Results 61 to 70 of about 212,981 (331)

Plant glutathione transferases

open access: yesGenome Biology, 2002
SummaryThe soluble glutathione transferases (GSTs, EC 2.5.1.18) are encoded by a large and diverse gene family in plants, which can be divided on the basis of sequence identity into the phi, tau, theta, zeta and lambda classes.
D. Dixon, A. Lapthorn, R. Edwards
semanticscholar   +1 more source

Mutant p53R273H disrupts PDPK1 homodimerization and contributes to PDPK1 activation

open access: yesMolecular Oncology, EarlyView.
How mutant p53R273H drives AKT signaling is unclear. We show that p53R273H, but not wild‐type, directly binds PDPK1 via a mutation‐dependent conformational change. This interaction disrupts inhibitory PDPK1 homodimerization and enhances AKT phosphorylation.
Mei Chee Lim   +11 more
wiley   +1 more source

Regulation of Signal Transduction by Glutathione Transferases

open access: yesInternational Journal of Hepatology, 2012
Glutathione transferases (GST) are essentially known as enzymes that catalyse the conjugation of glutathione to various electrophilic compounds such as chemical carcinogens, environmental pollutants, and antitumor agents.
Julie Pajaud   +4 more
doaj   +1 more source

Conserved sequence motifs in human TMTC1, TMTC2, TMTC3, and TMTC4, new O-mannosyltransferases from the GT-C/PMT clan, are rationalized as ligand binding sites

open access: yesBiology Direct, 2021
Background The human proteins TMTC1, TMTC2, TMTC3 and TMTC4 have been experimentally shown to be components of a new O-mannosylation pathway. Their own mannosyl-transferase activity has been suspected but their actual enzymatic potential has not been ...
Birgit Eisenhaber   +6 more
doaj   +1 more source

Versatile vector tools for efficient protein screening across multiple expression systems

open access: yesFEBS Open Bio, EarlyView.
A unified vector toolkit enables rapid protein expression screening across E. coli, insect, and mammalian cells. A single primer pair amplifies the target gene, which is inserted into any vector via a standardized interface. This streamlined workflow eliminates repeated cloning steps, accelerating the identification of optimal expression conditions for
Zhimin Zhu   +5 more
wiley   +1 more source

Genetic Polymorphisms of Glutathione S-Transferases T1 (GSTT1) and M1 (GSTM1) in Iranian Mandaeans Population

open access: yesIranian Journal of Public Health, 2019
Genetic Polymorphisms of Glutathione S-Transferases T1 (GSTT1) and M1 (GSTM1) in Iranian Mandaeans ...
Fariba BOROUMAND   +2 more
doaj   +1 more source

Heterotropic regulation and negative homotropic cooperativity

open access: yesFEBS Open Bio, EarlyView.
We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea   +5 more
wiley   +1 more source

Structure and functions of glutathione transferases

open access: yesThe Ukrainian Biochemical Journal, 2014
Data about classification, nomenclature, structure, substrate specificity and role of many glutathione transferase’s isoenzymes in cell functions have been summarised. The enzyme has been discovered more than 50 years ago.
O. M. Fedets
doaj   +1 more source

The Phosphopantetheinyl Transferases: Catalysis of a Posttranslational Modification Crucial for Life

open access: yesNatural product reports (Print), 2014
Although holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark paper by Lambalot et al.
Joris Beld   +4 more
semanticscholar   +1 more source

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

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