Results 51 to 60 of about 196,977 (320)

Temperature Fluctuations Affected the Activity of Triosephosphate Isomerase by Regulating Phosphorylation and Nitrosylation [PDF]

open access: yesShipin Kexue
In this study, triosephosphate isomerase was incubated in the presence of exogenous protein kinase A and S-nitrosoglutathione to elucidate the regulatory effects of phosphorylation and nitrosylation on the enzyme’s activity as a function of incubation ...
WU Saisai, WANG Zhenyu, BAI Yuqiang, HOU Chengli, RAO Weili, LI Xin, ZHANG Zhisheng, ZHANG Dequan
doaj   +1 more source

Structure-based directed evolution improves S. cerevisiae growth on xylose by influencing in vivo enzyme performance

open access: yesBiotechnology for Biofuels, 2020
Background Efficient bioethanol production from hemicellulose feedstocks by Saccharomyces cerevisiae requires xylose utilization. Whereas S. cerevisiae does not metabolize xylose, engineered strains that express xylose isomerase can metabolize xylose by ...
Misun Lee   +4 more
doaj   +1 more source

NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase. [PDF]

open access: yes, 2016
We cordially thank Alma Rute for excellent technical assistance and the DFG (GRK 1431-1 and 1431-2) for financial support (PB). We thank the Microscope and Histology Facility of the University of Aberdeen for providing their equipment.
Bayer, Peter   +5 more
core   +2 more sources

Cytosolic redox components regulate protein homeostasis via additional localisation in the mitochondrial intermembrane space [PDF]

open access: yes, 2017
Oxidative protein folding is confined to the bacterial periplasm, endoplasmic reticulum and the mitochondrial intermembrane space. Maintaining a redox balance requires the presence of reductive pathways.
Cardenas-Rodriguez, Mauricio   +1 more
core   +1 more source

Production of a recombinant membrane protein in an Escherichia coli strain for the whole cell biosynthesis of phenylacetic acids

open access: yesBiotechnology Reports, 2015
The styrene oxide isomerase (SOI) represents a membrane-bound enzyme of the microbial styrene degradation pathway and has been discussed as promising biocatalyst. It catalyzes the isomerization of styrene oxide to phenylacetaldehyde. In this study a styC
Michel Oelschlägel   +3 more
doaj   +1 more source

The Construction of a Prognostic Model Based on a Peptidyl Prolyl Cis–Trans Isomerase Gene Signature in Hepatocellular Carcinoma

open access: yesFrontiers in Genetics, 2021
Objective: The aim of the present study was to construct a prognostic model based on the peptidyl prolyl cis–trans isomerase gene signature and explore the prognostic value of this model in patients with hepatocellular carcinoma.Methods: The ...
Huadi Shi   +6 more
doaj   +1 more source

Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]

open access: yes, 2016
Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the ...
Altieri, Fabio   +7 more
core   +1 more source

Characterization of the microsomal steroid-8-ene isomerase of cholesterol biosynthesis.

open access: yesJournal of Lipid Research, 1978
Rat liver microsomes contain an enzyme that catalyzes the isomerization of the nuclear double bond of steroids from the 8(9) position to the 7(8) position.
N Yamaga, J L Gaylor
doaj   +1 more source

Protein disulphide isomerase [PDF]

open access: yesCurrent Biology, 2003
What is it? Protein disulphide isomerase is an enzyme with two interrelated activities: as an oxidoreductase, it can catalyse the formation, reduction and isomerisation of disulphide bonds; and as a polypeptide binding protein, it can function as a molecular chaperone which assists the folding of polypeptides.
openaire   +2 more sources

Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy

open access: yesScientific Reports, 2015
Protein disulfide isomerase (PDI) family members including PDI and ERp57 emerge as novel targets for anti-thrombotic treatments, but chemical agents with selectivity remain to be explored.
G. Cui   +13 more
semanticscholar   +1 more source

Home - About - Disclaimer - Privacy