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dc.contributor.author | Anikeenok M. | |
dc.contributor.author | Churin Y. | |
dc.contributor.author | Meyer T. | |
dc.contributor.author | Ilinskaya O. | |
dc.date.accessioned | 2018-09-18T20:33:31Z | |
dc.date.available | 2018-09-18T20:33:31Z | |
dc.date.issued | 2010 | |
dc.identifier.issn | 1990-7508 | |
dc.identifier.uri | https://dspace.kpfu.ru/xmlui/handle/net/141133 | |
dc.description.abstract | Phosphorylation of ATM-kinase substrates in HeLa and AGS cells in response to Helicobacter pylori infection has been characterized. Infection with wild-type (cagPAI-positive) and corresponding isogenic cagPAI negative mutant induced activation of Chk1 and Chk2 kinases. However, only Chk1 was directly activated by ATM-kinase. Using 2D-electrophoresis and mass spectrometry a group of proteins phosphorylated in AGS cells by ATM1/ATR kinases during H. pylori infection has been identified. © 2010 Pleiades Publishing, Ltd. | |
dc.relation.ispartofseries | Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry | |
dc.subject | ATM/ATR kinases | |
dc.subject | Helicobacter pylori | |
dc.subject | phosphorylation | |
dc.subject | RPA32A | |
dc.subject | splicing-factor | |
dc.title | Phosphorylation of ATM/ATR substrates in eukaryotic cells after infection with Helicobacter pylori | |
dc.type | Article | |
dc.relation.ispartofseries-issue | 2 | |
dc.relation.ispartofseries-volume | 4 | |
dc.collection | Публикации сотрудников КФУ | |
dc.relation.startpage | 171 | |
dc.source.id | SCOPUS19907508-2010-4-2-SID77955947098 |