G
Graham C. Walker
Researcher at Massachusetts Institute of Technology
Publications - 386
Citations - 39252
Graham C. Walker is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Sinorhizobium meliloti & DNA polymerase. The author has an hindex of 93, co-authored 381 publications receiving 36875 citations. Previous affiliations of Graham C. Walker include Norwich Research Park & University of California, Santa Cruz.
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Journal ArticleDOI
Interrelations between glycine betaine catabolism and methionine biosynthesis in Sinorhizobium meliloti strain 102F34
Lise Barra,Catherine Fontenelle,Gwennola Ermel,Annie Trautwetter,Graham C. Walker,Carlos Blanco +5 more
TL;DR: Methionine inhibited the growth of an S. meliloti bmt mutant in low- and high-osmotic strength media, an effect that correlates with a decrease in the catabolism of glycine betaine, suggesting the existence of another catabolic pathway.
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Mutagenesis, by Methylating and Ethylating Agents, in mutH, mutL, mutS, and uvrD Mutants of Salmonella Typhimurium LT2
TL;DR: Various models are discussed in an effort to explain why strains thought to be deficient in methyl-instructed mismatch repair are sensitive to mutagenesis by methylating and ethylating agents.
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A monocysteine approach for probing the structure and interactions of the UmuD protein.
TL;DR: An approach based on the construction of a series of monocysteine derivatives of UmuD and the chemistry of the unique thiol group in each derivative suggests that Ala-89, Gln-100, and Asp-126 are probably not particularly solvent accessible and may play important roles in protein architecture.
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Comparative analysis of in vivo interactions between Rev1 protein and other Y-family DNA polymerases in animals and yeasts.
J. Nicole Kosarek,Rachel V. Woodruff,Amanda Rivera-Begeman,Caixia Guo,Sanjay D'Souza,Eugene V. Koonin,Graham C. Walker,Errol C. Friedberg +7 more
TL;DR: The results of this study suggest that special consideration should be exercised when making mechanistic extrapolations regarding translesion DNA synthesis from one eukaryotic system to another.
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Two processivity clamp interactions differentially alter the dual activities of UmuC
TL;DR: By designing compensatory mutations in the cleft between domains II and III in β, this work restored UV‐induced mutagenesis by a UmuC β‐binding motif variant and indicates subtle and sophisticated polymerase management by the β clamp.