Results 41 to 50 of about 4,213 (194)

Differential Effects of Mercurial on the Lipoyl Reductase and Diaphorase Activities of Lipoyl Dehydrogenase

open access: yesJournal of Biological Chemistry, 1966
Abstract The sensitivity of lipoyl dehydrogenase to phenylmercuric acetate, a reagent for —SH groups, has been investigated. Titration of available sulfhydryl groups in the enzyme brings about inactivation in the reduced diphosphopyridine nucleotide-lipoyl reductase activity, while activity with the artificial hydrogen acceptor 2,6-dichloroindophenol ...
L, Casola, V, Massey
openaire   +2 more sources

Glutarate regulates T cell metabolism and anti-tumour immunity [PDF]

open access: yes, 2023
T cell function and fate can be influenced by several metabolites: in some cases, acting through enzymatic inhibition of α-ketoglutarate-dependent dioxygenases, in others, through post-translational modification of lysines in important targets.
Antrobus, Robin   +16 more
core   +1 more source

Crystallographic snapshots of sulfur insertion by lipoyl synthase [PDF]

open access: yesProceedings of the National Academy of Sciences, 2016
Significance Lipoic acid, an enzyme cofactor in central metabolism and a livestock feed supplement, is produced on an industrial scale by a costly multistep synthesis. Nature makes lipoic acid in one step by the chemically challenging addition of two sulfur atoms to an inert fatty acid chain.
Lanz, Nicholas D.   +5 more
openaire   +3 more sources

Library of Apicomplexan Metabolic Pathways: a manually curated database for metabolic pathways of apicomplexan parasites. [PDF]

open access: yes, 2012
The Library of Apicomplexan Metabolic Pathways (LAMP, http://www.llamp.net) is a web database that provides near complete mapping from genes to the central metabolic functions for some of the prominent intracellular parasites of the phylum Apicomplexa ...
Gonzalez-Galarza, FF   +4 more
core   +1 more source

Crystal structure of lipoate‐bound lipoate ligase 1, LipL1, from Plasmodium falciparum [PDF]

open access: yes, 2017
Plasmodium falciparum lipoate protein ligase 1 (PfLipL1) is an ATP‐dependent ligase that belongs to the biotin/lipoate A/B protein ligase family (PFAM PF03099).
Afanador, Gustavo A.   +2 more
core   +1 more source

An Apicoplast Localized Ubiquitylation System Is Required for the Import of Nuclear-encoded Plastid Proteins

open access: yes, 2015
Apicomplexan parasites are responsible for numerous important human diseases including toxoplasmosis, cryptosporidiosis, and most importantly malaria.
Agrawal, Swati   +10 more
core   +1 more source

Defining Caenorhabditis elegans as a model system to investigate lipoic acid metabolism [PDF]

open access: yes, 2020
Lipoic acid (LA) is a sulfur-containing cofactor that covalently binds to a variety of cognate enzymes that are essential for redox reactions in all three domains of life.
de Mendoza, Diego   +2 more
core   +1 more source

Asymmetric Cu─N─Ru Bridgedsite Nanozyme‐Loaded Injectable Thermogel Boosts Cuproptosis‐Like Death for Multidrug‐Resistant Urinary Tract Infections

open access: yesAdvanced Science, EarlyView.
To address multidrug‐resistant urinary tract infections (MDR‐UTIs), we developed Cu‐ZIF8‐Ru nanozyme featuring an asymmetric Cu─N─Ru catalytic site. This unique structure enhances multienzyme‐mimetic activity, eradicating resistant bacteria by inducing a cuproptosis‐like death pathway through intracellular Cu2+ accumulation and energy depletion.
Guanlin Li   +9 more
wiley   +1 more source

Multifunctional H2S‐activated metal‐organic framework systems for targeted colorectal cancer imaging and synergistic copper‐induced tumor regression

open access: yesBMEMat, EarlyView.
The in situ reaction of Cu‐MOFs with endogenous H2S enabled PA imaging and facilitated combined PTT/chemotherapy for colorectal cancer therapy. Abstract Stimuli‐responsive nanomaterials offer significant potential for enhancing diagnostic accuracy, optimizing therapeutic efficacy, and advancing precision theranostics.
Nannan Zheng   +13 more
wiley   +1 more source

Evidence for two protein‐lipoylation activities in Escherichia coli [PDF]

open access: bronzeFEBS Letters, 1991
The lipoate acyltransferase subunits of the 2‐oxo acid dehydrogenase complexes are post‐translationally modified with one or more covalently‐bound lipoyl cofactors. Two distinct lipoate‐protein ligase activities, LPL‐A and LPL‐B, have been detected in E. coli by their ability to modify purified lipoyl apo‐domains of the bacterial pyruvate dehydrogenase
Dawn E. Brookfield   +4 more
openalex   +4 more sources

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