Results 51 to 60 of about 186,109 (312)

Single‐Molecule Force Spectroscopy Reveals Stability of mitoNEET and its [2Fe2Se] Cluster in Weakly Acidic and Basic Solutions

open access: yesChemistryOpen, 2022
The outer mitochondrial membrane protein mitoNEET (mNT) is a recently identified iron‐sulfur protein containing a unique Fe2S2(His)1(Cys)3 metal cluster with a single Fe−N(His87) coordinating bond.
Jing‐Yuan Nie   +3 more
doaj   +1 more source

Switching on Endogenous Metal Binding Proteins in Parkinson’s Disease

open access: yesCells, 2019
The formation of cytotoxic intracellular protein aggregates is a pathological signature of multiple neurodegenerative diseases. The principle aggregating protein in Parkinson’s disease (PD) and atypical Parkinson’s diseases is α ...
Fleur A. McLeary   +7 more
doaj   +1 more source

STUDIES ON IRON-PROTEIN METABOLISM WITH RADIOIRON (Fe-55 and Fe-59)

open access: yesThe Japanese Journal of Physiology, 1955
1. In the control group, the turnover rate of hemoglobin radioiron was higher than the appearance of ferritin radioiron in tissues.2. In tne early stage of the acute hemolytic anemia group, the turnover rate of hemoglobin radioiron was higher than the control group and disappearance of hemoglobin radioiron also faster.3.
openaire   +3 more sources

Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral [PDF]

open access: yesProceedings 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

Sulfur Administration in Fe–S Cluster Homeostasis

open access: yesAntioxidants, 2021
Mitochondria are the key organelles of Fe–S cluster synthesis. They contain the enzyme cysteine desulfurase, a scaffold protein, iron and electron donors, and specific chaperons all required for the formation of Fe–S clusters.
Leszek Rydz   +2 more
doaj   +1 more source

Transferrin receptor 1‐mediated iron uptake supports thermogenic activation in human cervical‐derived adipocytes

open access: yesFEBS Letters, EarlyView.
In this study, we found that human cervical‐derived adipocytes maintain intracellular iron level by regulating the expression of iron transport‐related proteins during adrenergic stimulation. Melanotransferrin is predicted to interact with transferrin receptor 1 based on in silico analysis.
Rahaf Alrifai   +9 more
wiley   +1 more source

Nucleotide binding by the nitrogenase Fe protein: a 31P NMR study of ADP and ATP interactions with the Fe protein of Klebsiella pneumoniae [PDF]

open access: yesBiochemical 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

Reciprocal allosteric modulation of carbon monoxide and warfarin binding to ferrous human serum heme-albumin. [PDF]

open access: yesPLoS ONE, 2013
Human serum albumin (HSA), the most abundant protein in human plasma, could be considered as a prototypic monomeric allosteric protein, since the ligand-dependent conformational adaptability of HSA spreads beyond the immediate proximity of the binding ...
Alessio Bocedi   +10 more
doaj   +1 more source

Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of Chlamydomonas reinhardtii Glutaredoxin 2

open access: yesAntioxidants, 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

Structural insights into an engineered feruloyl esterase with improved MHET degrading properties

open access: yesFEBS Letters, EarlyView.
A feruloyl esterase was engineered to mimic key features of MHETase, enhancing the degradation of PET oligomers. Structural and computational analysis reveal how a point mutation stabilizes the active site and reshapes the binding cleft, expading substrate scope.
Panagiota Karampa   +5 more
wiley   +1 more source

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