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YpkA phosphorylates OTUB1. 14 / 14
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"As otubain 1 has been shown to interact with the E3 ligase GRAIL, leading to GRAIL degradation and repression of T-cell anergy [12] , it is tempting to speculate that otubain 1 phosphorylation by YpkA[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Current efforts directed towards examining all possible consequences of otubain 1 phosphorylation by YpkA should aid in understanding the molecular details of how this mechanism is advantageous for Ye[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"We demonstrate phosphorylation of otubain 1 by YpkA in vitro and further demonstrate a connection between otubain 1 and the actin cytoskeleton."
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"Phosphorylation of OTUB1 by YpkA is actin-dependent, which is consistent to the model that YpkA uses actin as an allosteric activator ( xref )."
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"We demonstrate phosphorylation of otubain 1 by YpkA in vitro and further demonstrate a connection between otubain 1 and the actin cytoskeleton."
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"To verify that YpkA can phosphorylate otubain 1, different amounts of otubain 1 were incubated with YpkA and actin."
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"Phosphorylation of OTUB1 by YpkA is actin-dependent, which is consistent to the model that YpkA uses actin as an allosteric activator (Figure 2)."
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"YpkA phosphorylation of otubain 1 may regulate otubain in numerous ways including proteolytic activity, localization, or protein stability."
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"YpkA is capable of phosphorylating otubain 1 in vitro only when actin is present to activate YpkA ( Fig. 4 A)."
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"To verify that YpkA can phosphorylate otubain 1, different amounts of otubain 1 were incubated with YpkA and actin."
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"As otubain 1 has been shown to interact with the E3 ligase GRAIL, leading to GRAIL degradation and repression of T-cell anergy [12] , it is tempting to speculate that otubain 1 phosphorylation by YpkA[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
16364312
reach
"Current efforts directed towards examining all possible consequences of otubain 1 phosphorylation by YpkA should aid in understanding the molecular details of how this mechanism is advantageous for Ye[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
16364312
sparser
"YpkA phosphorylation of otubain 1 may regulate otubain in numerous ways including proteolytic activity, localization, or protein stability."
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"During Yersinia infection OTUB1 can be phosphorylated by a bacterial kinase YpkA which modulates cellular susceptibility to Yersinia invasion [ xref ]."
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