Title : Activated or dominant inhibitory mutants of Rap1A decrease the oxidative burst of Epstein-Barr virus-transformed human B lymphocytes.

Pub. Date : 1994 Jul 22

PMID : 8034626






2 Functional Relationships(s)
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1 Therefore, we have stably transfected human Epstein-Barr virus-transformed B lymphocytes that possess an activable NADPH oxidase complex with cDNAs for mutants of Rap1A "locked" in a GTP-bound (63E) and GDP-bound (17N) state. Guanosine Diphosphate RAP1A, member of RAS oncogene family Homo sapiens
2 Furthermore, the inhibitory effect of both GTP- as well as GDP-bound mutants indicates that Rap1A functions in a dynamic cycle as opposed to a unidirectional pathway, as is the case for the other NADPH oxidase regulatory GTP-binding protein, Rac. Guanosine Diphosphate RAP1A, member of RAS oncogene family Homo sapiens