<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>48(5)</volume><submitter>Fillet AM</submitter><pubmed_abstract>We described the natural polymorphism of cytomegalovirus DNA polymerase in 42 unrelated isolates susceptible to ganciclovir, foscarnet, and cidofovir. All variations, including an eight-amino-acid deletion, were located between domains delta-C and II and between domains III and I, suggesting that these specific residues are not involved in enzymatic functions.</pubmed_abstract><journal>Antimicrobial agents and chemotherapy</journal><pagination>1865-8</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC400574</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Natural polymorphism of cytomegalovirus DNA polymerase lies in two nonconserved regions located between domains delta-C and II and between domains III and I.</pubmed_title><pmcid>PMC400574</pmcid><pubmed_authors>Gouarin S</pubmed_authors><pubmed_authors>Gourlain K</pubmed_authors><pubmed_authors>Mazeron MC</pubmed_authors><pubmed_authors>Alain S</pubmed_authors><pubmed_authors>Champier G</pubmed_authors><pubmed_authors>Najioullah F</pubmed_authors><pubmed_authors>Carquin J</pubmed_authors><pubmed_authors>Auray L</pubmed_authors><pubmed_authors>Houhou N</pubmed_authors><pubmed_authors>Garrigue I</pubmed_authors><pubmed_authors>Ducancelle A</pubmed_authors><pubmed_authors>Fillet AM</pubmed_authors><pubmed_authors>Imbert BM</pubmed_authors><pubmed_authors>Thouvenot D</pubmed_authors></additional><is_claimable>false</is_claimable><name>Natural polymorphism of cytomegalovirus DNA polymerase lies in two nonconserved regions located between domains delta-C and II and between domains III and I.</name><description>We described the natural polymorphism of cytomegalovirus DNA polymerase in 42 unrelated isolates susceptible to ganciclovir, foscarnet, and cidofovir. All variations, including an eight-amino-acid deletion, were located between domains delta-C and II and between domains III and I, suggesting that these specific residues are not involved in enzymatic functions.</description><dates><release>2004-01-01T00:00:00Z</release><publication>2004 May</publication><modification>2025-04-26T04:25:29.377Z</modification><creation>2019-03-27T00:50:24Z</creation></dates><accession>S-EPMC400574</accession><cross_references><pubmed>15105145</pubmed><doi>10.1128/aac.48.5.1865-1868.2004</doi><doi>10.1128/AAC.48.5.1865-1868.2004</doi></cross_references></HashMap>