Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Adriana Julián-Sánchez"'
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0172376 (2017)
[This corrects the article DOI: 10.1371/journal.pone.0166851.].
Externí odkaz:
https://doaj.org/article/b0d6ad2aaa894b93bbde1e9bfb813563
Publikováno v:
PLoS ONE, Vol 11, Iss 11, p e0166851 (2016)
Alcohol dehydrogenase (ADH) activity is widely distributed in the three domains of life. Currently, there are three non-homologous NAD(P)+-dependent ADH families reported: Type I ADH comprises Zn-dependent ADHs; type II ADH comprises short-chain ADHs
Externí odkaz:
https://doaj.org/article/a4c23718f8674103a4de789b063caf95
Autor:
Rosario A. Muñoz-Clares, Héctor Riveros-Rosas, Gabriel Moreno-Hagelsieb, Adriana Julián-Sánchez
Publikováno v:
The FASEB Journal. 33
Autor:
Rosario A. Muñoz-Clares, Adriana Julián-Sánchez, Héctor Riveros-Rosas, Gabriel Moreno-Hagelsieb, Adeli P. Castrejón-Gonzaga
Publikováno v:
The FASEB Journal. 34:1-1
Autor:
Gabriel Moreno-Hagelsieb, Adriana Julián-Sánchez, Héctor Riveros-Rosas, Rosario A. Muñoz-Clares
Publikováno v:
Chemico-biological interactions. 304
Aldehyde dehydrogenases (ALDHs) comprise one of the most ancient protein superfamilies widely distributed in the three domains of life. Their members have been extensively studied in animals and plants, sorted out in different ALDH protein families a
Autor:
Héctor Riveros-Rosas, Rosario A. Muñoz-Clares, Lilian González-Segura, Adriana Julián-Sánchez
Publikováno v:
Chemico-Biological Interactions. 234:45-58
In the catalytic mechanism of hydrolytic aldehyde dehydrogenases (ALDHs) the role of Glu268 (mature human ALDH2 numbering) as a general base is of major relevance. Since Glu268 basicity depends on its protein environment, here we explore its interact
Autor:
Adriana Julián-Sánchez, Héctor Riveros-Rosas, Ángel G. Díaz-Sánchez, Rosario A. Muñoz-Clares, Lilian González-Segura
Publikováno v:
Chemico-Biological Interactions. 202:41-50
Potassium ions are non-essential activators of several aldehyde dehydrogenases (ALDHs), whereas a few others require the cation for activity. Two kinds of cation-binding sites, which we named intra-subunit and inter-subunit, have been observed in cry
Autor:
Adriana Julián-Sánchez, Héctor Riveros-Rosas, Rosario A. Muñoz-Clares, Ángel G. Díaz-Sánchez, Lilian González-Segura
Publikováno v:
Chemico-Biological Interactions. 202:51-61
Within the aldehyde dehydrogenase (ALDH) superfamily, proteins belonging to the ALDH9, ALDH10, ALDH25, ALDH26 and ALDH27 families display activity as ω-aminoaldehyde dehydrogenases (AMADHs). These enzymes participate in polyamine, choline and argini
Publikováno v:
PLoS ONE
PLoS ONE, Vol 11, Iss 11, p e0166851 (2016)
PLoS ONE, Vol 11, Iss 11, p e0166851 (2016)
Background Alcohol dehydrogenase (ADH) activity is widely distributed in the three domains of life. Currently, there are three non-homologous NAD(P)+-dependent ADH families reported: Type I ADH comprises Zn-dependent ADHs; type II ADH comprises short
Publikováno v:
Chemico-Biological Interactions. 191:14-25
Alcohol dehydrogenase (ADH) activity is widely distributed in all phyla. In animals, three non-homologous NAD(P)(+)-dependent ADH protein families are reported. These arose independently throughout evolution and possess different structures and mecha