistry. 276: 40668-79. PMID 11518714 DOI: 10.1074/Jbc.M106373200 |
0.716 |
|
| 2001 |
Glover BP, Pritchard AE, McHenry CS. tau binds and organizes Escherichia coli replication proteins through distinct domains: domain III, shared by gamma and tau, oligomerizes DnaX. The Journal of Biological Chemistry. 276: 35842-6. PMID 11463787 DOI: 10.1074/Jbc.M103719200 |
0.779 |
|
| 2001 |
Pritchard AE, McHenry CS. Assembly of DNA Polymerase III Holoenzyme: Co-assembly of γ and τ is inhibited by DnaX complex accessory proteins but stimulated by DNA polymerase III core Journal of Biological Chemistry. 276: 35217-35222. PMID 11463784 DOI: 10.1074/Jbc.M102735200 |
0.629 |
|
| 2001 |
Glover BP, McHenry CS. The DNA polymerase III holoenzyme: an asymmetric dimeric replicative complex with leading and lagging strand polymerases. Cell. 105: 925-34. PMID 11439188 DOI: 10.1016/S0092-8674(01)00400-7 |
0.809 |
|
| 2001 |
Song MS, Pham PT, Olson M, Carter JR, Franden MA, Schaaper RM, McHenry CS. The delta and delta ' subunits of the DNA polymerase III holoenzyme are essential for initiation complex formation and processive elongation. The Journal of Biological Chemistry. 276: 35165-75. PMID 11432857 DOI: 10.1074/Jbc.M100389200 |
0.738 |
|
| 2001 |
Gao D, McHenry CS. τ binds and organizes Escherichia coli replication proteins through distinct domains. Domain IV, located within the unique C terminus of τ, binds the replication fork helicase, DnaB Journal of Biological Chemistry. 276: 4441-4446. PMID 11078744 DOI: 10.1074/Jbc.M009830200 |
0.528 |
|
| 2001 |
Gao D, McHenry CS. τ binds and organizes Escherichia coli replication proteins Through distinct domains. Partial proteolysis of terminally tagged τ to determine candidate domains and to assign domain V as the α binding domain Journal of Biological Chemistry. 276: 4433-4440. PMID 11078743 DOI: 10.1074/Jbc.M009828200 |
0.503 |
|
| 2001 |
Gao D, McHenry CS. τ binds and organizes Escherichia coli replication proteins through distinct domains. Domain III, shared by γ and τ, binds δδ′ and χψ Journal of Biological Chemistry. 276: 4447-4453. PMID 11078742 DOI: 10.1074/Jbc.M009827200 |
0.516 |
|
| 2000 |
Pritchard AE, Dallmann HG, Glover BP, McHenry CS. A novel assembly mechanism for the DNA polymerase III holoenzyme DnaX complex: association of deltadelta' with DnaX(4) forms DnaX(3)deltadelta'. The Embo Journal. 19: 6536-45. PMID 11101526 DOI: 10.1093/Emboj/19.23.6536 |
0.79 |
|
| 2000 |
Dallmann HG, Kim S, Pritchard AE, Marians KJ, McHenry CS. Characterization of the unique C terminus of the Escherichia coli τ DnaX protein. Monomeric C-τ binds α and DnaB and can partially replace τ in reconstituted replication forks Journal of Biological Chemistry. 275: 15512-15519. PMID 10748120 DOI: 10.1074/jbc.M909257199 |
0.357 |
|
| 2000 |
Glover BP, McHenry CS. The DnaX-binding subunits delta' and psi are bound to gamma and not tau in the DNA polymerase III holoenzyme. The Journal of Biological Chemistry. 275: 3017-20. PMID 10652279 DOI: 10.1074/Jbc.275.5.3017 |
0.795 |
|
| 1999 |
Pham PT, Olson MW, McHenry CS, Schaaper RM. Mismatch extension by Escherichia coli DNA polymerase III holoenzyme Journal of Biological Chemistry. 274: 3705-3710. PMID 9920922 DOI: 10.1074/Jbc.274.6.3705 |
0.485 |
|
| 1999 |
Pritchard AE, McHenry CS. Identification of the acidic residues in the active site of DNA polymerase III Journal of Molecular Biology. 285: 1067-1080. PMID 9887268 DOI: 10.1006/Jmbi.1998.2352 |
0.39 |
|
| 1998 |
Pham PT, Olson MW, McHenry CS, Schaaper RM. The base substitution and frameshift fidelity of Escherichia coli DNA polymerase III holoenzyme in vitro Journal of Biological Chemistry. 273: 23575-23684. PMID 9722597 DOI: 10.1074/Jbc.273.36.23575 |
0.413 |
|
| 1998 |
Glover BP, McHenry CS. The chi psi subunits of DNA polymerase III holoenzyme bind to single-stranded DNA-binding protein (SSB) and facilitate replication of an SSB-coated template. The Journal of Biological Chemistry. 273: 23476-84. PMID 9722585 DOI: 10.1074/Jbc.273.36.23476 |
0.805 |
|
| 1998 |
Marians KJ, Hiasa H, Kim DR, McHenry CS. Role of the core DNA polymerase III subunits at the replication fork. Alpha is the only subunit required for processive replication. The Journal of Biological Chemistry. 273: 2452-7. PMID 9442096 DOI: 10.1074/Jbc.273.4.2452 |
0.534 |
|
| 1997 |
Kim DR, Pritchard AE, McHenry CS. Localization of the active site of the alpha subunit of the Escherichia coli DNA polymerase III holoenzyme. Journal of Bacteriology. 179: 6721-8. PMID 9352922 DOI: 10.1128/Jb.179.21.6721-6728.1997 |
0.478 |
|
| 1997 |
McHenry CS, Seville M, Cull MG. A DNA polymerase III holoenzyme-like subassembly from an extreme thermophilic eubacterium Journal of Molecular Biology. 272: 178-189. PMID 9299346 DOI: 10.1006/Jmbi.1997.1238 |
0.519 |
|
| 1997 |
Burnett BP, Mchenry CS. Posttranscriptional modification of retroviral primers is required for late stages of DNA replication Proceedings of the National Academy of Sciences of the United States of America. 94: 7210-7215. PMID 9207070 DOI: 10.1073/Pnas.94.14.7210 |
0.478 |
|
| 1996 |
Seville M, West AB, Cull MG, McHenry CS. Fluorometric assay for DNA polymerases and reverse transcriptase Biotechniques. 21: 664-672. PMID 8891218 DOI: 10.2144/96214St04 |
0.418 |
|
| 1996 |
Kim S, Dallmann HG, McHenry CS, Marians KJ. τ Couples the leading- and lagging-strand polymerases at the Escherichia coli DNA replication fork Journal of Biological Chemistry. 271: 21406-21412. PMID 8702922 DOI: 10.1074/jbc.271.35.21406 |
0.491 |
|
| 1996 |
Kim DR, McHenry CS. Identification of the beta-binding domain of the alpha subunit of Escherichia coli polymerase III holoenzyme. The Journal of Biological Chemistry. 271: 20699-704. PMID 8702820 DOI: 10.1074/Jbc.271.34.20699 |
0.479 |
|
| 1996 |
Kim DR, McHenry CS. Biotin tagging deletion analysis of domain limits involved in protein-macromolecular interactions. Mapping the tau binding domain of the DNA polymerase III alpha subunit. The Journal of Biological Chemistry. 271: 20690-8. PMID 8702819 DOI: 10.1074/Jbc.271.34.20690 |
0.504 |
|
| 1996 |
Kim DR, McHenry CS. In vivo assembly of overproduced DNA polymerase III. Overproduction, purification, and characterization of the alpha, alpha-epsilon, and alpha-epsilon-theta subunits. The Journal of Biological Chemistry. 271: 20681-9. PMID 8702818 DOI: 10.1074/Jbc.271.34.20681 |
0.513 |
|
| 1996 |
Kim S, Dallmann HG, McHenry CS, Marians KJ. τ Protects β in the leading-strand polymerase complex at the replication fork Journal of Biological Chemistry. 271: 4315-4318. PMID 8626779 DOI: 10.1074/Jbc.271.8.4315 |
0.468 |
|
| 1996 |
Pritchard AE, Garry Dallmann H, McHenry CS. In vivo assembly of the τ-complex of the DNA polymerase III holoenzyme expressed from a five-gene artificial operon: Cleavage of the τ-complex to form a mixed λ-γ-complex by the OmpT protease Journal of Biological Chemistry. 271: 10291-10298. PMID 8626597 DOI: 10.1074/jbc.271.17.10291 |
0.425 |
|
| 1996 |
Kim S, Dallmann HG, McHenry CS, Marians KJ. Coupling of a replicative polymerase and helicase: A τ-DnaB interaction mediates rapid replication fork movement Cell. 84: 643-650. PMID 8598050 DOI: 10.1016/S0092-8674(00)81039-9 |
0.49 |
|
| 1995 |
Cull MG, McHenry CS. Purification of Escherichia coli DNA polymerase III holoenzyme Methods in Enzymology. 262: 22-35. PMID 8594350 DOI: 10.1016/0076-6879(95)62005-2 |
0.599 |
|
| 1995 |
Reems JA, Wood S, McHenry CS. Escherichia coli DNA polymerase III holoenzyme subunits α, β, and γ directly contact the primer-template Journal of Biological Chemistry. 270: 5606-5613. PMID 7890680 DOI: 10.1074/Jbc.270.10.5606 |
0.499 |
|
| 1995 |
Olson MW, Dallmann HG, McHenry CS. DnaX complex of Escherichia coli DNA polymerase III holoenzyme: The χψ complex functions by increasing the affinity of τ and γ for δ·δ' to a physiologically relevant range Journal of Biological Chemistry. 270: 29570-29577. PMID 7494000 DOI: 10.1074/Jbc.270.49.29570 |
0.577 |
|
| 1995 |
Dallmann HG, McHenry CS. DnaX complex of Escherichia coli DNA polymerase III holoenzyme: Physical characterization of the DnaX subunits and complexes Journal of Biological Chemistry. 270: 29563-29569. PMID 7493999 DOI: 10.1074/jbc.270.49.29563 |
0.532 |
|
| 1995 |
Dallmann HG, Thimmig RL, McHenry CS. DnaX complex of Escherichia coli DNA polymerase III holoenzyme: Central role of τ in initiation complex assembly and in determining the functional asymmetry of holoenzyme Journal of Biological Chemistry. 270: 29555-29562. PMID 7493998 DOI: 10.1074/Jbc.270.49.29555 |
0.623 |
|
| 1994 |
Reems JA, McHenry CS. Escherichia coli DNA polymerase III holoenzyme footprints three helical turns of its primer Journal of Biological Chemistry. 269: 33091-33096. PMID 7806536 |
0.573 |
|
| 1993 |
Carter JR, Franden MA, Aebersold R, McHenry CS. Identification, isolation, and characterization of the structural gene encoding the δ' subunit of Escherichia coli DNA polymerase III holoenzyme Journal of Bacteriology. 175: 3812-3822. PMID 8509334 DOI: 10.1128/Jb.175.12.3812-3822.1993 |
0.451 |
|
| 1993 |
Carter JR, Franden MA, Aebersold R, McHenry CS. Identification, isolation, and overexpression of the gene encoding the ψ subunit of DNA polymerase III holoenzyme Journal of Bacteriology. 175: 5604-5610. PMID 8366044 DOI: 10.1128/Jb.175.17.5604-5610.1993 |
0.477 |
|
| 1993 |
Carter JR, Franden MA, Aebersold R, Kim DR, McHenry CS. Isolation, sequencing and overexpression of the gene encoding the theta subunit of DNA polymerase III holoenzyme. Nucleic Acids Research. 21: 3281-6. PMID 8341603 DOI: 10.1093/Nar/21.14.3281 |
0.472 |
|
| 1993 |
Carter JR, Franden MA, Lippincott JA, McHenry CS. Identification, molecular cloning and characterization of the gene encoding the χ subunit of DNA polymerase III holoenzyme of Escherichia coli Mgg Molecular &Amp; General Genetics. 241: 399-408. PMID 8246893 DOI: 10.1007/Bf00284693 |
0.506 |
|
| 1992 |
Wu CA, Zechner EL, Reems JA, McHenry CS, Marians KJ. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork V. Primase action regulates the cycle of Okazaki fragment synthesis Journal of Biological Chemistry. 267: 4074-4083. PMID 1740453 |
0.483 |
|
| 1992 |
Griep MA, McHenry CS. Fluorescence energy transfer between the primer and the β subunit of the DNA polymerase III holoenzyme Journal of Biological Chemistry. 267: 3052-3059. PMID 1737760 |
0.408 |
|
| 1992 |
Carter JR, Franden MA, Aebersold R, McHenry CS. Molecular cloning, sequencing, and overexpression of the structural gene encoding the δ subunit of Escherichia coli DNA polymerase III holoenzyme Journal of Bacteriology. 174: 7013-7025. PMID 1400251 DOI: 10.1128/Jb.174.21.7013-7025.1992 |
0.449 |
|
| 1992 |
Wu CA, Zechner EL, Hughes AJ, Franden MA, McHenry CS, Marians KJ. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork. IV. Reconstitution of an asymmetric, dimeric DNA polymerase III holoenzyme. The Journal of Biological Chemistry. 267: 4064-73. PMID 1346785 |
0.56 |
|
| 1991 |
Tomasiewicz HG, McHenry CS. Sequence analysis of the Escherichia coli dnaE gene Journal of Bacteriology. 173: 4549. PMID 2066347 DOI: 10.1128/jb.173.14.4549-4549.1991 |
0.367 |
|
| 1991 |
Reems JA, Griep MA, McHenry CS. Proofreading activity of DNA polymerase III responds like elongation activity to auxiliary subunits Journal of Biological Chemistry. 266: 4878-4882. PMID 2002034 |
0.508 |
|
| 1991 |
Hughes AJ, Bryan SK, Chen H, Moses RE, McHenry CS. Escherichia coli DNA polymerase II is stimulated by DNA polymerase III holoenzyme auxiliary subunits Journal of Biological Chemistry. 266: 4568-4573. PMID 1999435 |
0.507 |
|
| 1991 |
McHenry CS. DNA polymerase III holoenzyme. Components, structure, and mechanism of a true replicative complex Journal of Biological Chemistry. 266: 19127-19130. PMID 1918028 |
0.473 |
|
| 1991 |
Flower AM, McHenry CS. Transcriptional organization of the Escherichia coli dnaX gene Journal of Molecular Biology. 220: 649-658. PMID 1870125 DOI: 10.1016/0022-2836(91)90107-H |
0.329 |
|
| 1990 |
Flower AM, McHenry CS. The γ subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting Proceedings of the National Academy of Sciences of the United States of America. 87: 3713-3717. PMID 2187190 DOI: 10.1073/Pnas.87.10.3713 |
0.494 |
|
| 1990 |
Griep MA, Reems JA, Franden MA, McHenry CS. Reduction of the potent DNA polymerase III holoenzyme 3′→5′ exonuclease activity by template-primer analogues Biochemistry®. 29: 9006-9014. PMID 2176842 DOI: 10.1021/Bi00490A018 |
0.427 |
|
| 1989 |
Griep MA, McHenry CS. Glutamate overcomes the salt inhibition of DNA polymerase III holoenzyme Journal of Biological Chemistry. 264: 11294-11301. PMID 2567734 |
0.347 |
|
| 1988 |
Santi DV, McHenry CS, Raines RT, Ivanetich KM. Kinetics and thermodynamics of the interaction of 5-fluoro-2'-deoxyuridylate with thymidylate synthase. Biochemistry. 26: 8606-13. PMID 3126806 DOI: 10.1021/Bi00400A017 |
0.37 |
|
| 1988 |
McHenry CS. The asymmetric dimeric polymerase hypothesis: A progress report Bba - Gene Structure and Expression. 951: 240-248. PMID 3061467 DOI: 10.1016/0167-4781(88)90092-9 |
0.52 |
|
| 1988 |
Griep MA, McHenry CS. The dimer of the β subunit of Escherichia coli DNA polymerase III holoenzyme is dissociated into monomers upon binding magnesium(II) Biochemistry. 27: 5210-5215. PMID 3048397 DOI: 10.1021/Bi00414A040 |
0.313 |
|
| 1988 |
Franden MA, Mchenry CS. Detection of an epitope, not required for polymerization, that is conserved between E.coli DNA polymerases I and III and bacteriophage T4 DNA polymerase Nucleic Acids Research. 16: 6353-6360. PMID 2456526 DOI: 10.1093/nar/16.14.6353 |
0.487 |
|
| 1987 |
Oberfelder R, McHenry CS. Characterization of 2'(3')-trinitrophenyl-ATP as an inhibitor of ATP-dependent initiation complex formation between the DNA polymerase III holoenzyme and primed DNA Journal of Biological Chemistry. 262: 4190-4194. PMID 3549726 |
0.453 |
|
| 1987 |
Kwon-Shin O, Bodner JB, McHenry CS, Bambara RA. Properties of initiation complexes formed between Escherichia coli DNA polymerase III holoenzyme and primed DNA in the absence of ATP Journal of Biological Chemistry. 262: 2121-2130. PMID 3546285 |
0.48 |
|
| 1987 |
Hawker JR, McHenry CS. Monoclonal antibodies specific for the tau subunit of the DNA polymerase III holoenzyme of Escherichia coli. Use to demonstrate that tau is the product of the dnaZX gene and that both it and gamma, the dnaZ gene product, are integral components of the same enzyme assembly Journal of Biological Chemistry. 262: 12722-12727. PMID 3040763 |
0.434 |
|
| 1986 |
Johanson KO, Haynes TE, McHenry CS. Chemical characterization and purification of the beta subunit of the DNA polymerase III holoenzyme from an overproducing strain. The Journal of Biological Chemistry. 261: 11460-5. PMID 3528143 |
0.326 |
|
| 1986 |
LaDuca RJ, Crute JJ, McHenry CS, Bambara RA. The β subunit of the Escherichia coli DNA polymerase III holoenzyme interacts functionally with the catalytic core in the absence of other subunits Journal of Biological Chemistry. 261: 7550-7557. PMID 3519609 |
0.476 |
|
| 1985 |
McHenry CS. DNA polymerase III holoenzyme of Escherichia coli: Components and function of a true replicative complex Molecular and Cellular Biochemistry. 66: 71-85. PMID 3885002 DOI: 10.1007/BF00231826 |
0.495 |
|
| 1984 |
McHenry CS, Johanson KO. DNA polymerase III holoenzyme of Escherichia coli: an asymmetric dimeric replicative complex containing distinguishable leading and lagging strand polymerases. Advances in Experimental Medicine and Biology. 179: 315-9. PMID 6395660 |
0.552 |
|
| 1984 |
Johanson KO, McHenry CS. Adenosine 5'-O-(3-thiotriphosphate) can support the formation of an initiation complex between the DNA polymerase III holoenzyme and primed DNA. The Journal of Biological Chemistry. 259: 4589-95. PMID 6368560 |
0.562 |
|
| 1984 |
Johanson KO, McHenry CS. Mechanism of initiation complex formation between DNA polymerase III holoenzyme and primed DNA Federation Proceedings. 43. |
0.477 |
|
| 1983 |
LaDuca RJ, Fay PJ, Chuang C, McHenry CS, Bambara RA. Site-specific pausing of deoxyribonucleic acid synthesis catalyzed by four forms of Escherichia coli DNA polymerase III Biochemistry. 22: 5177-5188. PMID 6360204 DOI: 10.1021/Bi00291A018 |
0.553 |
|
| 1983 |
Crute JJ, LaDuca RJ, Johanson KO, McHenry CS, Bambara RA. Excess beta subunit can bypass the ATP requirement for highly processive synthesis by the Escherichia coli DNA polymerase III holoenzyme. The Journal of Biological Chemistry. 258: 11344-9. PMID 6350303 |
0.498 |
|
| 1982 |
Johanson KO, McHenry CS. The beta subunit of the DNA polymerase III holoenzyme becomes inaccessible to antibody after formation of an initiation complex with primed DNA. The Journal of Biological Chemistry. 257: 12310-5. PMID 7118945 |
0.394 |
|
| 1982 |
Fay PJ, Johanson KO, McHenry CS, Bambara RA. Size classes of products synthesized processively by two subassemblies of Escherichia coli DNA polymerase III holoenzyme. The Journal of Biological Chemistry. 257: 5692-9. PMID 7040370 |
0.514 |
|
| 1982 |
McHenry CS. Purification and characterization of DNA polymerase III'. Identification of tau as a subunit of the DNA polymerase III holoenzyme Journal of Biological Chemistry. 257: 2657-2663. PMID 7037770 |
0.51 |
|
| 1982 |
Welch MM, McHenry CS. Cloning and identification of the product of the dnaE gene of Escherichia coli Journal of Bacteriology. 152: 351-356. PMID 6288664 |
0.336 |
|
| 1981 |
Fay PJ, Johanson KO, McHenry CS, Bambara RA. Size classes of products synthesized processively by DNA polymerase III and DNA polymerase III holoenzyme of Escherichia coli. The Journal of Biological Chemistry. 256: 976-83. PMID 7005228 |
0.427 |
|
| 1980 |
Johanson KO, McHenry CS. Purification and characterization of the beta subunit of the DNA polymerase III holoenzyme of Escherichia coli. The Journal of Biological Chemistry. 255: 10984-90. PMID 6776124 |
0.445 |
|
| 1979 |
McHenry CS, Crow W. DNA polymerase III of Escherichia coli. Purification and identification of subunits Journal of Biological Chemistry. 254: 1748-1753. PMID 368075 |
0.52 |
|
| 1974 |
Santi DV, McHenry CS, Perriard ER. A filter assay for thymidylate synthetase using 5-fluoro-2′-deoxyuridylate as an active site titrant Biochemistry. 13: 467-470. PMID 4358948 DOI: 10.1021/Bi00700A011 |
0.312 |
|
| 1974 |
Santi DV, McHenry CS, Sommer H. Mechanism of interaction of thymidylate synthetase with 5-fluorodeoxyuridylate Biochemistry. 13: 471-481. PMID 4203910 DOI: 10.1021/Bi00700A012 |
0.406 |
|
| 1972 |
Santi DV, McHenry CS. 5-Fluoro-2'-deoxyuridylate: covalent complex with thymidylate synthetase Proceedings of the National Academy of Sciences of the United States of America. 69: 1855-1857. PMID 4505665 DOI: 10.1073/Pnas.69.7.1855 |
0.344 |
|
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