Results 1 to 10 of about 6,010 (138)

Heterologous production of active form of beta-lytic protease by Bacillus subtilis and improvement of staphylolytic activity by protein engineering

open access: yesMicrobial Cell Factories, 2021
Background Most of the proteases classified into the M23 family in the MEROPS database exhibit staphylolytic activity and have potential as antibacterial agents. The M23 family is further classified into two subfamilies, M23A and M23B.
Takahiro Hioki   +5 more
doaj   +1 more source

Towards a refined classification of class I dithiol glutaredoxins from poplar: biochemical basis for the definition of two subclasses

open access: yesFrontiers in Plant Science, 2013
Glutaredoxins (Grxs) are small oxidoreductases particularly specialized in the reduction of protein-glutathione adducts. Compared to other eukaryotic organisms, higher plants present an increased diversity of Grxs which are organized into four classes ...
Jérémy eCouturier   +5 more
doaj   +1 more source

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

Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]

open access: yes, 2014
Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog   +22 more
core   +1 more source

Richard Nelson Perham. 27 April 1937—14 February 2015 [PDF]

open access: yes, 2018
Richard Nelson Perham, FRS, FMedSci, FRSA, was a British professor of structural biochemistry. He undertook his academic career at the University of Cambridge, holding positions as lecturer, reader, chair and head of the Department of Biochemistry, as ...
Charoy, François   +6 more
core   +3 more sources

How are proteins reduced in the endoplasmic reticulum? [PDF]

open access: yes, 2018
The reversal of thiol oxidation in proteins within the endoplasmic reticulum (ER) is crucial for protein folding, degradation, chaperone function, and the ER stress response. Our understanding of this process is generally poor but progress has been made.
Bulleid, Neil   +2 more
core   +2 more sources

Review

open access: yes, 2020
The chalcogen elements oxygen, sulfur, and selenium are essential constituents of side chain functions of natural amino acids. Conversely, no structural and biological function has been discovered so far for the heavier and more metallic tellurium ...
Agh R   +13 more
core   +1 more source

Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]

open access: yes, 2010
The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian   +6 more
core   +3 more sources

Sn-Beta zeolites with borate salts catalyse the epimerization of carbohydrates via an intramolecular carbon shift [PDF]

open access: yes, 2012
Carbohydrate epimerization is an essential technology for the widespread production of rare sugars. In contrast to other enzymes, most epimerases are only active on sugars substituted with phosphate or nucleotide groups, thus drastically restricting ...
A Corma   +45 more
core   +1 more source

Dithiolopyrrolone Natural Products : Isolation, Synthesis and Biosynthesis [PDF]

open access: yes, 2013
Peer reviewedPublisher ...
Deng, Hai   +3 more
core   +2 more sources

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