DNA polymerase beta fidelity: halomethylene-modified leaving groups in pre-steady-state kinetic analysis reveal differences at the chemical transition state

scientific article published on 28 December 2007

DNA polymerase beta fidelity: halomethylene-modified leaving groups in pre-steady-state kinetic analysis reveal differences at the chemical transition state is …
instance of (P31):
scholarly articleQ13442814

External links are
P356DOI10.1021/BI7014162
P698PubMed publication ID18161950

P50authorKeriann OertellQ126898589
Arieh WarshelQ4790366
P2093author name stringBoris A Kashemirov
Charles E McKenna
Myron F Goodman
Samuel H Wilson
Thomas G Upton
William A Beard
Jan Florián
Christopher A Sucato
Jorge Osuna
P2860cites workStructure and mechanism of DNA polymerase Beta.Q36389634
DNA polymerase beta catalytic efficiency mirrors the Asn279-dCTP H-bonding strengthQ38304989
Polymerase beta simulations suggest that Arg258 rotation is a slow step rather than large subdomain motions per se.Q42674308
Application of Brønsted-type LFER in the study of the phospholipase C mechanismQ44358281
On the mechanism of hydrolysis of phosphate monoesters dianions in solutions and proteinsQ44955947
Progress report on integrating skill mix: the radiographer's perspective.Q45903752
Influence of DNA structure on DNA polymerase beta active site function: extension of mutagenic DNA intermediates.Q53639781
Structural insights into DNA polymerase beta fidelity: hold tight if you want it rightQ74232718
P433issue3
P407language of work or nameEnglishQ1860
P1104number of pages10
P304page(s)870-879
P577publication date2007-12-28
P1433published inBiochemistryQ764876
P1476titleDNA polymerase beta fidelity: halomethylene-modified leaving groups in pre-steady-state kinetic analysis reveal differences at the chemical transition state
P478volume47