Results 111 to 120 of about 6,159,973 (405)
Cell-based studies showed that several Mdm2-binding ribosomal proteins, upon overexpression, stabilize and activate p53. In contrast, here we show in a mouse knockout study that Mdm2-binding ribosomal protein S27-like (Rps27l), upon disruption, activates
Xiufang Xiong +8 more
doaj +1 more source
The ribosome is a large ribonucleoprotein complex that synthesizes protein in all living organisms. Ribosome biogenesis is a complex process that requires synchronization of various cellular events, including ribosomal RNA (rRNA) transcription, ribosome ...
Kumudie Jayalath +3 more
doaj +1 more source
RNA G-quadruplex structures control ribosomal protein production
Four-stranded G-quadruplex (G4) structures form from guanine-rich tracts, but the extent of their formation in cellular RNA and details of their role in RNA biology remain poorly defined.
Dhaval Varshney +5 more
doaj +1 more source
Mapping of the \u3cem\u3eSaccharomyces cerevisiae\u3c/em\u3e Oxa1-Mitochondrial Ribosome Interface and Identification of MrpL40, a Ribosomal Protein in Close Proximity to Oxa1 and Critical for Oxidative Phosphorylation Complex Assembly [PDF]
The Oxa1 protein plays a central role in facilitating the cotranslational insertion of the nascent polypeptide chains into the mitochondrial inner membrane. Mitochondrially encoded proteins are synthesized on matrix-localized ribosomes which are tethered
Jia, Lixia +2 more
core +1 more source
On the Renaturation of Ribosomal Protein L11 [PDF]
When urea‐denatured preparations of protein L11 from the ribosome of Escherichia coli are introduced into physiological buffers, two completely different configurations can be obtained. One form, by NMR criteria, shows little evidence of stable tertiary interactions; the other shows strong indications of a distinctive folding pattern. The configuration
Kime, M +3 more
openaire +4 more sources
TTT and R2TP chaperone complexes are required for the assembly and activation of mTORC1. WAC directly interacts with components of TTT, R2TP, and mTORC1, and these interactions are affected by the availability of glucose and glutamine, correlating with changes in mTORC1 activity.
Sofía Cabezudo +11 more
wiley +1 more source
This study reveals novel insights into how Escherichia coli ribosomal protein S1 functions as an RNA chaperone on the ribosome, unfolding and positioning mRNAs for translation initiation.
Mélodie Duval +11 more
semanticscholar +1 more source
The Double Life of Ribosomal Proteins [PDF]
Many integral proteins of the ribosome also carry out extra-ribosomal functions as independent polypeptides, raising questions as to their evolutionary derivation. In this issue of Cell, Mazumder et al. report a surprising new twist in the dual life of these molecules: as part of a cellular response to interferon, a large-subunit protein dramatically ...
openaire +3 more sources
Here, we introduced an intermittent electrical stimulation protocol mimicking the episodic nature of real‐life exercise in vitro by alternating low‐ and high‐frequency stimulation. In comparison with widely used continuous stimulation, it enhanced the rate of glucose and fatty acid oxidation, but not the myokine release.
Klára Gabrišová +11 more
wiley +1 more source
A rhodanine agent active against non-replicating intracellular Mycobacterium avium subspecies paratuberculosis. [PDF]
BACKGROUND: Antibiotic therapy targeting chronic mycobacterial disease is often ineffective due to problems with the emergence of drug resistance and non-replicating persistent intracellular antibiotic resistant phenotypes.
Bull, TJ +3 more
core +3 more sources

