Structural biology of ferritin nanocages
FEBS Letters, EarlyView.Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley +1 more source
Energies, 2022 The suitability of sewage-sludge derived washing agents (SS_WAs) (dissolved organic matter DOM; humic-like substances HLS; soluble humic substances SHS), was assessed for removing Cd from highly contaminated (300 mg/kg) sandy clay loam and clay.
Barbara K. Klik +2 more
doaj +1 more source
Glutamate biosynthesis in Bacillus azotofixans. 15N NMR and enzymatic studies [PDF]
, 1988 Pathways of ammonia assimilation into glutamic acid in Bacillus azotofixans, a recently characterized nitrogen-fixing species of Bacillus, were investigated through observation by NMR spectroscopy of in vivo incorporation of 15N into glutamine and ...
Kanamori, Keiko +2 more
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Solution structure of a bacterial microcompartment targeting peptide and its application in the construction of an ethanol bioreactor [PDF]
, 2014 Targeting of proteins to bacterial microcompartments (BMCs) is mediated by an 18-amino-acid peptide sequence. Herein, we report the solution structure of the N-terminal targeting peptide (P18) of PduP, the aldehyde dehydrogenase associated with the 1,2 ...
Brown, Ian R. +10 more
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Identification of 3-deoxyglucosone dehydrogenase as aldehyde dehydrogenase 1A1 (retinaldehyde dehydrogenase 1) [PDF]
Biochimie, 2007 One of the metabolic fates of 3-deoxyglucosone, a product of protein deglycation and a potent glycating agent, is to be oxidized to 2-keto-3-deoxygluconate, but the enzyme that catalyzes this reaction is presently unknown. Starting from human erythrocytes, which are known to convert 3-deoxyglucosone to 2-keto-3-deoxygluconate, we have purified to near ...
Collard, François +4 more
openaire +3 more sources
Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
FEBS Letters, EarlyView.Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz +11 more
wiley +1 more source
FEBS Letters, EarlyView.Mitochondrial remodeling shapes neural and glial lineage progression by matching metabolic supply with demand. Elevated OXPHOS supports differentiation and myelin formation, while myelin compaction lowers mitochondrial dependence, revealing mitochondria as key drivers of developmental energy adaptation.
Sahitya Ranjan Biswas +3 more
wiley +1 more source
Effect of ZnO Nanoparticles on Growth and Biochemical Responses of Wheat and Maize
Plants, 2021 Zinc is an essential element that is also renowned for widespread contamination and toxicity at high concentrations. The present study was carried out to analyze the responses induced by lower, as well as higher, doses of zinc (0–200 mg/L), in the form ...
Akansha Srivastav +7 more
doaj +1 more source
Sheep liver cytosolic aldehyde dehydrogenase : a fresh perspective : a thesis presented in partial fulfilment of the requirements for the degree of Master of Science in Chemistry at Massey University, New Zealand [PDF]
, 1995 The pre-steady-state mechanism of aldehyde dehydrogenase has been further investigated using synthesised deuterated 4-trans-(N,N-dimethylamino) cinnamaldehyde as a substrate.
Sime, Richard Malcolm
core
Functional studies on oligotropha carboxidovorans molybdenum–copper CO dehydrogenase produced in escherichia coli [PDF]
, 2018 The Mo/Cu-dependent CO dehydrogenase (CODH) from Oligotropha carboxidovorans is an enzyme that is able to catalyze both the oxidation of CO to CO2 and the oxidation of H2 to protons and electrons. Despite the close to atomic resolution structure (1.1 Å),
Duffus, Benjamin R. +3 more
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