Results 21 to 30 of about 12,847 (298)

Proline Isomerization: From the Chemistry and Biology to Therapeutic Opportunities

open access: yesBiology, 2023
Proline isomerization, the process of interconversion between the cis- and trans-forms of proline, is an important and unique post-translational modification that can affect protein folding and conformations, and ultimately regulate protein functions and
Deepti Gurung   +5 more
doaj   +1 more source

Peptidyl-prolyl isomerases : A full cast of critical actors in cardiovascular diseases [PDF]

open access: yes, 2015
Peptidyl-prolyl cis-trans-isomerases are a highly conserved family of immunophilins. The three peptidyl-prolyl cis-trans-isomerase subfamilies are cyclophilins, FK-506-binding proteins, and parvulins. Peptidyl-prolyl cis-trans-isomerases are expressed in
G.L. Perrucci   +5 more
core   +1 more source

RETINENE ISOMERASE [PDF]

open access: yesThe 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.
openaire   +2 more sources

Overcoming the thermodynamic equilibrium of an isomerization reaction through oxidoreductive reactions for biotransformation

open access: yesNature Communications, 2019
A desired product cannot be obtained at higher concentration than its equilibrium concentration when isomerases are used for biotransformation. Here, the authors engineer in vivo oxidoreductive reactions in yeast to overcome the equilibrium limitation of
Jing-Jing Liu   +7 more
doaj   +1 more source

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   +2 more sources

The importance of arginine codons AGA and AGG for the expression in E. coli of triosephosphate isomerase from seven different species

open access: yesBiotechnology Reports, 2017
Rare arginine codons AGA and AGG affect the heterologous expression of proteins in Eschericha coli. The tRNAs necessary for protein synthesis are scarce in E. coli strain BL21(DE3) pLysS and plentiful in strain BL21(DE3) CodonPlus −RIL.
Beatriz Aguirre-López   +4 more
doaj   +1 more source

Introduction to Peptidyl-Prolyl cis/trans Isomerase (PPIase) Series

open access: yesBiomolecules, 2019
About 30 years after the discovery of peptidyl-prolyl cis/trans isomerases (PPIases), research on this group of proteins has become somewhat calmer than it used to be, but it still generates lots of interest [...]
Andrzej Galat
doaj   +1 more source

Molecular Chaperones in Cancer Stem Cells: Determinants of Stemness and Potential Targets for Antitumor Therapy

open access: yesCells, 2020
Cancer stem cells (CSCs) are a great challenge in the fight against cancer because these self-renewing tumorigenic cell fractions are thought to be responsible for metastasis dissemination and cases of tumor recurrence. In comparison with non-stem cancer
Alexander Kabakov   +2 more
doaj   +1 more source

Three unrelated and unexpected amino acids determine the susceptibility of the interface cysteine to a sulfhydryl reagent in the triosephosphate isomerases of two trypanosomes. [PDF]

open access: yesPLoS ONE, 2018
Proteins with great sequence similarity usually have similar structure, function and other physicochemical properties. But in many cases, one or more of the physicochemical or functional characteristics differ, sometimes very considerably, among these ...
Selma Díaz-Mazariegos   +2 more
doaj   +1 more source

Artificial disulfide isomerases and uses thereof [PDF]

open access: yes, 2007
The present invention provides artificial enzymes comprising, e.g., an N-terminal domain derived from E. coli FkpA that allows for dimerization and provides a substrate binding region, and a C-terminal thioredoxin domain derived from E.
Georgiou, George M., Segatori, Laura
core   +1 more source

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