Results 1 to 10 of about 11,998 (164)
Regulation of HDM2 activity by the ribosomal protein L11 [PDF]
Cancer Cell, 2003 The HDM2 protein plays an important role in regulating the stability and function of the p53 tumor suppressor protein. In this report, we show that the ribosomal protein L11 can interact with HDM2 and inhibit HDM2 function, thus leading to the stabilization and activation of p53.
Robert L Ludwig +2 more
exaly +4 more sources
Identification and Genomic Insights into the Biological Control and Growth-Promoting Mechanism of Bacillus velezensis L11-7, a Potential Biocontrol Agent of Passion Fruit Stem Basal Rot [PDF]
MicroorganismsBasal stem rot caused by Fusarium solani is among the most destructive soil-borne diseases affecting passion fruit (Passiflora spp.). While biological control employing antagonistic microorganisms offers a promising plant protection strategy, reports on ...
Ming Jin +6 more
doaj +2 more sources
Crystallographic analysis of archaeal ribosomal protein L11 [PDF]
Acta Crystallographica Section F, Structural Biology Communications, 2015 Ribosomal protein L11 is an important part of the GTPase-associated centre in ribosomes of all organisms. L11 is a highly conserved two-domain ribosomal protein. The C-terminal domain of L11 is an RNA-binding domain that binds to a fragment of 23S rRNA and stabilizes its structure. The complex between L11 and 23S rRNA is involved in the GTPase activity
Maria Garber +2 more
exaly +3 more sources
Regulation of nucleolar signalling to p53 through NEDDylation of L11 [PDF]
EMBO Reports, 2009 Several studies have shown that ribosomal proteins (RPs) are important mediators of p53 activation in response to nucleolar disruption; however, the pathways that control this signalling function of RPs are currently unknown. We have recently shown that RPs are targets for the ubiquitin-like molecule NEDD8, and that NEDDylation protects RPs from ...
Geng Liu, Dimitris P Xirodimas
exaly +3 more sources
Cooperation between the ribosomal proteins L5 and L11 in the p53 pathway [PDF]
Oncogene, 2008 MDM2 is a ubiquitin ligase that plays a key role in regulating the stability of the p53 tumor suppressor protein. Several proteins have been shown to activate the p53 pathway by interacting with and inhibiting the E3 function of MDM2, thereby leading to an accumulation of p53.
Henning F Horn, Vousden K H
exaly +3 more sources
Animals, 2022 Selection for the number of living pigs on day 11 (L11) aims to reduce piglet mortality and increase litter size simultaneously. This approach could be sub-optimal, especially for organic pig breeding.
Roos M. Zaalberg +3 more
doaj +1 more source
Myeloma overexpressed 2 (Myeov2) regulates L11 subnuclear localization through Nedd8 modification. [PDF]
PLoS ONE, 2013 Nucleolus is a dynamic structure that controls biogenesis of ribosomal RNA and senses cellular stresses. Nucleolus contains a number of proteins including ribosomal proteins that conduct cellular stresses to downstream signaling such as p53 pathway ...
Manato Ebina +5 more
doaj +1 more source
Development Features of the Domestic Consumer Goods Market in Ukraine
Studia Ekonomiczne i Regionalne, 2022 Subject and purpose of work: The main purpose of the article is to assess the functioning of the domestic market for consumer products and to characterise its development.
Popadynets Nazariy
doaj +1 more source
The Structure of Free L11 and Functional Dynamics of L11 in Free, L11-rRNA(58 nt) Binary and L11-rRNA(58 nt)-thiostrepton Ternary Complexes [PDF]
Journal of Molecular Biology, 2007 The L11 binding site is one of the most important functional sites in the ribosome. The N-terminal domain of L11 has been implicated as a "reversible switch" in facilitating the coordinated movements associated with EF-G-driven GTP hydrolysis. The reversible switch mechanism has been hypothesized to require conformational flexibility involving re ...
Donghan, Lee +8 more
openaire +2 more sources
On the Renaturation of Ribosomal Protein L11 [PDF]
European Journal of Biochemistry, 1980 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 +3 more sources