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Journal articles on the topic 'Iron proteins'

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Published: 4 June 2021
Last updated: 27 July 2024

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1

BROCK, J. H. "Iron-binding Proteins." Acta Paediatrica 78 (October 1989): 31–43. http://dx.doi.org/10.1111/apa.1989.78.s361.31.

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2

Cammack, Richard. "Iron–sulfur proteins." Biochemist 34, no. 5 (October 1, 2012): 14–17. http://dx.doi.org/10.1042/bio03405014.

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Iron makes up 35% of the Earth's mass, and is plentiful in its crust (approximately 5%), so it is not surprising that Biology has found many different applications for it. Iron–sulfur (Fe–S) clusters are essential, ubiquitous inorganic cofactors in electron-transport proteins of respiration and photosynthesis, and are responsible for the activity of hundreds of enzymes1. Various types of clusters (Figure 1) occur in iron-sulfur proteins, bound covalently to protein ligands, usually cysteine sulfur. Their activity is not confined to oxidation/reduction; in enzymes such as aconitase, they are involved in substrate binding and conversion. Fe–S enzymes that catalyse difficult reactions, such as nitrogenase in nitrogen fixation and hydrogenase in hydrogen production, contain complex ‘superclusters’2.
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3

RAWIS, REBECCA L. "IRON-SULFUR PROTEINS." Chemical & Engineering News 78, no. 47 (November 20, 2000): 43–51. http://dx.doi.org/10.1021/cen-v078n047.p043.

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4

Eisenstein, Richard S., and Kenneth P. Blemings. "Iron Regulatory Proteins, Iron Responsive Elements and Iron Homeostasis." Journal of Nutrition 128, no. 12 (December 1, 1998): 2295–98. http://dx.doi.org/10.1093/jn/128.12.2295.

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5

Zhu, Mingang, Marianne Valdebenito, Günther Winkelmann, and Klaus Hantke. "Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization." Microbiology 151, no. 7 (July 1, 2005): 2363–72. http://dx.doi.org/10.1099/mic.0.27888-0.

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The siderophore salmochelin is produced under iron-poor conditions by Salmonella and many uropathogenic Escherichia coli strains. The production of salmochelin, a C-glucosylated enterobactin, is dependent on the synthesis of enterobactin and the iroBCDEN gene cluster. An E. coli IroD protein with an N-terminal His-tag cleaved cyclic salmochelin S4 to the linear trimer salmochelin S2, the dimer salmochelin S1, and the monomers dihydroxybenzoylserine and C-glucosylated dihydroxybenzoylserine (salmochelin SX, pacifarinic acid). The periplasmic IroE protein was purified as a MalE–IroE fusion protein. This enzyme degraded salmochelin S4 and ferric-salmochelin S4 to salmochelin S2 and ferric-salmochelin S2, respectively. In E. coli, uptake of ferric-salmochelin S4 was dependent on the cleavage by IroE, and independent of the FepBDGC ABC transporter in the cytoplasmic membrane. IroC, which has similarities to ABC-multidrug-resistance proteins, was necessary for the uptake of salmochelin S2 from the periplasm into the cytoplasm. IroE did not function as a classical binding protein since salmochelin S2 was taken up in the absence of a functional IroE protein. IroC mediated the uptake of iron via enterobactin in a fepB mutant. IroE was also necessary in this case for the uptake of ferric-enterobactin, which indicated that only the linear degradation products of enterobactin were taken up via IroC. PfeE, the Pseudomonas aeruginosa IroE homologue, was cloned, and its enzymic activity was shown to be very similar to that of IroE. It is suggested that homologues in other bacteria are also periplasmic IroE-type esterases of siderophores.
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6

Ghio, Andrew J., Elizabeth N. Pavlisko, and Victor L. Roggli. "Iron and Iron-Related Proteins in Asbestosis." Journal of Environmental Pathology, Toxicology and Oncology 34, no. 4 (2015): 277–85. http://dx.doi.org/10.1615/jenvironpatholtoxicoloncol.2015013397.

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7

Connor, James R., Sharon L. Menzies, Joseph R. Burdo, and Philip J. Boyer. "Iron and iron management proteins in neurobiology." Pediatric Neurology 25, no. 2 (August 2001): 118–29. http://dx.doi.org/10.1016/s0887-8994(01)00303-4.

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8

Bidlack, Wayne R. "Proteins of Iron Metabolism." Journal of the American College of Nutrition 21, no. 3 (June 2002): 290–91. http://dx.doi.org/10.1080/07315724.2002.10719225.

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9

Pietrangelo, Antonello. "Proteins of iron metabolism." Gastroenterology 125, no. 6 (December 2003): 1906. http://dx.doi.org/10.1053/j.gastro.2003.08.039.

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10

Nordlund, Pär, and Hans Eklund. "Di-iron—carboxylate proteins." Current Opinion in Structural Biology 5, no. 6 (December 1995): 758–66. http://dx.doi.org/10.1016/0959-440x(95)80008-5.

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11

CAIRO, Gaetano, and Antonello PIETRANGELO. "Iron regulatory proteins in pathobiology." Biochemical Journal 352, no. 2 (November 24, 2000): 241–50. http://dx.doi.org/10.1042/bj3520241.

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The capacity of readily exchanging electrons makes iron not only essential for fundamental cell functions, but also a potential catalyst for chemical reactions involving free-radical formation and subsequent oxidative stress and cell damage. Cellular iron levels are therefore carefully regulated in order to maintain an adequate substrate while also minimizing the pool of potentially toxic ‘free iron’. Iron homoeostasis is controlled through several genes, an increasing number of which have been found to contain non-coding sequences [i.e. the iron-responsive elements (IREs)] which are recognized at the mRNA level by two cytoplasmic iron-regulatory proteins (IRP-1 and IRP-2). The IRPs belong to the aconitase superfamily. By means of an Fe-S-cluster-dependent switch, IRP-1 can function as an mRNA-binding protein or as an enzyme that converts citrate into isocitrate. Although structurally and functionally similar to IRP-1, IRP-2 does not seem to assemble a cluster nor to possess aconitase activity; moreover, it has a distinct pattern of tissue expression and is modulated by means of proteasome-mediated degradation. In response to fluctuations in the level of the ‘labile iron pool’, IRPs act as key regulators of cellular iron homoeostasis as a result of the translational control of the expression of a number of iron metabolism-related genes. Conversely, various agents and conditions may affect IRP activity, thereby modulating iron and oxygen radical levels in different pathobiological settings. As the number of mRNAs regulated through IRE–IRP interactions keeps growing, the definition of IRPs as iron-regulatory proteins may in the near future become limiting as their role expands to other essential metabolic pathways.
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12

Prasannavadhana, A., Santosh Kumar, Prasad Thomas, Laxmi Narayan Sarangi, Santosh Kumar Gupta, Adyasha Priyadarshini, Viswas Konasagara Nagaleekar, and Vijendra Pal Singh. "Outer Membrane Proteome Analysis of Indian Strain ofPasteurella multocidaSerotype B:2 by MALDI-TOF/MS Analysis." Scientific World Journal 2014 (2014): 1–10. http://dx.doi.org/10.1155/2014/617034.

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Identification of outer membrane proteins (OMPs) is important to understand the bacteria structure and function, host-pathogen interaction, development of novel vaccine candidates, and diagnostic antigens. But till now the key antigens ofP. multocidaB:2 isolate causing haemorrhagic septicaemia (HS) in animals are not clearly defined. In this study, P52 strain ofP. multocidaserotype B:2 was grownin vitrounder iron-rich and iron-limited condition. The OMPs were extracted by sarkosyl method followed by SDS-PAGE and the proteins were identified by MALDI-TOF/MS analysis. In total, 22 proteins were identified, of which 7 were observed exclusively under iron-limited condition. Most of the high molecular weight proteins (TbpA, HgbA, HgbB, HasR, IroA, and HemR) identified in this study were involved in iron acquisition. Some hypothetical proteins (HP-KCU-10206, HP and AAUPMB 08244, HP AAUPMB 21592, HP AAUPMB 19766, AAUPMB 11295) were observed for the first time in this study which could be unique to serotype B:2. Further functionalin vivostudy of the proteins identified are required to explore the utility of these proteins in developing diagnostics and vaccine against HS.
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13

Chiancone, Emilia, Pierpaolo Ceci, Andrea Ilari, Frederica Ribacchi, and Simonetta Stefanini. "Iron and proteins for iron storage and detoxification." BioMetals 17, no. 3 (June 2004): 197–202. http://dx.doi.org/10.1023/b:biom.0000027692.24395.76.

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14

Sousa, Maria, Ferdinand Breedvelt, Roselynn Dynesius-Trentham, David Trentham, and Jean Lum. "Iron, Iron-binding Proteins and Immune System Cells." Annals of the New York Academy of Sciences 526, no. 1 Hemochromatos (June 1988): 310–22. http://dx.doi.org/10.1111/j.1749-6632.1988.tb55515.x.

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15

Weinberg, Eugene D. "Iron Carriers and Iron Proteins. Thomas M. Loehr." Quarterly Review of Biology 65, no. 2 (June 1990): 218. http://dx.doi.org/10.1086/416736.

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16

Silva, Liliana S. O., Pedro M. Matias, Célia V. Romão, and Lígia M. Saraiva. "Repair of Iron Center Proteins—A Different Class of Hemerythrin-Like Proteins." Molecules 27, no. 13 (June 23, 2022): 4051. http://dx.doi.org/10.3390/molecules27134051.

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Repair of Iron Center proteins (RIC) form a family of di-iron proteins that are widely spread in the microbial world. RICs contain a binuclear nonheme iron site in a four-helix bundle fold, two basic features of hemerythrin-like proteins. In this work, we review the data on microbial RICs including how their genes are regulated and contribute to the survival of pathogenic bacteria. We gathered the currently available biochemical, spectroscopic and structural data on RICs with a particular focus on Escherichia coli RIC (also known as YtfE), which remains the best-studied protein with extensive biochemical characterization. Additionally, we present novel structural data for Escherichia coli YtfE harboring a di-manganese site and the protein’s affinity for this metal. The networking of protein interactions involving YtfE is also described and integrated into the proposed physiological role as an iron donor for reassembling of stress-damaged iron-sulfur centers.
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17

Shahverdiyeva, I. J., A. H. Orujov, and U. H. Azizova. "IRON METABOLISM PROTEINS DURING PREGNANCY." Biological Markers in Fundamental and Clinical Medicine (collection of abstracts) 3, no. 1 (November 7, 2019): 90–91. http://dx.doi.org/10.29256/v.03.01.2019.escbm61.

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18

CAIRO, Gaetano, and Antonello PIETRANGELO. "Iron regulatory proteins in pathobiology." Biochemical Journal 352, no. 2 (December 1, 2000): 241. http://dx.doi.org/10.1042/0264-6021:3520241.

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19

Cooper, Chris E. "Nitric oxide and iron proteins." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1411, no. 2-3 (May 1999): 290–309. http://dx.doi.org/10.1016/s0005-2728(99)00021-3.

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20

Bradley, Justin M., Nick E. Le Brun, and Geoffrey R. Moore. "Ferritins: furnishing proteins with iron." JBIC Journal of Biological Inorganic Chemistry 21, no. 1 (January 29, 2016): 13–28. http://dx.doi.org/10.1007/s00775-016-1336-0.

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21

Wilkins, Ralph G. "Binuclear iron centres in proteins." Chemical Society Reviews 21, no. 3 (1992): 171. http://dx.doi.org/10.1039/cs9922100171.

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22

He, Chuan, and Yukiko Mishina. "Modeling non-heme iron proteins." Current Opinion in Chemical Biology 8, no. 2 (April 2004): 201–8. http://dx.doi.org/10.1016/j.cbpa.2004.02.002.

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23

Debrunner, Peter G. "Enzymes and other iron proteins." Hyperfine Interactions 53, no. 1-4 (July 1990): 21–35. http://dx.doi.org/10.1007/bf02101037.

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24

Brock, Jeremy H., and Maria de Sousa. "Immunoregulation by iron-binding proteins." Immunology Today 7, no. 2 (February 1986): 30–31. http://dx.doi.org/10.1016/0167-5699(86)90117-9.

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25

Behnke, Joerg, and Julie LaRoche. "Iron uptake proteins in algae and the role of Iron Starvation-Induced Proteins (ISIPs)." European Journal of Phycology 55, no. 3 (June 8, 2020): 339–60. http://dx.doi.org/10.1080/09670262.2020.1744039.

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26

Kooi, Cora, and Pamela A. Sokol. "Characterization of monoclonal antibodies to Yersinia enterocolitica iron-regulated proteins." Canadian Journal of Microbiology 41, no. 7 (July 1, 1995): 562–71. http://dx.doi.org/10.1139/m95-075.

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Yersinia enterocolitica 1165 (0:8) expressed several iron-regulated proteins with molecular masses of 240, 194, 80, 79, 70, and 67 kDa. These proteins were not detected in cells grown in iron-rich conditions. Cell surface iodination indicated that the 240- and 190-kDa proteins (HMWPs) were not surface exposed, whereas the 67- and 70-kDa proteins appeared to be exposed to the cell surface. Incubation with iron protected the 67- and 70-kDa proteins from proteinase K treatment, suggesting that they may be involved in iron acquisition. Monoclonal antibodies (MAbs) were produced against the HMWPs and the 67-kDa iron-regulated protein. MAbs to the HMWPs not only recognized the 240- and 194-kDa proteins but also reacted with the 67- and 70-kDa iron-regulated proteins. Similarly, MAbs to the 67-kDa protein reacted with the 67- and 70-kDa proteins and the HMWPs, suggesting that these iron-regulated proteins are related immunologically. In addition, the MAbs recognized the 67- and 70-kDa proteins and HMWPs from other Y. enterocolitica serotypes, suggesting that the antigenic sites recognized on these iron-regulated proteins are conserved. The MAbs examined did not inhibit iron binding or iron uptake and did not provide protection against a Y. enterocolitica 1165 (0:8) infection in a systemic mouse infection model. Although these MAbs were not protective in this model, these iron-regulated proteins may play a role in iron acquisition and virulence, but the MAbs examined are probably not directed against epitopes involved in iron acquisition or virulence.Key words: Yersinia enterocolitica, monoclonal antibodies, iron-regulated proteins.
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27

Cheng, H., and J. L. Markley. "NMR Spectroscopic Studies of Paramagnetic Proteins: Iron-Sulfur Proteins." Annual Review of Biophysics and Biomolecular Structure 24, no. 1 (June 1995): 209–37. http://dx.doi.org/10.1146/annurev.bb.24.060195.001233.

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28

Peake, Ian. "Biotechnology of Plasma Proteins, Haemostasis, Thrombosis and Iron Proteins." Blood Coagulation & Fibrinolysis 2, no. 6 (December 1991): 779. http://dx.doi.org/10.1097/00001721-199112000-00014.

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29

Ledesma-Colunga, Maria G., Heike Weidner, Maja Vujic Spasic, Lorenz C. Hofbauer, Ulrike Baschant, and Martina Rauner. "Shaping the bone through iron and iron-related proteins." Seminars in Hematology 58, no. 3 (July 2021): 188–200. http://dx.doi.org/10.1053/j.seminhematol.2021.06.002.

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30

Bleackley, Mark R., Ann Y. K. Wong, David M. Hudson, Christopher H.-Y. Wu, and Ross T. A. MacGillivray. "Blood Iron Homeostasis: Newly Discovered Proteins and Iron Imbalance." Transfusion Medicine Reviews 23, no. 2 (April 2009): 103–23. http://dx.doi.org/10.1016/j.tmrv.2008.12.001.

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31

Galy, Bruno, Dunja Ferring-Appel, Sven W. Sauer, Sylvia Kaden, Saïd Lyoumi, Herve Puy, Stefan Kölker, Hermann-Josef Gröne, and Matthias W. Hentze. "Iron Regulatory Proteins Secure Mitochondrial Iron Sufficiency and Function." Cell Metabolism 12, no. 2 (August 2010): 194–201. http://dx.doi.org/10.1016/j.cmet.2010.06.007.

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32

Hentze, Matthias W. "Iron Regulatory Proteins in Systemic Iron Metabolism and Erythropoiesis." Blood 118, no. 21 (November 18, 2011): SCI—22—SCI—22. http://dx.doi.org/10.1182/blood.v118.21.sci-22.sci-22.

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Abstract Abstract SCI-22 Imbalances of iron homeostasis account for some of the most common human diseases. Pathologies can result from both iron deficiency or overload. The hepcidin/ferroportin and the IRE/IRP regulatory systems balance systemic and cellular iron metabolism, respectively, and understanding their points of intersection and crosstalk represents a major challenge in iron biology. I will discuss an emerging picture from studies with different mutant mouse lines according to which the “cellular” IRE/IRP system determines “set points” via its targets (including ferroportin and HIF2α). These are then subject to modulation via hepcidin in response to systemic cues. Disclosures: No relevant conflicts of interest to declare.
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33

Azman, Adleen, Kalidasan Vasodavan, Narcisse Joseph, Suresh Kumar, Rukman A. Hamat, Syafinaz A. Nordin, Wan M. Aizat, Alex van Belkum, and Vasantha K. Neela. "Physiological and proteomic analysis of Stenotrophomonas maltophilia grown under the iron-limited condition." Future Microbiology 14, no. 16 (November 2019): 1417–28. http://dx.doi.org/10.2217/fmb-2019-0174.

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Aims: To study physiological and proteomic analysis of Stenotrophomonas maltophilia grown under iron-limited condition. Methods: One clinical and environmental S. maltophilia isolates grown under iron-depleted conditions were studied for siderophore production, ability to kill nematodes and alteration in protein expression using isobaric tags for relative and absolute quantification (ITRAQ). Results & conclusions: Siderophore production was observed in both clinical and environmental strains under iron-depleted conditions. Caenorhabditis elegans assay showed higher killing rate under iron-depleted (96%) compared with normal condition (76%). The proteins identified revealed, 96 proteins upregulated and 26 proteins downregulated for the two isolates under iron depletion. The upregulated proteins included several iron acquisition proteins, metabolic proteins and putative virulence proteins.
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34

Mashuta, Mark S., Robert J. Webb, Kenneth J. Oberhausen, John F. Richardson, Robert M. Buchanan, and David N. Hendrickson. "Valence detrapping in iron(II)-iron(III) models of iron-oxo proteins." Journal of the American Chemical Society 111, no. 7 (March 1989): 2745–46. http://dx.doi.org/10.1021/ja00189a074.

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35

Chen, J., J. Christiansen, R. C. Tittsworth, B. J. Hales, S. J. George, D. Coucouvanis, and S. P. Cramer. "Iron EXAFS of Azotobacter vinelandii nitrogenase molybdenum-iron and vanadium-iron proteins." Journal of the American Chemical Society 115, no. 13 (June 1993): 5509–15. http://dx.doi.org/10.1021/ja00066a019.

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36

Jolivet-Gougeon, A., and M. Bonnaure-Mallet. "Treponema, Iron and Neurodegeneration." Current Alzheimer Research 15, no. 8 (June 11, 2018): 716–22. http://dx.doi.org/10.2174/1567205013666161122093404.

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Spirochetes are suspected to be linked to the genesis of neurological diseases, including neurosyphillis or neurodegeneration (ND). Impaired iron homeostasis has been implicated in loss of function in several enzymes requiring iron as a cofactor, formation of toxic oxidative species, inflammation and elevated production of beta-amyloid proteins. This review proposes to discuss the link that may exist between the involvement of Treponema spp. in the genesis or worsening of ND, and iron dyshomeostasis. Proteins secreted by Treponema can act directly on iron metabolism, with hemin binding ability (HbpA and HbpB) and iron reductase able to reduce the central ferric iron of hemin, iron-containing proteins (rubredoxin, neelaredoxin, desulfoferrodoxin metalloproteins, bacterioferritins etc). Treponema can also interact with cellular compounds, especially plasma proteins involved in iron metabolism, contributing to the virulence of the syphilis spirochetes (e.g. treponemal motility and survival). Fibronectin, transferrin and lactoferrin were also shown to be receptors for treponemal adherence to host cells and extracellular matrix. Association between Treponema and iron binding proteins results in iron accumulation and sequestration by Treponema from host macromolecules during systemic and mucosal infections.
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37

Thorp, H. Holden. "Proteins, proteins everywhere." Science 374, no. 6574 (December 17, 2021): 1415. http://dx.doi.org/10.1126/science.abn5795.

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The first protein structures were determined by x-ray crystallography in 1957 by John C. Kendrew and Max F. Perutz. As a bioinorganic chemist, I was delighted that the structures were myoglobin and hemoglobin, both heme proteins with big, beautiful iron atoms. It must have been an extraordinary experience to stare at a physical model of the structures and see something that had previously only been imagined. Not long afterward, Christian B. Anfinsen Jr. proposed that the structure of a protein was thermodynamically stable. It seemed possible that the three-dimensional structure of a protein could be predicted based on the sequence of its amino acids. This “protein-folding problem,” as it came to be known, baffled scientists until this year, when the papers we’ve deemed the 2021 Breakthrough of the Year were published.
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38

Kühn, Lukas C. "Iron regulatory proteins and their role in controlling iron metabolism." Metallomics 7, no. 2 (2015): 232–43. http://dx.doi.org/10.1039/c4mt00164h.

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39

Liu, Jian She, Yan Fei Zhang, Mei Mei Geng, Jia Zeng, and Guan Zhou Qiu. "Research on isc Operon in Acidithiobacillus ferrooxidans ATCC 23270." Advanced Materials Research 20-21 (July 2007): 509–12. http://dx.doi.org/10.4028/www.scientific.net/amr.20-21.509.

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The highly conserved operon iron–sulfur cluster (iscSUA) is essential for the general biogenesis and transfer of iron–sulfur proteins in bacteria. In this study, expression, purification and characterization of the proteins of the isc operon (iscSUA) of Acidithiobacillus ferrooxidans ATCC 23270 was studied. Assembly and transfer of [Fe4S4] in vitro during the isc proteins and other iron sulfur proteins was studied in order to detect the pathway and mechanism of [Fe4S4] assembly and transfer in vivo. The [Fe4S4] cluster was successfully assembled in iron-sulfur proteins in vitro in the presence of Fe2+ and sulfide, and it was successfully transferred from IscA or IscU to iron- sulfur proteins. Our results support and extend certain models of iron-sulfur clusters assembly and transfer.
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40

Skarżyńska, Ewa, Artur Jakimiuk, Tadeusz Issat, and Barbara Lisowska-Myjak. "Meconium Proteins Involved in Iron Metabolism." International Journal of Molecular Sciences 25, no. 13 (June 25, 2024): 6948. http://dx.doi.org/10.3390/ijms25136948.

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The lack of specific biological materials and biomarkers limits our knowledge of the mechanisms underlying intrauterine regulation of iron supply to the fetus. Determining the meconium content of proteins commonly used in the laboratory to assess the transport, storage, and distribution of iron in the body may elucidate their roles in fetal development. Ferritin, transferrin, haptoglobin, ceruloplasmin, lactoferrin, myeloperoxidase (MPO), neutrophil gelatinase-associated lipocalin (NGAL), and calprotectin were determined by ELISA in meconium samples obtained from 122 neonates. There were strong correlations between the meconium concentrations of haptoglobin, transferrin, and NGAL (p < 0.05). Meconium concentrations of ferritin were several-fold higher than the concentrations of the other proteins, with the exception of calprotectin whose concentration was approximately three-fold higher than that of ferritin. Meconium ceruloplasmin concentration significantly correlated with the concentrations of MPO, NGAL, lactoferrin, and calprotectin. Correlations between the meconium concentrations of haptoglobin, transferrin, and NGAL may reflect their collaborative involvement in the storage and transport of iron in the intrauterine environment in line with their recognized biological properties. High meconium concentrations of ferritin may provide information about the demand for iron and its utilization by the fetus. The associations between ceruloplasmin and neutrophil proteins may indicate the involvement of ceruloplasmin in the regulation of neutrophil activity in the intrauterine environment.
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41

Cairo, Gaetano, and Stefania Recalcati. "Iron-regulatory proteins: molecular biology and pathophysiological implications." Expert Reviews in Molecular Medicine 9, no. 33 (December 2007): 1–13. http://dx.doi.org/10.1017/s1462399407000531.

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AbstractIron is required for key cellular functions, and there is a strong link between iron metabolism and important metabolic processes, such as cell growth, apoptosis and inflammation. Diseases that are directly or indirectly related to iron metabolism represent major health problems. Iron-regulatory proteins (IRPs) 1 and 2 are key controllers of vertebrate iron metabolism and post-transcriptionally regulate expression of the major iron homeostasis genes. Here we discuss how dysregulation of the IRP system can result from both iron-related and unrelated effectors and explain how this can have important pathological consequences in several human disorders.
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42

Ohgami, Robert S., Dean R. Campagna, Alice McDonald, and Mark D. Fleming. "The Steap proteins are metalloreductases." Blood 108, no. 4 (August 15, 2006): 1388–94. http://dx.doi.org/10.1182/blood-2006-02-003681.

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Abstract Iron and copper are essential for all organisms, assuming critical roles as cofactors in many enzymes. In eukaryotes, the transmembrane transport of these elements is a highly regulated process facilitated by the single electron reduction of each metal. Previously, we identified a mammalian ferrireductase, Steap3, critical for erythroid iron homeostasis. Now, through homology, expression, and functional studies, we characterize all 4 members of this protein family and demonstrate that 3 of them, Steap2, Steap3, and Steap4, are not only ferrireductases but also cupric reductases that stimulate cellular uptake of both iron and copper in vitro. Finally, the pattern of tissue expression and subcellular localization of these proteins suggest they are physiologically relevant cupric reductases and ferrireductases in vivo.
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43

Borovik, A. S., and Lawrence Que. "Models for the iron(II)iron(III) and iron(II)iron(II) forms of iron-oxo proteins." Journal of the American Chemical Society 110, no. 7 (March 1988): 2345–47. http://dx.doi.org/10.1021/ja00215a079.

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44

Sage, J. T. "Vibrational dynamics of iron in proteins." Acta Crystallographica Section A Foundations of Crystallography 61, a1 (August 23, 2005): c26. http://dx.doi.org/10.1107/s0108767305098880.

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45

Fillebeen, Carine, and Kostas Pantopoulos. "Redox control of iron regulatory proteins." Redox Report 7, no. 1 (February 2002): 15–22. http://dx.doi.org/10.1179/135100002125000136.

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46

Panossian, R., H. Zineddine, M. Asso, and M. Guiliano. "Models Studies of Iron—Tyrosinate Proteins." Spectroscopy Letters 24, no. 6 (July 1991): 779–84. http://dx.doi.org/10.1080/00387019108018158.

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47

White, K. N., D. Cunninghame Graham, and A. Bomford. "Nuclear localisation of iron regulatory proteins." Biochemical Society Transactions 30, no. 1 (February 1, 2002): A38. http://dx.doi.org/10.1042/bst030a038.

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48

Beutler, E. "CELL BIOLOGY: " Pumping" Iron: The Proteins." Science 306, no. 5704 (December 17, 2004): 2051–53. http://dx.doi.org/10.1126/science.1107224.

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49

Barresi, G., and G. Tuccari. "Iron-Binding Proteins in Thyroid Tumours." Pathology - Research and Practice 182, no. 3 (June 1987): 344–51. http://dx.doi.org/10.1016/s0344-0338(87)80070-5.

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50

Pyrz, Joseph W., A. Lawrence Roe, Lawrence J. Stern, and Lawrence Que. "Model studies of iron-tyrosinate proteins." Journal of the American Chemical Society 107, no. 3 (February 1985): 614–20. http://dx.doi.org/10.1021/ja00289a013.

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