Results 61 to 70 of about 553,570 (305)
Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral [PDF]
Proceedings of the National Academy of Sciences, 2003 Iron is concentrated in ferritin, a spherical protein with a capacious cavity for ferric nanominerals of <4,500 Fe atoms. Global ferritin structure is very stable, resisting 6 M urea and heat (85°C) at neutral pH. Eight pores, each formed by six helices from 3 of the 24 polypeptide subunits, restrict mineral access to reductant,
Xiaofeng, Liu +2 more
openaire +2 more sources
Characterization of Fe-S Clusters in Proteins by Mӧssbauer Spectroscopy
, 2021 57Fe Mӧssbauer spectroscopy is unparalleled in the study of Fe-S cluster-containing proteins because of its unique ability to detect all forms of iron. Enrichment of biological samples with the 57Fe isotope and manipulation of experimental parameters such as temperature and magnetic field allow for elucidation of the number of Fe-S clusters present in ...
Ueda, Chie +2 more
openaire +2 more sources
Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae [PDF]
Biochemical Journal, 1998 Investigation of the interaction of MgADP- and MgATP2- with the Fe protein of Klebsiella pneumoniae nitrogenase by 31P NMR showed that the adenine nucleotides are reversibly bound in slow exchange with free nucleotides. Dissociation of the MgADP-–Fe protein complex was slow enough to enable its isolation by gel filtration, thus permitting the ...
R W, Miller +4 more
openaire +2 more sources
Therapeutic Apheresis and Dialysis, EarlyView.ABSTRACT Objective To compare the efficacy and safety of roxarestat versus recombinant human erythropoietin (rhEPO) in the management of renal anemia in patients undergoing maintenance hemodialysis. Methods This was a prospective, open‐label, randomized controlled trial.
Lingling Chen, Junjie Zhu, Qiaonan Ge
wiley +1 more source
Poultry Science, 2023 : The Korat chicken (KR) is a slow-growing Thai chicken breed with relatively poor feed efficiency (FE) but very tasty meat with high protein and low fat contents, and a unique texture.
Pramin Kaewsatuan +6 more
doaj +1 more source
Fe/S protein biogenesis in trypanosomes — A review
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2015 Trypanosoma brucei, the causative agent of the African sleeping sickness of humans, and other kinetoplastid flagellates belong to the eukarytotic supergroup Excavata. This early-branching model protist is known for a broad range of unique features. As it is amenable to most techniques of forward and reverse genetics, T.
Lukeš, Julius, Basu, Somsuvro
openaire +2 more sources
Mapping the evolution of mitochondrial complex I through structural variation
FEBS Letters, EarlyView.Respiratory complex I (CI) is crucial for bioenergetic metabolism in many prokaryotes and eukaryotes. It is composed of a conserved set of core subunits and additional accessory subunits that vary depending on the organism. Here, we categorize CI subunits from available structures to map the evolution of CI across eukaryotes. Respiratory complex I (CI)
Dong‐Woo Shin +2 more
wiley +1 more source
Antioxidants, 2021 Glutaredoxins (GRXs) are thioredoxin superfamily members exhibiting thiol-disulfide oxidoreductase activity and/or iron-sulfur (Fe-S) cluster binding capacities. These properties are determined by specific structural factors.
Thomas Roret +9 more
doaj +1 more source
Multiple QTL-effects of wheat Gpc-B1 locus on grain protein and micronutrient concentrations [PDF]
, 2007 Micronutrient malnutrition afflicts over three billion peopleworldwide and the numbers are continuously increasing. Developing genetically micronutrientenriched cereals, which are the predominant source of human dietary, is essential to alleviate ...
Asher CJ +22 more
core +1 more source
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