Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Vivian R. Moure"'
Autor:
Mateus S. Lopes, Gabriel B. Baptistella, Giovana G. Nunes, Matheus V. Ferreira, Joice Maria Cunha, Kauê Marcel de Oliveira, Alexandra Acco, Maria Luiza C. Lopes, Alexessander Couto Alves, Glaucio Valdameri, Vivian R. Moure, Geraldo Picheth, Graciele C. M. Manica, Fabiane G. M. Rego
Publikováno v:
Pharmaceuticals, Vol 17, Iss 4, p 486 (2024)
Diabetes mellitus (DM) complications are a burden to health care systems due to the associated consequences of poor glycemic control and the side effects of insulin therapy. Recently. adjuvant therapies, such as vanadium compounds, have gained attent
Externí odkaz:
https://doaj.org/article/e83ef2c85677421784bbdc5685a2402e
Autor:
Edileusa C M, Gerhardt, Vivian R, Moure, Andrey W, Souza, Fabio O, Pedrosa, Emanuel M, Souza, Lautaro, Diacovich, Hugo, Gramajo, Luciano F, Huergo
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
EXCLI Journal
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
EXCLI Journal
The PII protein family constitutes one of the most conserved and well distributed family of signal transduction proteins in nature. These proteins play key roles in nitrogen and carbon metabolism. PII function has been well documented in Gram-negativ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9e6ed53bd1bce1b274bbc9a652accb6
Autor:
Edileusa C. M. Gerhardt, Shannon Wendroth, Vivian R. Moure, Zhi-Yong Yang, Lance C. Seefeldt, Karamatullah Danyal, Marcelo Scarduelli, Luciano F. Huergo, Emanuel Maltempi de Souza, Marcelo Müller-Santos, Fábio O. Pedrosa
Publikováno v:
Journal of Bacteriology. 195:279-286
Fe protein (dinitrogenase reductase) activity is reversibly inactivated by dinitrogenase reductase ADP-ribosyltransferase (DraT) in response to an increase in the ammonium concentration or a decrease in cellular energy in Azospirillum brasilense , Rh
Publikováno v:
Proceedings of the National Academy of Sciences. 109:19644-19648
A doubly substituted form of the nitrogenase MoFe protein (α-70 Val →Ala , α-195 His→Gln ) has the capacity to catalyze the reduction of carbon dioxide (CO 2 ) to yield methane (CH 4 ). Under optimized conditions, 1 nmol of the substituted MoFe
Autor:
Vivian R, Moure, Flavia F, Costa, Leonardo M, Cruz, Fabio O, Pedrosa, Emanuel M, Souza, Xiao-Dan, Li, Fritz, Winkler, Luciano F, Huergo
Publikováno v:
Current topics in microbiology and immunology. 384
Posttranslational modification of proteins plays a key role in the regulation of a plethora of metabolic functions. Protein modification by mono-ADP-ribosylation was first described as a mechanism of action of bacterial toxins. Since these pioneering