Results 251 to 260 of about 212,981 (331)

Metagenomic Comparison of Bat Colony Resistomes Across Anthropogenic and Pristine Habitats. [PDF]

open access: yesAntibiotics (Basel)
Soto-López JD   +6 more
europepmc   +1 more source

Glutathione transferases.

Annual Review of Pharmacology and Toxicology, 2005
▪ Abstract  This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β ...
J. Hayes, J. Flanagan, I. Jowsey
semanticscholar   +4 more sources

Insect glutathione transferases and insecticide resistance

Insect Molecular Biology, 2005
Janet Hemingway, Hilary Ranson
exaly   +2 more sources

Glutathione Transferases and Cancer

Critical Reviews in Biochemistry and Molecular Biology, 1992
The glutathione transferases, a family of multifunctional proteins, catalyze the glutathione conjugation reaction with electrophilic compounds biotransformed from xenobiotics, including carcinogens. In preneoplastic cells as well as neoplastic cells, specific molecular forms of glutathione transferase are known to be expressed and have been known to ...
Shigeki Tsuchida, Kiyomi Sato
exaly   +3 more sources

“Plant Glutathione S-transferases: An overview”

, 2020
Summary Glutathione S-transferases (GST) belong to a super-family of multifunctional proteins and are one of the most important families of detoxifying enzymes in nature.
Ingrid Hernández Estévez   +1 more
semanticscholar   +1 more source

The role of glutathione S-transferases (GSTs) in insecticide resistance in crop pests and disease vectors.

Current Opinion in Insect Science, 2018
Insecticide resistance seriously threatens efficient arthropod pest management. Arthropod glutathione S-transferases (GSTs) confer resistance via direct metabolism or sequestration of chemicals, but also indirectly by providing protection against ...
N. Pavlidi, J. Vontas, T. van Leeuwen
semanticscholar   +1 more source

Glucosyl transferase activity of bovine galactosyl transferase

Biochimica et Biophysica Acta (BBA) - General Subjects, 1978
Bovine galactosyl transferase was found to utilize UDPglucose as a substrate and elicit disaccharide biosynthesis with glucose and N-acetylglucosamine as acceptors. The relative rate of glucosyl transferase with N-acetylglucosamine as acceptor was 0.3%, the rate for N-acetyllactosamine biosynthesis.
P J, Andree, L J, Berliner
openaire   +2 more sources

Transferases in Biocatalysis:

2020
Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity.
openaire   +3 more sources

Electron Transferases

2014
The flavin isoalloxazine ring in electron transferases functions in a redox capacity, being able to take up electrons from a donor to subsequently deliver them to an acceptor. The main characteristics of these flavoproteins, including their unique ability to mediate obligatory processes of two-electron transfers with those involving single-electron ...
Patricia, Ferreira   +2 more
openaire   +2 more sources

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