 Iron-Sulfur Proteins
"Iron-Sulfur Proteins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
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.
| Descriptor ID |
D007506
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| MeSH Number(s) |
D12.776.157.427.374.375 D12.776.556.579.374.375
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| Concept/Terms |
Iron-Sulfur Proteins- Iron-Sulfur Proteins
- Proteins, Iron-Sulfur
- Iron Sulfur Proteins
- Proteins, Iron Sulfur
- Sulfur Proteins, Iron
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Below are MeSH descriptors whose meaning is more general than "Iron-Sulfur Proteins".
Below are MeSH descriptors whose meaning is more specific than "Iron-Sulfur Proteins".
This graph shows the total number of publications written about "Iron-Sulfur Proteins" by people in this website by year, and whether "Iron-Sulfur Proteins" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2000 | 1 | 0 | 1 | | 2001 | 1 | 0 | 1 | | 2006 | 1 | 0 | 1 | | 2007 | 4 | 0 | 4 | | 2008 | 5 | 0 | 5 | | 2009 | 0 | 1 | 1 | | 2010 | 1 | 0 | 1 | | 2011 | 2 | 1 | 3 | | 2012 | 2 | 0 | 2 | | 2013 | 1 | 0 | 1 | | 2014 | 5 | 0 | 5 | | 2015 | 2 | 0 | 2 | | 2016 | 0 | 1 | 1 | | 2017 | 2 | 1 | 3 | | 2018 | 4 | 1 | 5 | | 2019 | 0 | 1 | 1 | | 2020 | 1 | 1 | 2 | | 2022 | 1 | 0 | 1 |
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Below are the most recent publications written about "Iron-Sulfur Proteins" by people in Profiles.
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Yang JH, Friederich MW, Ellsworth KA, Frederick A, Foreman E, Malicki D, Dimmock D, Lenberg J, Prasad C, Yu AC, Anthony Rupar C, Hegele RA, Manickam K, Koboldt DC, Crist E, Choi SS, Farhan SMK, Harvey H, Sattar S, Karp N, Wong T, Haas R, Van Hove JLK, Wigby K. Expanding the phenotypic and molecular spectrum of NFS1-related disorders that cause functional deficiencies in mitochondrial and cytosolic iron-sulfur cluster containing enzymes. Hum Mutat. 2022 03; 43(3):305-315.
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Cai K, Frederick RO, Markley JL. ISCU interacts with NFU1, and ISCU[4Fe-4S] transfers its Fe-S cluster to NFU1 leading to the production of holo-NFU1. J Struct Biol. 2020 05 01; 210(2):107491.
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Utterback JK, Ruzicka JL, Keller HR, Pellows LM, Dukovic G. Electron Transfer from Semiconductor Nanocrystals to Redox Enzymes. Annu Rev Phys Chem. 2020 04 20; 71:335-359.
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Yu Q, Tai YY, Tang Y, Zhao J, Negi V, Culley MK, Pilli J, Sun W, Brugger K, Mayr J, Saggar R, Saggar R, Wallace WD, Ross DJ, Waxman AB, Wendell SG, Mullett SJ, Sembrat J, Rojas M, Khan OF, Dahlman JE, Sugahara M, Kagiyama N, Satoh T, Zhang M, Feng N, Gorcsan J, Vargas SO, Haley KJ, Kumar R, Graham BB, Langer R, Anderson DG, Wang B, Shiva S, Bertero T, Chan SY. BOLA (BolA Family Member 3) Deficiency Controls Endothelial Metabolism and Glycine Homeostasis in Pulmonary Hypertension. Circulation. 2019 05 07; 139(19):2238-2255.
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Cai K, Markley JL. NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis. Molecules. 2018 Aug 31; 23(9).
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Cai K, Frederick RO, Dashti H, Markley JL. Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering. Structure. 2018 08 07; 26(8):1127-1136.e4.
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Vögtle FN, Brändl B, Larson A, Pendziwiat M, Friederich MW, White SM, Basinger A, Kücükköse C, Muhle H, Jähn JA, Keminer O, Helbig KL, Delto CF, Myketin L, Mossmann D, Burger N, Miyake N, Burnett A, van Baalen A, Lovell MA, Matsumoto N, Walsh M, Yu HC, Shinde DN, Stephani U, Van Hove JLK, Müller FJ, Helbig I. Mutations in PMPCB Encoding the Catalytic Subunit of the Mitochondrial Presequence Protease Cause Neurodegeneration in Early Childhood. Am J Hum Genet. 2018 04 05; 102(4):557-573.
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Cai K, Frederick RO, Tonelli M, Markley JL. Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly. J Inorg Biochem. 2018 06; 183:107-116.
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Cai K, Frederick RO, Tonelli M, Markley JL. ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin. Biochemistry. 2018 03 06; 57(9):1491-1500.
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Ratzloff MW, Wilker MB, Mulder DW, Lubner CE, Hamby H, Brown KA, Dukovic G, King PW. Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to HredH+ Transition in [FeFe] Hydrogenase. J Am Chem Soc. 2017 09 20; 139(37):12879-12882.
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