Title : The Helminthosporium victoriae 190S mycovirus has two forms distinguishable by capsid protein composition and phosphorylation state.

Pub. Date : 1992 Jun

PMID : 1585640






4 Functional Relationships(s)
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Protein Name
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1 The in vitro results suggest that the Hv190S virions copurify with a protein kinase activity that catalyzes the transfer of gamma-phosphate from ATP to a target protein, presumably p78 in the 190S-2 virions and p83 in the 190S-1 component. gamma-phosphate Rho related BTB domain containing 2 Homo sapiens
2 The in vitro results suggest that the Hv190S virions copurify with a protein kinase activity that catalyzes the transfer of gamma-phosphate from ATP to a target protein, presumably p78 in the 190S-2 virions and p83 in the 190S-1 component. Adenosine Triphosphate Rho related BTB domain containing 2 Homo sapiens
3 Selective chemical cleavage at tryptophan residues of in vitro 32P-labeled capsid proteins revealed four labeled peptides among the cleavage products of both p83 and p88. Tryptophan Rho related BTB domain containing 2 Homo sapiens
4 Selective chemical cleavage at tryptophan residues of in vitro 32P-labeled capsid proteins revealed four labeled peptides among the cleavage products of both p83 and p88. Phosphorus-32 Rho related BTB domain containing 2 Homo sapiens