Year |
Citation |
Score |
2024 |
Conlon SG, Khuu C, Trasviña-Arenas CH, Xia T, Hamm ML, Raetz AG, David SS. Cellular Repair of Synthetic Analogs of Oxidative DNA Damage Reveals a Key Structure-Activity Relationship of the Cancer-Associated MUTYH DNA Repair Glycosylase. Acs Central Science. 10: 291-301. PMID 38435525 DOI: 10.1021/acscentsci.3c00784 |
0.539 |
|
2023 |
Eckenroth BE, Bumgarner JD, Matsumoto-Elliott O, David SS, Doublié S. Structural and biochemical insights into NEIL2's preference for abasic sites. Nucleic Acids Research. PMID 37971311 DOI: 10.1093/nar/gkad1075 |
0.535 |
|
2023 |
Demir M, Russelburg LP, Lin WJ, Trasviña-Arenas CH, Huang B, Yuen PK, Horvath MP, David SS. Structural snapshots of base excision by the cancer-associated variant MutY N146S reveal a retaining mechanism. Nucleic Acids Research. PMID 36631987 DOI: 10.1093/nar/gkac1246 |
0.367 |
|
2022 |
Lotsof ER, Krajewski AE, Anderson-Steele B, Rogers J, Zhang L, Yeo J, Conlon SG, Manlove AH, Lee JK, David SS. NEIL1 Recoding due to RNA Editing Impacts Lesion-Specific Recognition and Excision. Journal of the American Chemical Society. 144: 14578-14589. PMID 35917336 DOI: 10.1021/jacs.2c03625 |
0.346 |
|
2021 |
Trasviña-Arenas CH, Demir M, Lin WJ, David SS. Structure, function and evolution of the Helix-hairpin-Helix DNA glycosylase superfamily: Piecing together the evolutionary puzzle of DNA base damage repair mechanisms. Dna Repair. 108: 103231. PMID 34649144 DOI: 10.1016/j.dnarep.2021.103231 |
0.53 |
|
2021 |
Jang S, Schaich MA, Khuu C, Schnable BL, Majumdar C, Watkins SC, David SS, Van Houten B. Single molecule analysis indicates stimulation of MUTYH by UV-DDB through enzyme turnover. Nucleic Acids Research. PMID 34232996 DOI: 10.1093/nar/gkab591 |
0.442 |
|
2021 |
Pidugu LS, Bright H, Lin WJ, Majumdar C, Van Ostrand RP, David SS, Pozharski E, Drohat AC. Structural Insights into the Mechanism of Base Excision by MBD4. Journal of Molecular Biology. 167097. PMID 34107280 DOI: 10.1016/j.jmb.2021.167097 |
0.521 |
|
2021 |
Yeo J, Lotsof ER, Anderson-Steele BM, David SS. RNA Editing of the Human DNA Glycosylase NEIL1 Alters Its Removal of 5-Hydroxyuracil Lesions in DNA. Biochemistry. PMID 33929180 DOI: 10.1021/acs.biochem.1c00062 |
0.51 |
|
2020 |
Majumdar C, McKibbin PL, Krajewski AE, Manlove AH, Lee JK, David SS. Unique Hydrogen Bonding of Adenine with the Oxidatively Damaged Base 8-Oxoguanine Enables Specific Recognition and Repair by DNA Glycosylase MutY. Journal of the American Chemical Society. PMID 33202125 DOI: 10.1021/jacs.0c06767 |
0.837 |
|
2020 |
Zhu RY, Majumdar C, Khuu C, De Rosa M, Opresko PL, David SS, Kool ET. Designer Fluorescent Adenines Enable Real-Time Monitoring of MUTYH Activity. Acs Central Science. 6: 1735-1742. PMID 33145410 DOI: 10.1021/Acscentsci.0C00369 |
0.548 |
|
2020 |
Lee A, Majumdar C, Kathe SD, Van Ostrand RP, Vickery HR, Averill AM, Nelson SR, Manlove AH, McCord MA, David SS. Detection of OG:A lesion mispairs by MutY relies on a single His residue and the 2-amino group of 8-oxoguanine. Journal of the American Chemical Society. PMID 32664726 DOI: 10.1021/Jacs.0C04284 |
0.529 |
|
2020 |
Jun YW, Wilson DL, Kietrys AM, Lotsof ER, Conlon SG, David SS, Kool ET. An Excimer Clamp for Measuring Damaged Base Excision by the DNA Repair Enzyme NTH1. Angewandte Chemie (International Ed. in English). PMID 32109332 DOI: 10.1002/Anie.202001516 |
0.59 |
|
2020 |
Cao S, Rogers J, Yeo J, Anderson-Steele B, Ashby J, David SS. 2'-Fluorinated Hydantoins as Chemical Biology Tools for Base Excision Repair Glycosylases. Acs Chemical Biology. PMID 32069022 DOI: 10.1021/Acschembio.9B00923 |
0.459 |
|
2020 |
Raetz AG, Banda DM, Ma X, Xu G, Rajavel AN, McKibbin PL, Lebrilla CB, David SS. The DNA repair enzyme MUTYH potentiates cytotoxicity of the alkylating agent MNNG by interacting with abasic sites. The Journal of Biological Chemistry. PMID 32001618 DOI: 10.1074/Jbc.Ra119.010497 |
0.814 |
|
2019 |
Russelburg LP, O'Shea Murray VL, Demir M, Knutsen KR, Sehgal SL, Cao S, David SS, Horvath MP. Structural basis for finding OG lesions and avoiding undamaged G by the DNA glycosylase MutY. Acs Chemical Biology. PMID 31829624 DOI: 10.1021/Acschembio.9B00639 |
0.527 |
|
2019 |
Minko IG, Vartanian VL, Tozaki NN, Coskun E, Coskun SH, Jaruga P, Yeo J, David SS, Stone MP, Egli M, Dizdaroglu M, McCullough AK, Lloyd RS. Recognition of DNA adducts by edited and unedited forms of DNA glycosylase NEIL1. Dna Repair. 85: 102741. PMID 31733589 DOI: 10.1016/J.Dnarep.2019.102741 |
0.573 |
|
2019 |
Jang S, Kumar N, Beckwitt EC, Kong M, Fouquerel E, Rapić-Otrin V, Prasad R, Watkins SC, Khuu C, Majumdar C, David SS, Wilson SH, Bruchez MP, Opresko PL, Van Houten B. Damage sensor role of UV-DDB during base excision repair. Nature Structural & Molecular Biology. PMID 31332353 DOI: 10.1038/S41594-019-0261-7 |
0.614 |
|
2019 |
Raetz AG, David SS. When you're strange: Unusual features of the MUTYH glycosylase and implications in cancer. Dna Repair. 80: 16-25. PMID 31203172 DOI: 10.1016/J.Dnarep.2019.05.005 |
0.848 |
|
2019 |
Trasviña-Arenas CH, David SS, Delaye L, Azuara-Liceaga E, Brieba LG. Evolution of Base Excision Repair in Entamoeba histolytica is shaped by gene loss, gene duplication, and lateral gene transfer. Dna Repair. 76: 76-88. PMID 30822689 DOI: 10.1016/J.Dnarep.2019.02.009 |
0.501 |
|
2018 |
Yuen PK, Green SA, Ashby J, Lay KT, Santra A, Chen X, Horvath MP, David SS. Targeting Base Excision Repair Glycosylases with DNA containing Transition State Mimics prepared via Click Chemistry. Acs Chemical Biology. PMID 30500207 DOI: 10.1021/Acschembio.8B00771 |
0.547 |
|
2018 |
Nuñez NN, Khuu C, Babu CS, Bertolani SJ, Rajavel AN, Spear JE, Armas JA, Wright JD, Siegel JB, Lim C, David SS. The Zinc Linchpin Motif in the DNA Repair Glycosylase MUTYH: Identifying the Zn2+ Ligands and Roles in Damage Recognition and Repair. Journal of the American Chemical Society. PMID 30208271 DOI: 10.1021/Jacs.8B06923 |
0.581 |
|
2018 |
Majumdar C, Nuñez NN, Raetz AG, Khuu C, David SS. Cellular Assays for Studying the Fe-S Cluster Containing Base Excision Repair Glycosylase MUTYH and Homologs. Methods in Enzymology. 599: 69-99. PMID 29746250 DOI: 10.1016/Bs.Mie.2017.12.006 |
0.847 |
|
2018 |
Nuñez NN, Majumdar C, Lay KT, David SS. Fe-S Clusters and MutY Base Excision Repair Glycosylases: Purification, Kinetics, and DNA Affinity Measurements. Methods in Enzymology. 599: 21-68. PMID 29746241 DOI: 10.1016/Bs.Mie.2017.11.035 |
0.473 |
|
2017 |
Shi R, Mullins EA, Shen XX, Lay KT, Yuen PK, David SS, Rokas A, Eichman BF. Selective base excision repair of DNA damage by the non-base-flipping DNA glycosylase AlkC. The Embo Journal. PMID 29054852 DOI: 10.15252/Embj.201797833 |
0.628 |
|
2017 |
Manlove AH, McKibbin PL, Doyle EL, Majumdar C, Hamm ML, David SS. Structure Activity Relationships Reveal Key Features of 8-Oxoguanine:Adenine Mismatch Detection by the MutY DNA Glycosylase. Acs Chemical Biology. PMID 28723094 DOI: 10.1021/Acschembio.7B00389 |
0.833 |
|
2017 |
Ha Y, Arnold AR, Nuñez NN, Bartels PL, Zhou A, David SS, Barton JK, Hedman B, Hodgson KO, Solomon EI. Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY. Journal of the American Chemical Society. 139: 11434-11442. PMID 28715891 DOI: 10.1021/Jacs.7B03966 |
0.473 |
|
2017 |
Bartels PL, Zhou A, Arnold AR, Nuñez NN, Crespilho FN, David SS, Barton JK. Electrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA. Langmuir : the Acs Journal of Surfaces and Colloids. 33: 2523-2530. PMID 28219007 DOI: 10.1021/Acs.Langmuir.6B04581 |
0.519 |
|
2017 |
Banda DM, Nuñez NN, Burnside MA, Bradshaw KM, David SS. Repair of 8-oxoG:A Mismatches by the MUTYH Glycosylase: Mechanism, Metals & Medicine. Free Radical Biology & Medicine. PMID 28087410 DOI: 10.1016/J.Freeradbiomed.2017.01.008 |
0.596 |
|
2017 |
Horvath MP, Drage EP, Dart E, Russelburg P, O'Shea VL, Woods RD, Chu A, Cao S, Richards JL, David SS. Mechanism and evolution of the DNA repair enzyme MutY Acta Crystallographica Section a Foundations and Advances. 73: a272-a272. DOI: 10.1107/S010876731709732X |
0.787 |
|
2016 |
Wickramaratne SS, Banda D, Ji S, Manlove AH, Malayappan B, Nuñez NN, Samson LD, Campbell C, David SS, Tretyakova NY. Base Excision Repair of N(6)-Deoxyadenosine Adducts of 1,3-Butadiene. Biochemistry. PMID 27552084 DOI: 10.1021/Acs.Biochem.6B00553 |
0.406 |
|
2016 |
Shen Y, McMackin MZ, Shan Y, Raetz A, David S, Cortopassi G. Frataxin Deficiency Promotes Excess Microglial DNA Damage and Inflammation that Is Rescued by PJ34. Plos One. 11: e0151026. PMID 26954031 DOI: 10.1371/Journal.Pone.0151026 |
0.834 |
|
2015 |
Woods RD, O'Shea VL, Chu A, Cao S, Richards JL, Horvath MP, David SS. Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases. Nucleic Acids Research. PMID 26673696 DOI: 10.1093/Nar/Gkv1469 |
0.75 |
|
2015 |
Mullins EA, Shi R, Parsons ZD, Yuen PK, David SS, Igarashi Y, Eichman BF. The DNA glycosylase AlkD uses a non-base-flipping mechanism to excise bulky lesions. Nature. PMID 26524531 DOI: 10.1038/Nature15728 |
0.633 |
|
2015 |
Brinkmeyer MK, David SS. Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1. Dna Repair. 34: 39-51. PMID 26377631 DOI: 10.1016/J.Dnarep.2015.08.001 |
0.838 |
|
2014 |
Rowland MM, Schonhoft JD, McKibbin PL, David SS, Stivers JT. Microscopic mechanism of DNA damage searching by hOGG1. Nucleic Acids Research. 42: 9295-303. PMID 25016526 DOI: 10.1093/Nar/Gku621 |
0.834 |
|
2014 |
Engstrom LM, Brinkmeyer MK, Ha Y, Raetz AG, Hedman B, Hodgson KO, Solomon EI, David SS. A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage. Journal of the American Chemical Society. 136: 7829-32. PMID 24841533 DOI: 10.1021/Ja502942D |
0.764 |
|
2013 |
McKibbin PL, Fleming AM, Towheed MA, Van Houten B, Burrows CJ, David SS. Repair of hydantoin lesions and their amine adducts in DNA by base and nucleotide excision repair. Journal of the American Chemical Society. 135: 13851-61. PMID 23930966 DOI: 10.1021/Ja4059469 |
0.817 |
|
2012 |
Michelson AZ, Rozenberg A, Tian Y, Sun X, Davis J, Francis AW, O'Shea VL, Halasyam M, Manlove AH, David SS, Lee JK. Gas-phase studies of substrates for the DNA mismatch repair enzyme MutY. Journal of the American Chemical Society. 134: 19839-50. PMID 23106240 DOI: 10.1021/Ja309082K |
0.37 |
|
2012 |
Raetz AG, Xie Y, Kundu S, Brinkmeyer MK, Chang C, David SS. Cancer-associated variants and a common polymorphism of MUTYH exhibit reduced repair of oxidative DNA damage using a GFP-based assay in mammalian cells. Carcinogenesis. 33: 2301-9. PMID 22926731 DOI: 10.1093/Carcin/Bgs270 |
0.791 |
|
2012 |
Engstrom LM, Partington OA, David SS. An iron-sulfur cluster loop motif in the Archaeoglobus fulgidus uracil-DNA glycosylase mediates efficient uracil recognition and removal. Biochemistry. 51: 5187-97. PMID 22646210 DOI: 10.1021/Bi3000462 |
0.846 |
|
2012 |
Onizuka K, Yeo J, David SS, Beal PA. NEIL1 binding to DNA containing 2'-fluorothymidine glycol stereoisomers and the effect of editing. Chembiochem : a European Journal of Chemical Biology. 13: 1338-48. PMID 22639086 DOI: 10.1002/Cbic.201200139 |
0.587 |
|
2012 |
Brinkmeyer MK, Pope MA, David SS. Catalytic contributions of key residues in the adenine glycosylase MutY revealed by pH-dependent kinetics and cellular repair assays. Chemistry & Biology. 19: 276-86. PMID 22365610 DOI: 10.1016/J.Chembiol.2011.11.011 |
0.84 |
|
2012 |
Ono T, Wang S, Koo CK, Engstrom L, David SS, Kool ET. Direct fluorescence monitoring of DNA base excision repair. Angewandte Chemie (International Ed. in English). 51: 1689-92. PMID 22241823 DOI: 10.1002/Anie.201108135 |
0.854 |
|
2012 |
McKibbin PL, Kobori A, Taniguchi Y, Kool ET, David SS. Surprising repair activities of nonpolar analogs of 8-oxoG expose features of recognition and catalysis by base excision repair glycosylases. Journal of the American Chemical Society. 134: 1653-61. PMID 22175854 DOI: 10.1021/Ja208510M |
0.828 |
|
2011 |
Chu AM, Fettinger JC, David SS. Profiling base excision repair glycosylases with synthesized transition state analogs. Bioorganic & Medicinal Chemistry Letters. 21: 4969-72. PMID 21689934 DOI: 10.1016/J.Bmcl.2011.05.085 |
0.763 |
|
2010 |
Yeo J, Goodman RA, Schirle NT, David SS, Beal PA. RNA editing changes the lesion specificity for the DNA repair enzyme NEIL1 Proceedings of the National Academy of Sciences of the United States of America. 107: 20715-20719. PMID 21068368 DOI: 10.1073/Pnas.1009231107 |
0.544 |
|
2010 |
Kundu S, Brinkmeyer MK, Eigenheer RA, David SS. Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): a mismatch recognition. Dna Repair. 9: 1026-37. PMID 20724227 DOI: 10.1016/J.Dnarep.2010.07.002 |
0.813 |
|
2010 |
Zhao X, Krishnamurthy N, Burrows CJ, David SS. Mutation versus repair: NEILl removal of hydantoin lesions in single-stranded, bulge, bubble, and duplex DNA contexts Biochemistry. 49: 1658-1666. PMID 20099873 DOI: 10.1021/Bi901852Q |
0.559 |
|
2009 |
Kundu S, Brinkmeyer MK, Livingston AL, David SS. Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer. Dna Repair. 8: 1400-10. PMID 19836313 DOI: 10.1016/J.Dnarep.2009.09.009 |
0.792 |
|
2008 |
Krishnamurthy N, Zhao X, Burrows CJ, David SS. Superior removal of hydantoin lesions relative to other oxidized bases by the human DNA glycosylase hNEIL1 Biochemistry. 47: 7137-7146. PMID 18543945 DOI: 10.1021/Bi800160S |
0.44 |
|
2008 |
David SS, Meggers E. Inorganic chemical biology: from small metal complexes in biological systems to metalloproteins. Current Opinion in Chemical Biology. 12: 194-6. PMID 18374664 DOI: 10.1016/J.Cbpa.2008.03.008 |
0.395 |
|
2008 |
Krishnamurthy N, Haraguchi K, Greenberg MM, David SS. Efficient removal of formamidopyrimidines by 8-oxoguanine glycosylases. Biochemistry. 47: 1043-50. PMID 18154319 DOI: 10.1021/Bi701619U |
0.389 |
|
2008 |
Livingston AL, O'Shea VL, Kim T, Kool ET, David SS. Unnatural substrates reveal the importance of 8-oxoguanine for in vivo mismatch repair by MutY. Nature Chemical Biology. 4: 51-8. PMID 18026095 DOI: 10.1038/Nchembio.2007.40 |
0.602 |
|
2007 |
Krishnamurthy N, Muller JG, Burrows CJ, David SS. Unusual structural features of hydantoin lesions translate into efficient recognition by Escherichia coli Fpg Biochemistry. 46: 9355-9365. PMID 17655276 DOI: 10.1021/Bi602459V |
0.445 |
|
2007 |
David SS, O'Shea VL, Kundu S. Base-excision repair of oxidative DNA damage. Nature. 447: 941-50. PMID 17581577 DOI: 10.1038/Nature05978 |
0.614 |
|
2007 |
Zhao X, Muller JG, Halasyam M, David SS, Burrows CJ. In vitro ligation of oligodeoxynucleotides containing C8-oxidized purine lesions using bacteriophage T4 DNA ligase Biochemistry. 46: 3734-3744. PMID 17323928 DOI: 10.1021/Bi062214K |
0.477 |
|
2006 |
Yavin E, Stemp ED, O'shea VL, David SS, Barton JK. Electron trap for DNA-bound repair enzymes: a strategy for DNA-mediated signaling. Proceedings of the National Academy of Sciences of the United States of America. 103: 3610-4. PMID 16505354 DOI: 10.1073/Pnas.0600239103 |
0.604 |
|
2005 |
Livingston AL, Kundu S, Pozzi MH, Anderson DW, David SS. Insight into the roles of tyrosine 82 and glycine 253 in the Escherichia coli adenine glycosylase MutY Biochemistry. 44: 14179-14190. PMID 16245934 DOI: 10.1021/Bi050976U |
0.485 |
|
2005 |
Boal AK, Yavin E, Lukianova OA, O'Shea VL, David SS, Barton JK. DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters. Biochemistry. 44: 8397-407. PMID 15938629 DOI: 10.1021/Bi047494N |
0.585 |
|
2005 |
Lukianova OA, David SS. A role for iron-sulfur clusters in DNA repair. Current Opinion in Chemical Biology. 9: 145-51. PMID 15811798 DOI: 10.1016/J.Cbpa.2005.02.006 |
0.571 |
|
2005 |
David SS. Structural biology: DNA search and rescue. Nature. 434: 569-70. PMID 15800603 DOI: 10.1038/434569A |
0.566 |
|
2005 |
Yavin E, Boal AK, Stemp ED, Boon EM, Livingston AL, O'Shea VL, David SS, Barton JK. Protein-DNA charge transport: redox activation of a DNA repair protein by guanine radical. Proceedings of the National Academy of Sciences of the United States of America. 102: 3546-51. PMID 15738421 DOI: 10.1073/Pnas.0409410102 |
0.547 |
|
2005 |
Pope MA, Chmiel NH, David SS. Insight into the functional consequences of hMYH variants associated with colorectal cancer: Distinct differences in the adenine glycosylase activity and the response to AP endonucleases of Y150C and G365D murine MYH Dna Repair. 4: 315-325. PMID 15661655 DOI: 10.1016/J.Dnarep.2004.10.003 |
0.515 |
|
2005 |
Pope MA, David SS. DNA damage recognition and repair by the murine MutY homologue Dna Repair. 4: 91-102. PMID 15533841 DOI: 10.1016/J.Dnarep.2004.08.004 |
0.478 |
|
2004 |
Chepanoske CL, Lukianova OA, Lombard M, Golinelli-Cohen MP, David SS. A residue in MutY important for catalysis identified by photocross-linking and mass spectrometry. Biochemistry. 43: 651-62. PMID 14730969 DOI: 10.1021/Bi035537E |
0.589 |
|
2003 |
Francis AW, Helquist SA, Kool ET, David SS. Probing the requirements for recognition and catalysis in Fpg and MutY with nonpolar adenine isosteres. Journal of the American Chemical Society. 125: 16235-42. PMID 14692765 DOI: 10.1021/Ja0374426 |
0.449 |
|
2003 |
Boon EM, Livingston AL, Chmiel NH, David SS, Barton JK. DNA-mediated charge transport for DNA repair. Proceedings of the National Academy of Sciences of the United States of America. 100: 12543-7. PMID 14559969 DOI: 10.1073/Pnas.2035257100 |
0.573 |
|
2003 |
Leipold MD, Workman H, Muller JG, Burrows CJ, David SS. Recognition and removal of oxidized guanines in duplex DNA by the base excision repair enzymes hOGG1, yOGG1, and yOGG2 Biochemistry. 42: 11373-11381. PMID 14503888 DOI: 10.1021/Bi034951B |
0.499 |
|
2003 |
Wiederholt CJ, Delaney MO, Pope MA, David SS, Greenberg MM. Repair of DNA containing Fapy·dG and its β-C-nucleoside analogue by formamidopyrimidine DNA glycosylase and MutY Biochemistry. 42: 9755-9760. PMID 12911318 DOI: 10.1021/Bi034844H |
0.559 |
|
2003 |
Chmiel NH, Livingston AL, David SS. Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E.coli enzymes. Journal of Molecular Biology. 327: 431-43. PMID 12628248 DOI: 10.1016/S0022-2836(03)00124-4 |
0.416 |
|
2003 |
Francis AW, David SS. Escherichia coli MutY and Fpg utilize a processive mechanism for target location. Biochemistry. 42: 801-10. PMID 12534293 DOI: 10.1021/Bi026375+ |
0.529 |
|
2002 |
Burrows CJ, Muller JG, Kornyushyna O, Luo W, Duarte V, Leipold MD, David SS. Structure and potential mutagenicity of new hydantoin products from guanosine and 8-oxo-7,8-dihydroguanine oxidation by transition metals. Environmental Health Perspectives. 110: 713-7. PMID 12426118 DOI: 10.1289/Ehp.02110S5713 |
0.526 |
|
2002 |
Boon EM, Pope MA, Williams SD, David SS, Barton JK. DNA-mediated charge transport as a probe of MutY/DNA interaction. Biochemistry. 41: 8464-70. PMID 12081496 DOI: 10.1021/Bi012068C |
0.548 |
|
2002 |
Pope MA, Porello SL, David SS. Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates Journal of Biological Chemistry. 277: 22605-22615. PMID 11960995 DOI: 10.1074/Jbc.M203037200 |
0.563 |
|
2002 |
Messick TE, Chmiel NH, Golinelli MP, Langer MR, Joshua-Tor L, David SS. Noncysteinyl coordination to the [4Fe-4S]2+ cluster of the DNA repair adenine glycosylase MutY introduced via site-directed mutagenesis. Structural characterization of an unusual histidinyl-coordinated cluster. Biochemistry. 41: 3931-42. PMID 11900536 DOI: 10.1021/Bi012035X |
0.447 |
|
2002 |
Al-Tassan N, Chmiel NH, Maynard J, Fleming N, Livingston AL, Williams GT, Hodges AK, Davies DR, David SS, Sampson JR, Cheadle JP. Inherited variants of MYH associated with somatic G:C-->T:A mutations in colorectal tumors. Nature Genetics. 30: 227-32. PMID 11818965 DOI: 10.1038/Ng828 |
0.395 |
|
2001 |
Chmiel NH, Golinelli MP, Francis AW, David SS. Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain. Nucleic Acids Research. 29: 553-64. PMID 11139626 DOI: 10.1093/Nar/29.2.553 |
0.585 |
|
2000 |
Leipold MD, Muller JG, Burrows CJ, David SS. Removal of hydantoin products of 8-oxoguanine oxidation by the Escherichia coli DNA repair enzyme, FPG. Biochemistry. 39: 14984-92. PMID 11101315 DOI: 10.1021/Bi0017982 |
0.537 |
|
2000 |
Williams SD, David SS. A single engineered point mutation in the adenine glycosylase MutY confers bifunctional glycosylase/AP lyase activity Biochemistry. 39: 10098-10109. PMID 10955998 DOI: 10.1021/Bi0004652 |
0.597 |
|
2000 |
Chepanoske CL, Golinelli MP, Williams SD, David SS. Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal Archives of Biochemistry and Biophysics. 380: 11-19. PMID 10900127 DOI: 10.1006/Abbi.2000.1890 |
0.525 |
|
2000 |
Chepanoske CL, Langelier CR, Chmiel NH, David SS. Recognition of the nonpolar base 4-methylindole in DNA by the DNA repair adenine glycosylase MutY Organic Letters. 2: 1341-1344. PMID 10810743 DOI: 10.1021/Ol005831O |
0.547 |
|
1999 |
Williams SD, David SS. Formation of a schiff base intermediate is not required for the adenine glycosylase activity of Escherichia coli MutY Biochemistry. 38: 15417-15424. PMID 10569924 DOI: 10.1021/Bi992013Z |
0.584 |
|
1999 |
Chepanoske CL, Porello SL, Fujiwara T, Sugiyama H, David SS. Substrate recognition by Escherichia coli MutY using substrate analogs Nucleic Acids Research. 27: 3197-3204. PMID 10454618 DOI: 10.1093/Nar/27.15.3197 |
0.554 |
|
1999 |
Golinelli MP, Chmiel NH, David SS. Site-directed mutagenesis of the cysteine ligands to the [4Fe-4S] cluster of Escherichia coli MutY Biochemistry. 38: 6997-7007. PMID 10353811 DOI: 10.1021/Bi982300N |
0.555 |
|
1999 |
Hickerson RP, Chepanoske CL, Williams SD, David SS, Burrows CJ. Mechanism-based DNA-protein cross-linking of MutY via oxidation of 8- oxoguanosine [16] Journal of the American Chemical Society. 121: 9901-9902. DOI: 10.1021/Ja9923484 |
0.466 |
|
1998 |
David SS, Williams SD. Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair. Chemical Reviews. 98: 1221-1262. PMID 11848931 DOI: 10.1021/Cr980321H |
0.527 |
|
1998 |
Williams SD, David SS. Evidence that MutY is a monofunctional glycosylase capable of forming a covalent Schiff base intermediate with substrate DNA Nucleic Acids Research. 26: 5123-5133. PMID 9801309 DOI: 10.1093/Nar/26.22.5123 |
0.592 |
|
1998 |
Porello SL, Leyes AE, David SS. Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates Biochemistry. 37: 14756-14764. PMID 9778350 DOI: 10.1021/Bi981594+ |
0.593 |
|
1998 |
Porello SL, Cannon MJ, David SS. A substrate recognition role for the [4Fe-4S]2+ cluster of the DNA repair glycosylase MutY Biochemistry. 37: 6465-6475. PMID 9572864 DOI: 10.1021/Bi972433T |
0.497 |
|
1998 |
David SS, Williams SD. Chemistry of glycosylases and endonucleases involved in base-excision repair Chemical Reviews. 98: 1221-1261. |
0.434 |
|
1996 |
Eason RG, Burkhardt DM, Phillips SJ, Smith DP, David SS. Synthesis and characterization of 8-methoxy-2'- deoxyadenosine-containing oligonucleotides to probe the syn glycosidic conformation of 2'-deoxyadenosine within DNA. Nucleic Acids Research. 24: 890-7. PMID 8600457 DOI: 10.1093/Nar/24.5.890 |
0.456 |
|
1996 |
Porello SL, Williams SD, Kuhn H, Michaels ML, David SS. Specific recognition of substrate analogs by the DNA mismatch repair enzyme MutY Journal of the American Chemical Society. 118: 10684-10692. DOI: 10.1021/Ja9602206 |
0.497 |
|
1995 |
Kuhn H, Smith DP, David SS. Efficient synthesis of 2′-deoxyformycin A containing oligonucleotides and characterization of their stability in duplex DNA The Journal of Organic Chemistry. 60: 7094-7095. DOI: 10.1021/Jo00127A010 |
0.496 |
|
1994 |
Tan JD, Farinas ET, David SS, Mascharak PK. NMR evidence of sequence specific DNA binding by a cobalt(III)-bleomycin analogue with tethered acridine Inorganic Chemistry. 33: 4295-4308. DOI: 10.1021/Ic00097A017 |
0.457 |
|
1993 |
David SS, Barton JK. NMR evidence for specific intercalation of .DELTA.-rh(phen)2.phi.3+ in [d(GTCGAC)2] Journal of the American Chemical Society. 115: 2984-2985. DOI: 10.1021/Ja00060A060 |
0.466 |
|
1993 |
Meads B, David S. Mismatch repair by the [4Fe-4S] cluster containing DNA repair enzyme, muty Journal of Inorganic Biochemistry. 51: 552. DOI: 10.1016/0162-0134(93)85578-V |
0.429 |
|
1990 |
David SS, Que L. Anion binding to uteroferrin. Evidence for phosphate coordination to the iron(III) ion of the dinuclear active site and interaction with the hydroxo bridge Journal of the American Chemical Society. 112. DOI: 10.1021/Ja00174A001 |
0.327 |
|
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