ribosomal protein L9
Reference Gene Selection and Evaluation for Gene Expression Studies Using qRT-PCR in the White-Backed Planthopper, Sogatella furcifera (Hemiptera: Delphacidae).
Beijing, China. In J Econ Entomol, Dec 2015
In the present study, nine commonly used reference genes, elongation factor 1-α (EF1-α), polyubiquitin (UB), ribosomal protein S18 (RPS18), actin 1 (ACT), α-1 tubulin (TUB), glyceraldehyde-3-phosphate (GAPDH), ribosomal protein L9 (RPL9), ribosomal protein L10 (RPL10), and 18S ribosomal RNA (18S), were evaluated by qRT-PCR for their expression stability under four different experimental conditions (different developmental stages, acquisition of Southern rice black-streaked dwarf virus (SRBSDV), different tissues, and different temperature stress).
First Passage Times, Lifetimes, and Relaxation Times of Unfolded Proteins.
United States. In Phys Rev Lett, Aug 2015
We validate these concepts by analyzing a Markov state model of the kinetics in the unfolded state and folding of the miniprotein NTL9 (where NTL9 is the N-terminal domain of the ribosomal protein L9), constructed from a 2.9 ms simulation provided by D. E. Shaw Research.
Immune- and ribosome-related genes were associated with systemic vasculitis.
Shanghai, China. In Scand J Immunol, Feb 2015
Furthermore, human leucocyte antigen (HLA)-DRB1, HLA-DPA1, HLA-DPB1, HLA-DOA and HLA-DRA in the downregulated modules were significantly linked to immune-related pathways (intestinal immune network for IgA production and systemic lupus erythematosus pathways), while ribosomal protein L 31 (RPL31), RPS3A and RPL9 in the upregulated module were enriched in ribosome pathway.
Stress response of Pseudomonas species to silver nanoparticles at the molecular level.
Nāgpur, India. In Environ Toxicol Chem, 2014
The results showed increased expression of ribosomal protein S2, KHGA, AhpC/TSA, and ribosomal protein L9 by 1.09-, 3.41-, 1.52-, and 1.56-fold, respectively (p < 0.05), after AgNP exposure compared with control.
Energetically significant networks of coupled interactions within an unfolded protein.
Würzburg, Germany. In Proc Natl Acad Sci U S A, 2014
Using the N-terminal domain of the ribosomal protein L9, a small α-β protein, as an experimental model system, we demonstrate that networks of energetically significant, coupled interactions can form in the DSE of globular proteins, and can involve residues that are distant in sequence and spatially well separated in the native structure.