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The E295K Cancer Variant of Human Polymerase Favors the

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the e295k cancer variant of human polymerase favors the

The E295K Cancer Variant of Human Polymerase Favors the Nov 29,2013 The weak polymerase activity of the E295K variant allowed for the soaking of DNA-bound crystals with natural rather than nonhydrolyzable nucleotides.Addition of dTTP (2.4 The E295K Cancer Variant of Human Polymerase Favors the#197;,R free = 22.8%) as cognate to the template dA position resulted in low occupancy binding of the nucleotide ( Fig.3 A ),as shown in theUnfavorable Electrostatic and Steric Interactions in DNA E295K appears to lack DNA polymerase activity as a result of its inability to assume an active polymerase conformation [28,29].During BER,neither of these variants fills single nucleotide gaps Title Faculty Scientist at The RobertLocation Burlington,VermontConnections 86Substrate-induced DNA Polymerase ActivationNov 07,2014 The E295K Cancer Variant of Human Polymerase Favors the#0183;Eckenroth B.E.,Towle-Weicksel J.B.,Sweasy J.B.,Doubli The E295K Cancer Variant of Human Polymerase Favors the#233; S.(2013) The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J.Biol.Chem.288,3485034860 [PMC free article]

Title Associate Professor at RhodeLocation Providence,Rhode IslandConnections 256Substrate-induced DNA Polymerase Activation - Europe

Eckenroth B.E.,Towle-Weicksel J.B.,Sweasy J.B.,Doubli The E295K Cancer Variant of Human Polymerase Favors the#233; S.(2013) The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J.Biol.Chem.288,3485034860 [PMC free article]The Leu22Pro tumor-associated variant of DNA polymerase Approximately 30% of human tumors characterized to date express DNA polymerase beta (pol ) variant proteins.Two of the polymerase beta cancer-associated variants are sequence-specific mutators,and one of them binds to DNA but has no polymerase activity.The Leu22Pro (L22P) DNA polymerase beta variant was identified in a gastric carcinoma.The E295K cancer variant of human polymerase favors the We showed that expression of the carcinoma variant E295K induces cellular transformation.The poor polymerase activity exhibited by the variant was hypothesized to be caused by the destabilization of proper active site assembly by the glutamate to lysine mutation.

The E295K DNA Polymerase Beta Gastric Cancer-Associated

The E295K DNA Polymerase Beta Gastric Cancer-Associated Variant Interferes with Base Excision Repair and Induces Cellular Transformation By Tieming Lang,Shibani Dalal,Anna Chikova,Daniel DiMaio and Joann B.Sweasy.Abstract.Approximately 30% of human tumors examined for mutations in polymerase beta (pol ) appear to express pol The E295K Cancer Variant of Human Polymerase Favors the The E295K variant of pol has been identified in gastric (33) and colon carcinomas (42) and shown to have low activity (Table 2) (43,44).Although the overall conformation is similar to that Substrate-induced DNA Polymerase Activation* - Journal The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J.Biol.Chem.2013; 288 34850-34860 View in Article

Some results are removed in response to a notice of local law requirement.For more information,please see here.Previous123456NextRCSB PDB - 4M9G DNA Polymerase Beta E295K Binary

We showed that expression of the carcinoma variant E295K induces cellular transformation.The poor polymerase activity exhibited by the variant was hypothesized to be caused by the destabilization of proper active site assembly by the glutamate to lysine mutation.Pre-Steady-State Kinetic Studies of the Fidelity and Apr 30,2004 The E295K Cancer Variant of Human Polymerase Favors the#0183;The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection.Journal of Biological Chemistry 2013 ,288 (48) ,

Polbase - Polbase Reference Browser

The E295K cancer variant of human polymerase beta favors the mismatch conformational pathway during nucleotide selection.Brian E Eckenroth,Jamie B Towle-Weicksel,Joann B Sweasy,Sylvie Doubli Eacute The Journal of biological chemistry 2013 topics setNew structural snapshots provide molecular insights into Aug 01,2015 The E295K Cancer Variant of Human Polymerase Favors the#0183;The closed/open equilibrium is also altered by another mutation,the E295K variant. J.B.Sweasy,S.Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J.Biol.Chem.,288 (2013),pp.34850-34860.New structural snapshots provide molecular insights into Apr 30,2015 The E295K Cancer Variant of Human Polymerase Favors the#0183;The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J Biol Chem.2013; 288 :3485034860.[ Europe PMC free article ] [ Abstract ] [ Google Scholar ]

L452R mutation potentially favors adaptive evolution of

Feb 23,2021 The E295K Cancer Variant of Human Polymerase Favors the#0183;Please use one of the following formats to cite this article in your essay,paper or report APA.Dutta,Sanchari Sinha.(2021,February 23).L452R mutation potentially favors adaptive evolution Joann Sweasy UA ProfilesThe E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.The Journal of biological chemistry ,288(48),34850-60.More infoJamie Towle-Weicksel - Associate Professor - Rhode Island The E295K cancer variant of human polymerase beta favors the mismatch conformational pathway during nucleotide selection.Journal of Biological Chemistry October 18,2013 Other authors

Jamie TOWLE-WEICKSEL Assistant Professor Rhode Island

DNA polymerase beta (Pol ) functions in Base Excision Repair (BER) to fill in single-nucleotide gaps,and variants of Pol have been associated with cancer.Specifically,the E288K Pol Jamie B.Towle-Weicksel - PublicationsThe E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.The Journal of Biological Chemistry.288 34850-60.PMID 24133209 DOI 10.1074/jbc.M113.510891 0.44 Show low-probability matches.Jamie B.Towle-Weicksel - PublicationsThe E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.The Journal of Biological Chemistry.288 34850-60.PMID 24133209 DOI 10.1074/jbc.M113.510891 0.44 Show low-probability matches.

DNA Polymerase Beta Cancer-Associated Variant I260M

Eckenroth BE,Towle-Weicksel JB,Sweasy JB,Doublie S.The E295K cancer variant of human polymerase beta favors the mismatch conformational pathway during nucleotide selection.J Biol Chem.2013; 288:3485034860.[PMC free article]DNA Polymerase StructureFidelity Relationship from Pre The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection.Journal of Biological Chemistry 2013 ,288 (48) ,34850-34860.Cysteine Racemization on IgG Heavy and Light Chains Background Cysteine racemization occurs at heavy chain position 220 of an IgG1under high pH stress.Results d-Cysteine forms on both heavy and light chains of an IgGs under mild conditions.Conclusion The terminal cysteine impairs racemization on the light chain.Significance Because d-cysteine is naturally occurring on antibodies,its presence on therapeutic antibodies poses

Crystal structures of the Klenow fragment of DNA

The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection.Journal of Biological Chemistry 2013 ,288 (48) ,34850-34860.Crystal structure of DNA polymerase with DNA containing The E295K Cancer Variant of Human Polymerase Favors the#0183;The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J Biol Chem.2013; 288 :3485034860.[ Europe PMC free article ] [ Abstract ] [ Google Scholar ]Cited by 14Publish Year 2012Author Yunlang Li,Chelsea L.Gridley,Joachim Jaeger,Joachim Jaeger,Joann B.Sweasy,Tamar SchlickUnfavorable Electrostatic and Steric Interactions in DNA The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection.Journal of Biological Chemistry 2013,288 (48) ,34850-34860.DOI 10.1074/jbc.M113.510891.Tamar Schlick,Karunesh Arora,William A.Beard,Samuel H.Wilson.

Cited by 14Publish Year 2012Author Yunlang Li,Chelsea L.Gridley,Joachim Jaeger,Joachim Jaeger,Joann B.Sweasy,Tamar SchlickCrystal Structure of DNA Polymerase with DNA Containing

The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection Eckenroth,Brian E.; Towle-Weicksel,Jamie B.; Sweasy,Joann B.; Doublie,Sylvie Journal of Biological Chemistry ( 2013 ),288 ( 48 ),34850-34860 CODEN JBCHA3 ;Cited by 13Publish Year 2013Author Brian E.Eckenroth,Jamie B.Towle-Weicksel,Joann B.Sweasy,Sylvie Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;TheE295KCancerVariantofHumanPolymerase Favorsthe The E295K variant of pol was first identified in a gastric carcinoma and subsequently found by us in a colon carcinoma (21,22).Expression of the E295K variant in mouse mammary epithelialcellsinducessisterchromatidexchangesandcellular transformation (23).The mutation lies within the fingers domainoftheenzymeproximaltothetemplatestrandneartheCited by 13Publish Year 2013Author Brian E.Eckenroth,Jamie B.Towle-Weicksel,Joann B.Sweasy,Sylvie Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;The E295K DNA polymerase beta gastric cancer-associated In the work described here,we show that the E295K gastric carcinoma pol beta variant acts in a dominant-negative manner by interfering with base excision repair.This leads to an increase in sister chromatid exchanges.Expression of the E295K variant also induces cellular transformation.

Cited by 13Publish Year 2013Author Brian E.Eckenroth,Jamie B.Towle-Weicksel,Joann B.Sweasy,Sylvie Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;The E295K Cancer Variant of Human Polymerase Favors the

Nov 29,2013 The E295K Cancer Variant of Human Polymerase Favors the#0183;The E295K variant was generated using the polymerase chain reaction (PCR) from the WT plasmid followed by site-directed mutagenesis using the QuikChange kit (Stratagene).Both WT and E295K plasmids were transformed into Escherichia coli Rosetta 2 DE3 (Novagen) and grown in Luria brothCited by 13Publish Year 2013Author Brian E.Eckenroth,Jamie B.Towle-Weicksel,Joann B.Sweasy,Sylvie Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;The E295K Cancer Variant of Human Polymerase Favors the Nov 29,2013 The E295K Cancer Variant of Human Polymerase Favors the#0183;DNA polymerase (pol ) is responsible for gap filling synthesis during repair of damaged DNA as part of the base excision repair pathway.Human polCited by 13Publish Year 2013Author Brian E.Eckenroth,Jamie B.Towle-Weicksel,Joann B.Sweasy,Sylvie Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;The E295K Cancer Variant of Human Polymerase Favors the Background Human DNA polymerase is mutated in a high percentage of cancers with specific variants impacting enzymatic activity and/or fidelity.Results In the E295K carcinoma variant,dCTP competes with cognate dTTP with dA as templating base.Conclusion Structures verify that the E295K variant favors the mismatch over cognate dNTP.Significance Relevant mutations may have the

Cited by 13Publish Year 2013Author Brian E.Eckenroth,Jamie B.Towle-Weicksel,Joann B.Sweasy,Sylvie Doubli The E295K Cancer Variant of Human Polymerase Favors the#233;RCSB PDB - 4M9J DNA Polymerase Beta E295K Soaked with

We showed that expression of the carcinoma variant E295K induces cellular transformation.The poor polymerase activity exhibited by the variant was hypothesized to be caused by the destabilization of proper active site assembly by the glutamate to lysine mutation.Cited by 123Publish Year 2007Author Tieming Lang,Shibani Dalal,Anna Chikova,Daniel DiMaio,Joann B.SweasyUnfavorable Electrostatic and Steric Interactions in DNA The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection.Journal of Biological Chemistry 2013,288 (48) ,34850-34860.https://doi/10.1074/jbc.M113.510891; Tamar Schlick,Karunesh Arora,Cited by 123Publish Year 2007Author Tieming Lang,Shibani Dalal,Anna Chikova,Daniel DiMaio,Joann B.SweasyThe E295K DNA Polymerase Beta Gastric Cancer-Associated In the work described here,we show that the E295K gastric carcinoma pol variant acts in a dominant-negative manner by interfering with base excision repair.This leads to an increase in sister chromatid exchanges.Expression of the E295K variant also induces cellular transformation.

Cancer-Associated DNA Polymerase Beta Variants

E295K result in cellular transformation. Polymerase Beta Variants During Base Excision Repair ROS,ALKYLATING AGENTS C C G C.Mutator Phenotype Hypothesis Loeb LA et al.(1974) Cancer Res.34:2311-2321 of human cancer.Daniel DiMaio CA16038.Title Microsoft PowerPoint - sweasynih.pptBrian E.Eckenroth - Faculty Scientist - The Robert Larner The E295K cancer variant of human polymerase beta favors the mismatch conformational pathway during nucleotide selection.Journal of Biological Chemistry December 1,2013 Eckenroth BE,Towle A cancer-associated DNA polymerase variant modeled in Jan 05,2010 The E295K Cancer Variant of Human Polymerase Favors the#0183;Results Effects of SNPs and the Cancer-Associated yR511H/hR506H Mutation of Pol on Viability,Mutagenesis,and DNA Damage Sensitivity.The structural and functional conservation of the DNA replication machinery provides an opportunity to evaluate the consequences of human DNA polymerase variants by studying analogous mutations in yeast.

A cancer-associated DNA polymerase variant genomic

14.Lang T,Dalal S,Chikova A,DiMaio D,Sweasy JB (2007) The E295K DNA polymerase gastric cancer-associated variant interferes with base excision repair and induces cellular transformation.Mol Cell Biol 27:55875596.15.Ou J,et al.(2007) Functional analysis helps toA Structural Solution for the DNA Polymerase -Dependent The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection. We showed that expression of the carcinoma variant E295K12345NextFluorescence Resonance Energy Transfer Studies of DNA The E295K cancer variant of human polymerase favors the mismatch conformational pathway during nucleotide selection.J.Biol.Chem.2013; 288 34850-34860 View in Article

(PDF) A Reexamination of the Nucleotide Incorporation

The E295K Cancer Variant of Human Polymerase Favors the Mismatch Conformational Pathway during Nucleotide Selection.By J.Towle-weicksel.The effect of oxidatively damaged DNA on the active site pre-organization during nucleotide incorporation in a high fidelity polymerase from Bacillus stearothermophilus.(PDF) A Change in the Rate-Determining Step of The E295K cancer variant of human .polymerase beta favors the mismatch conformational pathway during nucleotide selection.J Biol .Chem.2013; 288:3485034860.[PubMed 24133209]

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