David D. Shock
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View article: Requirement for transient metal ions revealed through computational analysis for DNA polymerase going in reverse
Requirement for transient metal ions revealed through computational analysis for DNA polymerase going in reverse Open
DNA polymerases use a general two-metal ion mechanism for DNA synthesis. Recent time-lapse crystallographic studies identified additional adjunct metal ions in the polymerase active site. One of these ions correlates with appearance of pyr…
View article: Amino Acid Substitution in the Active Site of DNA Polymerase β Explains the Energy Barrier of the Nucleotidyl Transfer Reaction
Amino Acid Substitution in the Active Site of DNA Polymerase β Explains the Energy Barrier of the Nucleotidyl Transfer Reaction Open
DNA polymerase β (pol β) is a bifunctional enzyme widely studied for its roles in base excision DNA repair where one key function is gap-filling DNA synthesis. In spite of significant progress in recent years, the atomic level mechanism of…
View article: Ras activation in platelets after stimulation of the thrombin receptor, thromboxane A2 receptor or protein kinase C
Ras activation in platelets after stimulation of the thrombin receptor, thromboxane A2 receptor or protein kinase C Open
Several reports have indicated that the small G-protein Ras is not present immunologically in platelets. However, here we report the identification of Ras in platelets by immunoprecipitation with the Ras-specific monoclonal antibodies Y13-…
View article: Preferential DNA Polymerase β Reverse Reaction with Imidodiphosphate
Preferential DNA Polymerase β Reverse Reaction with Imidodiphosphate Open
DNA replication and repair reactions involve the addition of a deoxynucleoside monophosphate onto a growing DNA strand with the loss of pyrophosphate. This chemical reaction is also reversible; the addition of pyrophosphate generates a deo…
View article: DNA polymerase β nucleotide-stabilized template misalignment fidelity depends on local sequence context
DNA polymerase β nucleotide-stabilized template misalignment fidelity depends on local sequence context Open
DNA polymerase β has two DNA-binding domains that interact with the opposite sides of short DNA gaps. These domains contribute two activities that modify the 5' and 3' margins of gapped DNA during base excision repair. DNA gaps greater tha…
View article: A guardian residue hinders insertion of a Fapy•dGTP analog by modulating the open-closed DNA polymerase transition
A guardian residue hinders insertion of a Fapy•dGTP analog by modulating the open-closed DNA polymerase transition Open
4,6-Diamino-5-formamidopyrimidine (Fapy•dG) is an abundant form of oxidative DNA damage that is mutagenic and contributes to the pathogenesis of human disease. When Fapy•dG is in its nucleotide triphosphate form, Fapy•dGTP, it is inefficie…
View article: Time-lapse crystallography snapshots of a double-strand break repair polymerase in action
Time-lapse crystallography snapshots of a double-strand break repair polymerase in action Open
DNA polymerase (pol) μ is a DNA-dependent polymerase that incorporates nucleotides during gap-filling synthesis in the non-homologous end-joining pathway of double-strand break repair. Here we report time-lapse X-ray crystallography snapsh…