RACK1 has been shown to interact with several proteins, this suggesting that it may play a central role in cell growth regulation. Some recent articles have described RACK1 as a component of the small ribosomal subunit. To investigate the relationship between RACK1 and ribosome, we analyzed RACK1 mRNA structure and regulation. Translational regulation was studied in HeLa cells subjected to serum or amino acid deprivation and stimulation. The results show that RACK1 mRNA has a 5' terminal oligopyrimidine sequence and that its translation is dependent on the availability of serum and amino acids in exactly the same way as any other vertebrate ribosomal protein mRNA. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier ...
RACK1 (Receptor for activated protein C kinase 1) est une protéine ribosomale associée à de nombreus...
RACK1 (Receptor for activated C kinase 1) is an evolutionary conserved protein which has essential r...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.Cataloged from PD...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
AbstractRACK1 has been shown to interact with several proteins, this suggesting that it may play a c...
Abstract: Translation is a fundamental cellular process performed by ribosomes and is regulated by s...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) est une protéine ribosomale associée à de nombreus...
RACK1 (Receptor for activated protein C kinase 1) est une protéine ribosomale associée à de nombreus...
RACK1 (Receptor for activated C kinase 1) is an evolutionary conserved protein which has essential r...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.Cataloged from PD...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
RACK1 has been shown to interact with several proteins, this suggesting that it may play a central r...
AbstractRACK1 has been shown to interact with several proteins, this suggesting that it may play a c...
Abstract: Translation is a fundamental cellular process performed by ribosomes and is regulated by s...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) is a ribosomal protein associated to many signalin...
RACK1 (Receptor for activated protein C kinase 1) est une protéine ribosomale associée à de nombreus...
RACK1 (Receptor for activated protein C kinase 1) est une protéine ribosomale associée à de nombreus...
RACK1 (Receptor for activated C kinase 1) is an evolutionary conserved protein which has essential r...
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.Cataloged from PD...