Results 61 to 70 of about 6,425 (174)

Ectopic Expression of ScALDH21 From a Desert Moss Enhances Cotton Resistance to Verticillium Wilt via the Modulation of Jasmonates and Phenylpropanoid Pathways

open access: yesPlant Biotechnology Journal, Volume 24, Issue 8, Page 4916-4932, August 2026.
ABSTRACT Biotic stresses, particularly Verticillium wilt (VW), lead to a global decline in cotton yields. Here, we demonstrate that ectopic expression of ScALDH21, a gene from the desiccation‐tolerant moss Syntrichia caninervis Mitt. and absent in angiosperms, enhances cotton's resistance to VW.
Honglan Yang   +13 more
wiley   +1 more source

Electroenzymatic CO2 Fixation

open access: yesAngewandte Chemie International Edition, Volume 65, Issue 28, 6 July 2026.
Electroenzymatic CO2 fixation enables energy‐efficient, highly selective synthesis of complex molecules. Unlocking its full potential requires fundamental understanding of electrode‐coupled reductases and carboxylases. This review critically discusses available enzymes, product scope, and key thermodynamic and kinetic considerations, highlighting ...
Leonardo Castañeda‐Losada   +4 more
wiley   +1 more source

Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase [PDF]

open access: yes, 2006
J Biol Inorg Chem (2007) 12:353–366 DOI 10.1007/s00775-006-0191-9Two arsenite-inhibited forms of each of the aldehyde oxidoreductases from Desulfovibrio gigas and Desulfovibrio desulfuricans have been studied by X-ray crystallography and electron ...
Carlos D. Brondino   +15 more
core   +1 more source

Bioresponsive pseudoGlucosinolates (psGSLs) Release Isothiocyanates (ITCs) in the Presence of Nitroreductases

open access: yesChemistry – A European Journal, Volume 32, Issue 25, 2 July 2026.
This work introduces the concept of pseudoglucosinolates (psGSLs) and reports the synthesis and evaluation of nitroreductase‐responsive psGSLs. These compounds represent a complementary prodrug strategy to natural glucosinolates (GSLs) for the controlled release of isothiocyanates (ITCs), enabling bio‐responsive protein labeling, as demonstrated in ...
Claire C. Jimidar   +13 more
wiley   +1 more source

Additional file 1: Figure S1. of Genome and catabolic subproteomes of the marine, nutritionally versatile, sulfate-reducing bacterium Desulfococcus multivorans DSM 2059 [PDF]

open access: yes, 2016
Distribution of the 1,307 detected proteins by 2D DIGE, whole cell shotgun analysis and preparation of the membrane protein-enriched fraction of D. multivorans grown with 17 different substrates.
Michael Kube (41124)   +4 more
core   +1 more source

Aldose and aldehyde reductases: Correlation of molecular modeling and mass spectrometric studies on the binding of inhibitors to the active site [PDF]

open access: yes, 2000
Aldose and aldehyde reductases are monomeric NADPH-dependent oxidoreductases that catalyze the reduction of a wide variety of aldehydes and ketones to their corresponding alcohols.
Fletcher, Elisabeth V.   +6 more
core   +1 more source

In vitro oxidative metabolism of 6-mercaptopurine in human liver: insights into the role of the molybdoflavoenzymes aldehyde oxidase, xanthine oxidase, and xanthine dehydrogenase [PDF]

open access: yes, 2014
Anticancer agent 6-mercaptopurine (6MP) has been in use since 1953 for the treatment of childhood acute lymphoblastic leukemia (ALL) and inflammatory bowel disease.
Joswig-Jones, Carolyn A   +3 more
core   +1 more source

WOR5, a Novel Tungsten-Containing Aldehyde Oxidoreductase from Pyrococcus furiosus with a Broad Substrate Specificity [PDF]

open access: yes, 2005
WOR5 is the fifth and last member of the family of tungsten-containing oxidoreductases purified from the hyperthermophilic archaeon Pyrococcus furiosus.
Bevers, L.E. (author)   +11 more
core  

Mechanistic and structural studies of apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase At5g16970 [PDF]

open access: yes, 2006
In this study, we determined the crystal structures of the apoform, binary, and ternary complexes of the Arabidopsis alkenal double bond reductase encoded by At5g16970.
Harper, Athena R   +8 more
core   +1 more source

Mechanism of substrate and inhibitor binding of Rhodobacter capsulatus xanthine dehydrogenase [PDF]

open access: yes, 2009
Rhodobacter capsulatus xanthine dehydrogenase (XDH) is an (alpha beta)(2) heterotetrameric cytoplasmic enzyme that resembles eukaryotic xanthine oxidoreductases in respect to both amino acid sequence and structural fold.
Schulte, Antje   +6 more
core   +1 more source

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