Results 11 to 20 of about 6,010 (138)

Cryo-EM reveals an ensemble of cytochrome P450 reductase conformations in solution. [PDF]

open access: yesProtein Sci
Abstract The eukaryotic electron transport system, mediated by cytochrome P450 reductase (CPR), plays a crucial role in driving myriads of reactions involved in the biosynthesis of physiologically active compounds (such as sterols, steroids, vitamins, and natural products), as well as in the metabolism of drugs, toxins, and carcinogens.
Lepesheva GI, Hargrove TY, Ren Y.
europepmc   +2 more sources

Protein disulphide isomerase-assisted functionalization of proteinaceous substrates [PDF]

open access: yes, 2012
Protein disulphide isomerase (PDI) is an enzyme that catalyzes thiol-disulphide exchange reactions among a broad spectrum of substrates, including proteins and low-molecular thiols and disulphides.
Anfinsen CB   +143 more
core   +1 more source

The mucin-degradation strategy of Ruminococcus gnavus:The importance of intramolecular trans-sialidases [PDF]

open access: yes, 2016
We previously identified and characterized an intramolecular trans-sialidase (IT-sialidase) in the gut symbiont Ruminococcus gnavus ATCC 29149, which is associated to the ability of the strain to grow on mucins. In this work we have obtained and analyzed
Crossman, Lisa C.   +6 more
core   +2 more sources

Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]

open access: yes, 2017
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J.   +3 more
core   +1 more source

Promiscuous Substrate-Binding explains the Enzymatic stereo and Regiocontrolled Synthesis of Enantiopure Hydroxy Ketones and Diols [PDF]

open access: yes, 2009
Financial support from the Spanish Ministerio de Ciencia e Innovación (MICINN, Project CTQ2007-61126) and the Spanish Ministerio de Asuntos Exteriores y de Cooperación (Programa de Cooperación Interuniversitaria, PCI Iberoamérica MAEC-AECID, Project A ...
Bennet   +51 more
core   +2 more sources

Electron Transfer Pathways and Dynamics of Chloroplast NADPH-dependent Thioredoxin Reductase C (NTRC) [PDF]

open access: yes, 2012
NADPH-dependent thioredoxin reductases (NTRs) contain a flavin cofactor and a disulfide as redox-active groups. The catalytic mechanism of standard NTR involves a large conformational change between two configurations.
Bernal Bayard, Pilar   +3 more
core   +1 more source

Members of the chloride intracellular ion channel protein family demonstrate glutaredoxin-like enzymatic activity [PDF]

open access: yes, 2015
© 2015 Al Khamici et al. The Chloride Intracellular Ion Channel (CLIC) family consists of six evolutionarily conserved proteins in humans. Members of this family are unusual, existing as both monomeric soluble proteins and as integral membrane proteins ...
Brown, LJ   +11 more
core   +1 more source

Oxidative protein folding in the mitochondrial intermembrane space [PDF]

open access: yes, 2010
Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB   +4 more
core   +1 more source

New Perspectives Related to the Bioluminescent System in Dinoflagellates: Pyrocystis lunula, a Case Study [PDF]

open access: yes, 2020
Pyrocystis lunula is considered a model organism due to its bioluminescence capacity linked to circadian rhythms. The mechanisms underlying the bioluminescent phenomenon have been well characterized in dinoflagellates; however, there are still some ...
Costas, Benjamin   +6 more
core   +1 more source

The role of peroxiredoxins in cancer [PDF]

open access: yes, 2017
Peroxiredoxins (PRDXs) are a ubiquitously expressed family of small (22-27 kDa) non-seleno peroxidases that catalyze the peroxide reduction of H2O2, organic hydroperoxides and peroxynitrite.
CAPALBO, CARLO   +4 more
core   +1 more source

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