Zobrazeno 1 - 10
of 12
pro vyhledávání: '"María S Orellana"'
Autor:
Pablo Maturana, María S. Orellana, Sixto M. Herrera, Ignacio Martínez, Maximiliano Figueroa, José Martínez-Oyanedel, Victor Castro-Fernandez, Elena Uribe
Publikováno v:
International Journal of Molecular Sciences, Vol 22, Iss 9, p 4769 (2021)
Agmatine is the product of the decarboxylation of L-arginine by the enzyme arginine decarboxylase. This amine has been attributed to neurotransmitter functions, anticonvulsant, anti-neurotoxic, and antidepressant in mammals and is a potential therape
Externí odkaz:
https://doaj.org/article/fa3ebac47197432fa54d760509f29877
Publikováno v:
Formación universitaria. 15:163-174
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f52203fffec54c8b6cc3fd1b7a505370
https://doi.org/10.4067/s0718-50062022000200163
https://doi.org/10.4067/s0718-50062022000200163
Autor:
Maximiliano Figueroa, Pablo Maturana, Elena Uribe, Ignacio Martínez, José Martínez-Oyanedel, Sixto M. Herrera, Victor Castro-Fernandez, María S Orellana
Publikováno v:
International Journal of Molecular Sciences
Volume 22
Issue 9
International Journal of Molecular Sciences, Vol 22, Iss 4769, p 4769 (2021)
Volume 22
Issue 9
International Journal of Molecular Sciences, Vol 22, Iss 4769, p 4769 (2021)
Agmatine is the product of the decarboxylation of L-arginine by the enzyme arginine decarboxylase. This amine has been attributed to neurotransmitter functions, anticonvulsant, anti-neurotoxic, and antidepressant in mammals and is a potential therape
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3dd24f61b9bbdee4717b7bd34f8b717e
Autor:
Pablo, Maturana, María S, Orellana, Sixto M, Herrera, Ignacio, Martínez, Maximiliano, Figueroa, José, Martínez-Oyanedel, Victor, Castro-Fernandez, Elena, Uribe
Publikováno v:
International Journal of Molecular Sciences
Agmatine is the product of the decarboxylation of L-arginine by the enzyme arginine decarboxylase. This amine has been attributed to neurotransmitter functions, anticonvulsant, anti-neurotoxic, and antidepressant in mammals and is a potential therape
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::03f41f38846e0efad809afe8f42dd4ef
https://pubmed.ncbi.nlm.nih.gov/33946272
https://pubmed.ncbi.nlm.nih.gov/33946272
Publikováno v:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
Artículos CONICYT
CONICYT Chile
instacron:CONICYT
The functional significance of a C-terminal S-shaped motif (residues 304–322) in human arginase I was explored by examining the kinetic properties of the R308A mutant and truncated species terminating in either Arg-308 or Ala-308. Replacement of Ar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6c8e8f118baaf21d29049213705e9cb
https://doi.org/10.1016/j.abb.2008.10.015
https://doi.org/10.1016/j.abb.2008.10.015
Autor:
Ricardo Alarcón, Nelson Carvajal, Elena Uribe, María S. Orellana, Benita Neira, José Renán García
Publikováno v:
FEBS Journal. 273:5625-5631
Upon mutation of Asn130 to aspartate, the catalytic activity of human arginase I was reduced to ∼ 17% of wild-type activity, the Km value for arginine was increased ∼ 9-fold, and the kcat/Km value was reduced ∼ 50-fold. The kinetic properties w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::93d699b27379faf0ecf00aec221356ef
https://doi.org/10.1111/j.1742-4658.2006.05551.x
https://doi.org/10.1111/j.1742-4658.2006.05551.x
Autor:
Elena Uribe, Mónica Salas, Ricardo Alarcón, Paula Enrı́quez, María S. Orellana, Nelson Carvajal, Vasthi López
Publikováno v:
Archives of Biochemistry and Biophysics. 430:185-190
The interaction of Escherichia coli agmatinase (EC 3.5.3.11) with the substrate guanidinium group was investigated by kinetic and site-directed mutagenesis studies. Putrescine and guanidinium ions (Gdn + ) were slope-linear, competitive inhibitors wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::626a4a47ee2b8dfcf7c1f822d1b65c9a
https://doi.org/10.1016/j.abb.2004.07.005
https://doi.org/10.1016/j.abb.2004.07.005
Autor:
Ricardo, Alarcón, María S, Orellana, Benita, Neira, Elena, Uribe, José R, García, Nelson, Carvajal
Publikováno v:
The FEBS journal. 273(24)
Upon mutation of Asn130 to aspartate, the catalytic activity of human arginase I was reduced to approximately 17% of wild-type activity, the Km value for arginine was increased approximately 9-fold, and the kcat/Km value was reduced approximately 50-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c45e97c4a04b92c064adb2eab1ac086b
https://pubmed.ncbi.nlm.nih.gov/17212779
https://pubmed.ncbi.nlm.nih.gov/17212779
Publikováno v:
Archives of biochemistry and biophysics. 461(1)
A rat brain cDNA encoding for a novel protein with agmatinase activity was cloned and functionally expressed. The protein was expressed as a histidine-tagged fusion product with a molecular weight of about 63 kDa. Agmatine hydrolysis was strictly dep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d1aa112c41d87c2c660478b05388b6a
https://pubmed.ncbi.nlm.nih.gov/17291445
https://pubmed.ncbi.nlm.nih.gov/17291445
Autor:
Elena Uribe, José Martínez, María S. Orellana, Ricardo Alarcón, Nelson Carvajal, Paula Enrı́quez, Vasthi López
Publikováno v:
The FEBS journal. 272(17)
To examine the interaction of human arginase II (EC 3.5.3.1) with substrate and manganese ions, the Hisl20Asn, Hisl45Asn and Asnl49Asp mutations were introduced separately. About 53% and 95% of wild-type arginase activitywere expressed by fully manga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14cbd81574e25f33ed518f5cafa2b2c8
https://pubmed.ncbi.nlm.nih.gov/16128822
https://pubmed.ncbi.nlm.nih.gov/16128822