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Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.. Additionally we are shipping SRP19 Antibodies (55) and and many more products for this protein.
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The crystal structures of the SRP68 protein-binding domain (PBD) in complex with SRP72-PBD and of the SRP72-RBD bound to the SRP S domain (SRP RNA, SRP19 and SRP68) detailing all interactions of SRP72 within SRP have been presented.
anti-SRP19 antibody is highly expressed in muscle tissues of patients with autoimmune necrotizing myopathy.
crystal structures of a crenarchaeal and the all-human SRP19-signal recognition particle RNA binary complexes presented here show that the asymmetric loop is bulged out in both binary complexes.
Structure of the SRP19 RNA complex
crystal structure of a human SRP ternary complex consisting of SRP19, the M domain of SRP54 and the S domain of 7SL RNA
Data show that the presence of SRP54 during SRP19-RNA assembly dramatically alters the folding energy landscape to create a non-native folding pathway that leads to an aberrant SRP19-RNA conformation.
1.8 angstrom resolution crystal structure of human SRP19 in complex with its primary binding site on helix 6 of SRP RNA was determined
srp19 is produced in the amplified nucleoli of Xenopus oocytes, presumably as a global developmental strategy for stockpiling translational machinery for early embryogenesis
Signal-recognition-particle assembly, binds directly to 7S RNA and mediates binding of the 54 kDa subunit of the SRP.
signal recognition particle 19 kDa protein
, signal recognition particle 19
, signal recognition particle 19kDa
, signal recognition particle 19 kD protein
, signal recognition particle protein 19