Zobrazeno 1 - 6
of 6
pro vyhledávání: '"José Humberto M. Tambor"'
Publikováno v:
Gene. 424:33-39
The mitochondrial genome of the chytrid Blastocladiella emersonii was sequenced and annotated, revealing the complete set of oxidative phosphorylation genes and tRNAs/rRNAs necessary for the translation process. Phylogenetic reconstructions reinforce
Autor:
Marina P. Nobrega, Francisco G. Nobrega, José Humberto M. Tambor, Rafael Santos, Ghislaine V. Fonseca
Publikováno v:
Genetics and Molecular Biology. 24:175-181
Mitochondria function as metabolic powerhouses by generating energy through oxidative phosphorylation and have become the focus of renewed interest due to progress in understanding the subtleties of their biogenesis and the discovery of the important
Autor:
Nicholas D. Gold, Vincent J. J. Martin, José Humberto M. Tambor, Nancy Bawa, Caroline Wilde, Reginald Storms, Lina Mougharbel
Publikováno v:
Applied microbiology and biotechnology. 95(3)
Converting cellulosic biomass to ethanol involves the enzymatic hydrolysis of cellulose and the fermentation of the resulting glucose. The yeast Saccharomyces cerevisiae is naturally ethanologenic, but lacks the enzymes necessary to degrade cellulose
Autor:
Anja M. Riemens, Reginald Storms, Justin Powlowski, José Humberto M. Tambor, Yun Zheng, Adrian Tsang, Sophia Ushinsky, Christopher St-Francois, Huanan Ren
Publikováno v:
Applied microbiology and biotechnology. 93(1)
The hydrolysis of cellulose into fermentable sugars is a costly and rate-limiting step in the production of biofuels from renewable feedstocks. Developing new cellulase systems capable of increased cellulose hydrolysis rates would reduce biofuel prod
Publikováno v:
Yeast (Chichester, England). 24(7)
We present here the sequence of the mitochondrial DNA of the pathogenic thermodimorphic fungus Paracoccidioides brasiliensis, agent of an endemic disease in most South American countries. The sequenced genome has 71 334 bp and is organized as a circu
Autor:
Andrea M. Macedo, Philip T. LoVerde, Adlane Vilas-Boas, Francisco G. Nobrega, Sérgio D.J. Pena, Carlos Renato Machado, Analina F. Valadão, Francisco Pereira Lobo, Glória Regina Franco, José Humberto M. Tambor, Débora Santos, Pedro Henrique Nascimento Aguiar, Marina de Moraes Mourão
Publikováno v:
Experimental parasitology. 116(4)
The SCF (Skp1–Cul1–F-box) complex is one of the several E3 ligase enzymes and it catalyzes protein ubiquitination and degradation by the 26S proteasome. Rbx1 is a member of the SCF complex in humans and HRT1 is its yeast orthologue. A cDNA encodi