| scholarly article | Q13442814 |
| P2093 | author name string | Sheila S David | |
| Chandrima Majumdar | |||
| Nicole N Nuñez | |||
| Kori T Lay | |||
| P2860 | cites work | Functional characterization of two human MutY homolog (hMYH) missense mutations (R227W and V232F) that lie within the putative hMSH6 binding domain and are associated with hMYH polyposis | Q24801922 |
| Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA | Q27621681 | ||
| Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase | Q27643123 | ||
| Crystal Structure of the FeS Cluster–Containing Nucleotide Excision Repair Helicase XPD | Q27650943 | ||
| Atomic substitution reveals the structural basis for substrate adenine recognition and removal by adenine DNA glycosylase | Q27657850 | ||
| A Structural Hinge in Eukaryotic MutY Homologues Mediates Catalytic Activity and Rad9–Rad1–Hus1 Checkpoint Complex Interactions | Q27664268 | ||
| MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily | Q27766319 | ||
| Base-excision repair of oxidative DNA damage | Q29615373 | ||
| The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine) | Q29619959 | ||
| Structure and stereochemistry of the base excision repair glycosylase MutY reveal a mechanism similar to retaining glycosidases | Q31032369 | ||
| Transition-state analysis of the DNA repair enzyme MutY. | Q31151684 | ||
| Electrochemistry of the [4Fe4S] Cluster in Base Excision Repair Proteins: Tuning the Redox Potential with DNA. | Q33652775 | ||
| Escherichia coli mutY gene product is required for specific A-G----C.G mismatch correction | Q33680797 | ||
| Ser 524 is a phosphorylation site in MUTYH and Ser 524 mutations alter 8-oxoguanine (OG): A mismatch recognition | Q34172846 | ||
| Efficient recognition of substrates and substrate analogs by the adenine glycosylase MutY requires the C-terminal domain | Q34249739 | ||
| Escherichia coli mutY gene encodes an adenine glycosylase active on G-A mispairs | Q34319463 | ||
| Gas-phase studies of substrates for the DNA mismatch repair enzyme MutY. | Q34377569 | ||
| Profiling base excision repair glycosylases with synthesized transition state analogs | Q35165256 | ||
| Structural Basis for Avoidance of Promutagenic DNA Repair by MutY Adenine DNA Glycosylase | Q35837084 | ||
| MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. | Q35848055 | ||
| A role for iron-sulfur clusters in DNA repair | Q36089869 | ||
| Cancer-associated variants and a common polymorphism of MUTYH exhibit reduced repair of oxidative DNA damage using a GFP-based assay in mammalian cells | Q36353057 | ||
| DNA-mediated charge transport for DNA repair | Q36689389 | ||
| DNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport? | Q36864161 | ||
| Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA | Q37132610 | ||
| Redox signaling between DNA repair proteins for efficient lesion detection | Q37340789 | ||
| Distinct functional consequences of MUTYH variants associated with colorectal cancer: Damaged DNA affinity, glycosylase activity and interaction with PCNA and Hus1. | Q37397651 | ||
| Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associated with colorectal cancer | Q37464076 | ||
| The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport | Q37682254 | ||
| Building Fe-S proteins: bacterial strategies. | Q37751865 | ||
| Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates | Q38332366 | ||
| Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme | Q38355637 | ||
| 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 | Q38356866 | ||
| Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY. | Q38675374 | ||
| Repair of 8-oxoG:A mismatches by the MUTYH glycosylase: Mechanism, metals and medicine | Q39087831 | ||
| Dispensability of the [4Fe-4S] cluster in novel homologues of adenine glycosylase MutY. | Q40267970 | ||
| A zinc linchpin motif in the MUTYH glycosylase interdomain connector is required for efficient repair of DNA damage | Q40878567 | ||
| Finding new mutator strains of Escherichia coli--a review | Q41256968 | ||
| Structure-Activity Relationships Reveal Key Features of 8-Oxoguanine: A Mismatch Detection by the MutY Glycosylase | Q41703841 | ||
| A repair system for 8-oxo-7,8-dihydrodeoxyguanine | Q43687308 | ||
| Inherited variants of MYH associated with somatic G:C-->T:A mutations in colorectal tumors | Q43871566 | ||
| Escherichia coli apurinic-apyrimidinic endonucleases enhance the turnover of the adenine glycosylase MutY with G:A substrates | Q43964510 | ||
| 16 Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA | Q44249816 | ||
| A residue in MutY important for catalysis identified by photocross-linking and mass spectrometry | Q44733805 | ||
| DNA-bound redox activity of DNA repair glycosylases containing [4Fe-4S] clusters | Q46118094 | ||
| Electrical Probes of DNA-Binding Proteins. | Q46337648 | ||
| Insight into the roles of tyrosine 82 and glycine 253 in the Escherichia coli adenine glycosylase MutY. | Q46771307 | ||
| Techniques for the production, isolation, and analysis of iron-sulfur proteins | Q50459293 | ||
| Structural Basis for the Lesion-scanning Mechanism of the MutY DNA Glycosylase. | Q50927527 | ||
| Genetic analysis of the isc operon in Escherichia coli involved in the biogenesis of cellular iron-sulfur proteins. | Q53889877 | ||
| Gel retardation. | Q54703956 | ||
| Nature of Forces between Large Molecules of Biological Interest* | Q59063408 | ||
| Positively charged residues within the iron-sulfur cluster loop of E. coli MutY participate in damage recognition and removal | Q74016433 | ||
| A substrate recognition role for the [4Fe-4S]2+ cluster of the DNA repair glycosylase MutY | Q74511045 | ||
| Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair | Q77646696 | ||
| Site-directed mutagenesis of the cysteine ligands to the [4Fe-4S] cluster of Escherichia coli MutY | Q77828155 | ||
| P304 | page(s) | 21-68 | |
| P577 | publication date | 2018-01-10 | |
| P1433 | published in | Methods in Enzymology | Q2076903 |
| P1476 | title | Fe-S Clusters and MutY Base Excision Repair Glycosylases: Purification, Kinetics, and DNA Affinity Measurements | |
| P478 | volume | 599 |
Search more.