Zobrazeno 1 - 10
of 74
pro vyhledávání: '"Nelson Carvajal"'
Publikováno v:
In Transplantation Proceedings March 2024 56(2):297-305
Autor:
Dahyana Cadavid Aljure, Verónica Posada-Vélez, Laura Betancur Vásquez, Juan Sebastián Gómez Villalobos, Juan Pablo Villa Franco, Juan Carlos Tobón Pereira, María Alejandra Muñoz Cifuentes, José Nelson Carvajal
Publikováno v:
IDCases, Vol 21, Iss , Pp e00914- (2020)
Streptococcus bovis bacteremia (currently called S. gallolyticus) represents an infrequent condition, but associated with a high rate of morbidity and mortality Amado et al. (2015). The clinical presentation is characterized by symptoms associated wi
Externí odkaz:
https://doaj.org/article/2a4ae99f7eeb4ef3b69ea6660ddf641d
Autor:
María-Soledad Orellana, Gonzalo A. Jaña, Maximiliano Figueroa, José Martínez-Oyanedel, Fabiola E. Medina, Estefanía Tarifeño-Saldivia, Marcell Gatica, María Ángeles García-Robles, Nelson Carvajal, Elena Uribe
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 12; Pages: 6438
Arginase catalyzes the hydrolysis of L-arginine into L-ornithine and urea. This enzyme has several analogies with agmatinase, which catalyzes the hydrolysis of agmatine into putrescine and urea. However, this contrasts with the highlighted specificit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93f6e1e9c985496490df1466ed4f0e29
https://doi.org/10.3390/ijms23126438
https://doi.org/10.3390/ijms23126438
Autor:
Juan Sebastián Gómez Villalobos, Juan Carlos Tobón Pereira, José Nelson Carvajal, María Alejandra Muñoz Cifuentes, Juan Pablo Villa Franco, Dahyana Cadavid Aljure, Laura Betancur Vásquez, Verónica Posada-Vélez
Publikováno v:
IDCases
IDCases, Vol 21, Iss, Pp e00914-(2020)
IDCases, Vol 21, Iss, Pp e00914-(2020)
Highlights • Disseminated S. bovis group infections are unusual in adults. • S. bovis infections are usually related to colorectal neoplasia o biliary tract disease. • S. bovis group zoonotic transmission could be biologically plausible, as inf
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56a656b88c883b1fed1a0ccb5a2d7321
http://europepmc.org/articles/PMC7369581
http://europepmc.org/articles/PMC7369581
Autor:
María De Los Ángeles García-Robles, Maximiliano Figueroa, Vasthi López, Elena Uribe, Nelson Carvajal, Marcela Lobos, José Martínez-Oyanedel, Estefanía Tarifeño-Saldivia
Publikováno v:
Journal of structural biology. 211(2)
Arginase (EC 3.5.3.1) catalyzes the hydrolysis of L-arginine to L-ornithine and urea, and requires a bivalent cation, especially Mn2+ for its catalytic activity. It is a component of the urea cycle and regulates the intracellular levels of l-arginine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c4c40f95b2ef1581cc2852eaac21137
https://pubmed.ncbi.nlm.nih.gov/32450233
https://pubmed.ncbi.nlm.nih.gov/32450233
Autor:
Nelson Carvajal, Liam A. Wilson, Elena Uribe, David García, José Manuel Benítez, María De Los Ángeles García-Robles, Vasthi López, Gerhard Schenk, Arlette González, Nicol Romero, Leonardo Bennun
Publikováno v:
Journal of Inorganic Biochemistry. 166:122-125
Agmatine (1-amino-4-guanidinobutane) plays an important role in a range of metabolic functions, in particular in the brain. Agmatinases (AGMs) are enzymes capable of converting agmatine to the polyamine putrescine and urea. AGMs belong to the family
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e3a4b2d1881f6301786db4ab719f68e5
https://doi.org/10.1016/j.jinorgbio.2016.11.015
https://doi.org/10.1016/j.jinorgbio.2016.11.015
Autor:
Elena, Uribe, María-Belen, Reyes, Ignacio, Martínez, Kelly, Mella, Mónica, Salas, Estefanía, Tarifeño-Saldivia, Vasthi, López, María, García-Robles, José, Martínez-Oyanedel, Maximiliano, Figueroa, Nelson, Carvajal, Gerhard, Schenk
Publikováno v:
Journal of inorganic biochemistry. 202
Ureohydrolases form a conserved family of enzymes with a strict requirement for divalent metal ions for catalytic activity. They catalyze the hydrolysis of the guanidino group and produce urea. In their active sites six highly conserved amino acid re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eaaa2dcb8985e61934946d3b7ea6b2fa
https://pubmed.ncbi.nlm.nih.gov/31731096
https://pubmed.ncbi.nlm.nih.gov/31731096
Autor:
Elena Uribe, Estefanía Tarifeño-Saldivia, Ignacio Martínez, Vasthi López, Gerhard Schenk, Kelly Mella, Nelson Carvajal, José Martínez-Oyanedel, Mónica Salas, María-Belen Reyes, María De Los Ángeles García-Robles, Maximiliano Figueroa
Publikováno v:
Journal of Inorganic Biochemistry. 202:110812
Ureohydrolases form a conserved family of enzymes with a strict requirement for divalent metal ions for catalytic activity. They catalyze the hydrolysis of the guanidino group and produce urea. In their active sites six highly conserved amino acid re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::55f0463f7df2c56cc20446ad81c4a503
https://doi.org/10.1016/j.jinorgbio.2019.110812
https://doi.org/10.1016/j.jinorgbio.2019.110812
Autor:
Arlette González, Vasthi López, Patricio Ordenes, María De Los Ángeles García-Robles, Elena Uribe, José Manuel Benítez, David García, Nelson Carvajal
Publikováno v:
Histochemistry and Cell Biology. 145:305-313
Agmatine, a precursor for polyamine biosynthesis, is also associated with neurotransmitter, anticonvulsant, antineurotoxic and antidepressant actions in the brain. This molecule results from the decarboxylation of L-arginine by arginine decarboxylase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef87a66961ed2cbb6dcc7899793e1efe
https://doi.org/10.1007/s00418-015-1389-0
https://doi.org/10.1007/s00418-015-1389-0
Publikováno v:
Biochimie. 108:8-12
To substantiate the functionality of a crystallographically evidenced allosteric site in Bacillus caldovelox arginase (Bewley et al., 1999), we have examined the kinetic consequences of the single mutations of Asp199 and Glu256, which interact with l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42dc38c4fbc62b320b8c7353fc280595
https://doi.org/10.1016/j.biochi.2014.10.017
https://doi.org/10.1016/j.biochi.2014.10.017