Iron regulatory protein-1 protects against mitoferrin-1-deficient porphyria

Two to tango: Regulation of Mammalian iron metabolism

Hentze, M. W., Muckenthaler, M. U., Galy, B., & Camaschella, C. (2010) · Cell · doi:10.1016/j.cell.2010.06.028 · Cited by 2,120 · see citing works

Function and biogenesis of iron-sulphur proteins

Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167 · see citing works

The role of iron regulatory proteins in mammalian iron homeostasis and disease

Rouault, T. A. (2006) · Nature Chemical Biology · doi:10.1038/nchembio807 · Cited by 1,055 · see citing works

Teratocarcinomas and Embryonic Stem Cells: A Practical Approach

Robertson, E. J., & Beddington, R. (1988) · Development · doi:10.1242/dev.102.1.3 · Cited by 1,034 · see citing works

The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins

Kispál, G., Csere, P., Prohl, C., & Lill, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.14.3981 · Cited by 699 · 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

Mammalian iron metabolism and its control by iron regulatory proteins

Anderson, C. P., Shen, M., Eisenstein, R. S., & Leibold, E. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.010 · Cited by 493 · see citing works

An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis

Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H.-W., Kinch, L. N., Li, Q., Grishin, N. V., & Bruick, R. K. (2009) · Science · doi:10.1126/science.1176326 · Cited by 432 · see citing works

Control of iron homeostasis by an iron-regulated ubiquitin ligase

Vashisht, A. A., Zumbrennen, K. B., Huang, X., Powers, D. N., Durazo, A., Sun, D., Bhaskaran, N., Persson, A., Uhlen, M., Sangfelt, O., et al. (2009) · Science · doi:10.1126/science.1176333 · Cited by 429 · see citing works

Genetic ablations of iron regulatory proteins 1 and 2 reveal why iron regulatory protein 2 dominates iron homeostasis.

Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408 · see citing works

Iron–sulfur cluster biogenesis and human disease

Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 387 · see citing works

Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.

The Tübingen 2000 Screen Consortium, Wingert, R. A., Galloway, J. L., Barut, B., Foott, H., Fraenkel, P., Axe, J. L., Weber, G. J., Dooley, K., Davidson, A. J., et al. (2005) · Nature · doi:10.1038/nature03887 · Cited by 370 · see citing works

Regulation of Mitochondrial Iron Import through Differential Turnover of Mitoferrin 1 and Mitoferrin 2

Paradkar, P. N., Zumbrennen, K. B., Paw, B. H., Ward, D. M., & Kaplan, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01685-08 · Cited by 362 · see citing works

CCC1 Is a Transporter That Mediates Vacuolar Iron Storage in Yeast

Li, L., Chen, O. S., Ward, D. M., & Kaplan, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103944200 · Cited by 354 · see citing works

Identification of a novel iron‐responsive element in murine and human erythroid delta‐aminolevulinic acid synthase mRNA.

Dandekar, T., Stripecke, R., Gray, N. K., Goossen, B., Constable, A., Johansson, H. E., & Hentze, M. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07716.x · Cited by 347 · see citing works

C-Terminal Deletions in the ALAS2 Gene Lead to Gain of Function and Cause X-linked Dominant Protoporphyria without Anemia or Iron Overload

Whatley, S. D., Ducamp, S., Gouya, L., Grandchamp, B., Beaumont, C., Badminton, M. N., Elder, G. H., Holme, S. A., Anstey, A. V., Parker, M., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.08.003 · Cited by 289 · see citing works

Positional cloning of the zebrafish sauternes gene: a model for congenital sideroblastic anaemia

Brownlie, A., Donovan, A., Pratt, S. J. P., Paw, B. H., Oates, A. C., Brugnara, C., Witkowska, H. E., Sassa, S., & Zon, L. I. (1998) · Nature Genetics · doi:10.1038/3049 · Cited by 244 · see citing works

Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts

Ye, H., Jeong, S. Y., Ghosh, M. C., Kovtunovych, G., Silvestri, L., Ortillo, D., Uchida, N., Tisdale, J. F., Camaschella, C., & Rouault, T. A. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40372 · Cited by 239 · see citing works

BayGenomics: a resource of insertional mutations in mouse embryonic stem cells

Stryke, D. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg064 · Cited by 239 · see citing works

Human Iron−Sulfur Cluster Assembly, Cellular Iron Homeostasis, and Disease

Ye, H., & Rouault, T. A. (2010) · Biochemistry · doi:10.1021/bi1004798 · Cited by 238 · see citing works

One ring to rule them all: Trafficking of heme and heme synthesis intermediates in the metazoans

Hamza, I., & Dailey, H. A. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.04.009 · Cited by 237 · see citing works

Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2

Cooperman, S. S., Meyron-Holtz, E. G., Olivierre-Wilson, H., Ghosh, M. C., McConnell, J. P., & Rouault, T. A. (2005) · Blood · doi:10.1182/blood-2004-12-4703 · Cited by 235 · see citing works

Altered body iron distribution and microcytosis in mice deficient in iron regulatory protein 2 (IRP2)

Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 222 · see citing works

The IRP1-HIF-2α Axis Coordinates Iron and Oxygen Sensing with Erythropoiesis and Iron Absorption

Anderson, S. A., Nizzi, C. P., Chang, Y.-I., Deck, K. M., Schmidt, P. J., Galy, B., Damnernsawad, A., Broman, A. T., Kendziorski, C., Hentze, M. W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.007 · Cited by 211 · see citing works

The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron–sulfur cluster biogenesis

Pondarré, C., Antiochos, B., Campagna, D. R., Clarke, S. L., Greer, E. L., Deck, K. M., McDonald, A. A., Han, A., Medlock, A. E., Kutok, J. L., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl012 · Cited by 208 · see citing works

Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells

Tong, W., & Rouault, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5692 · Cited by 194 · see citing works

RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload

Cavadini, P., Biasiotto, G., Poli, M., Levi, S., Verardi, R., Zanella, I., Derosas, M., Ingrassia, R., Corrado, M., & Arosio, P. (2006) · Blood · doi:10.1182/blood-2006-08-041632 · Cited by 155 · see citing works

Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p

Csere, P., Lill, R., & Kispál, G. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01560-9 · Cited by 132 · see citing works

Genetic regulation of primitive hematopoietic stem cell senescence

Chen, J., Astle, C. M., & Harrison, D. E. (2000) · Experimental Hematology · doi:10.1016/s0301-472x(99)00157-5 · Cited by 131 · see citing works

Iron and Porphyrin Trafficking in Heme Biogenesis

Schultz, I. J., Chen, C., Paw, B. H., & Hamza, I. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.r110.119503 · Cited by 129 · see citing works

Snx3 Regulates Recycling of the Transferrin Receptor and Iron Assimilation

Chen, C., Garcia‐Santos, D., Ishikawa, Y., Seguin, A., Li, L., Fegan, K. H., Hildick-Smith, G. J., Shah, D. I., Cooney, J. D., Chen, W., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.01.013 · Cited by 124 · see citing works

Posttranslational stability of the heme biosynthetic enzyme ferrochelatase is dependent on iron availability and intact iron-sulfur cluster assembly machinery

Crooks, D. R., Ghosh, M. C., Haller, R. G., Tong, W.-H., & Rouault, T. A. (2009) · Blood · doi:10.1182/blood-2009-09-243105 · Cited by 112 · see citing works

Loss-of-Function Ferrochelatase and Gain-of-Function Erythroid-Specific 5-Aminolevulinate Synthase Mutations Causing Erythropoietic Protoporphyria and X-Linked Protoporphyria in North American Patients Reveal Novel Mutations and a High Prevalence of X-Linked Protoporphyria

Balwani, M., Doheny, D. O., Bishop, D. F., Nazarenko, I. A., Yasuda, M., Dailey, H. A., Anderson, K. E., Bissell, D. M., Bloomer, J. R., Bonkovsky, H. L., et al. (2013) · Molecular Medicine · doi:10.2119/molmed.2012.00340 · Cited by 98 · see citing works

Targeted deletion of the mouse Mitoferrin1 gene: from anemia to protoporphyria

Troadec, M.-B., Warner, D., Wallace, J., Thomas, K., Spangrude, G. J., Phillips, J., Khalimonchuk, O., Paw, B. H., Ward, D. M., & Kaplan, J. (2011) · Blood · doi:10.1182/blood-2010-11-319483 · Cited by 97 · see citing works

Iron‐responsive degradation of iron‐regulatory protein 1 does not require the Fe–S cluster

Clarke, S. L., Vasanthakumar, A., Anderson, S. A., Pondarré, C., Koh, C. M., Deck, K. M., Pitula, J. S., Epstein, C. J., Fleming, M. D., & Eisenstein, R. S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7600954 · Cited by 95 · see citing works

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria

To‐Figueras, J., Ducamp, S., Clayton, J., et al. (2011) · Blood · doi:10.1182/blood-2011-03-342873 · Cited by 93 · see citing works

Heme metabolism and erythropoiesis

Chung, J., Chen, C., & Paw, B. H. (2012) · Current Opinion in Hematology · doi:10.1097/moh.0b013e328351c48b · Cited by 92 · see citing works

Mitochondrial Atpif1 regulates haem synthesis in developing erythroblasts

Shah, D. I., Takahashi‐Makise, N., Cooney, J. D., Li, L., Schultz, I. J., Pierce, E. L., Narla, A., Seguin, A., Hattangadi, S. M., Medlock, A. E., et al. (2012) · Nature · doi:10.1038/nature11536 · Cited by 90 · see citing works

Remodeling the regulation of iron metabolism during erythroid differentiation to ensure efficient heme biosynthesis

Schranzhofer, M., Schifrer, M., Cabrera, J. A., Kopp, S., Chiba, P., Beug, H., & Müllner, E. W. (2006) · Blood · doi:10.1182/blood-2005-05-1809 · Cited by 89 · see citing works

Zebrafish kidney stromal cell lines support multilineage hematopoiesis

Stachura, D. L., Reyes, J. R., Bartůněk, P., Paw, B. H., Zon, L. I., & Traver, D. J. (2009) · Blood · doi:10.1182/blood-2009-02-203638 · Cited by 86 · see citing works

Rapid sequence analysis of gene trap integrations to generate a resource of insertional mutations in mice.Preprint

Townley, D. J., Avery, B. J., Rosen, B. P., et al. (1997) · Genome Research · doi:10.1101/gr.7.3.293 · Cited by 79 · see citing works

Identification of ZBP-89 as a Novel GATA-1-Associated Transcription Factor Involved in Megakaryocytic and Erythroid Development

Woo, A. J., Moran, T. B., Schindler, Y. L., Choe, S., Langer, N. B., Sullivan, M. R., Fujiwara, Y., Paw, B. H., & Cantor, A. B. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01945-07 · Cited by 64 · see citing works

SATB2 augments ΔNp63α in head and neck squamous cell carcinoma

Chung, J., Lau, M. J., Cheng, L. S., Grant, R., Robinson, F., Ketela, T. W., Reis, P. P., Roche, O., Kamel‐Reid, S., Moffat, J., et al. (2010) · EMBO Reports · doi:10.1038/embor.2010.125 · Cited by 59 · see citing works

X-linked Sideroblastic Anemia Due to Carboxyl-terminal ALAS2 Mutations That Cause Loss of Binding to the β-Subunit of Succinyl-CoA Synthetase (SUCLA2)

Bishop, D. F., Tchaikovskii, V., Hoffbrand, A. V., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306423 · Cited by 56 · see citing works

Targeted mutagenesis of the murine IRP1 and IRP2 genes reveals context-dependent RNA processing differences in vivo

Galy, B., Ferring–Appel, D., Benešová, M., Beneš, V., & Hentze, M. W. (2004) · RNA · doi:10.1261/rna.7220704 · Cited by 55 · see citing works

Abnormal mitoferrin-1 expression in patients with erythropoietic protoporphyria

Wang, Y., Langer, N. B., Shaw, G., Yang, G., Li, L., Kaplan, J., Paw, B. H., & Bloomer, J. R. (2011) · Experimental Hematology · doi:10.1016/j.exphem.2011.05.003 · Cited by 45 · see citing works

Identification of Distal cis-Regulatory Elements at Mouse Mitoferrin Loci Using Zebrafish Transgenesis

Amigo, J. D., Yu, M., Troadec, M., Gwynn, B., Cooney, J. D., Lambert, A. J., Chi, N. C., Weiss, M. J., Peters, L. L., Kaplan, J., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01010-10 · Cited by 44 · see citing works

The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability

Kadirvel, S., Furuyama, K., Harigae, H., et al. (2012) · Experimental Hematology · doi:10.1016/j.exphem.2012.01.013 · Cited by 27 · see citing works

An Ancient Gauge for Iron

Rouault, T. A. (2009) · Science · doi:10.1126/science.1181938 · Cited by 25 · see citing works

A Red carpet for iron metabolism

Muckenthaler, M. U., Rivella, S., Hentze, M. W., & Galy, B. (2017) · Cell · doi:10.1016/j.cell.2016.12.034 · Cited by 1,319 · see citing works

Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease

Lane, 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 · see citing works

The Role of Iron Regulation in Immunometabolism and Immune-Related Disease

Cronin, S. J. F., Woolf, C. J., Weiss, G., & Penninger, J. M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00116 · Cited by 299 · see citing works

Compartmentalization of iron between mitochondria and the cytosol and its regulation

Mühlenhoff, U., Hoffmann, B., Richter, N., Rietzschel, N., Spantgar, F., Stehling, O., Uzarska, M. A., & Lill, R. (2015) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2015.05.003 · Cited by 95 · see citing works

Photohemolysis. The Comparative Behavior of Erythrocytes from Patients with Different Types of Porphyria

Haining, R. G., Hulse, T. E., & Labbé, R. F. (1969) · Experimental Biology and Medicine · doi:10.3181/00379727-132-34274 · Cited by 16 · see citing works

Diagnosis With Wood's Light

Halprin, K. M. (1967) · JAMA · doi:10.1001/jama.1967.03120190086015 · Cited by 11 · see citing works

The origin of the increased protoporphyrin in erythrocytes of mice with experimentally induced porphyria.

Nakao, K., Wada, O., Takaku, F., et al. (1967) · PubMed · Cited by 36 · see citing works

Studies of porphyrin synthesis in fibroblasts of patients with congenital erythropoietic porphyria and one patient with homozygous coproporphyria

Grandchamp, B., Deybach, J. C., Grelier, M., de Verneuil, H., & NORDMANN, Y. (1980) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(80)90163-4 · Cited by 111 · see citing works

Symptomatic porphyria secondary to hepatocellular carcinoma

Ochiai, T., MORISHIMA, T., & Kondo, M. (1997) · British Journal of Dermatology · doi:10.1046/j.1365-2133.1997.d01-1159.x · Cited by 13 · see citing works