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scopus(4)
Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L
ArticleAbstract: Background: GroESL is a heat-shock protein ubiquitous in bacteria and eukaryotic organelles. This evPalabras claves:Autores:Fares M.A., Mario X. Ruiz-GonzalezFuentes:scopusArabidopsis heat stress-induced proteins are enriched in electrostatically charged amino acids and intrinsically disordered regions
ArticleAbstract: Comparison of the proteins of thermophilic, mesophilic, and psychrophilic prokaryotes has revealed sPalabras claves:Intrinsically disordered proteins, Protein thermostability, Salt bridges, Temperature responseAutores:Alvarez-Ponce D., Fares M.A., Feyertag F., Mario X. Ruiz-Gonzalez, Perez-Amador M.A., Vera-Sirera F.Fuentes:scopusProteasome-related HslU and HslV genes typical of eubacteria are widespread in eukaryotes
ArticleAbstract: Many eubacteria contain an ATP-dependent protease complex, which is built by multiple copies of thePalabras claves:Comparative genomics, Early evolution, Endosymbiosis, HslVU complex, Proteasome, Protein quality controlAutores:Marín I., Mario X. Ruiz-GonzalezFuentes:scopusProtein coadaptation and the design of novel approaches to identify protein-protein interactions
ReviewAbstract: Proteins rarely function in isolation but they form part of complex networks of interactions with otPalabras claves:coadaptation, Coevolution, Protein interaction, yeast 2 hybridAutores:Fares M.A., Labrador J.P., Mario X. Ruiz-GonzalezFuentes:scopus