protein | Protein subunit | Protein-protein interaction | Hfq protein | protein domain | Protein-protein_interaction | Ghost in the Shell: Stand Alone Complex | Theodore Roosevelt National Wildlife Refuge Complex | Protein Data Bank | The Chimpanzee Complex | RNA-binding protein | Oedipus complex | Meadowlands Sports Complex | Promyelocytic leukemia protein | military-industrial complex | Kennedy Space Center Visitor Complex | G protein | Goldstone Deep Space Communications Complex | complex | Y-12 National Security Complex | Wiskott–Aldrich syndrome protein | Watergate complex | Protein G | protein dimer | Protein A | Mi-2/NuRD complex | Ladd S. Gordon Waterfowl Complex | Faliro Coastal Zone Olympic Complex | C-reactive protein | Complex (magazine) |
In molecular biology, the arfaptin domain is a protein domain which interacts with ARF1, a small GTPase involved in vesicle budding at the Golgi complex and immature secretory granules.
SMAR1 (Scaffold/Matrix attachment region-binding protein 1; also known as BANP), a tumour-suppressor MAR-binding protein that down-regulates Cyclin D1 expression by recruiting HDAC1-mSin3A co-repressor complex at Cyclin D1 promoter locus; SMAR1 is the target of prostaglandin A2 (PGA2) induced growth arrest.
building on the library, a set of programs for solving specific tasks, for example, the automatic prediction of Protein structures by Homology modeling or (an attempt at) the prediction of Protein complex structures through flexible Protein-protein docking
The MRX complex is a heterotrimeric protein complex consisting of Mre11, Rad50, and Xrs2.
DNA damage-binding protein is a protein complex that is responsible for repair of UV-damaged DNA.
He recently demonstrated a critical and direct role for a protein complex called Ndc80 (coded for by the gene NDC80) in directly associating with microtubules.
Mutations in the HADHA gene lead to inadequate levels of an enzyme called long-chain 3-hydroxyacyl-coenzyme A (CoA) dehydrogenase, which is part of a protein complex known as mitochondrial trifunctional protein.
Tuberous sclerosis proteins 1 and 2, also known as TSC1 (hamartin) and TSC2 (tuberin), form a protein-complex.
This protein has also been shown to be a member of the NELF (negative elongation factor) protein complex that participates in the regulation of RNA polymerase II transcription elongation.