Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Hydroxyacylglutathione hydrolase"'
Autor:
Wu, Zhexue1, Shon, Jong1, Lee, Doohyun1, Park, Kab-Tae1, Park, Chang2, Lee, Taeho1, Lee, Hye3 sianalee@catholic.ac.kr, Liu, Kwang-Hyeon1 dstlkh@gmail.com
Publikováno v:
Analytical & Bioanalytical Chemistry. Mar2016, Vol. 408 Issue 8, p2069-2082. 14p.
Autor:
Mezzar, Serena1, De Schryver, Evelyn1, Asselberghs, Stanny1, Meyhi, Els1, Morvay, Petruta L.1, Baes, Myriam2, Van Veldhoven, Paul P.1 paul.vanveldhoven@med.kuleuven.be
Publikováno v:
BBA - Molecular & Cell Biology of Lipids. Sep2017, Vol. 1862 Issue 9, p972-990. 19p.
Publikováno v:
BMC Genomics; 3/15/2016, Vol. 17, p1-17, 17p, 1 Diagram, 5 Charts, 7 Graphs
Autor:
Marwa O. Mikati, Yasaman Barekatain, Damon M. Osbourn, Carey-Ann D. Burnham, Rachel L. Edwards, Victoria C. Yan, Cynthia S. Dowd, Florian L. Muller, Naomi Ghebremichael, Justin J. Miller, Kenneth M. Heidel, Audrey R. Odom John, Ishaan T. Shah
Publikováno v:
ACS Infect Dis
With the rising prevalence of multidrug-resistance, there is an urgent need to develop novel antibiotics. Many putative antibiotics demonstrate promising in vitro potency but fail in vivo due to poor drug-like qualities (e.g. serum half-life, oral ab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da808b9eb618297e0a5c7d55b8690ea8
https://doi.org/10.1101/2020.07.23.214460
https://doi.org/10.1101/2020.07.23.214460
Publikováno v:
Biochemistry and Biophysics Reports
Biochemistry and Biophysics Reports, Vol 28, Iss, Pp 101138-(2021)
Biochemistry and Biophysics Reports, Vol 28, Iss, Pp 101138-(2021)
Objective Hydroxyacylglutathione hydrolase (aka as GLO-2) is a component of the glyoxalase pathway involved in the detoxification of the reactive oxoaldehydes, glyoxal and methylglyoxal. These reactive metabolites have been linked to a variety of pat
Autor:
John O. Marentette, James R. Roede, Anne Mette Schou Oxvig, James J. Galligan, Eli Chapman, David Spiegel, Matthew D. Streeter, Colin C. Anderson, Mogens Johannsen, Taoda Shi, Erin Q. Jennings, Dominique O. Gaffney
Publikováno v:
Cell Chem Biol
Gaffney, D O, Jennings, E Q, Anderson, C C, Marentette, J O, Shi, T, Schou Oxvig, A M, Streeter, M D, Johannsen, M, Spiegel, D A, Chapman, E, Roede, J R & Galligan, J J 2020, ' Non-enzymatic Lysine Lactoylation of Glycolytic Enzymes ', Cell Chemical Biology, vol. 27, no. 2, pp. 206-213.e6 . https://doi.org/10.1016/j.chembiol.2019.11.005
Gaffney, D O, Jennings, E Q, Anderson, C C, Marentette, J O, Shi, T, Schou Oxvig, A M, Streeter, M D, Johannsen, M, Spiegel, D A, Chapman, E, Roede, J R & Galligan, J J 2020, ' Non-enzymatic Lysine Lactoylation of Glycolytic Enzymes ', Cell Chemical Biology, vol. 27, no. 2, pp. 206-213.e6 . https://doi.org/10.1016/j.chembiol.2019.11.005
Post-translational modifications (PTMs) regulate enzyme structure and function to expand the functional proteome. Many of these PTMs are derived from cellular metabolites and serve as feedback and feedforward mechanisms of regulation. We have identif
Autor:
Carla Emiliani, Luca Massaccesi, Giovanni Principato, Roberta Galeazzi, Laura Cianfruglia, Adolfo Amici, Lorena Urbanelli, Andrea Scirè, Francesco Piva, Tatiana Armeni, Luisa Ercolani
Publikováno v:
Cell Biochemistry and Function. 34:620-627
Glyoxalase II, the second of 2 enzymes in the glyoxalase system, is a hydroxyacylglutathione hydrolase that catalyses the hydrolysis of S-d-lactoylglutathione to form d-lactic acid and glutathione, which is released from the active site. The tripepti
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Publikováno v:
European Child & Adolescent Psychiatry. 24:75-82
The prevalence of the autism spectrum disorder (ASD) was recently estimated to 1 in 88 children by the CDC MMWR. In up to 25 % of the cases, the genetic cause can be identified. Past studies identified increased level of advanced glycation end produc
Publikováno v:
Biochemical Society Transactions. 42:419-424
Molecular, catalytic and structural properties of glyoxalase pathway enzymes of many species are now known. Current research has focused on the regulation of activity and expression of Glo1 (glyoxalase I) and Glo2 (glyoxalase II) and their role in he