Results 131 to 140 of about 1,564 (203)
Background: Mitochondrial dysfunction and metabolic reprogramming can lead to the development and progression of hepatocellular carcinoma (HCC). Ferredoxin 1 (FDX1) is a small mitochondrial protein and recent studies have shown that FDX1 plays an ...
Bo Sun +6 more
doaj +1 more source
Moorella thermoacetica was long the only model organism used to study the biochemistry of acetogenesis from CO2. Depending on the growth substrate, this Gram-positive bacterium can either form H-2 or consume it.
Thauer, R. +3 more
core +1 more source
Exploring and Targeting the Connection of Iron and Copper Homeostasis to Neurodegenerative Diseases
Iron and copper dyshomeostasis, along with their interactions with key intrinsically disordered proteins (e.g., Aβ, tau, α‐synuclein) have a strong implication in the onset and progression of neurodegenerative diseases, including Alzheimer's disease (AD), Parkinson's disease (PD), Prion diseases (PrDs), Huntington's disease (HD), Wilson's disease (WD),
Xin Liu +9 more
wiley +1 more source
Cuproptosis, a copper-dependent distinct form of cell death, holds a critical role in tumor development. However, further investigation is needed to elucidate the impact of the cuproptosis signaling on thyroid cancer.
Shiyue He +3 more
doaj +1 more source
Formation of Fe-S clusters in apo-ferredoxin mediated by RIC.
A. UV-Visible spectra of ferredoxin upon incubation, under anaerobic conditions, of apo-ferredoxin (25 µM) with RIC (50 µM), IscS (2.5 µM), and L-cysteine (3 mM) for 15, 30 and 75 min (from bottom to top).
Peter Hildebrandt (373077) +6 more
core +1 more source
The Role of N6‐Methyladenosine Modification in Health and Disease
N6‐methyladenosine (m6A) is the most prevalent internal RNA modification in eukaryotes, acting as a pivotal epitranscriptomic regulator of RNA metabolism. This modification plays a dual role: it maintains physiological homeostasis under normal conditions but drives disease progression when dysregulated.
Linghuan Li +6 more
wiley +1 more source
Pyrococcus furiosus ferredoxin is a functional dimer
Pyrococcus furiosus ferredoxin is subject to a monomer/dimer equilibrium as a function of ionic strength. At physiological ionic strength, approximately 0.35 M NaCl, the protein is very predominantly homodimer.
Hagedoorn, P.L +5 more
core +1 more source
Structural Analysis and Inhibitor Modeling of Bacterioferritin From Brucella abortus
ABSTRACT Iron homeostasis in various pathogenic bacteria is regulated by bacterioferritins (Bfr) which function to store Fe3+ and release Fe2+ as needed for metabolic processes. The Bfr structure consists of 18 kDa subunits in which dimer pairs bind a heme molecule and are assembled into a highly symmetrical 24‐meric spherical structure with an ...
Lijun Liu +9 more
wiley +1 more source
Ferredoxin-Mediated Electron Transport and Photophosphorylation Reactions in Spinach Chloroplasts.
ATP synthesis and electron transport are measured in an aerobic reconstituted system of thylakoid membranes plus purified ferredoxin. Electron transport is supported by substrate levels of ferredoxin with oxygen as the terminal electron acceptor, or by ...
Hosler, Jonathan Paul
core
Kinetic Studies of a Ferredoxin-Dependent Cyanobacterial Nitrate Reductase
A flash photolysis study of electron transfer (ET) kinetics from reduced ferredoxin (photoreduced by Photosystem I) to the ferredoxin-dependent nitrate reductase from the cyanobacterium Synechococcus sp. PCC 7942 has been carried out.
David B. Knaff (1767325) +2 more
core +1 more source

