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 |
|