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The protein encoded by PAIP1 interacts with poly(A)-binding protein and with the cap-binding complex eIF4A.
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Data provide evidence that the stability of Paip1 can be regulated by ubiquitin-mediated degradation, thus highlighting the importance of WWP2 (zeige WWP2 Proteine) as a suppressor of translation.
The Paip1-eIF3 (zeige EIF3A Proteine) interaction is impaired by the mTORC1 inhibitors.
the crystal structure of the middle domain of Paip1 isoform 2 (Paip1M) as determined by single-wavelength anomalous dispersion phasing is reported.
Paip1 is translational activator in 5' cap-dependent translation by interacting with PABP (zeige PABPC1 Proteine) & initiation factors eIF4A (zeige EIF4A1 Proteine) & eIF3 (zeige EIF3A Proteine). Crystallization & preliminary diffraction analysis of middle domain of Paip1 gives crystals that diffract to resolution of 2.2 A.
Paip1 interacts with poly(A) binding protein through two independent binding motifs.
eIF3 (zeige EIF3A Proteine)-Paip1 stabilizes the interaction between PABP (zeige PABPC1 Proteine) and eIF4G (zeige EIF4G1 Proteine), which brings about the circularization of the mRNA.
The protein encoded by this gene interacts with poly(A)-binding protein and with the cap-binding complex eIF4A. It is involved in translational initiation and protein biosynthesis. Overexpression of this gene in COS7 cells stimulates translation. Alternative splicing occurs at this locus and three transcript variants encoding three distinct isoforms have been identified.
PABC1-interacting protein 1
, PABP-interacting protein 1
, poly(A)-binding protein-interacting protein 1
, polyadenylate binding protein-interacting protein 1
, polyadenylate-binding protein-interacting protein 1
, poly(A) binding protein interacting protein 1
, polyadenylate-binding protein-interacting protein 1-like