About: Point mutations in human guanylate kinase account for acquired resistance to anticancer nucleotide analogue PMEG     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
Description
  • The ability of a nucleotide analogue PMEG to induce resistance and the mechanisms involved were adressed. CCRF-CEM cells resistant to either PMEG or its congener PMEDAP were assayed for the expression of membrane transporters, PMEG and PMEDAP uptake and metabolism. PMEG phosphorylation to PMEG mono- and diphosphate was completely impaired in resistant cells. Guanylate kinase (GUK) obtained from PMEG-resistant cells revealed two point mutations S(35)N V(168)F that significantly suppressed its catalytic activity. Transfection with wtGUK led to the recovery of phosphorylating activity and sensitivity towards PMEG cytotoxicity. Primary sequence of adenylate kinase (AK) from PMEDAP resistant cells was unaffected. Resistance induced by PMEDAP is thus conferred by other mechanisms. No differences in PMEG uptake have been found between sensitive and resistant cells. GUK was identified as the sole molecular target for the development of resistance to PMEG.
  • The ability of a nucleotide analogue PMEG to induce resistance and the mechanisms involved were adressed. CCRF-CEM cells resistant to either PMEG or its congener PMEDAP were assayed for the expression of membrane transporters, PMEG and PMEDAP uptake and metabolism. PMEG phosphorylation to PMEG mono- and diphosphate was completely impaired in resistant cells. Guanylate kinase (GUK) obtained from PMEG-resistant cells revealed two point mutations S(35)N V(168)F that significantly suppressed its catalytic activity. Transfection with wtGUK led to the recovery of phosphorylating activity and sensitivity towards PMEG cytotoxicity. Primary sequence of adenylate kinase (AK) from PMEDAP resistant cells was unaffected. Resistance induced by PMEDAP is thus conferred by other mechanisms. No differences in PMEG uptake have been found between sensitive and resistant cells. GUK was identified as the sole molecular target for the development of resistance to PMEG. (en)
Title
  • Point mutations in human guanylate kinase account for acquired resistance to anticancer nucleotide analogue PMEG
  • Point mutations in human guanylate kinase account for acquired resistance to anticancer nucleotide analogue PMEG (en)
skos:prefLabel
  • Point mutations in human guanylate kinase account for acquired resistance to anticancer nucleotide analogue PMEG
  • Point mutations in human guanylate kinase account for acquired resistance to anticancer nucleotide analogue PMEG (en)
skos:notation
  • RIV/61388963:_____/11:00360711!RIV12-AV0-61388963
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(1M0508), Z(AV0Z40550506)
http://linked.open...iv/cisloPeriodika
  • 2
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 220965
http://linked.open...ai/riv/idVysledku
  • RIV/61388963:_____/11:00360711
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • resistance; acyclic nucleoside phosphonates; PMEG; PMEDAP (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [986D0C17453C]
http://linked.open...i/riv/nazevZdroje
  • Biochemical Pharmacology
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 82
http://linked.open...iv/tvurceVysledku
  • Holý, Antonín
  • Mertlíková-Kaiserová, Helena
  • Votruba, Ivan
  • Procházková, Eliška
  • Rumlová, Michaela
  • Tloušťová, Eva
http://linked.open...ain/vavai/riv/wos
  • 000291760700005
http://linked.open...n/vavai/riv/zamer
issn
  • 0006-2952
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.bcp.2011.04.002
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 48 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software