ArticleProtein science : a publication of the Protein Society2016
Structural characterization of NRAS isoform 5.
Article in Protein science : a publication of the Protein Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Roles and mechanisms of aberrant alternative splicing in melanoma - implications for targeted therapy and immunotherapy resistance.Cancer cell international · 2024Review
- Structural modifications and kinetic effects ofFrontiers in molecular biosciences · 2024Article
- Splice variants of RAS-translational significance.Cancer metastasis reviews · 2020Review
- Neuroblastoma RAS viral oncogene homolog mRNA is differentially spliced to give five distinct isoforms: implications for melanoma therapy.Melanoma research · 2019Article
- 1-Amino-2'-fucosyllactose inhibits biofilm formation by Streptococcus agalactiae.The Journal of antibiotics · 2019Article
- 5-Arylidene(chromenyl-methylene)-thiazolidinediones: Potential New Agents against Mutant Oncoproteins K-Ras, N-Ras and B-Raf in Colorectal Cancer and Melanoma.Medicina (Kaunas, Lithuania) · 2019Article
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Authors and funding
11 authors.
Funding
Abstract
It was recently discovered that the NRAS isoform 5 (20 amino acids) is expressed in melanoma and results in a more aggressive cell phenotype. This novel isoform is responsible for increased phosphorylation of downstream targets such as AKT, MEK, and ERK as well as increased cellular proliferation. This structure report describes the NMR solution structure of NRAS isoform 5 to be used as a starting point to understand its biophysical interactions. The isoform is highly flexible in aqueous solution, but forms a helix-turn-coil structure in the presence of trifluoroethanol as determined by NMR and CD spectroscopy.
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Registered trials
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