Year |
Citation |
Score |
2023 |
McNally JR, Ames AM, Admiraal SJ, O'Brien PJ. Human DNA ligases I and III have stand-alone end-joining capability, but differ in ligation efficiency and specificity. Nucleic Acids Research. 51: 796-805. PMID 36625284 DOI: 10.1093/nar/gkac1263 |
0.384 |
|
2021 |
Jurkiw TJ, Tumbale PP, Schellenberg MJ, Cunningham-Rundles C, Williams RS, O'Brien PJ. LIG1 syndrome mutations remodel a cooperative network of ligand binding interactions to compromise ligation efficiency. Nucleic Acids Research. PMID 33444456 DOI: 10.1093/nar/gkaa1297 |
0.337 |
|
2020 |
Baldwin MR, Admiraal SJ, O'Brien PJ. Transient kinetic analysis of oxidative dealkylation by the direct reversal DNA repair enzyme AlkB. The Journal of Biological Chemistry. PMID 32284330 DOI: 10.1074/jbc.RA120.013517 |
0.393 |
|
2019 |
Thelen AZ, O'Brien PJ. Recognition of 1,-ethenoguanine by alkyladenine DNA glycosylase is restricted by a conserved active site residue. The Journal of Biological Chemistry. PMID 31882538 DOI: 10.1074/jbc.RA119.011459 |
0.337 |
|
2019 |
Tumbale PP, Jurkiw TJ, Schellenberg MJ, Riccio AA, O'Brien PJ, Williams RS. Two-tiered enforcement of high-fidelity DNA ligation. Nature Communications. 10: 5431. PMID 31780661 DOI: 10.1038/s41467-019-13478-7 |
0.371 |
|
2019 |
Admiraal SJ, Eyler DE, Baldwin MR, Brines EM, Lohans CT, Schofield CJ, O'Brien PJ. Expansion of base excision repair compensates for a lack of DNA repair by oxidative dealkylation in budding yeast. The Journal of Biological Chemistry. PMID 31320474 DOI: 10.1074/Jbc.Ra119.009813 |
0.338 |
|
2018 |
Taylor EL, Kesavan PM, Wolfe AE, O'Brien PJ. Distinguishing Specific and Nonspecific Complexes of Alkyladenine DNA Glycosylase. Biochemistry. PMID 29940097 DOI: 10.1021/acs.biochem.8b00531 |
0.381 |
|
2017 |
McNally JR, O'Brien PJ. Kinetic Analyses of Single-Strand Break Repair by Human DNA Ligase III Isoforms Reveals Biochemical Differences from DNA Ligase I. The Journal of Biological Chemistry. PMID 28751376 DOI: 10.1074/jbc.M117.804625 |
0.363 |
|
2017 |
Hendershot JM, O'Brien PJ. Search for DNA Damage by Human Alkyladenine DNA Glycosylase Involves Early Intercalation by an Aromatic Residue. The Journal of Biological Chemistry. PMID 28747435 DOI: 10.1074/jbc.M117.782813 |
0.426 |
|
2017 |
Hendershot JM, O'Brien PJ. Transient Kinetic Methods for Mechanistic Characterization of DNA Binding and Nucleotide Flipping. Methods in Enzymology. 592: 377-415. PMID 28668128 DOI: 10.1016/bs.mie.2017.04.003 |
0.424 |
|
2017 |
Admiraal SJ, O'Brien PJ. Reactivity and Cross-Linking of 5'-Terminal Abasic Sites Within DNA. Chemical Research in Toxicology. PMID 28485930 DOI: 10.1021/acs.chemrestox.7b00057 |
0.381 |
|
2015 |
Zhang Y, O'Brien PJ. Repair of Alkylation Damage in Eukaryotic Chromatin Depends on Searching Ability of Alkyladenine DNA Glycosylase. Acs Chemical Biology. PMID 26317160 DOI: 10.1021/acschembio.5b00409 |
0.402 |
|
2015 |
Admiraal SJ, O'Brien PJ. Base excision repair enzymes protect abasic sites in duplex DNA from interstrand cross-links. Biochemistry. 54: 1849-57. PMID 25679877 DOI: 10.1021/bi501491z |
0.439 |
|
2015 |
Taylor EL, O'Brien PJ. Kinetic mechanism for the flipping and excision of 1,N(6)-ethenoadenine by AlkA. Biochemistry. 54: 898-908. PMID 25537480 DOI: 10.1021/bi501356x |
0.431 |
|
2015 |
Hedglin M, Zhang Y, O'Brien PJ. Probing the DNA structural requirements for facilitated diffusion. Biochemistry. 54: 557-66. PMID 25495964 DOI: 10.1021/Bi5013707 |
0.713 |
|
2014 |
Hendershot JM, O'Brien PJ. Critical role of DNA intercalation in enzyme-catalyzed nucleotide flipping. Nucleic Acids Research. 42: 12681-90. PMID 25324304 DOI: 10.1093/nar/gku919 |
0.373 |
|
2013 |
Hedglin M, Zhang Y, O'Brien PJ. Isolating contributions from intersegmental transfer to DNA searching by alkyladenine DNA glycosylase. The Journal of Biological Chemistry. 288: 24550-9. PMID 23839988 DOI: 10.1074/Jbc.M113.477018 |
0.727 |
|
2013 |
Admiraal SJ, O'Brien PJ. DNA-N-glycosylases process novel O-glycosidic sites in DNA. Biochemistry. 52: 4066-74. PMID 23688261 DOI: 10.1021/bi400218j |
0.372 |
|
2011 |
Taylor MR, Conrad JA, Wahl D, O'Brien PJ. Kinetic mechanism of human DNA ligase I reveals magnesium-dependent changes in the rate-limiting step that compromise ligation efficiency. The Journal of Biological Chemistry. 286: 23054-62. PMID 21561855 DOI: 10.1074/Jbc.M111.248831 |
0.432 |
|
2011 |
Zhao B, O'Brien PJ. Kinetic mechanism for the excision of hypoxanthine by Escherichia coli AlkA and evidence for binding to DNA ends. Biochemistry. 50: 4350-9. PMID 21491902 DOI: 10.1021/bi200232c |
0.346 |
|
2011 |
Nikolova EN, Kim E, Wise AA, O'Brien PJ, Andricioaei I, Al-Hashimi HM. Transient Hoogsteen base pairs in canonical duplex DNA. Nature. 470: 498-502. PMID 21270796 DOI: 10.1038/Nature09775 |
0.319 |
|
2011 |
Hendershot JM, Wolfe AE, O'Brien PJ. Substitution of active site tyrosines with tryptophan alters the free energy for nucleotide flipping by human alkyladenine DNA glycosylase. Biochemistry. 50: 1864-74. PMID 21244040 DOI: 10.1021/bi101856a |
0.362 |
|
2010 |
Admiraal SJ, O'Brien PJ. N-glycosyl bond formation catalyzed by human alkyladenine DNA glycosylase. Biochemistry. 49: 9024-6. PMID 20873830 DOI: 10.1021/bi101380d |
0.357 |
|
2010 |
Baldwin MR, O'Brien PJ. Nonspecific DNA binding and coordination of the first two steps of base excision repair. Biochemistry. 49: 7879-91. PMID 20701268 DOI: 10.1021/bi100889r |
0.336 |
|
2010 |
Hedglin M, O'Brien PJ. Hopping enables a DNA repair glycosylase to search both strands and bypass a bound protein. Acs Chemical Biology. 5: 427-36. PMID 20201599 DOI: 10.1021/Cb1000185 |
0.725 |
|
2008 |
Hedglin M, O'Brien PJ. Human alkyladenine DNA glycosylase employs a processive search for DNA damage. Biochemistry. 47: 11434-45. PMID 18839966 DOI: 10.1021/Bi801046Y |
0.727 |
|
2008 |
O'Brien PJ, Lassila JK, Fenn TD, Zalatan JG, Herschlag D. Arginine coordination in enzymatic phosphoryl transfer: evaluation of the effect of Arg166 mutations in Escherichia coli alkaline phosphatase. Biochemistry. 47: 7663-72. PMID 18627128 DOI: 10.1021/Bi800545N |
0.732 |
|
2007 |
Zalatan JG, Catrina I, Mitchell R, Grzyska PK, O'brien PJ, Herschlag D, Hengge AC. Kinetic isotope effects for alkaline phosphatase reactions: implications for the role of active-site metal ions in catalysis. Journal of the American Chemical Society. 129: 9789-98. PMID 17630738 DOI: 10.1021/Ja072196+ |
0.732 |
|
2007 |
Catrina I, O'Brien PJ, Purcell J, Nikolic-Hughes I, Zalatan JG, Hengge AC, Herschlag D. Probing the origin of the compromised catalysis of E. coli alkaline phosphatase in its promiscuous sulfatase reaction. Journal of the American Chemical Society. 129: 5760-5. PMID 17411045 DOI: 10.1021/Ja069111+ |
0.726 |
|
2006 |
O'Brien PJ. Catalytic promiscuity and the divergent evolution of DNA repair enzymes. Chemical Reviews. 106: 720-52. PMID 16464022 DOI: 10.1021/cr040481v |
0.382 |
|
2005 |
Nikolic-Hughes I, O'brien PJ, Herschlag D. Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions. Journal of the American Chemical Society. 127: 9314-5. PMID 15984827 DOI: 10.1021/Ja051603J |
0.613 |
|
2004 |
Pascal JM, O'Brien PJ, Tomkinson AE, Ellenberger T. Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature. 432: 473-8. PMID 15565146 DOI: 10.1038/Nature03082 |
0.475 |
|
2004 |
O'Brien PJ, Ellenberger T. The Escherichia coli 3-methyladenine DNA glycosylase AlkA has a remarkably versatile active site. The Journal of Biological Chemistry. 279: 26876-84. PMID 15126496 DOI: 10.1074/Jbc.M403860200 |
0.516 |
|
2004 |
O'Brien PJ, Ellenberger T. Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase. The Journal of Biological Chemistry. 279: 9750-7. PMID 14688248 DOI: 10.1074/Jbc.M312232200 |
0.448 |
|
2003 |
O'Brien PJ, Ellenberger T. Human alkyladenine DNA glycosylase uses acid-base catalysis for selective excision of damaged purines. Biochemistry. 42: 12418-29. PMID 14567703 DOI: 10.1021/Bi035177V |
0.513 |
|
2002 |
O'Brien PJ, Herschlag D. Alkaline Phosphatase Revisited: Hydrolysis of Alkyl Phosphates (†). Biochemistry. 41: 3207-3225. PMID 28212002 DOI: 10.1021/bi012166y |
0.572 |
|
2002 |
Cheng H, Nikolic-Hughes I, Wang JH, Deng H, O'Brien PJ, Wu L, Zhang ZY, Herschlag D, Callender R. Environmental effects on phosphoryl group bonding probed by vibrational spectroscopy: implications for understanding phosphoryl transfer and enzymatic catalysis. Journal of the American Chemical Society. 124: 11295-306. PMID 12236744 DOI: 10.1021/Ja026481Z |
0.512 |
|
2002 |
O'Brien PJ, Herschlag D. Alkaline phosphatase revisited: hydrolysis of alkyl phosphates. Biochemistry. 41: 3207-25. PMID 11863460 DOI: 10.1021/Bi012166Y |
0.609 |
|
2001 |
O'Brien PJ, Herschlag D. Functional interrelationships in the alkaline phosphatase superfamily: phosphodiesterase activity of Escherichia coli alkaline phosphatase. Biochemistry. 40: 5691-9. PMID 11341834 DOI: 10.1021/Bi0028892 |
0.594 |
|
1999 |
O'Brien PJ, Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chemistry & Biology. 6: R91-R105. PMID 10099128 DOI: 10.1016/S1074-5521(99)80033-7 |
0.568 |
|
1999 |
O'Brien PJ, Herschlag D. Does the active site arginine change the nature of the transition state for alkaline phosphatase-catalyzed phosphoryl transfer? [[11] Journal of the American Chemical Society. 121: 11022-11023. DOI: 10.1021/Ja9932582 |
0.588 |
|
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