The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer
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reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1. These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.
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PCBP2 accepts ferrous iron, acts as a chaperone and accompanies iron to the basolateral membrane.
“Therein, PCBP2 (for poly(rC)-binding protein-2) accepts ferrous iron, acts as chaperone and as such accompanies iron to the basolateral membrane (Philpott and Jadhav, 2019;Shi et al., 2008;Yanatori et al., 2017).”
From Iron in infection and immunity (2020) · cites this paper as Yanatori et al., 2017
The paper states that PCBP2 receives ferrous iron, functions as an iron chaperone, and can transfer iron to ferroportin (Abstract and Discussion; page numbers unavailable). It does not specify that PCBP2 accompanies iron to the basolateral membrane, so that location is not supported by our copy. (LLM, conf=0.86)
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Cites
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 315,771 · see citing works
Cloning and characterization of a mammalian proton-coupled metal-ion transporter
Gunshin, H., Mackenzie, B., Berger, U. V., Gunshin, Y., Romero, M. F., Boron, W. F., Nussberger, S., Gollan, J. L., & Hediger, M. A. (1997) · Nature · doi:10.1038/41343 · Cited by 3,166 · see citing works
The enzymatic conversion of heme to bilirubin by microsomal heme oxygenase.
Tenhunen, R., Marver, H. S., & Schmid, R. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.2.748 · Cited by 1,803 · see citing works
Iron bioavailability and dietary reference values
Hurrell, R., & Egli, I. (2010) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.28674f · Cited by 1,359 · see citing works
Tenhunen, R., Marver, H. S., & Schmid, R. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63477-5 · Cited by 1,357 · see citing works
Pharmacological and Clinical Aspects of Heme Oxygenase
Abraham, N. G., & Kappas, A. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.07104 · Cited by 1,115 · see citing works
Maines, M. D., Trakshel, G. M., & Kutty, R. K. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42488-4 · Cited by 759 · see citing works
Signaling to heme oxygenase-1 and its anti-inflammatory therapeutic potential
Paine, A., Eiz‐Vesper, B., Blasczyk, R., & Immenschuh, S. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.07.014 · Cited by 698 · see citing works
Mitoferrin is essential for erythroid iron assimilation
Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624 · see citing works
Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells
Liuzzi, J. P., Aydemir, F., Nam, H., Knutson, M. D., & Cousins, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606424103 · Cited by 577 · see citing works
Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells
Riemer, J., Hoepken, H. H., Czerwinska, H., Robinson, S. R., & Dringen, R. (2004) · Analytical Biochemistry · doi:10.1016/j.ab.2004.03.049 · Cited by 566 · see citing works
Iron-induced carcinogenesis: The role of redox regulation
Toyokuni, S. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02111-6 · Cited by 562 · see citing works
Self-citationRichardson, D. R., Lane, D. J. R., Becker, E. M., Huang, M. L.-H., Whitnall, M., Rahmanto, Y. S., Sheftel, A. D., & Ponka, P. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912925107 · Cited by 536 · see citing works
Self-citationA cytosolic iron chaperone that delivers iron to ferritin
Shi, H., Bencze, K. Z., Stemmler, T. L., & Philpott, C. C. (2008) · Science · doi:10.1126/science.1157643 · Cited by 536 · see citing works
Function and regulation of transferrin and ferritin.
Ponka, P., Beaumont, C., & Richardson, D. R. (1998) · PubMed · Cited by 524 · see citing works
Self-citationHaem oxygenase-1 prevents cell death by regulating cellular iron
Ferris, C. D., Jaffrey, S. R., Sawa, A., Takahashi, M., Brady, S. D., Barrow, R. K., Tysoe, S. A., Wolosker, H., Barañano, D. E., Doré, S., et al. (1999) · Nature Cell Biology · doi:10.1038/11072 · Cited by 509 · see citing works
Mustafa, A. K., Gadalla, M. M., & Snyder, S. H. (2009) · Science Signaling · doi:10.1126/scisignal.268re2 · Cited by 497 · see citing works
The poly(C)-binding proteins: A multiplicity of functions and a search for mechanisms
Makeyev, A. V., & Liebhaber, S. A. (2002) · RNA · doi:10.1017/s1355838202024627 · Cited by 469 · see citing works
Cloning and expression of cDNA for rat heme oxygenase.
Shibahara, S., Müller, R., Taguchi, H., & Yoshida, T. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.7865 · Cited by 452 · see citing works
Iron uptake and metabolism in the new millennium
Dunn, L., Rahmanto, Y. S., & Richardson, D. R. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.12.003 · Cited by 419 · see citing works
Self-citationLane, D. J. R., Merlot, A. M., Huang, M. L.-H., Bae, D.-H., Jansson, P. J., Sahni, S., Kalinowski, D. S., & Richardson, D. R. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.01.021 · Cited by 399 · cited 1× · see citing works
“PCBP2 shares highly conserved amino acid sequences with PCBP1, PCBP3, and PCBP4 (46), and the functions of these molecules appear to be non-redundant in the metabolism of cellular iron (47).”
BackgroundThe Structure of Calnexin, an ER Chaperone Involved in Quality Control of Protein Folding
Schrag, J. D., Bergeron, J. J. M., Li, Y., Borisova, S. N., Hahn, M. G., Thomas, D. Y., & Cygler, M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00318-5 · Cited by 394 · see citing works
Green, R., Charlton, R. W., Seftel, H. C., Bothwell, T. H., Mayet, F., Adams, B., Finch, C. A., & Layrisse, M. (1968) · The American Journal of Medicine · doi:10.1016/0002-9343(68)90069-7 · Cited by 392 · see citing works
PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4
You, F., Sun, H., Zhou, X., Sun, W., Liang, S., Zhai, Z., & Jiang, Z. (2009) · Nature Immunology · doi:10.1038/ni.1815 · Cited by 340 · see citing works
Swanson, M. S., & Dreyfuss, G. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.5.2237 · Cited by 331 · see citing works
Novel mechanism for translational control in regulation of ferritin synthesis by iron.
Zähringer, J., Baliga, B. S., & Munro, H. N. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.3.857 · Cited by 318 · see citing works
Mechanisms of heme iron absorption: Current questions and controversies
West, A. R., & Oates, P. S. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.4101 · Cited by 257 · see citing works
Ziman, M., Preuss, D., Mulholland, J., O’Brien, J. M., Botstein, D., & Johnson, D. I. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.12.1307 · Cited by 254 · see citing works
Schacter, B., NELSON, E. B., Marver, H. S., & Masters, B. S. S. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45183-1 · Cited by 253 · see citing works
A precious metal: Iron, an essential nutrient for all cells
Cairo, G., Bernuzzi, F., & Recalcati, S. (2006) · Genes & Nutrition · doi:10.1007/bf02829934 · Cited by 252 · see citing works
Heme Oxygenases in Cardiovascular Health and Disease
Ayer, A., Zarjou, A., Agarwal, A., & Stocker, R. (2016) · Physiological Reviews · doi:10.1152/physrev.00003.2016 · Cited by 243 · see citing works
Tabuchi, M., Yoshimori, T., Yamaguchi, K., Yoshida, T., & Kishi, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001478200 · Cited by 236 · see citing works
Self-citationGamarnik, A. V., & Andino, R. (2000) · Journal of Virology · doi:10.1128/jvi.74.5.2219-2226.2000 · Cited by 235 · see citing works
Ronnebaum, S. M., Ilkayeva, O., Burgess, S. C., Joseph, J. W., Lu, D., Stevens, R. D., Becker, T. C., Sherry, A. D., Newgard, C. B., & Jensen, M. V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511908200 · Cited by 230 · see citing works
Gao, J., & Richardson, D. R. (2001) · Blood · doi:10.1182/blood.v98.3.842 · Cited by 224 · see citing works
Self-citationIntestinal Absorption of Hemoglobin Iron-Heme Cleavage by Mucosal Heme Oxygenase
Raffin, S. B., Woo, C. H., Roost, K. T., Price, D. C., & Schmid, R. (1974) · Journal of Clinical Investigation · doi:10.1172/jci107881 · Cited by 217 · see citing works
Huang, M. L.-H., Becker, E. M., Whitnall, M., Rahmanto, Y. S., Ponka, P., & Richardson, D. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906784106 · Cited by 212 · see citing works
Self-citationMammalian Cdc42 Is a Brefeldin A-sensitive Component of the Golgi Apparatus
Erickson, J. W., Zhang, C., Kahn, R., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26850 · Cited by 205 · see citing works
Expression and Characterization of a Heme Oxygenase (Hmu O) fromCorynebacterium diphtheriae
Wilks, A., & Schmitt, M. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.2.837 · Cited by 205 · see citing works
Molecular Basis of Heme Oxygenase-1 Induction: Implications for Chemoprevention and Chemoprotection
Prawan, A., Kundu, J. K., & Surh, Y. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.1688 · Cited by 195 · see citing works
Leidgens, S., Zumbrennen‐Bullough, K. B., Shi, H., Li, F., Shakoury‐Elizeh, M., Yabe‐Wada, T., Subramanian, P., Hsu, E., Natarajan, N., Nandal, A., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.460253 · Cited by 193 · see citing works
Zhu, W., Wilks, A., & Stojiljkovic, I. (2000) · Journal of Bacteriology · doi:10.1128/jb.182.23.6783-6790.2000 · Cited by 186 · see citing works
McCoubrey, W. K., Ewing, J. F., & Maines, M. D. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90481-b · Cited by 183 · see citing works
Mechanism of heme degradation by heme oxygenase
Yoshida, T., & Migita, C. T. (2000) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)00156-2 · Cited by 175 · see citing works
Iron export through the transporter ferroportin 1 is modulated by the iron chaperone PCBP2
Yanatori, I., Richardson, D. R., Imada, K., & Kishi, F. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.721936 · Cited by 170 · see citing works
Sardana, M. K., & Kappas, A. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.8.2464 · Cited by 169 · see citing works
Both subunits of rat liver ferritin are regulated at a translational level by iron induction
Aziz, N., & Munro, H. N. (1986) · Nucleic Acids Research · doi:10.1093/nar/14.2.915 · Cited by 161 · see citing works
Duodenal Cytochrome b (DCYTB) in Iron Metabolism: An Update on Function and Regulation
Lane, D. J. R., Bae, D.-H., Merlot, A. M., Sahni, S., & Richardson, D. R. (2015) · Nutrients · doi:10.3390/nu7042274 · Cited by 153 · see citing works
Self-citationWalter, B. L., Nguyen, J. H. C., Ehrenfeld, E., & Semler, B. L. (1999) · RNA · doi:10.1017/s1355838299991483 · Cited by 144 · see citing works
Tabuchi, M., Yanatori, I., Kawai, Y., & Kishi, F. (2010) · Journal of Cell Science · doi:10.1242/jcs.060574 · Cited by 143 · see citing works
Self-citationAlternative Splicing Regulates the Subcellular Localization of Divalent Metal Transporter 1 Isoforms
Tabuchi, M., Tanaka, N., Nishida-Kitayama, J., Ohno, H., & Kishi, F. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-03-0165 · Cited by 141 · cited 1× · see citing works
“Another isoform with an IRE domain in its 3 region (DMT1B-I) is localized in the late endosome/lysosome to retrieve iron released during lysosomal catabolism of iron-containing proteins (16, 17).”
BackgroundSelf-citationChaperone protein involved in transmembrane transport of iron
Yanatori, I., Yasui, Y., Tabuchi, M., & Kishi, F. (2014) · Biochemical Journal · doi:10.1042/bj20140225 · Cited by 134 · see citing works
Self-citationA Review on Hemeoxygenase-2: Focus on Cellular Protection and Oxygen Response
Muñoz‐Sánchez, J., & Chánez‐Cárdenas, M. E. (2014) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2014/604981 · Cited by 132 · see citing works
Poly(C)-binding proteins as transcriptional regulators of gene expression
Choi, H. S., Hwang, C. K., Song, K. Y., Law, P., Wei, L., & Loh, H. H. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.136 · Cited by 131 · see citing works
Kalinowski, D. S., Stefani, C., Toyokuni, S., Ganz, T., Anderson, G. J., Subramaniam, V. N., Trinder, D., Olynyk, J. K., Chua, A. C. G., Jansson, P. J., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.01.026 · Cited by 129 · see citing works
Self-citationDejgaard, K., & Leffers, H. C. B. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.00425.x · Cited by 128 · see citing works
Calabrese, V., Butterfield, D. A., Scapagnini, G., Stella, A. M. G., & Maines, M. D. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.444 · Cited by 121 · see citing works
Finch, C. A. (1959) · Journal of Clinical Investigation · doi:10.1172/jci103813 · Cited by 119 · see citing works
Comparison of the Heme-free and -bound Crystal Structures of Human Heme Oxygenase-1
Lad, L., Schuller, D. J., Shimizu, H., Friedman, J., Li, H., de Montellano, P. R. O., & Poulos, T. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211450200 · Cited by 117 · see citing works
Zukor, H., Song, W., Liberman, A., Mui, J., Vali, H., Fillebeen, C., Pantopoulos, K., Wu, T., Guerquin‐Kern, J., & Schipper, H. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06007.x · Cited by 105 · see citing works
Identification of Histidine 25 as the Heme Ligand in Human Liver Heme Oxygenase
Sun, J., Loehr, T. M., Wilks, A., et al. (1994) · Biochemistry · doi:10.1021/bi00250a026 · Cited by 103 · see citing works
The metal transporter ZIP13 supplies iron into the secretory pathway in Drosophila melanogaster
Xiao, G., Wan, Z., Fan, Q., Tang, X., & Zhou, B. (2014) · eLife · doi:10.7554/elife.03191 · Cited by 103 · see citing works
Hematin Compounds and Bile Pigments: Their Constitution, Metabolism, and Function
(1950) · JAMA · doi:10.1001/jama.1950.02910390076039 · Cited by 101 · see citing works
Gisk, B., Yasui, Y., Kohchi, T., & Frankenberg‐Dinkel, N. (2009) · Biochemical Journal · doi:10.1042/bj20090775 · Cited by 95 · see citing works
Toyoda, H., Franco, D., Fujita, K., Paul, A. V., & Wimmer, E. (2007) · Journal of Virology · doi:10.1128/jvi.00516-07 · Cited by 90 · see citing works
Parfenova, H., Leffler, C. W., Basuroy, S., Liu, J., & Fedinec, A. L. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.13 · Cited by 88 · see citing works
Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol
Gottlieb, Y., Truman-Rosentsvit, M., Cohen, L. A., Leichtmann‐Bardoogo, Y., & Meyron‐Holtz, E. G. (2012) · Haematologica · doi:10.3324/haematol.2012.063651 · Cited by 86 · see citing works
Sugishima, M., Sato, H., Higashimoto, Y., Harada, J., Wada, K., Fukuyama, K., & Noguchi, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322034111 · Cited by 85 · see citing works
Fujimura, K., Kano, F., & Murata, M. (2008) · RNA · doi:10.1261/rna.780708 · Cited by 84 · see citing works
Heme and non-heme iron transporters in non-polarized and polarized cells
Yanatori, I., Tabuchi, M., Kawai, Y., Yasui, Y., Akagi, R., & Kishi, F. (2010) · BMC Cell Biology · doi:10.1186/1471-2121-11-39 · Cited by 83 · see citing works
Self-citationWardrop, S. L., & Richardson, D. R. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00447.x · Cited by 79 · see citing works
Self-citationFrataxin: its role in iron metabolism and the pathogenesis of Friedreich's ataxia
Becker, E., & Richardson, D. R. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00067-4 · Cited by 71 · see citing works
Self-citationGhanem, L. R., Kromer, A., Silverman, I. M., Chatterji, P., Traxler, E. A., Penzo‐Méndez, A., Weiss, M. J., Stanger, B. Z., & Liebhaber, S. A. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00936-15 · Cited by 71 · see citing works
Makeyev, A. V., & Liebhaber, S. A. (2000) · Genomics · doi:10.1006/geno.2000.6244 · Cited by 65 · see citing works
Sugishima, M., Sakamoto, H., Kakuta, Y., et al. (2002) · Biochemistry · doi:10.1021/bi025662a · Cited by 63 · see citing works
Du, Z., Fenn, S., Tjhen, R., & James, T. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803046200 · Cited by 63 · see citing works
Itomaki, M., Ishikawa, K., Matera, K. M., Sato, M. N., Ikeda‐Saito, M., & Yoshida, T. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1160 · Cited by 61 · see citing works
Ghattas, M. H., Chuang, L. T., Kappas, A., & Abraham, N. G. (2002) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00097-3 · Cited by 58 · see citing works
Andrade, B. B., Araújo-Santos, T., Luz, N. F., Khouri, R., Bozza, M. T., Camargo, L. M. A., Barral, A. M. P., Borges, V. M., & Barral‐Netto, M. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0904179 · Cited by 53 · see citing works
Crystal Structure of Dimeric Heme Oxygenase-2 from Synechocystis sp. PCC 6803 in Complex with Heme,
Sugishima, M., HAGIWARA, Y., Zhang, X., Yoshida, T., Migita, C. T., & Fukuyama, K. (2005) · Biochemistry · doi:10.1021/bi0480483 · Cited by 48 · see citing works
Hwang, H., Lee, J., Chou, K., Suen, C., Hwang, M., Chen, C., Shieh, R., & Chau, L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028001 · Cited by 47 · see citing works
Choi, K. H. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh300 · Cited by 45 · see citing works
Complete nucleotide sequence of human NRAMP2 cDNA
Kishi, F., & Tabuchi, M. (1997) · Molecular Immunology · doi:10.1016/s0161-5890(97)00110-7 · Cited by 45 · see citing works
Self-citationInvolvement of NADP(H) in the Interaction between Heme Oxygenase-1 and Cytochrome P450 Reductase
Higashimoto, Y., Sakamoto, H., Hayashi, S., Sugishima, M., Fukuyama, K., Palmer, G., & Noguchi, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406203200 · Cited by 44 · see citing works
Membrane Topology of NADPH–Cytochrome P450 Reductase on the Endoplasmic Reticulum
Kida, Y., Ohgiya, S., Mihara, K., & Sakaguchi, M. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0553 · Cited by 39 · see citing works
Inositol polyphosphate 1-phosphatase is present in the nucleus and inhibits DNA synthesis.
York, J. D., Saffitz, J. E., & Majerus, P. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32118-x · Cited by 35 · see citing works
Burke, J. M., Cao, F., & Irving, P. E. (2000) · PubMed · Cited by 32 · see citing works
The role of Bach1 in the induction of heme oxygenase by tin mesoporphyrin
Abate, A., Zhao, H. F., Wong, R. J., & Stevenson, D. K. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.01.050 · Cited by 27 · see citing works
Iron and Malaria: Absorption, Efficacy and Safety
Hurrell, R. F. (2010) · International Journal for Vitamin and Nutrition Research · doi:10.1024/0300-9831/a000035 · Cited by 26 · see citing works
Huber, W. J., Scruggs, B. A., & Backes, W. L. (2008) · Biochemistry · doi:10.1021/bi801912z · Cited by 25 · see citing works
Sustained expression of heme oxygenase-1 alters iron homeostasis in nonerythroid cells
Li, C., Lönn, M. E., Xu, X., Maghzal, G. J., Frazer, D. M., Thomas, S. R., Halliwell, B. B., Richardson, D. R., Anderson, G. J., & Stocker, R. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.03.007 · Cited by 22 · see citing works
Self-citationChaperone turns gatekeeper: PCBP2 and DMT1 form an iron-transport pipeline
Lane, D. J. R., & Richardson, D. R. (2014) · Biochemical Journal · doi:10.1042/bj20140720 · Cited by 22 · see citing works
Self-citationWatts, R. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.02.004 · Cited by 20 · see citing works
Higashimoto, Y., Sato, H., Sakamoto, H., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606163200 · Cited by 19 · see citing works
Sakamoto, H., Omata, Y., Hayashi, S., et al. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03230.x · Cited by 18 · see citing works
Yanatori, I., Yasui, Y., Noguchi, Y., & Kishi, F. (2014) · Cell Biology International · doi:10.1002/cbin.10403 · Cited by 17 · see citing works
Self-citationLiping, Z., Hongbo, S., Xiaohua, L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053835 · Cited by 11 · see citing works
Xia (2009) · International Journal of Molecular Medicine · doi:10.3892/ijmm_00000142 · Cited by 3 · see citing works
Calò, L. A., Savoia, C., Davis, P. A., et al. (2015) · PubMed · Cited by 2 · see citing works
Murahashi, M., Simizu, S., Morioka, M., et al. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.05.142 · Cited by 2 · see citing works
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Nairz, M., & Weiss, G. (2020) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2020.100864 · Cited by 359 · see citing works
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Toyokuni, S., Yanatori, I., Kong, Y., Zheng, H., Motooka, Y., & Jiang, L. (2020) · Cancer Science · doi:10.1111/cas.14496 · Cited by 142 · see citing works
Self-citation
- Authors
- Yanatori, I., Richardson, D. R., Toyokuni, S., & Kishi, F.
- Affiliations
- Kawasaki Medical School (JP)
- The University of Sydney (AU)
- Corresponding author
- Kishi, Fumio
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2017-08
- Volume
- 292
- Issue
- 32
- Pages
- 13205-13229
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC5555184
- OpenAlex
- W2724653687
- Cited by
- 69
- References
- 100
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 5 · 2023: 9 · 2022: 7 · 2021: 8 · 2020: 8 · 2019: 10 · 2018: 9 · 2017: 1
- FWCI
- 3.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Griffith Research Online (submittedVersion, cc-by)
- Funders
- Japan Agency for Medical Research and Development (Research Program on Hepatitis)
- National Health and Medical Research Council (APP1128152, APP1060482, APP1062607)
- Japan Society for the Promotion of Science (Invitation Fellowship & 22591052)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heme Oxygenase-1 and Carbon Monoxide
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Keywords
- heme oxygenase-1, NADPH-cytochrome P450 reductase, heme degradation, iron transfer, metabolon, ferrous iron, iron chaperone, protein-protein interaction
- MeSH terms
- Binding Sites, Binding, Competitive, Biological Transport, Cell Line, Heme, Heme Oxygenase (Decyclizing), Humans, Iron, Metalloporphyrins, Mutation, NADPH-Ferrihemoprotein Reductase, Recombinant Fusion Proteins, Transcription Factors, RNA-Binding Proteins, Gene Deletion, Amino Acid Substitution, Protein Transport, RNA Interference, Structural Homology, Protein, Heme Oxygenase-1, Protein Interaction Domains and Motifs, Protein Multimerization
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