Iron homeostasis and toxicity in retinal degeneration

He, Xining; Hahn, Paul; Iacovelli, Jared; Wong, Robert; King, Chih; Bhisitkul, Robert; Massaro-Giordano, Mina; Dunaief, Joshua L.

doi:10.1016/j.preteyeres.2007.07.004

Cited by 261Iron Metabolism and DisordersRetinal Development and DisordersRetinal Diseases and Treatments

Iron homeostasis and toxicity in retinal degeneration

Open access

He, Xining, Hahn, Paul, Iacovelli, Jared, Wong, Robert, King, Chih, Bhisitkul, Robert, Massaro-Giordano, Mina, Dunaief, Joshua L.·2007·Progress in Retinal and Eye Research

DOI 10.1016/j.preteyeres.2007.07.004PMC PMC2093950

Open this paper in CoChat — free account

Abstract

Iron is essential for many metabolic processes but can also cause damage. As a potent generator of hydroxyl radical, the most reactive of the free radicals, iron can cause considerable oxidative stress. Since iron is absorbed through diet but not excreted except through menstruation, total body iron levels buildup with age. Macular iron levels increase with age, in both men and women. This iron has the potential to contribute to retinal degeneration. Here we present an overview of the evidence suggesting that iron may contribute to retinal degenerations. Intraocular iron foreign bodies cause retinal degeneration. Retinal iron buildup resulting from hereditary iron homeostasis disorders aceruloplasminemia, Friedreich's ataxia, and panthothenate kinase-associated neurodegeneration cause retinal degeneration. Mice with targeted mutation of the iron exporter ceruloplasmin have age-dependent retinal iron overload and a resulting retinal degeneration with features of age-related macular degeneration (AMD). Post mortem retinas from patients with AMD have more iron and the iron carrier transferrin than age-matched controls. Over the past 10 years much has been learned about the intricate network of proteins involved in iron handling. Many of these, including transferrin, transferrin receptor, divalent metal transporter-1, ferritin, ferroportin, ceruloplasmin, hephaestin, iron-regulatory protein, and histocompatibility leukocyte antigen class I-like protein involved in iron homeostasis (HFE) have been found in the retina. Some of these proteins have been found in the cornea and lens as well. Levels of the iron carrier transferrin are high in the aqueous and vitreous humors. The functions of these proteins in other tissues, combined with studies on cultured ocular tissues, genetically engineered mice, and eye exams on patients with hereditary iron diseases provide clues regarding their ocular functions. Iron may play a role in a broad range of ocular diseases, including glaucoma, cataract, AMD, and conditions causing intraocular hemorrhage. While iron deficiency must be prevented, the therapeutic potential of limiting iron-induced ocular oxidative damage is high. Systemic, local, or topical iron chelation with an expanding repertoire of drugs has clinical potential.

Integrity signals

Registry

Crossref · 10.1016/j.preteyeres.2007.07.004

Cites

150 of 150 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Retinal iron levels increase with age, iron is significantly implicated in AMD, and iron chelation may help to reverse the process.
“Retinal iron levels increase with age [1322], iron is significantly implicated in AMD [1323-1329], and iron chelation may help to reverse the process [1330].”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [1328]

Oxygen toxicity, oxygen radicals, transition metals and disease
Halliwell, B., & Gutteridge, J. M. C. (1984) · Biochemical Journal · doi:10.1042/bj2190001 · Cited by 5,330 · see citing works
Hepcidin Regulates Cellular Iron Efflux by Binding to Ferroportin and Inducing Its Internalization
Nemeth, E., Tuttle, M. S., Powelson, J., Vaughn, M. B., Donovan, A., Ward, D. M., Ganz, T., & Kaplan, J. (2004) · Science · doi:10.1126/science.1104742 · Cited by 4,803 · see citing works
A novel MHC class I-like gene is mutated in patients with hereditary haemochromatosis
Feder, J. N., Gnirke, A., Thomas, W., Tsuchihashi, Z., Ruddy, D. A., Basava, A., Dormishian, F., Domingo, R., Ellis, M. C., Fullan, A., et al. (1996) · Nature Genetics · doi:10.1038/ng0896-399 · Cited by 3,664 · see citing works
A Randomized, Placebo-Controlled, Clinical Trial of High-Dose Supplementation With Vitamins C and E, Beta Carotene, and Zinc for Age-Related Macular Degeneration and Vision Loss: AREDS Report No. 8
(2001) · Archives of Ophthalmology · doi:10.1001/archopht.119.10.1417 · Cited by 3,285 · 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
Hepcidin, a urinary antimicrobial peptide synthesized in the liver
Park, C. H., Valore, E. V., Waring, A. J., & Ganz, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008922200 · Cited by 2,168 · see citing works
The Role of Oxidative Stress in the Pathogenesis of Age-Related Macular Degeneration
Beatty, S., Koh, H.-H., Phil, M., Henson, D., & Boulton, M. (2000) · Survey of Ophthalmology · doi:10.1016/s0039-6257(00)00140-5 · Cited by 2,051 · see citing works
A New Mouse Liver-specific Gene, Encoding a Protein Homologous to Human Antimicrobial Peptide Hepcidin, Is Overexpressed during Iron Overload
Pigeon, C., Ilyin, G., Courselaud, B., Leroyer, P., Turlin, B., Brissot, P., & Loréal, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008923200 · Cited by 1,697 · see citing works
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667 · see citing works
A Novel Duodenal Iron-Regulated Transporter, IREG1, Implicated in the Basolateral Transfer of Iron to the Circulation
McKie, A. T., Marciani, P., Rolfs, A., Brennan, K., Wehr, K., Barrow, D., Miret, S., Bomford, A., Peters, T. J., Farzaneh, F., et al. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80425-6 · Cited by 1,422 · see citing works
Iron accumulation in Alzheimer disease is a source of redox-generated free radicals
Smith, M. A., Harris, P. L. R., Sayre, L. M., & Perry, G. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9866 · Cited by 1,357 · see citing works
LEAP-1, a novel highly disulfide-bonded human peptide, exhibits antimicrobial activity
Krause, A., Neitz, S., Mägert, H.-J., Schulz, A., Forssmann, W.-G., Schulz-Knappe, P., & Adermann, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01920-7 · Cited by 1,324 · see citing works
Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress.
Hentze, M. W., & Kühn, L. C. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8175 · Cited by 1,292 · see citing works
The iron exporter ferroportin/Slc40a1 is essential for iron homeostasis
Donovan, A., Lima, C. A., Pinkus, J. L., Pinkus, G. S., Zon, L. I., Robine, S., & Andrews, N. C. (2005) · Cell Metabolism · doi:10.1016/j.cmet.2005.01.003 · Cited by 1,275 · see citing works
A Novel Mammalian Iron-regulated Protein Involved in Intracellular Iron Metabolism
Abboud, S., & Haile, D. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000713200 · Cited by 1,267 · see citing works
The Framingham Eye Study monograph: An ophthalmological and epidemiological study of cataract, glaucoma, diabetic retinopathy, macular degeneration, and visual acuity in a general population of 2631 adults, 1973-1975.
Leibowitz, H. M., Krueger, D. E., Maunder, L. R., Milton, R. C., KINI, M. M., Kahn, H. A., Nickerson, R. J., Pool, J., Colton, T., Ganley, J. P., et al. (1980) · PubMed · Cited by 1,250 · see citing works
Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 ( <i>USF2</i> ) knockout mice
Nicolas, G., Bennoun, M., Devaux, I., Beaumont, C., Grandchamp, B., Kahn, A., & Vaulont, S. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151179498 · Cited by 1,233 · see citing works
The gene encoding the iron regulatory peptide hepcidin is regulated by anemia, hypoxia, and inflammation
Nicolas, G., Chauvet, C., Viatte, L., Danan, J. L., Bigard, X., Devaux, I., Beaumont, C., Kahn, A., & Vaulont, S. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215686 · Cited by 1,214 · see citing works
pH and the recycling of transferrin during receptor-mediated endocytosis.
Dautry‐Varsat, A., Ciechanover, A. J., & Lodish, H. F. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.8.2258 · Cited by 1,178 · see citing works
Hephaestin, a ceruloplasmin homologue implicated in intestinal iron transport, is defective in the sla mouse
Vulpe, C. D., Kuo, Y.-M., Murphy, T. L., Cowley, L., Askwith, C., Libina, N., Gitschier, J., & Anderson, G. J. (1999) · Nature Genetics · doi:10.1038/5979 · Cited by 1,084 · see citing works
Heme oxygenase 1 is required for mammalian iron reutilization
Poss, K. D., & Tonegawa, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10919 · Cited by 1,016 · see citing works
Current concepts in the pathogenesis of age-related macular degeneration
Zarbin, M. A. (2004) · Archives of Ophthalmology · doi:10.1001/archopht.122.4.598 · Cited by 1,006 · see citing works
Severe iron deficiency anemia in transgenic mice expressing liver hepcidin
Nicolas, G., Bennoun, M., Porteu, A., Mativet, S., Beaumont, C., Grandchamp, B., Sirito, M., Sawadogo, M., Kahn, A., & Vaulont, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072632499 · Cited by 880 · see citing works
The hemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
Feder, J. N., Penny, D. M., Irrinki, A., Lee, V. K., Lebrón, J. A., Watson, N., Tsuchihashi, Z., Sigal, E., Bjorkman, P. J., & Schatzman, R. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1472 · Cited by 827 · see citing works
Chemistry and biology of eukaryotic iron metabolism
Aisen, P. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(01)00063-2 · Cited by 804 · see citing works
A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome
Zhou, B., Westaway, S. K., Levinson, B., Johnson, M., Gitschier, J. M., & Hayflick, S. J. (2001) · Nature Genetics · doi:10.1038/ng572 · Cited by 756 · see citing works
Regulation of Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756 · cited 1× · see citing works
“Most of these mutations affect hepcidin transcription and lead to hepcidin deficiency (Nemeth and Ganz, 2006).”
Background
The Evolution of Iron Chelators for the Treatment of Iron Overload Disease and Cancer
Kalinowski, D. S., & Richardson, D. R. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.4.2 · Cited by 721 · see citing works
The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.
Osaki, S., Johnson, D. A., & Frieden, E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96527-0 · Cited by 679 · see citing works
Cyclic GMP-Activated Conductance of Retinal Photoreceptor Cells
Yau, K., & Baylor, D. A. (1989) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.12.030189.001445 · Cited by 592 · see citing works
Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
Harris, Z. L., Durley, A. P., Man, T. K., & Gitlin, J. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.19.10812 · Cited by 568 · see citing works
Aceruloplasminemia: molecular characterization of this disorder of iron metabolism.
Harris, Z. L., Takahashi, Y., Miyajima, H., Serizawa, M., MacGillivray, R. T., & Gitlin, J. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.7.2539 · Cited by 558 · cited 2× · see citing works
“1 Aceruloplasminemia—Aceruloplasminemia is a rare adult-onset autosomal recessive disease caused by mutations in the ceruloplasmin gene on chromosome 3q (Harris et al., 1995).”
BackgroundInfluential
RPE65 is the isomerohydrolase in the retinoid visual cycle
Moiseyev, G., Chen, Y., Takahashi, Y., Wu, B. X., & Ma, J.-X. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503460102 · Cited by 536 · see citing works
Iron release from macrophages after erythrophagocytosis is up-regulated by ferroportin 1 overexpression and down-regulated by hepcidin
Knutson, M. D., Oukka, M., Koss, L. M., Aydemir, F., & Wessling-Resnick, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409409102 · Cited by 479 · see citing works
The relationship of age-related maculopathy, cataract, and glaucoma to visual acuity.
Klein, R., Wang, Q., Klein, R., Moss, S. E., & Meuer, S. M. (1995) · PubMed · Cited by 461 · see citing works
Comparison of effects of oral deferiprone and subcutaneous desferrioxamine on myocardial iron concentrations and ventricular function in beta-thalassaemia
Anderson, L. J., Wonke, B., Prescott, E., Holden, S., Walker, J. M., & Pennell, D. J. (2002) · The Lancet · doi:10.1016/s0140-6736(02)09740-4 · Cited by 431 · see citing works
Visual and Auditory Neurotoxicity in Patients Receiving Subcutaneous Deferoxamine Infusions
Olivieri, N. F., Buncic, J. R., Chew, E., Gallant, T., Harrison, R. V., Keenan, N. K., Logan, W. J., Mitchell, D., Ricci, G., Skarf, B., et al. (1986) · New England Journal of Medicine · doi:10.1056/nejm198604033141402 · Cited by 425 · see citing works
Selective iron chelation in Friedreich ataxia: biologic and clinical implications
Boddaert, N., Le Quan Sang, K. H., Rötig, A., Leroy-Willig, A., Gallet, S., Brunelle, F., Sidi, D., Thalabard, J.-C., Munnich, A., & Cabantchik, Z. I. (2007) · Blood · doi:10.1182/blood-2006-12-065433 · Cited by 409 · see citing works
Experimental subretinal hemorrhage in rabbits
Glatt, H., & Machemer, R. (1982) · American Journal of Ophthalmology · doi:10.1016/0002-9394(82)90301-4 · Cited by 401 · see citing works
A human mitochondrial ferritin encoded by an intronless gene
Levi, S., Corsi, B., Bosisio, M., Invernizzi, R., Volz, A., Sanford, D., Arosio, P., & Drysdale, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100141200 · Cited by 400 · see citing works
Iron metabolism in health and disease
Baldus, W. P. (1995) · Gastroenterology · doi:10.1016/0016-5085(95)90247-3 · Cited by 380 · see citing works
The ferroportin disease
Pietrangelo, A. (2003) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2003.08.003 · Cited by 380 · see citing works
Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury
Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J.-P., & David, S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-15-06578.2002 · Cited by 379 · see citing works
Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
Jeong, S. Y., & David, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301988200 · Cited by 377 · see citing works
Evidence of altered central nervous system development in infants with iron deficiency anemia at 6 mo: delayed maturation of auditory brainstem responses
Roncagliolo, M., Marcelo Garrido, S., Walter, T., Peirano, P. D., & Lozoff, B. (1998) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/68.3.683 · Cited by 371 · see citing works
A Novel Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin Is Expressed by Mammalian Astrocytes
Patel, B. N., & David, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.32.20185 · Cited by 327 · see citing works
Safety and effectiveness of long-term therapy with the oral iron chelator deferiprone
Cohen, A. R., Galanello, R., Piga, A. G., Sanctis, V. D., & Tricta, F. (2003) · Blood · doi:10.1182/blood-2002-10-3280 · Cited by 321 · see citing works
Distribution of divalent metal transporter 1 and metal transport protein 1 in the normal and Belgrade rat
Burdo, J. R., Menzies, S. L., Simpson, I. A., Garrick, L. M., Garrick, M. D., Dolan, K. G., Haile, D. J., Beard, J. L., & Connor, J. R. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.1256 · Cited by 297 · see citing works
Iron-dependent oxidation, ubiquitination, and degradation of iron regulatory protein 2: Implications for degradation of oxidized proteins
Iwai, K., Drake, S. K., Wehr, N. B., Weissman, A. M., LaVaute, T., Minato, N., Klausner, R. D., Levine, R. L., & Rouault, T. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.9.4924 · Cited by 293 · see citing works
Iron Regulates the Intracellular Degradation of Iron Regulatory Protein 2 by the Proteasome
Guo, B., Phillips, J. D., Yu, Y., & Leibold, E. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21645 · Cited by 287 · see citing works
Iron metabolism in health and disease
Brock, J. H., Halliday, J. W., Pippard, M. J., & Powell, L. W. (1994) · Cited by 286 · see citing works
NMDA Receptor-Nitric Oxide Transmission Mediates Neuronal Iron Homeostasis via the GTPase Dexras1
Cheah, J. H., Kim, S. F., Hester, L. D., Clancy, K. W., Patterson, S. E., Papadopoulos, V., & Snyder, S. H. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.011 · Cited by 285 · see citing works
Brain Iron Metabolism
Rouault, T. A., & Cooperman, S. (2006) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2006.08.002 · Cited by 280 · see citing works
Design, synthesis, and evaluation of novel bifunctional iron-chelators as potential agents for neuroprotection in Alzheimer’s, Parkinson’s, and other neurodegenerative diseases
Zheng, H., Weiner, L. M., Bar-Am, O., Epsztejn, S., Cabantchik, Z. I., Warshawsky, A., Youdim, M. B. H., & Fridkin, M. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2004.10.037 · Cited by 278 · see citing works
Design of clinically useful iron(III)‐selective chelators
Liu, Z. D., & Hider, R. C. (2002) · Medicinal Research Reviews · doi:10.1002/med.1027 · Cited by 266 · see citing works
Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration
Hahn, P., Qian, Y., Dentchev, T., Chen, L., Beard, J., Harris, Z. L., & Dunaief, J. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405146101 · Cited by 264 · see citing works
Self-citation
Expression of Acute-Phase Response Proteins in Retinal Muller Cells in Diabetes
Gerhardinger, C., Costa, M. B. ́., Coulombe, M. C., Toth, I., Hoehn, T., & Grosu, P. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.04-0860 · Cited by 260 · see citing works
Maculas Affected by Age-Related Macular Degeneration Contain Increased Chelatable Iron in the Retinal Pigment Epithelium and Bruch's Membrane
Hahn, P. (2003) · Archives of Ophthalmology · doi:10.1001/archopht.121.8.1099 · Cited by 258 · see citing works
Self-citation
Overexpression of Wild Type and Mutated Human Ferritin H-chain in HeLa Cells
Cozzi, A., Corsi, B., Levi, S., Santambrogio, P., Albertini, A., & Arosio, P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003797200 · Cited by 242 · see citing works
Iron-sulfur clusters as biosensors of oxidants and iron.
Rouault, T. A., & Klausner, R. D. (1996) · PubMed · Cited by 238 · see citing works
The molecular basis of ferroportin-linked hemochromatosis
De Domenico, I., Ward, D. M., Nemeth, E., Vaughn, M. B., Musci, G., Ganz, T., & Kaplan, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503804102 · Cited by 230 · see citing works
Histochemical Distribution of Non-Haem Iron in the Human Brain
Morris, C. M., Candy, J., Oakley, A. E., Bloxham, C. A., & Edwardson, J. A. (1992) · Cells Tissues Organs · doi:10.1159/000147312 · Cited by 218 · see citing works
The safety and effectiveness of deferiprone in a large‐scale, 3‐year study in Italian patients
Ceci, A., Baiardi, P., Felisi, M., Cappellini, M. D., Carnelli, V., Sanctis, V. D., Galanello, R., Maggio, A., Masera, G., Piga, A. G., et al. (2002) · British Journal of Haematology · doi:10.1046/j.1365-2141.2002.03554.x · Cited by 214 · see citing works
Iron-sulfur clusters as biosensors of oxidants and iron
Rouault, T. A., & Klausner, R. D. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)10024-4 · Cited by 207 · see citing works
Deferoxamine-induced growth retardation in patients with thalassemia major
Virgillis, S. D., Congia, M., Frau, F., Argiolu, F., Diana, G., Cucca, F., Varsi, A., Sanna, G., Podda, G., Fodde, M., et al. (1988) · The Journal of Pediatrics · doi:10.1016/s0022-3476(88)80375-5 · Cited by 205 · see citing works
Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
Cazzola, M., Invernizzi, R., Bergamaschi, G., Levi, S., Corsi, B., Travaglino, E., Rolandi, V., Biasiotto, G., Drysdale, J., & Arosio, P. (2003) · Blood · doi:10.1182/blood-2002-07-2006 · Cited by 205 · see citing works
Lactulose 51Cr-labelled ethylenediaminetetra-acetate, l -rhamnose and polyethyleneglycol 500 as probe markers for assessment in vivo of human intestinal permeability
Maxton, D. G., Bjarnason, I., Reynolds, A., Catt, S. D., Peters, T. J., & Menzies, I. S. (1986) · Clinical Science · doi:10.1042/cs0710071 · Cited by 204 · see citing works
Alternative RNA Splicing Generates a Glycosylphosphatidylinositol-anchored Form of Ceruloplasmin in Mammalian Brain
Patel, B. N., Dunn, R. J., & David, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4305 · Cited by 202 · see citing works
The Role of the L-Chain in Ferritin Iron Incorporation
Levi, S., Santambrogio, P., Cozzi, A., Rovida, E., Corsi, B., Tamborini, E., Spada, S., Albertini, A., & Arosio, P. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1325 · Cited by 180 · see citing works
Reduced signal intensity on MR images of thalamus and putamen in multiple sclerosis: increased iron content?
Drayer, B. P., Burger, P. C., Hurwitz, B. J., Dawson, D. V., & Cain, J. (1987) · American Journal of Roentgenology · doi:10.2214/ajr.149.2.357 · Cited by 178 · see citing works
Safety, tolerability, and pharmacokinetics of ICL670, a new orally active iron-chelating agent in patients with transfusion-dependent iron overload due to beta-thalassemia.
Galanello, R., Piga, A. G., Alberti, D., Rouan, M. C., Bigler, H., & Séchaud, R. (2003) · PubMed · Cited by 169 · see citing works
Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase (Ceruloplasmin)
Osaki, S. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99669-9 · Cited by 160 · see citing works
Iron Induced Oxidative Damage As a Potential Factor in Age-Related Macular Degeneration: The Cogan Lecture
Dunaief, J. L. (2006) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.06-0568 · Cited by 154 · see citing works
Self-citation
Essays in neurochemistry and neuropharmacology
(1979) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(79)90033-8 · Cited by 144 · see citing works
Safety, Tolerability, and Pharmacokinetics of ICL670, a New Orally Active Iron-Chelating Agent in Patients with Transfusion-Dependent Iron Overload Due to β-Thalassemia
Galanello, R., Piga, A. G., Alberti, D., Rouan, M. C., Bigler, H., & Séchaud, R. (2003) · The Journal of Clinical Pharmacology · doi:10.1177/0091270003253350 · Cited by 140 · see citing works
Deficiency of pantothenate kinase 2 ( Pank2 ) in mice leads to retinal degeneration and azoospermia
Kuo, Y., Duncan, J. L., Westaway, S. K., Yang, H., Nune, G. C., Xu, E. Y., Hayflick, S. J., & Gitschier, J. M. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddi005 · Cited by 139 · see citing works
Cellular distribution of iron in the brain of the Belgrade rat
Burdo, J. R., Martin, J., Menzies, S. L., Dolan, K. G., Romano, M. A., Fletcher, R. J., Garrick, M. D., Garrick, L. M., & Connor, J. R. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00207-9 · Cited by 130 · see citing works
Pulmonary toxic effects of continuous desferrioxamine administration in acute iron poisoning
Tenenbein, M., Kowalski, S., Sienko, A. E., Bowden, D. H., Adamson, I. Y. R., & Tenenbein, M. (1992) · The Lancet · doi:10.1016/0140-6736(92)90598-w · Cited by 125 · see citing works
Binding to cellular receptors results in increased iron release from transferrin at mildly acidic pH
Sipe, D. M., & Murphy, R. F. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)92931-5 · Cited by 122 · see citing works
Macular Degeneration in a Patient with Aceruloplasminemia, a Disease Associated with Retinal Iron Overload
Dunaief, J. L., Richa, C. G., Franks, E. P., Schultze, R. L., Alemán, T. S., Schenck, J. F., Zimmerman, E. A., & BROOKS, D. (2005) · Ophthalmology · doi:10.1016/j.ophtha.2004.12.029 · Cited by 118 · see citing works
Self-citation
Iron, ferritin, transferrin, and transferrin receptor in the adult rat retina.
Yéfimova, M., Jeanny, J., Guillonneau, X., Keller, N., Nguyen-Legros, J., Sergeant, C., Guillou, F., & Courtois, Y. (2000) · PubMed · Cited by 112 · see citing works
The expanded clinical spectrum of deferoxamine retinopathy11The authors have no commercial or proprietary interest in any of the materials noted in this article.
Haimovici, R., D’Amico, D. J., Gragoudas, E. S., & Sokol, S. (2002) · Ophthalmology · doi:10.1016/s0161-6420(01)00947-2 · Cited by 110 · see citing works
Mechanisms and regulation of transferrin and iron transport in a model blood–brain barrier system
Burdo, J. R., Antonetti, D. A., Wolpert, E. B., & Connor, J. R. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00590-6 · Cited by 106 · see citing works
Gene Microarray Analysis of Experimental Glaucomatous Retina from Cynomologous Monkey
Miyahara, T., Kikuchi, T., Akimoto, M., Kurokawa, T., Shibuki, H., & Yoshimura, N. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.02-1032 · Cited by 106 · see citing works
Novel Chelators for Central Nervous System Disorders That Involve Alterations in the Metabolism of Iron and Other Metal Ions
Richardson, D. R. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.026 · Cited by 104 · see citing works
Non-HFE Hemochromatosis
Pietrangelo, A. (2005) · Seminars in Liver Disease · doi:10.1055/s-2005-923316 · Cited by 102 · see citing works
The Iron Carrier Transferrin Is Upregulated in Retinas from Patients with Age-Related Macular Degeneration
Chowers, I., Wong, R., Dentchev, T., Farkas, R. H., Iacovelli, J., Gunatilaka, T. L., Medeiros, N. E., Presley, J. B., Campochiaro, P. A., Curcio, C. A., et al. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.05-1135 · Cited by 102 · see citing works
Self-citation
Role of Ceruloplasmin in Macrophage Iron Efflux during Hypoxia
Sarkar, J., Seshadri, V., Tripoulas, N. A., Ketterer, M. E., & Fox, P. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304926200 · Cited by 101 · see citing works
Increased Expression of Iron-Regulating Genes in Monkey and Human Glaucoma
Farkas, R. H. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0872 · Cited by 101 · see citing works
Hereditary hemochromatosis
Pietrangelo, A. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.013 · Cited by 99 · see citing works
Deferoxamine-induced bone dysplasia in patients with thalassemia major.
Brill, P. W., Winchester, P., Giardina, P. J., & Cunningham-Rundles, S. (1991) · American Journal of Roentgenology · doi:10.2214/ajr.156.3.1899759 · Cited by 97 · see citing works
Intravenous infusion pharmacokinetics of desferrioxamine in thalassaemic patients.
Lee, P., Mohammed, N., Marshall, L., Abeysinghe, R. D., Hider, R. C., Porter, J. B., & Singh, S. (1993) · Drug Metabolism and Disposition · doi:10.1016/s0090-9556(25)07467-7 · Cited by 92 · see citing works
Iron‐enriched oligodendrocytes: A reexamination of their spatial distribution
LeVine, S. M., & Macklin, W. B. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490260415 · Cited by 91 · see citing works
SIH—a novel lipophilic iron chelator—protects H9c2 cardiomyoblasts from oxidative stress-induced mitochondrial injury and cell death
Šimůnek, T., Boer, C., Bouwman, R. A., VLASBLOM, R., Versteilen, A. M. G., Štěrba, M., Geršl, V., Hrdina, R., Poňka, P., & DELANGE, J. (2005) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2005.05.008 · Cited by 91 · see citing works
Iron levels in human retina: sex difference and increase with age
Hahn, P., Ying, G.-S., Beard, J., & Dunaief, J. L. (2006) · NeuroReport · doi:10.1097/wnr.0b013e3280107776 · Cited by 90 · see citing works
Self-citation
Effects of the carbohydrate-binding protein galectin-3 on the invasiveness of human breast carcinoma cells
Marer, N. L., & Hughes, R. C. (1996) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199607)168:1 · Cited by 84 · see citing works
Increased expression of ceruloplasmin in the retina following photic injury.
Chen, L., Dentchev, T., Wong, R., Hahn, P., Wen, R., Bennett, J., & Dunaief, J. L. (2003) · PubMed · Cited by 84 · see citing works
Self-citation
Is stored iron safe?
Sullivan, J. L. (2004) · Journal of Laboratory and Clinical Medicine · doi:10.1016/j.lab.2004.10.006 · Cited by 82 · see citing works
Differential Sensitivity of Cones to Iron-Mediated Oxidative Damage
Rogers, B. S., Symons, R. C. A., Komeima, K., Shen, J., Xiao, W., Swaim, M., Gong, Y., Kachi, S., & Campochiaro, P. A. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.06-0528 · Cited by 80 · see citing works
Iron increases expression of iron-export protein MTP1 in lung cells
Yang, F., Wang, X., Haile, D. J., Piantadosi, C. A., & Ghio, A. J. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00114.2002 · Cited by 78 · see citing works
Immunolocalization and regulation of iron handling proteins ferritin and ferroportin in the retina.
Hahn, P., Dentchev, T., Qian, Y., Rouault, T. A., Harris, Z. L., & Dunaief, J. L. (2004) · PubMed · Cited by 74 · see citing works
Self-citation
Iron Chelation Therapy
Hershko, C., Link, G., Konijn, A. M., & Cabantchik, Z. I. (2002) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-0593-8 · Cited by 72 · see citing works
Impaired retinal iron homeostasis associated with defective phagocytosis in Royal College of Surgeons rats.
Yéfimova, M., Jeanny, J., Keller, N., Sergeant, C., Guillonneau, X., Beaumont, C., & Courtois, Y. (2002) · PubMed · Cited by 70 · see citing works
Visual Results and Prognostic Factors for Vision Following Surgery for Stage V Retinopathy of Prematurity
Trese, M. T. (1986) · Ophthalmology · doi:10.1016/s0161-6420(86)33681-9 · Cited by 66 · see citing works
Iron chelators of the pyridoxal isonicotinoyl hydrazone class Part I. Ionisation characteristics of the ligands and their relevance to biological properties
Richardson, D. R., Vitolo, L. M. W., Hefter, G. T., May, P. M., Clare, B. W., Webb, J. M., & Wilairat, P. (1990) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)80471-5 · Cited by 66 · see citing works
Iron chelation therapy
Hoffbrand, A. V., & Wonke, B. (1997) · Journal of Internal Medicine · doi:10.1111/joim.1997.242.s740.37 · Cited by 65 · see citing works
Strong Labeling for Iron and the Iron-Handling Proteins Ferritin and Ferroportin in the Photoreceptor Layer in Age-Related Macular Degeneration
Dentchev, T. (2005) · Archives of Ophthalmology · doi:10.1001/archopht.123.12.1745 · Cited by 65 · see citing works
Microsomal electron transfer system of bovine retinal pigment epithelium
Shichi, H. (1969) · Experimental Eye Research · doi:10.1016/s0014-4835(69)80081-3 · Cited by 61 · see citing works
Inhibition of iron absorption prolongs the life span of Drosophila
Massie, H. R., Aiello, V. R., & Williams, T. R. (1993) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(93)90001-8 · Cited by 61 · see citing works
Iron in the Hallervorden-Spatz syndrome
Koeppen, A. H., & Dickson, A. C. (2001) · Pediatric Neurology · doi:10.1016/s0887-8994(01)00269-7 · Cited by 59 · see citing works
Deferasirox—An Oral Agent for Chronic Iron Overload
VanOrden, H. E., & Hagemann, T. M. (2006) · Annals of Pharmacotherapy · doi:10.1345/aph.1g566 · Cited by 59 · see citing works
Evaluation of new iron chelators and their therapeutic potential
Aouad, F., Florence, A., Zhang, Y., Collins, F., Henry, C., Ward, R. J., & Crichton, R. R. (2002) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(02)01040-x · Cited by 58 · see citing works
Post-Transcriptional Regulation of Human Iron Metabolism by Iron Regulatory Proteins
Rouault, T. A. (2002) · Blood Cells Molecules and Diseases · doi:10.1006/bcmd.2002.0571 · Cited by 58 · see citing works
4 Desferrioxamine-induced iron excretion in humans
Pippard, M. J. (1989) · Baillière s Clinical Haematology · doi:10.1016/s0950-3536(89)80020-4 · Cited by 58 · see citing works
Ocular Clinicopathologic Correlation of Hallervorden-Spatz Syndrome with Acanthocytosis and Pigmentary Retinopathy
Luckenbach, M. W., Green, W. R., Miller, N. R., Moser, H. W., Clark, A. W., & Tennekoon, G. I. (1983) · American Journal of Ophthalmology · doi:10.1016/s0002-9394(14)78308-4 · Cited by 57 · see citing works
Iron accumulation during development and ageing of Drosophila
Massie, H. R., Aiello, V. R., & Williams, T. R. (1985) · Mechanisms of Ageing and Development · doi:10.1016/0047-6374(85)90020-x · Cited by 57 · see citing works
Experimental Siderosis in the Rabbit
Declercq, S. S. (1977) · Archives of Ophthalmology · doi:10.1001/archopht.1977.04450060138014 · Cited by 53 · see citing works
Redox control of gene expression involving iron‐sulfur proteins. Change of oxidation‐state or assembly/disassembly of Fe‐S clusters?
Beinert, H., & Kiley, P. J. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00140-8 · Cited by 53 · see citing works
Transferrin receptors on the surfaces of retinal pigment epithelial cells are associated with the cytoskeleton
Hunt, R. C., Dewey, A. R., & Davis, A. A. (1989) · Journal of Cell Science · doi:10.1242/jcs.92.4.655 · Cited by 52 · see citing works
Experimental Ocular Siderosis in the Squirrel Monkey
Masciulli, L., Anderson, D. R., & Charles, S. T. (1972) · American Journal of Ophthalmology · doi:10.1016/0002-9394(72)90826-4 · Cited by 50 · see citing works
Absorption of retinal and subretinal hemorrhages.
Gillies, A., & Lahav, M. (1983) · PubMed · Cited by 49 · see citing works
Neuropharmacological and Neurobiochemical Aspects of Iron Deficiency
Youdim, M. B. H. (1990) · Springer eBooks · doi:10.1007/978-1-4471-1766-7_9 · Cited by 47 · see citing works
Expression and Polarized Localization of the Hemochromatosis Gene Product HFE in Retinal Pigment Epithelium
Martin, P. M. (2006) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.06-0026 · Cited by 47 · see citing works
Expression of ceruloplasmin in the retina: induction after optic nerve crush.
Levin, L. A., & Geszvain, K. (1998) · PubMed · Cited by 43 · see citing works
Hemoglobin-Induced Lipid Peroxidation in the Retina: A Possible Mechanism for Macular Degeneration
Ito, T. K., Nakano, M., Yamamoto, Y., Hiramitsu, T., & Mizuno, Y. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.1116 · Cited by 43 · see citing works
HBED ligand: preclinical studies of a potential alternative to deferoxamine for treatment of chronic iron overload and acute iron poisoning
Bergeron, R. J., Wiegand, J., & Brittenham, G. M. (2002) · Blood · doi:10.1182/blood.v99.8.3019 · Cited by 43 · see citing works
Clinical aspects of ocular siderosis and hemosiderosis.
Cibis, P. A., YAMASHITA, T., & Rodriguez, F. R. (1959) · PubMed · Cited by 42 · see citing works
Retinal Degeneration in Hereditary Ceruloplasmin Deficiency
Yamaguchi, K., Takahashi, S., Kawanami, T., Kato, T., & Sasaki, H. (1997) · Ophthalmologica · doi:10.1159/000027251 · Cited by 40 · see citing works
Ocular Pathologic Changes in Primary Hemochromatosis
Roth, A. M., & Foos, R. Y. (1972) · Archives of Ophthalmology · doi:10.1001/archopht.1972.01000020509003 · Cited by 39 · see citing works
Nuclear ferritin in corneal epithelial cells: tissue–specific nuclear transport and protection from UV–damage
Linsenmayer, T. F., Cai, C. X., Millholland, J. M., Beazley, K. E., & Fitch, J. M. (2004) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2004.08.004 · Cited by 37 · see citing works
Pigmentary Degeneration of the Retina in the Hallervorden-Spatz Syndrome
Newell, F. W., Johnson, R. O., & Huttenlocher, P. R. (1979) · American Journal of Ophthalmology · doi:10.1016/0002-9394(79)90648-2 · Cited by 37 · see citing works
Ultrastructural Studies of Cornea, Iris and Lens in a Case of Siderosis Bulbi
Talamo, J. H., Topping, T. M., Maumenee, A. E., & Green, W. R. (1985) · Ophthalmology · doi:10.1016/s0161-6420(85)34090-3 · Cited by 35 · see citing works
Regulation of Ferritin Levels in Cultured Lens Epithelial Cells
McGahan, M. C., Harned, J., Grimes, A. M., & Fleisher, L. N. (1994) · Experimental Eye Research · doi:10.1006/exer.1994.1140 · Cited by 34 · see citing works
Transferrin, One of the Major Vitreous Proteins, is Produced Within the Eye
Laicine, E. M., & Haddad, A. (1994) · Experimental Eye Research · doi:10.1006/exer.1994.1129 · Cited by 33 · see citing works
Overexpression of H- and L-ferritin subunits in lens epithelial cells: Fe metabolism and cellular response to UVB irradiation.
Goralska, M., Holley, B. L., & McGahan, M. C. (2001) · PubMed · Cited by 32 · see citing works
Release of iron by human retinal pigment epithelial cells
Hunt, R. C., & Davis, A. A. (1992) · Journal of Cellular Physiology · doi:10.1002/jcp.1041520114 · Cited by 31 · see citing works
Transferrin secretion by lens epithelial cells in culture
McGahan, M. C., Harned, J., Goralska, M., Sherry, B., & Fleisher, L. N. (1995) · Experimental Eye Research · doi:10.1016/s0014-4835(05)80008-9 · Cited by 30 · see citing works
Gene Therapy for Ocular Neovascularization
Campochiaro, P. A. (2007) · Current Gene Therapy · doi:10.2174/156652307779940252 · Cited by 24 · see citing works
Catastrophic Visual Loss in a Patient With Friedreich Ataxia
Porter, N. (2007) · Archives of Ophthalmology · doi:10.1001/archopht.125.2.273 · Cited by 23 · see citing works
Contribution of plasma proteins to the vitreous of the rat
Hawkins, K. N. (1986) · Current Eye Research · doi:10.3109/02713688609015133 · Cited by 23 · see citing works
Antioxidant activity of aqueous and vitreous humor from the inflamed rabbit eye
McGahan, M. C., & Fleisher, L. N. (1986) · Current Eye Research · doi:10.3109/02713688609015131 · Cited by 22 · see citing works
A Study of Potential Toxic Effects After Repeated 10-Week Administration of a New Iron Chelator – Salicylaldehyde Isonicotinoyl Hydrazone (SIH) to Rabbits
Klimtová, I., Šimůnek, T., Mazurová, Y., Kaplanová, J., Štěrba, M., Hrdina, R., Geršl, V., Adamcová, M., & Poňka, P. (2003) · Acta Medica (Hradec Kralove Czech Republic) · doi:10.14712/18059694.2019.27 · Cited by 20 · see citing works
Ocular Siderosis
Sneed, S. R. (1988) · Archives of Ophthalmology · doi:10.1001/archopht.1988.01060140143041 · Cited by 19 · see citing works
Aqueous humor of cat contains fibroblast growth factor and transferrin similar to those in man
Tripathi, R. C., Millard, C. B., Tripathi, B. J., Chailertborisuth, N. S., Neely, K. A., & Ernest, J. T. (1990) · Experimental Eye Research · doi:10.1016/0014-4835(90)90016-n · Cited by 18 · see citing works
Fluorescein angiographic findings in ocular siderosis
Shaikh, S., & Blumenkranz, M. S. (2001) · American Journal of Ophthalmology · doi:10.1016/s0002-9394(00)00718-2 · Cited by 18 · see citing works
Binding of Iron to the 5th Component of Human Complement Directs Oxygen Radical-Mediated Conversion to Specific Sites and Causes Nonenzymic Activation
Vogt, W., Nolte, R., & Brunahl, D. (2017) · Complement and Inflammation · doi:10.1159/000463202 · Cited by 17 · see citing works
Lens epithelial cells synthesize and secrete ceruloplasmin: Effects of ceruloplasmin and transferrin on iron efflux and intracellular iron dynamics
Harned, J., Fleisher, L. N., & McGahan, M. C. (2006) · Experimental Eye Research · doi:10.1016/j.exer.2006.01.018 · Cited by 14 · see citing works
Quantitative study of characteristic aqueous humor transferrin, serum transferrin and desialized serum transferrin in aqueous humor.
Yu, T.-C., & Okamura, R. (1988) · PubMed · Cited by 14 · see citing works
Cluster analysis of genes with significant change in expression in cells conditioned to survive TBOOH
Li, D., Ma, W., Sun, F. Y., Pavlidis, P., & Spector, A. (2003) · Experimental Eye Research · doi:10.1016/j.exer.2003.10.016 · Cited by 8 · see citing works
Deferoxamine Reduces Retinal Toxicity from Subretinal Blood
Youssef, T., Trese, M. T., Hartzer, M. K., Mahgoub, M. M., Raza, H., Azrak, M. I., & Allredge, C. (2002) · Investigative Ophthalmology & Visual Science · Cited by 5 · see citing works

Flagged first, then by citations

3 of the 153 references couldn’t be matched to a known paper.

Sorted by citations

The Retinal Pigment Epithelium in Health and Disease
Sparrrow, J. R., Hicks, D., & Hamel, C. (2010) · Current Molecular Medicine · doi:10.2174/156652410793937813 · Cited by 625 · see citing works
The dynamic nature of Bruch's membrane
Booij, J. C., Baas, D. C., Beisekeeva, J., Gorgels, T. G. M. F., & Bergen, A. A. B. (2010) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2009.08.003 · Cited by 581 · see citing works
Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases
Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554 · see citing works
The proteasomal system
Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 389 · see citing works
Incomplete response to Anti-VEGF therapy in neovascular AMD: Exploring disease mechanisms and therapeutic opportunities
Mettu, P. S., Allingham, M. J., & Cousins, S. W. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100906 · Cited by 370 · see citing works
Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson’s, Huntington’s, Alzheimer’s, prions, bactericides, chemical toxicology and others as examples
Kell, D. B. (2010) · Archives of Toxicology · doi:10.1007/s00204-010-0577-x · Cited by 361 · see citing works
Age-Related Macular Degeneration Revisited – Piecing the Puzzle: The LXIX Edward Jackson Memorial Lecture
Miller, J. W. (2012) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2012.10.018 · Cited by 250 · see citing works
Age-related macular degeneration (AMD): Alzheimer's disease in the eye?
Kaarniranta, K., Salminen, A., Haapasalo, A., Soininen, H., & Hiltunen, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101908 · Cited by 248 · see citing works
Intravenous transferrin, RGD peptide and dual-targeted nanoparticles enhance anti-VEGF intraceptor gene delivery to laser-induced CNV
Singh, S. R., GROSSNIKLAUS, H. E., Kang, S. J., Edelhauser, H. F., Ambati, B. K., & Kompella, U. B. (2009) · Gene Therapy · doi:10.1038/gt.2008.185 · Cited by 204 · see citing works
Pathologically high intraocular pressure disturbs normal iron homeostasis and leads to retinal ganglion cell ferroptosis in glaucoma
Yao, F., Peng, J.-J., Zhang, E., Ji, D., Gao, Z., Tang, Y., Yao, X., & Xia, X. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01046-4 · Cited by 200 · see citing works
Iron Accumulation and Lipid Peroxidation in the Aging Retina: Implication of Ferroptosis in Age-Related Macular Degeneration
Zhao, T., Guo, X., & Sun, Y. (2021) · Aging and Disease · doi:10.14336/ad.2020.0912 · Cited by 176 · see citing works
Molecular regulation of neuroinflammation in glaucoma: Current knowledge and the ongoing search for new treatment targets
Tezel, G. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2021.100998 · Cited by 172 · see citing works
Retinal ultrastructure of murine models of dry age-related macular degeneration (AMD)
Ramkumar, H. L., Zhang, J., & Chan, C.-C. (2010) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2010.02.002 · Cited by 163 · see citing works
Molecular and Histopathological Changes Associated with Keratoconus
Khaled, M. L., Helwa, I., Drewry, M. D., Seremwe, M., Estes, A. J., & Liu, Y. (2017) · BioMed Research International · doi:10.1155/2017/7803029 · Cited by 157 · see citing works
Iron, zinc, and copper in retinal physiology and disease
Ugarte, M., Osborne, N. N., Brown, L. A., & Bishop, P. N. (2013) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2012.12.002 · Cited by 157 · see citing works
Safety Assessment of Nanomaterials to Eyes: An Important but Neglected Issue
Zhu, S., Gong, L., Li, Y., Xu, H., Gu, Z., & Zhao, Y. (2019) · Advanced Science · doi:10.1002/advs.201802289 · Cited by 153 · see citing works
Iron overload: Effects on cellular biochemistry
Nogueira, L. S., Oliveira, M. M., Pessoa, M. T., & Barbosa, L. A. (2019) · Clinica Chimica Acta · doi:10.1016/j.cca.2019.11.029 · Cited by 144 · see citing works
PATHWAY-BASED THERAPIES FOR AGE-RELATED MACULAR DEGENERATION
Zarbin, M. A., & Rosenfeld, P. J. (2010) · Retina · doi:10.1097/iae.0b013e3181f57e30 · Cited by 140 · see citing works
Iron homeostasis and eye disease
Loh, A. R., Hadziahmetovic, M., & Dunaief, J. L. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.11.001 · Cited by 125 · see citing works
Self-citation
Oxidative stress and its downstream signaling in aging eyes
Pinazo-Duran, M. D., Gallego‐Pinazo, R., García‐Medina, J. J., Zanón‐Moreno, V., Nucci, C., Dolz‐Marco, R., Martínez-Castillo, S., Galbis, C. C., Díaz-Llopis, M., Marco, C., et al. (2014) · Clinical Interventions in Aging · doi:10.2147/cia.s52662 · Cited by 126 · see citing works
Dysfunction of the Retinal Pigment Epithelium with Age: Increased Iron Decreases Phagocytosis and Lysosomal Activity
Chen, H., Lukas, T. J., Du, N. Y., Suyeoka, G. M., & Neufeld, A. H. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-2850 · Cited by 119 · see citing works
RPE phagocytic function declines in age-related macular degeneration and is rescued by human umbilical tissue derived cells
Inana, G., Murat, C., An, W., Yao, X., Harris, I. R., & Cao, J. (2018) · Journal of Translational Medicine · doi:10.1186/s12967-018-1434-6 · Cited by 113 · see citing works
Metal-organic frameworks, NH2-MIL-88(Fe), as carriers for ophthalmic delivery of brimonidine
Kim, S.-N., Park, C. G., Huh, B. K., Lee, S. H., Min, C. H., Lee, Y. Y., Kim, Y. K., Park, K. H., & Choy, Y. B. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.08.023 · Cited by 106 · see citing works
Aceruloplasminemia: A Severe Neurodegenerative Disorder Deserving an Early Diagnosis
Marchi, G., Busti, F., Zidanes, A. L., Castagna, A., & Girelli, D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00325 · Cited by 103 · see citing works
Unifying Mechanism for Eye Toxicity: Electron Transfer, Reactive Oxygen Species, Antioxidant Benefits, Cell Signaling and Cell Membranes
Kovacic, P., & Somanathan, R. (2008) · Cited by 101 · see citing works
Bilayer Hydrogel Sheet‐Type Intraocular Microrobot for Drug Delivery and Magnetic Nanoparticles Retrieval
Kim, D., Lee, H., Kwon, S.-H., Sung, Y. J., Song, W. K., & Park, S. (2020) · Advanced Healthcare Materials · doi:10.1002/adhm.202000118 · Cited by 97 · see citing works
Retinal pigment epithelium 65 kDa protein (RPE65): An update
Kiser, P. D. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2021.101013 · Cited by 96 · see citing works
Exposure, assessment and health hazards of particulate matter in metal additive manufacturing: A review
Chen, R., Yin, H. F., Cole, I. S., Shen, S., Zhou, X., Wang, Y., & Tang, S. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.127452 · Cited by 87 · see citing works
Iron accumulation in Bruch's membrane and melanosomes of donor eyes with age-related macular degeneration
Biesemeier, A., Yoeruek, E., Eibl, O., & Schraermeyer, U. (2015) · Experimental Eye Research · doi:10.1016/j.exer.2015.05.019 · Cited by 87 · see citing works
Increased proteasomal activity supports photoreceptor survival in inherited retinal degeneration
Lobanova, E. S., Finkelstein, S., Li, J., Travis, A. M., Hao, Y., Klingeborn, M., Skiba, N. P., Deshaies, R. J., & Arshavsky, V. Y. (2018) · Nature Communications · doi:10.1038/s41467-018-04117-8 · Cited by 82 · see citing works
The Importance of the Stem Cell Marker Prominin-1/CD133 in the Uptake of Transferrin and in Iron Metabolism in Human Colon Cancer Caco-2 Cells
Bourseau-Guilmain, E., Griveau, A., Benoît, J., & Garcion, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025515 · Cited by 80 · see citing works
Mechanisms of protein aggregation in the retinal pigment epithelial cells
Kaarniranta, K. (2010) · Frontiers in Bioscience-Elite · doi:10.2741/e198 · Cited by 78 · see citing works
Human RPE Melanosomes Protect from Photosensitized and Iron-Mediated Oxidation but Become Pro-oxidant in the Presence of Iron upon Photodegradation
Rozanowski, B., Burke, J. M., Boulton, M. E., Sarna, T., & Rozanowska, M. (2008) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-1700 · Cited by 76 · see citing works
Neuroprotective effect of intravitreal triamcinolone acetonide against photoreceptor apoptosis in a rabbit model of subretinal hemorrhage
Bhisitkul, R. B., Winn, B. J., Lee, O.-T., Wong, J., Pereira, D. D. S., Porco, T. C., He, X., Hahn, P., & Dunaief, J. L. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.08-1892 · Cited by 76 · see citing works
Self-citation
Iron: Effect of Overload and Deficiency
Hider, R. C., & Kong, X. (2013) · Metal ions in life sciences · doi:10.1007/978-94-007-7500-8_8 · Cited by 74 · see citing works
Cobalt–chromium toxic retinopathy case study
Apel, W., Stark, D. J., Stark, A. P., O’Hagan, S., & Ling, J. (2012) · Documenta Ophthalmologica · doi:10.1007/s10633-012-9356-8 · Cited by 68 · see citing works
Iron derived from NCOA4-mediated ferritinophagy causes cellular senescence via the cGAS-STING pathway
Li, H., Wei, T., Zhuang, M., Tan, C., Xie, T., Cai, J., Yao, Y., & Zhu, L. (2023) · Cell Death Discovery · doi:10.1038/s41420-023-01712-7 · Cited by 67 · see citing works
Iron promotes oxidative cell death caused by bisretinoids of retina
Ueda, K., Kim, H. J., Zhao, J., Song, Y., Dunaief, J. L., & Sparrow, J. R. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722601115 · Cited by 65 · see citing works
Self-citation
Beneficial and Detrimental Roles of Heme Oxygenase-1 in the Neurovascular System
Choi, Y. K., & Kim, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137041 · Cited by 63 · see citing works
The kinesin KIF16B mediates apical transcytosis of transferrin receptor in AP-1B-deficient epithelia
Perez Bay, A. E., Schreiner, R., Mazzoni, F., Carvajal‐Gonzalez, J. M., Gravotta, D., Perret, E., Lehmann Mantaras, G., Zhu, Y., & Rodriguez‐Boulan, E. J. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.130 · Cited by 63 · see citing works
Puerarin: A review of its mechanisms of action and clinical studies in ophthalmology
Meng, F., Guo, B., Ma, Y.-Q., Li, K., & Niu, F. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154465 · Cited by 63 · see citing works
Expression and function of iron‐regulatory proteins in retina
Gnana‐Prakasam, J. P., Martin, P. M., Smith, S. B., & Ganapathy, V. (2010) · IUBMB Life · doi:10.1002/iub.326 · Cited by 63 · see citing works
L-Ferritin Binding to Scara5: A New Iron Traffic Pathway Potentially Implicated in Retinopathy
Mendes-Jorge, L., Ramos, D., Valença, A., López‐Luppo, M., Pires, V. M. R., Catita, J., Nacher, V., Navarro, M., Carretero, A., Rodríguez‐Baeza, A., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0106974 · Cited by 63 · see citing works
Alpha-synuclein modulates retinal iron homeostasis by facilitating the uptake of transferrin-bound iron: Implications for visual manifestations of Parkinson's disease
Baksi, S., Tripathi, A. K., & Singh, N. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.06.025 · Cited by 63 · see citing works
Mitochondrial ferritin protects SH-SY5Y cells against H 2 O 2 -induced oxidative stress and modulates α-synuclein expression
Guan, H., Yang, H., Yang, M., Yanagisawa, D., Bellier, J., Mori, M., Takahata, S., Nonaka, T., Zhao, S., & Tooyama, I. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.02.001 · Cited by 63 · see citing works
Cholesterol homeostasis in the vertebrate retina: biology and pathobiology
Rao, S. R., & Fliesler, S. J. (2020) · Journal of Lipid Research · doi:10.1194/jlr.tr120000979 · Cited by 61 · see citing works
Stem Cells as Tools in Regenerative Therapy for Retinal Degeneration
Enzmann, V. (2009) · Archives of Ophthalmology · doi:10.1001/archophthalmol.2009.65 · Cited by 61 · see citing works
Mitochondrial ferritin in neurodegenerative diseases
Yang, H., Yang, M., Guan, H., Liu, Z., Zhao, S., Takeuchi, S., Yanagisawa, D., & Tooyama, I. (2013) · Neuroscience Research · doi:10.1016/j.neures.2013.07.005 · Cited by 59 · see citing works
Aceruloplasminemia: Waiting for an Efficient Therapy
Piperno, A., & Alessio, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00903 · Cited by 59 · see citing works
Iron is neurotoxic in retinal detachment and transferrin confers neuroprotection
Daruich, A., Rouzic, Q. L., Jonet, L., Naud, M., Kowalczuk, L., Pournaras, J.-A. C., Boatright, J. H., Thomas, A., Turck, N., Moulin, A., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau9940 · Cited by 58 · see citing works
Iron, the retina and the lens: A focused review
García-Castiñeiras, S. (2010) · Experimental Eye Research · doi:10.1016/j.exer.2010.03.003 · Cited by 58 · see citing works
5‐Lipoxygenase Inhibition Protects Retinal Pigment Epithelium from Sodium Iodate‐Induced Ferroptosis and Prevents Retinal Degeneration
Lee, J., Chang‐Chien, G., Lin, S., Hsiao, Y., Ke, M.-C., Chen, A., & Lin, T. (2022) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2022/1792894 · Cited by 56 · see citing works
Expression and Iron-Dependent Regulation of Succinate Receptor GPR91 in Retinal Pigment Epithelium
Gnana‐Prakasam, J. P., Ananth, S., Prasad, P. D., Zhang, M., Atherton, S. S., Martin, P. M., Smith, S. B., & Ganapathy, V. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-6722 · Cited by 56 · see citing works
Regulations of Retinal Inflammation: Focusing on Müller Glia
Chen, Y., Xia, Q., Zeng, Y., Zhang, Y., & Zhang, M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.898652 · Cited by 55 · see citing works
Iron Overload in Diabetic Retinopathy: A Cause or a Consequence of Impaired Mechanisms?
Ciudin, A., Hernández, C., & Simó, R. (2010) · Experimental Diabetes Research · doi:10.1155/2010/714108 · Cited by 53 · see citing works
Phenotypic heterogeneity in seven Italian cases of aceruloplasminemia
Pelucchi, S., Mariani, R., Ravasi, G., Pelloni, I., Marano, M., Tremolizzo, L., Alessio, M., & Piperno, A. (2018) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2018.02.036 · Cited by 53 · see citing works
From Rust to Quantum Biology: The Role of Iron in Retina Physiopathology
Picard, É., Daruich, A., Youale, J., Courtois, Y., & Béhar‐Cohen, F. (2020) · Cells · doi:10.3390/cells9030705 · Cited by 55 · see citing works
Iron overload and altered iron metabolism in ovarian cancer
Rockfield, S., Raffel, J., Mehta, R., Rehman, N., & Nanjundan, M. (2017) · Biological Chemistry · doi:10.1515/hsz-2016-0336 · Cited by 53 · see citing works
Ferroptosis: underlying mechanisms and involvement in neurodegenerative diseases
Wang, Y., Li, H., He, Q., Zou, R., Cai, J., & Zhang, L. (2023) · APOPTOSIS · doi:10.1007/s10495-023-01902-9 · Cited by 53 · see citing works
Regulation of the cholesterol efflux transporters ABCA1 and ABCG1 in retina in hemochromatosis and by the endogenous siderophore 2,5-dihydroxybenzoic acid
Ananth, S., Gnana‐Prakasam, J. P., Bhutia, Y. D., Veeranan‐Karmegam, R., Martin, P. M., Smith, S. B., & Ganapathy, V. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.01.010 · Cited by 50 · see citing works
Activated monocytes resist elimination by retinal pigment epithelium and downregulate their OTX 2 expression via TNF ‐α
Mathis, T., Housset, M., Eandi, C. M., Béguier, F., Touhami, S., Reichman, S., Augustin, S., Gondouin, P., Sahel, J., Kodjikian, L., et al. (2016) · Aging Cell · doi:10.1111/acel.12540 · Cited by 50 · see citing works
A new era in posterior segment ocular drug delivery: Translation of systemic, cell-targeted, dendrimer-based therapies
Kannan, R. M., Pitha, I., & Parikh, K. S. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.115005 · Cited by 49 · see citing works
The distribution of toxic metals in the human retina and optic nerve head: Implications for age-related macular degeneration
Pamphlett, R., Cherepanoff, S., Too, L. K., Jew, S. K., Doble, P., & Bishop, D. (2020) · PLoS ONE · doi:10.1371/journal.pone.0241054 · Cited by 47 · see citing works
Iron metabolism in the eye: A review
Goralska, M., Ferrell, J., Harned, J., Lall, M. M., Nagar, S., Fleisher, L. N., & McGahan, M. C. (2008) · Experimental Eye Research · doi:10.1016/j.exer.2008.10.026 · Cited by 47 · see citing works
Virus-mediated EpoR76E gene therapy preserves vision in a glaucoma model by modulating neuroinflammation and decreasing oxidative stress
Hines-Beard, J., Bond, W. S., Backstrom, J. R., & Rex, T. S. (2016) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0499-5 · Cited by 46 · see citing works
Serum Iron and Risk of Diabetic Retinopathy
Chen, Y.-J., Chen, J., Tai, M., Liang, C., Chen, Y., & Chen, W. (2020) · Nutrients · doi:10.3390/nu12082297 · Cited by 45 · see citing works
5′-Adenosine Monophosphate-Activated Protein Kinase–Mammalian Target of Rapamycin Axis As Therapeutic Target for Age-Related Macular Degeneration
Hyttinen, J. M. T., Petrovski, G., Salminen, A., & Kaarniranta, K. (2011) · Rejuvenation Research · doi:10.1089/rej.2011.1220 · Cited by 44 · see citing works
Systemic Administration of the Antioxidant/Iron Chelator α-Lipoic Acid Protects Against Light-Induced Photoreceptor Degeneration in the Mouse Retina
Zhao, L., Wang, C., Song, D., Li, Y., Song, Y., Su, G., & Dunaief, J. L. (2014) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.14-15025 · Cited by 43 · see citing works
Self-citation
Osmotic stress, not aldose reductase activity, directly induces growth factors and MAPK signaling changes during sugar cataract formation
Zhang, P., Xing, K., Randazzo, J., Blessing, K., Lou, M. F., & Kador, P. F. (2012) · Experimental Eye Research · doi:10.1016/j.exer.2012.05.007 · Cited by 42 · see citing works
Puerarin protects against iron overload-induced retinal injury through regulation of iron-handling proteins
Song, Q., Zhao, Y., Li, Q., Han, X., & Duan, J. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109690 · Cited by 42 · see citing works
Human umbilical tissue-derived cells rescue retinal pigment epithelium dysfunction in retinal degeneration
Cao, J., Murat, C., An, W., Yao, X., Lee, J., Santulli-Marotto, S., Harris, I. R., & Inana, G. (2015) · Stem Cells · doi:10.1002/stem.2239 · Cited by 41 · see citing works
Neuroprotection for Age-Related Macular Degeneration
Lin, J. B., Murakami, Y., Miller, J. W., & Vavvas, D. G. (2022) · Ophthalmology Science · doi:10.1016/j.xops.2022.100192 · Cited by 44 · see citing works
Cytochrome P450 1B1: A Key Regulator of Ocular Iron Homeostasis and Oxidative Stress
Song, Y., Annalora, A. J., Marcus, C. B., Jefcoate, C. R. E., Sorenson, C. M., & Sheibani, N. (2022) · Cells · doi:10.3390/cells11192930 · Cited by 42 · see citing works
Cell-Deposited Matrix Improves Retinal Pigment Epithelium Survival on Aged Submacular Human Bruch's Membrane
Sugino, I. K., Gullapalli, V. K., Sun, Q., Wang, J., Nunes, C. F., Cheewatrakoolpong, N., Johnson, A. C., Degner, B. C., Hua, J., Liu, T., et al. (2011) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-6112 · Cited by 39 · see citing works
Oxidative stress and docosahexaenoic acid injury lead to increased necroptosis and ferroptosis in retinal pigment epithelium
Neiteler, A., Palakkan, A., Gallagher, K., & Ross, J. A. (2023) · Scientific Reports · doi:10.1038/s41598-023-47721-5 · Cited by 35 · see citing works
Retinal abnormalities in β-thalassemia major
Bhoiwala, D. L., & Dunaief, J. L. (2015) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2015.08.005 · Cited by 37 · see citing works
Self-citation
Mice with hepcidin‐resistant ferroportin accumulate iron in the retina
Theurl, M., Song, D., Clark, E., Sterling, J., Grieco, S., Altamura, S., Galy, B., Hentze, M., Muckenthaler, M. U., & Dunaief, J. L. (2016) · The FASEB Journal · doi:10.1096/fj.15-276758 · Cited by 36 · see citing works
Self-citation
Iron-Chelating Drugs Enhance Cone Photoreceptor Survival in a Mouse Model of Retinitis Pigmentosa
Wang, K., Peng, B., Xiao, J., Weinreb, O., Youdim, M. B. H., & Lin, B. (2017) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.17-22096 · Cited by 36 · see citing works
Fenofibrate prevents iron induced activation of canonical Wnt/β-catenin and oxidative stress signaling in the retina
Mandala, A., Armstrong, A. T., Girresch, B., Zhu, J., Chilakala, A., Chavalmane, S., Chaudhary, K., Biswas, P., Ogilvie, J. M., & Gnana‐Prakasam, J. P. (2020) · npj Aging and Mechanisms of Disease · doi:10.1038/s41514-020-00050-7 · Cited by 36 · see citing works
Melanosome–iron interactions within retinal pigment epithelium‐derived cells
Kaczara, P., Zaręba, M., Herrnreiter, A. M., Skumatz, C. M. B., Żądło, A. C., Sarna, T., & Burke, J. M. (2012) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12008 · Cited by 36 · see citing works
Overexpressed or intraperitoneally injected human transferrin prevents photoreceptor degeneration in rd10 mice.
Picard, É., Jonet, L., Sergeant, C., Vesvres, M.-H., Béhar‐Cohen, F., Courtois, Y., & Jeanny, J. (2010) · PubMed Central · Cited by 36 · see citing works
Multiple types of programmed necrosis such as necroptosis, pyroptosis, oxytosis/ferroptosis, and parthanatos contribute simultaneously to retinal damage after ischemia–reperfusion
Dvoriantchikova, G., Lypka, K. R., Adis, E. V., & Ivanov, D. (2022) · Scientific Reports · doi:10.1038/s41598-022-22140-0 · Cited by 35 · see citing works
Changes in iron-regulatory proteins in the aged rodent neural retina
Chen, H., Liu, B., Lukas, T. J., Suyeoka, G. M., Wu, G., & Neufeld, A. H. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.01.002 · Cited by 35 · see citing works
Phosphorylation of the Usher syndrome 1G protein SANS controls Magi2-mediated endocytosis
Bauß, K., Knapp, B., Jores, P., Roepman, R., Kremer, H., van Wijk, E., Märker, T., & Uwe Wolfrum, B. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu104 · Cited by 34 · see citing works
Implications of altered iron homeostasis for age-related macular degeneration
Błasiak, J. (2010) · Frontiers in bioscience · doi:10.2741/3804 · Cited by 34 · see citing works
Key Nutrients for Optimal Blood Glucose Control and Mental Health in Individuals with Diabetes: A Review of the Evidence
Basiri, R., Seidu, B., & Cheskin, L. J. (2023) · Nutrients · doi:10.3390/nu15183929 · Cited by 34 · see citing works
Inflammatory and cell death mechanisms induced by 7-ketocholesterol in the retina. Implications for age-related macular degeneration
Pariente, A., Peláez, R., Pérez-Sala, Á., & Larráyoz, I. M. (2019) · Experimental Eye Research · doi:10.1016/j.exer.2019.107746 · Cited by 32 · see citing works
Cigarette smoke extract and heated tobacco products promote ferritin cleavage and iron accumulation in human corneal epithelial cells
Otsu, W., Ishida, K., Chinen, N., Nakamura, S., Shimazawa, M., Tsusaki, H., & Hara, H. (2021) · Scientific Reports · doi:10.1038/s41598-021-97956-3 · Cited by 31 · see citing works
Gun-related eye injuries: A primer
Erickson, B. P., Feng, P. W., Ko, M. J., Modi, Y. S., & Johnson, T. E. (2019) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2019.06.003 · Cited by 30 · see citing works
Environmental stress impairs photoreceptor outer segment (POS) phagocytosis and degradation and induces autofluorescent material accumulation in hiPSC-RPE cells
Dalvi, S., Galloway, C. A., Winschel, L., Hashim, A., Soto, C. A., Tang, C., MacDonald, L. A., & Singh, R. (2019) · Cell Death Discovery · doi:10.1038/s41420-019-0171-9 · Cited by 27 · see citing works
Light-Induced Retinal Degeneration Correlates with Changes in Iron Metabolism Gene Expression, Ferritin Level, and Aging
Picard, É., Ranchon‐Cole, I., Jonet, L., Beaumont, C., Béhar‐Cohen, F., Courtois, Y., & Jeanny, J. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.10-5705 · Cited by 30 · see citing works
Neuroprotective effects of tempol on retinal ganglion cells in a partial optic nerve crush rat model with and without iron load
Thaler, S., Fiedorowicz, M., Ręjdak, R., Chorągiewicz, T., Sulejczak, D., Stopa, P., Żarnowski, T., Zrenner, E., Grieb, P., & Schuettauf, F. (2009) · Experimental Eye Research · doi:10.1016/j.exer.2009.10.013 · Cited by 30 · see citing works
Magnetic Microrobots for In Vivo Cargo Delivery: A Review
Lin, J., Cong, Q., & Zhang, D. (2024) · Micromachines · doi:10.3390/mi15050664 · Cited by 30 · see citing works
HIF2α activation and mitochondrial deficit due to iron chelation cause retinal atrophy
Kong, Y., Liu, P., Li, Y., Nolan, N. D., Quinn, P. M. J., Hsu, C., Jenny, L. A., Zhao, J., Cui, X., Chang, Y., et al. (2023) · EMBO Molecular Medicine · doi:10.15252/emmm.202216525 · Cited by 29 · see citing works
Assessment of methylsulfonylmethane as a permeability enhancer for regional EDTA chelation therapy
Zhang, M., Wong, I. G., Gin, J. B., & Ansari, N. H. (2009) · Drug Delivery · doi:10.1080/10717540902896362 · Cited by 28 · see citing works
Regenerative nanomedicine and the treatment of degenerative retinal diseases
Zarbin, M. A., Montemagno, C. D., Leary, J. F., & Ritch, R. H. (2011) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.167 · Cited by 28 · see citing works
Tulp1 deficiency causes early-onset retinal degeneration through affecting ciliogenesis and activating ferroptosis in zebrafish
Jia, D., Gao, P., Lv, Y., Huang, Y., Reilly, J., Sun, K., Han, Y., Hu, H., Chen, X., Zhang, Z., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-05372-w · Cited by 26 · see citing works
Distribution of Copper, Iron, and Zinc in the Retina, Hippocampus, and Cortex of the Transgenic APP/PS1 Mouse Model of Alzheimer’s Disease
Hosseinpour-Mashkani, S. M., Bishop, D., Raoufi-Rad, N., Adlard, P. A., Shimoni, O., & Golzan, M. (2023) · Cells · doi:10.3390/cells12081144 · Cited by 25 · see citing works
An inadvertent issue of human retina exposure to endocrine disrupting chemicals: A safety assessment
Li, M., Yang, T., Gao, L., & Xu, H. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.128484 · Cited by 25 · see citing works
A vicious cycle of bisretinoid formation and oxidation relevant to recessive Stargardt disease
Zhao, J., Kim, H. J., Ueda, K., Zhang, K., Montenegro, D., Dunaief, J. L., & Sparrow, J. R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100259 · Cited by 25 · see citing works
Self-citation

The Role of Iron in Retinal Diseases
Mehta, S., & Dunaief, J. L. (2012) · Humana Press eBooks · doi:10.1007/978-1-61779-606-7_12 · Cited by 3 · see citing works
Self-citation
Retinal iron homeostasis in health and disease
Song, D., & Dunaief, J. L. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00024 · Cited by 118 · see citing works
Self-citation
Iron Induced Oxidative Damage As a Potential Factor in Age-Related Macular Degeneration: The Cogan Lecture
Dunaief, J. L. (2006) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.06-0568 · Cited by 154 · see citing works
Self-citation
Reviewed by:
宋德禄, Dunaief, J. L., Moos, T., Ugarte, M., Eye, M., Dunaief, J. L., Kirby, T. F. M., & Eye, O. S. (2013)
Self-citation
Iron and age-related macular degeneration.
Błasiak, J., Skłodowska, A., Ulińska, M., & Szaflik, J. P. (2009) · PubMed · Cited by 18 · see citing works

Authors: He, X., Hahn, P., Iacovelli, J., Wong, R., King, C., Bhisitkul, R., Massaro-Giordano, M., & Dunaief, J. L.
Affiliations: University of Pennsylvania (US)
University of California, San Francisco (US)
Corresponding author: Dunaief, Joshua L.
ORCID: Hahn, Paul
Bhisitkul, Robert
Dunaief, Joshua L.
Venue: Progress in Retinal and Eye Research
Publisher: Elsevier BV
Published: 2007-11
Volume: 26
Issue: 6
Pages: 649-673
ISSN: 1350-9462 (ISSN-L)
DOI: 10.1016/j.preteyeres.2007.07.004
PMC: PMC2093950
OpenAlex: W2055021524
Cited by: 260
References: 153
Citations by year: 2026: 8 · 2025: 6 · 2024: 18 · 2023: 17 · 2022: 18 · 2021: 19 · 2020: 20 · 2019: 14 · 2018: 15 · 2017: 13 · 2016: 10 · 2015: 11 · 2014: 13 · 2013: 9 · 2012: 17
FWCI: 1.64
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Progress in Retinal and Eye Research (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Eye Institute (EY 015240, R01EY015240)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinal Development and Disorders
Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
Keywords: iron homeostasis, retinal degeneration, iron toxicity, oxidative stress, hydroxyl radicals, age-related macular degeneration, ceruloplasmin, transferrin, aceruloplasminemia, Friedreich's ataxia, iron chelation, iron overload, glaucoma, cataract, intraocular hemorrhage
MeSH terms: Animals, Biological Transport, Epithelial Cells, Homeostasis, Humans, Iron, Lens, Crystalline, Retina, Retinal Degeneration, Oxidative Stress

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Iron homeostasis and toxicity in retinal degeneration

Abstract

Integrity signals

Claims the paper makes

Claims other papers make about this one

Cites

Cited by

Related

Record

About these checks