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- Bf0b10b2094794611ac27a42af32ffbc5 NCIT_P378 "NCI" @default.
- Bf0b10b2094794611ac27a42af32ffbc5 NCIT_P381 "On-line Medical Dictionary" @default.
- Bf0b10b2094794611ac27a42af32ffbc5 type Axiom @default.
- Bf0b10b2094794611ac27a42af32ffbc5 annotatedProperty IAO_0000115 @default.
- Bf0b10b2094794611ac27a42af32ffbc5 annotatedSource NCIT_C17764 @default.
- Bf0b10b2094794611ac27a42af32ffbc5 annotatedTarget "Cytoplasmic proteins of both prokaryotes and eukaryotes that bind to nascent or unfolded polypeptides and ensure correct folding or transport. Chaperone proteins do not covalently bind to their targets and do not form part of the finished product. Heat-shock proteins are an important sub set of chaperones. Three major families are recognised, the chaperonins (groEL and hsp60), the hsp70 family and the hsp90 family. Outside these major families are other proteins with similar functions including nucleoplasmin, secB and T-cell receptor associated protein." @default.