| Name | frataxin |
|---|---|
| Synonyms | CyaY; FA; FARR; FRDA; FXN; Frataxin; Friedreich ataxia protein; X25… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 20053667 | Condo I, Malisan F, Guccini I, Serio D, Rufini A, Testi R: Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum Mol Genet. 2010 Apr 1;19(7):1221-9. Epub 2010 Jan 6. Frataxin is an iron-binding protein involved in the biogenesis of iron-sulfur clusters (ISC), prosthetic groups allowing essential cellular functions such as oxidative phosphorylation, enzyme catalysis and gene regulation. |
119(1,2,2,9) | Details |
| 19703283 | Calmels N, Seznec H, Villa P, Reutenauer L, Hibert M, Haiech J, Rustin P, Koenig M, Puccio H: Limitations in a frataxin knockdown cell model for Friedreich ataxia in a high-throughput drug screen. BMC Neurol. 2009 Aug 24;9:46. FRDA, the most common recessive ataxia, results from a generalized deficiency of mitochondrial and cytosolic iron-sulfur cluster (ISC) proteins activity, due to a partial loss of frataxin function, a mitochondrial protein proposed to function as an iron-chaperone for ISC biosynthesis. |
40(0,1,1,10) | Details |
| 19629184 | Calmels N, Schmucker S, Wattenhofer-Donze M, Martelli A, Vaucamps N, Reutenauer L, Messaddeq N, Bouton C, Koenig M, Puccio H: The first cellular models based on frataxin missense mutations that reproduce spontaneously the defects associated with Friedreich ataxia. PLoS One. 2009 Jul 24;4(7):e6379. BACKGROUND: Friedreich ataxia (FRDA), the most common form of recessive ataxia, is due to reduced levels of frataxin, a highly conserved mitochondrial iron-chaperone involved in iron-sulfur cluster (ISC) biogenesis. |
39(0,1,1,9) | Details |
| 19283345 | Pandolfo M, Pastore A: The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J Neurol. 2009 Mar;256 Suppl 1:9-17. Frataxins are small essential proteins whose deficiency causes a range of metabolic disturbances, which include oxidative stress, deficit of iron- clusters, and defects in heme synthesis, sulfur amino acid and energy metabolism, stress response, and mitochondrial function. |
37(0,1,1,7) | Details |
| 19460301 | Seguin A, Bayot A, Dancis A, Rogowska-Wrzesinska A, Auchere F, Camadro JM, Bulteau AL, Lesuisse E: Overexpression of the yeast frataxin homolog (Yfh1): contrasting effects on iron-sulfur cluster assembly, heme synthesis and resistance to oxidative stress. Mitochondrion. 2009 Apr;9(2):130-8. Epub 2009 Jan 22. |
35(0,1,1,5) | Details |
| 19884169 | Leidgens S, De Smet S, Foury F: Frataxin interacts with Isu1 through a conserved in its beta-sheet. Hum Mol Genet. 2010 Jan 15;19(2):276-86. Epub 2009 Nov 2. Friedreich's ataxia is a neurodegenerative disease caused by the low expression of frataxin, a mitochondrial iron-binding protein which plays an important, but non-essential, role in the formation of iron-sulfur (Fe/S) clusters. |
35(0,1,1,5) | Details |
| 19805308 | Huang ML, Becker EM, Whitnall M, Rahmanto YS, Ponka P, Richardson DR: Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant. Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16381-6. Epub 2009 Sep 4. Using cardiac tissues, we demonstrate that frataxin deficiency leads to down-regulation of key molecules involved in 3 mitochondrial utilization pathways: iron-sulfur cluster (ISC) synthesis (iron-sulfur cluster scaffold protein1/2 and the desulferase Nfs1), mitochondrial iron storage (mitochondrial ferritin), and heme synthesis dehydratase, coproporphyrinogen oxidase, hydroxymethylbilane synthase, uroporphyrinogen III synthase, and ferrochelatase). |
34(0,1,1,4) | Details |
| 20141512 | Lane DJ, Richardson DR: Frataxin, a molecule of mystery: trading stability for function in its iron-binding site. Biochem J. 2010 Feb 9;426(2):e1-3. What are the structural implications for iron binding by frataxin, the mitochondrial protein whose decreased expression results in Friedreich's ataxia? Though frataxin has been shown to be essential for proper handling of iron within mitochondria (e.g. for iron-sulfur cluster and haem biosynthesis), its exact molecular function remains unclear. |
34(0,1,1,4) | Details |
| 19491103 | Li H, Gakh O, Smith DY 4th, Isaya G: Oligomeric yeast frataxin drives assembly of core machinery for mitochondrial iron-sulfur cluster synthesis. J Biol Chem. 2009 Aug 14;284(33):21971-80. Epub 2009 Jun 2. |
31(0,1,1,1) | Details |
| 20108066 | Kondapalli KC, Bencze KZ, Dizin E, Cowan JA, Stemmler TL: NMR assignments of a stable processing intermediate of human frataxin. . Biomol NMR Assign. 2010 Jan 28. |
6(0,0,0,6) | Details |
| 20156111 | Santos R, Lefevre S, Sliwa D, Seguin A, Camadro JM, Lesuisse E: FRIEDREICH'S ATAXIA: MOLECULAR MECHANISMS, REDOX CONSIDERATIONS AND THERAPEUTIC OPPORTUNITIES. Antioxid Redox Signal. 2010 Feb 16. Friedreich's ataxia (FRDA) is the most common hereditary ataxia with one individual affected in 50,000. The affected functions include respiration, iron-sulfur cluster assembly, iron homeostasis and maintenance of the redox status. |
4(0,0,0,4) | Details |
| 19649569 | Pynyaha YV, Boretsky YR, Fedorovych DV, Fayura LR, Levkiv AI, Ubiyvovk VM, Protchenko OV, Philpott CC, Sibirny AA: Deficiency in frataxin homologue YFH1 in the yeast Pichia guilliermondii leads to missregulation of iron acquisition and biosynthesis and affects assimilation. Biometals. 2009 Aug 1. |
3(0,0,0,3) | Details |
| 19997898 | Richardson DR, Huang ML, Whitnall M, Becker EM, Ponka P, Rahmanto YS: The ins and outs of mitochondrial iron-loading: the metabolic defect in Friedreich's ataxia. J Mol Med. 2010 Apr;88(4):323-9. Epub 2009 Dec 9. Friedreich's ataxia is a cardio- and neurodegenerative disease due to decreased expression of the mitochondrial protein, frataxin. This stimulation of iron uptake probably attempts to rescue the deficit in mitochondrial iron metabolism that is due to downregulation of mitochondrial iron utilization, namely, heme and iron-sulfur cluster (ISC) synthesis and also iron storage (mitochondrial ferritin). |
2(0,0,0,2) | Details |
| 19761223 | Miao R, Kim H, Koppolu UM, Ellis EA, Scott RA, Lindahl PA: Biophysical characterization of the iron in mitochondria from Atm1p-depleted Saccharomyces cerevisiae. Biochemistry. 2009 Oct 13;48(40):9556-68. Reactive species generated under these conditions might degrade iron-sulfur clusters and lower heme levels in the organelle. The Fe that accumulated in aerobically grown cells was in the form of iron (III) nanoparticles similar to that which accumulates in yeast frataxin Yfh1p-deleted or yeast ferredoxin Yah1p-depleted cells. |
1(0,0,0,1) | Details |
| 19347027 | Schulz JB, Boesch S, Burk K, Durr A, Giunti P, Mariotti C, Pousset F, Schols L, Vankan P, Pandolfo M: Diagnosis and treatment of Friedreich ataxia: a European perspective. Nat Rev Neurol. 2009 Apr;5(4):222-34. Friedreich ataxia is usually caused by a large GAA-triplet-repeat expansion within the first intron of the frataxin (FXN) gene. FXN mutations cause deficiencies of the iron-sulfur cluster-containing subunits of the mitochondrial electron transport complexes I, II, and III, and of the iron-sulfur protein aconitase. |
1(0,0,0,1) | Details |
| 19635800 | Berrisford JM, Sazanov LA: Structural basis for the mechanism of respiratory complex I. . J Biol Chem. 2009 Oct 23;284(43):29773-83. Epub 2009 Jul 27. Bound metals were identified in the channel at the interface with the frataxin-like subunit Nqo15, indicating possible iron-binding sites. |
1(0,0,0,1) | Details |