Results 11 to 20 of about 90,505 (292)

RETINENE ISOMERASE [PDF]

open access: greenThe Journal of General Physiology, 1956
Rhodopsin is formed by the condensation of opsin with a cis isomer of retinene, called neo-b. The bleaching of rhodopsin releases all-trans retinene which must be isomerized back to neo-b in order for rhodopsin to regenerate. Both retinene isomers are in equilibrium with the corresponding isomers of vitamin A, through the alcohol dehydrogenase system.
Ruth Hubbard
openalex   +3 more sources

Tetraoxypteridine Isomerase

open access: hybridJournal of Biological Chemistry, 1964
Walter S. McNutt, Shridhar P. Damle
openalex   +3 more sources

Studies on Glucose Isomerase of Bacteria

open access: bronzeAgricultural and Biological Chemistry, 1964
A bacterial strain, HN-56, having an activity of d-glucose isomerization was isolated from soil, and was identified to be similar to Aerobacter aerogenes (Kruse) Beijerink. d-Glucose-isomerizing activity was induced when HN-56 was precultured in the media containing d-xylose, d-mannose, lactate, especially d-mannitol.
Masato Natake, Sadahiko Yoshimura
  +8 more sources

Vascular thiol isomerases [PDF]

open access: yesBlood, 2016
AbstractThiol isomerases are multifunctional enzymes that influence protein structure via their oxidoreductase, isomerase, and chaperone activities. These enzymes localize at high concentrations in the endoplasmic reticulum of all eukaryotic cells where they serve an essential function in folding nascent proteins.
Robert Flaumenhaft, Bruce Furie
openaire   +3 more sources

Human Triosephosphate Isomerase Is a Potential Target in Cancer Due to Commonly Occurring Post-Translational Modifications

open access: yesMolecules, 2023
Cancer involves a series of diseases where cellular growth is not controlled. Cancer is a leading cause of death worldwide, and the burden of cancer incidence and mortality is rapidly growing, mainly in developing countries. Many drugs are currently used,
Sergio Enríquez-Flores   +5 more
doaj   +1 more source

Glutathione Transferases as Efficient Ketosteroid Isomerases

open access: yesFrontiers in Molecular Biosciences, 2021
In addition to their well-established role in detoxication, glutathione transferases (GSTs) have other biological functions. We are focusing on the ketosteroid isomerase activity, which appears to contribute to steroid hormone biosynthesis in mammalian ...
Bengt Mannervik   +4 more
doaj   +1 more source

Comparing the xylose reductase/xylitol dehydrogenase and xylose isomerase pathways in arabinose and xylose fermenting Saccharomyces cerevisiae strains

open access: yesBiotechnology for Biofuels, 2008
Background Ethanolic fermentation of lignocellulosic biomass is a sustainable option for the production of bioethanol. This process would greatly benefit from recombinant Saccharomyces cerevisiae strains also able to ferment, besides the hexose sugar ...
Hahn-Hägerdal Bärbel   +2 more
doaj   +1 more source

The NADPH oxidase NOX4 regulates redox and metabolic homeostasis preventing HCC progression

open access: yesHepatology, EarlyView., 2022
Loss of NOX4 in HCC tumor cells induces metabolic reprogramming in a Nrf2/MYC‐dependent manner to promote HCC progression. Abstract Background and Aims The NADPH oxidase NOX4 plays a tumor‐suppressor function in HCC. Silencing NOX4 confers higher proliferative and migratory capacity to HCC cells and increases their in vivo tumorigenic potential in ...
Irene Peñuelas‐Haro   +14 more
wiley   +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

Protein disulphide isomerase inhibition as a potential cancer therapeutic strategy

open access: yesCancer Medicine, 2021
The protein disulphide isomerase (PDI) gene family is a large, diverse group of enzymes recognised for their roles in disulphide bond formation within the endoplasmic reticulum (ER).
Lauren E. Powell, Paul A. Foster
doaj   +1 more source

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