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Iron-Sulfur Proteins

A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
Also Known As:
Iron Sulfur Proteins; Iron Sulfur Protein; Protein, Iron-Sulfur; Proteins, Iron Sulfur; Proteins, Iron-Sulfur; Sulfur Proteins, Iron; Iron-Sulfur Protein
Networked: 42 relevant articles (1 outcomes, 6 trials/studies)

Relationship Network

Bio-Agent Context: Research Results

Experts

1. Lill, Roland: 3 articles (01/2018 - 03/2010)
2. Ben-Aroya, Shay: 2 articles (01/2018 - 01/2013)
3. Mühlenhoff, Ulrich: 2 articles (01/2018 - 03/2010)
4. Volpe, Marina: 2 articles (01/2018 - 01/2013)
5. Bhave, Devayani P: 2 articles (01/2011 - 09/2009)
6. Carroll, Kate S: 2 articles (01/2011 - 09/2009)
7. Hong, Jiyoung A: 2 articles (01/2011 - 09/2009)
8. Aydin, Kürşad: 1 article (11/2020)
9. Seyhan, Serhat: 1 article (11/2020)
10. Uzunhan, Tuğçe Aksu: 1 article (11/2020)

Related Diseases

1. Ischemia
2. Hypoxia (Hypoxemia)
10/01/2009 - "In turn, by repressing ISCU1/2 during hypoxia, miR-210 decreases the activity of prototypical iron-sulfur proteins controlling mitochondrial metabolism, including Complex I and aconitase. "
05/01/2017 - "In the present study, we studied the mechanism of mitochondrial ATP-sensitive potassium (mitoKATP) channels regulating hypoxia-inducible factor (HIF)-1α/microRNA (miR)-210/mitochondrial iron-sulfur protein integrin (ISCU) signaling axis and forming a positive feedback loop in chronic hypoxia-induced pulmonary arterial hypertension (PAH) by using in vivo animal model. "
01/01/2019 - "Lung Ndufs2 cysteine residues became reduced during acute hypoxia and both hypoxia and reducing agents caused functional inhibition of Complex I. In PASMC, siNdufs2 (cells/tissue treated with Ndufs2 siRNA) decreased normoxic H2O2, prevented hypoxic increases in [Ca2+]i, and mimicked aspects of chronic hypoxia, including decreasing Complex I activity, elevating the nicotinamide adenine dinucleotide (NADH/NAD+) ratio and decreasing expression of the O2-sensitive ion channel, Kv1.5. Knocking down another Fe-S center within Complex I (Ndufs1, NADH [nicotinamide adenine dinucleotide] dehydrogenase [ubiquinone] iron-sulfur protein 1) or other mitochondrial subunits proposed as putative oxygen sensors (Complex III's Rieske Fe-S center and COX4i2 [cytochrome c oxidase subunit 4 isoform 2] in Complex IV) had no effect on hypoxic increases in [Ca2+]i. In vivo, siNdufs2 significantly decreased hypoxia- and rotenone-induced constriction while enhancing phenylephrine-induced constriction. "
3. Infections
4. Leukoencephalopathies
5. Poisoning

Related Drugs and Biologics

1. Peptides (Polypeptides)
2. Proteins (Proteins, Gene)
3. Iron
4. Electron Transport Complex I (NADH-CoQ Reductase)
5. Ferritins (Ferritin)
6. Adenosine Triphosphate (ATP)
7. MicroRNAs (MicroRNA)
8. Integrins
9. Potassium
10. Phenobarbital (Luminal)