The DOI matches its Crossref record; 127 of the 131 references it cites were found in a registry or an index.
The role of the photoreceptor ABC transporter ABCA4 in lipid transport and Stargardt macular degeneration
Open accessAbstract
ABCA4 is a member of the ABCA subfamily of ATP binding cassette (ABC) transporters that is expressed in rod and cone photoreceptors of the vertebrate retina. ABCA4, also known as the Rim protein and ABCR, is a large 2,273 amino acid glycoprotein organized as two tandem halves, each containing a single membrane spanning segment followed sequentially by a large exocytoplasmic domain, a multispanning membrane domain and a nucleotide binding domain. Over 500 mutations in the gene encoding ABCA4 are associated with a spectrum of related autosomal recessive retinal degenerative diseases including Stargardt macular degeneration, cone-rod dystrophy and a subset of retinitis pigmentosa. Biochemical studies on the purified ABCA4 together with analysis of abca4 knockout mice and patients with Stargardt disease have implicated ABCA4 as a retinylidene-phosphatidylethanolamine transporter that facilitates the removal of potentially reactive retinal derivatives from photoreceptors following photoexcitation. Knowledge of the genetic and molecular basis for ABCA4 related retinal degenerative diseases is being used to develop rationale therapeutic treatments for this set of disorders.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“As A2E can not be further metabolized and as RPE cells are postmitotic, A2E and related bisretinoids accumulate in the RPE in the form of lipofuscin deposits.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In the membranes of outer photoreceptor segments are nonenzymatically formed toxic bisretinoids. Upon phagocytosis, these bisretinoids are in the acidic environment of RPE phagolysosomes converted to bisretinoid pyridinium compound A2E and related bisretinoids [54,69,70,71,72,73,74].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“ABCA4 dysfunction leads to the accumulation of vitamin A derivatives and toxic compounds, as they cannot be efficiently removed from the photoreceptor outer segment.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“In STGD1, cone degeneration is more severe and occurs before rod degeneration [69,94].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The latter are insoluble, have a tendency to aggregate and accumulate as lipofuscin deposits in the RPE cells, compromising RPE function and leading to cell death.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
Experimental — accuracy not yet measured
The cited source says what the claim attributes to it.
In the citing paper
“But this process could be facilitated by ATP-dependent transporters such as ABCA476,485−487 or the channel-like property of STRA6.488−492”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [487]
The cited source says what the claim attributes to it.
In the citing paper
“The connection between delayed all-trans-retinal clearance, lipofuscin buildup, and retinal degeneration is exemplified by Stargardt disease, a human condition in which juvenile macular degeneration is caused by mutations in both alleles of the ABCA4 gene.487,545”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [487]
The cited source says what the claim attributes to it.
In the citing paper
“Through this process, a new membrane is added at the base of the outer segments while aged outer segment ends are removed by shedding and phagocytosis by adjacent RPE cells [69].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
The cited source says what the claim attributes to it.
In the citing paper
“Lipofuscin is an autofluorescent cellular waste product that compromises the function and viability of RPE cells and ultimately results in photoreceptor degeneration and a loss of vision [54,69,73,74,75].”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
The cited source says what the claim attributes to it.
In the citing paper
“Trapped vitamin A derivatives and toxic compounds can react nonenzymatically, leading to the formation of toxic bisretinoids.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
The cited source says what the claim attributes to it.
In the citing paper
“Upon phagocytosis of outer segments by adjacent RPE cells, the bisretinal compounds can be hydrolyzed by lysosomal enzymes to highly toxic metabolite A2E.”
From The Role of Vitamin A in Retinal Diseases (2022) · cites this paper as [69]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Comparative Protein Modelling by Satisfaction of Spatial Restraints
Šali, A., & Blundell, T. L. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1626 · Cited by 12,977
ABC Transporters: From Microorganisms to Man
Higgins, C. F. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.000435 · Cited by 3,985
Safety and Efficacy of Gene Transfer for Leber's Congenital Amaurosis
Maguire, A. M., Simonelli, F., Pierce, E. A., Pugh, E. N., Mingozzi, F., Bennicelli, J., Banfi, S., Marshall, K. A., Testa, F., Surace, E. M., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0802315 · Cited by 2,145
Effect of gene therapy on visual function in Leber’s congenital amaurosis
Bainbridge, J. W. B., Smith, A. J., Barker, S. S., Robbie, S., Henderson, R., Balaggan, K., Viswanathan, A., Holder, G. E., Stockman, A., Tyler, N., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0802268 · Cited by 1,924
Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency
Brooks-Wilson, A., Marcil, M., Clee, S. M., Zhang, L.-H., Roomp, K., van Dam, M., Yu, L., Brewer, C., Collins, J. A., Molhuizen, H. O. F., et al. (1999) · Nature Genetics · doi:10.1038/11905 · Cited by 1,687
Berge, K. E., Tian, H., Graf, G. A., Yu, L., Grishin, N. V., Schultz, J. R., Kwiterovich, P. O., Shan, B., Barnes, R., & Hobbs, H. H. (2000) · Science · doi:10.1126/science.290.5497.1771 · Cited by 1,645
The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease
Bodzioch, M., Orsó, E., Klucken, J., Langmann, T., Böttcher, A., Diederich, W., Drobnik, W., Barlage, S., Büchler, C., Porsch-Özcürümez, M., et al. (1999) · Nature Genetics · doi:10.1038/11914 · Cited by 1,512
Allikmets, R., Singh, N., Sun, H., Shroyer, N. F., Hutchinson, A., Chidambaram, A., Gerrard, B., Baird, L., Stauffer, D., Peiffer, A., et al. (1997) · Nature Genetics · doi:10.1038/ng0397-236 · Cited by 1,435
Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1
Rust, S., Rosier, M., Funke, H., Real, J., Amoura, Z., Piette, J.-C., Deleuze, J.-F., Brewer, H. B., Duverger, N., Denèfle, P., et al. (1999) · Nature Genetics · doi:10.1038/11921 · Cited by 1,433
Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters
Mosser, J., Douar, A.-M., Sarde, C.-O., Kioschis, P., Feil, R., Moser, H., Poustka, A.-M., Mandel, J.-L., & Aubourg, P. (1993) · Nature · doi:10.1038/361726a0 · Cited by 1,202
Research works printed but not linked: 1
- Oram, 2002, ATP-binding cassette transporter A1 and cholesterol trafficking, Curr. Opin. Lipidol., 13, 373, 10.1097/00041433-200208000-00004 · DOI
Cited by
Sorted by citations
The bisretinoids of retinal pigment epithelium
Sparrow, J. R., Gregory-Roberts, E., Yamamoto, K., Blonska, A., Ghosh, S. K., Ueda, K., & Zhou, J. (2012) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2011.12.001 · Cited by 392
Chemistry of the Retinoid (Visual) Cycle
Kiser, P. D., Golczak, M., & Palczewski, K. (2014) · Chemical Reviews · doi:10.1021/cr400107q · Cited by 353
Mehat, M., Sundaram, V., Ripamonti, C., Robson, A. G., Smith, A. J., Borooah, S., Robinson, M. R., Rosenthal, A. N., Innes, W. A., Weleber, R. G., et al. (2018) · Ophthalmology · doi:10.1016/j.ophtha.2018.04.037 · Cited by 281
ABCA4 is an N-retinylidene-phosphatidylethanolamine and phosphatidylethanolamine importer
Quazi, F., Lenevich, S., & Molday, R. S. (2012) · Nature Communications · doi:10.1038/ncomms1927 · Cited by 276
Self-citationLiu, X. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-7647-4_2 · Cited by 269
A comprehensive review of retinal gene therapy
Boye, S. E., Boye, S. L., Lewin, A. S., & Hauswirth, W. W. (2013) · Molecular Therapy · doi:10.1038/mt.2012.280 · Cited by 262
Molday, R. S., & Moritz, O. L. (2015) · Journal of Cell Science · doi:10.1242/jcs.175687 · Cited by 235
Self-citationABC Transporter-Mediated Multidrug-Resistant Cancer
Amawi, H. A., Sim, H., Tiwari, A. K., Ambudkar, S. V., & Shukla, S. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-7647-4_12 · Cited by 243
Liu, X. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-7647-4_3 · Cited by 231
Quazi, F., & Molday, R. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.508812 · Cited by 210
Self-citationTsybovsky, Y., Molday, R. S., & Palczewski, K. (2010) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4419-5635-4_8 · Cited by 200
Self-citationPhospholipid meets all-trans-retinal: the making of RPE bisretinoids
Sparrow, J. R., Wu, Y., Kim, C. Y., & Zhou, J. (2010) · Journal of Lipid Research · doi:10.1194/jlr.r000687 · Cited by 193
The human ATP‐binding cassette (ABC) transporter superfamily
Dean, M. C., Moitra, K., & Allikmets, R. L. (2022) · Human Mutation · doi:10.1002/humu.24418 · Cited by 205
Joyal, J., Gantner, M. L., & Smith, L. E. H. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.11.002 · Cited by 193
Coleman, J. A., Kwok, M. C. M., & Molday, R. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047415 · Cited by 181
Self-citationOpsin Is a Phospholipid Flippase
Menon, I. A., Huber, T., Sanyal, S., Banerjee, S., Barré, P., Canis, S., Warren, J. D., Hwa, J., Sakmar, T. P., & Menon, A. K. (2011) · Current Biology · doi:10.1016/j.cub.2010.12.031 · Cited by 159
Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport
Coleman, J. A., Quazi, F., & Molday, R. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2012.10.006 · Cited by 160
Self-citationDiverse relations between ABC transporters and lipids: An overview
Neumann, J., Rose-Sperling, D., & Hellmich, U. A. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.09.023 · Cited by 157
ABC transporters as cancer drivers: Potential functions in cancer development
Domenichini, A., Adamska, A., & Falasca, M. (2018) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2018.09.019 · Cited by 137
Boyer, N. P., Higbee, D., Currin, M. B., Blakeley, L. R., Chen, C., Ablonczy, Z., Crouch, R. K., & Koutalos, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.329235 · Cited by 133
In SilicoFunctional Meta-Analysis of 5,962ABCA4Variants in 3,928 Retinal Dystrophy Cases
Cornelis, S. S., Bax, N. M., Zernant, J., Allikmets, R. L., Fritsche, L. G., den Dunnen, J. T., Ajmal, M., Hoyng, C. B., & Cremers, F. P. M. (2017) · Human Mutation · doi:10.1002/humu.23165 · Cited by 133
Quazi, F., & Molday, R. S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1400780111 · Cited by 129
Self-citationChen, P. M., Gombart, Z. J., & Chen, J. W. (2011) · Cell & Bioscience · doi:10.1186/2045-3701-1-10 · Cited by 122
Sangermano, R., Bax, N. M., Bauwens, M., van den Born, L. I., Baere, E. B. W. D., Garanto, A., Collin, R. W. J., Goercharn-Ramlal, A., van Dijk, A. H. A., Rohrschneider, K., et al. (2016) · Ophthalmology · doi:10.1016/j.ophtha.2016.01.053 · Cited by 118
Membrane proteins structures: A review on computational modeling tools
de Almeida, J. G., Preto, A. J., Koukos, P. I., Bonvin, A. M. J. J., & Moreira, I. S. (2017) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2017.07.008 · Cited by 115
The population genomics of rhesus macaques ( Macaca mulatta ) based on whole-genome sequencesPreprint
Xue, C., Raveendran, M., Harris, R. A., Fawcett, G. L., Liu, X., White, S. J., Dahdouli, M., Deiros, D. R., Below, J. E., Salerno, W. J., et al. (2016) · Genome Research · doi:10.1101/gr.204255.116 · Cited by 117
Animal Models of Retinal Disease
Fletcher, E. L., Jobling, A. I., Vessey, K. A., Luu, C. D., Guymer, R. H., & Baird, P. N. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-384878-9.00006-6 · Cited by 111
The Role of Vitamin A in Retinal Diseases
Sajovic, J., Meglič, A., Glavač, D., Markelj, Š., Hawlina, M., & Fakin, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031014 · Cited by 109
“Consequently, dysfunction and loss of photoreceptors they support occurs [69,71,93].”
BackgroundLipid transport by mammalian ABC proteins
Quazi, F., & Molday, R. S. (2011) · Essays in Biochemistry · doi:10.1042/bse0500265 · Cited by 111
Self-citationLimited Roles of Rdh8, Rdh12, and Abca4 in all- trans -Retinal Clearance in Mouse Retina
Maeda, A., Golczak, M., Maeda, T., & Palczewski, K. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-3944 · Cited by 94
Retina, retinol, retinal and the natural history of vitamin A as a light sensor
Zhong, M., Kawaguchi, R., Kassai, M., & Sun, H. (2012) · Nutrients · doi:10.3390/nu4122069 · Cited by 89
Self-citationDefective lipid transport and biosynthesis in recessive and dominant Stargardt macular degeneration
Molday, R. S., & Zhang, K. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.07.002 · Cited by 82
Self-citationCheepala, S., Hulot, J., Morgan, J. A., Sassi, Y., Zhang, W., Naren, A. P., & Schuetz, J. D. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134609 · Cited by 81
Structural basis of substrate recognition and translocation by human ABCA4
Xie, T., Zhang, Z., Fang, Q., Du, B., & Gong, X. (2021) · Nature Communications · doi:10.1038/s41467-021-24194-6 · Cited by 73
Permanyer, J., Navarro, R., Friedman, J. S., Pomares, E., Castro-Navarro, J., Marfany, G., Swaroop, A., & Gonzàlez‐Duarte, R. (2010) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.09-4857 · Cited by 73
An Overview of the Genetics of ABCA4 Retinopathies, an Evolving Story
Al‐Khuzaei, S., Broadgate, S., Foster, C. R., Shah, M., Yu, J., Downes, S. M., & Halford, S. (2021) · Genes · doi:10.3390/genes12081241 · Cited by 74
Molday, R. S. (2015) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2015.06.008 · Cited by 70
Self-citationVery long chain fatty acid-containing lipids: A decade of novel insights from the study of ELOVL4.
Yeboah, G. K., Lobanova, E. S., Brush, R. S., & Agbaga, M.-P. (2021) · Journal of Lipid Research · doi:10.1016/j.jlr.2021.100030 · Cited by 69
Garces, F. A., Jiang, K., Molday, L. L., Stöhr, H., Weber, B. H. F., Lyons, C. J., Maberley, D., & Molday, R. S. (2018) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.17-23364 · Cited by 68
Self-citationGaranto, A., Duijkers, L., Tomkiewicz, T. Z., & Collin, R. W. J. (2019) · Genes · doi:10.3390/genes10060452 · Cited by 67
An overview of inborn errors of complex lipid biosynthesis and remodelling
Lamari, F., Mochel, F., & Saudubray, J. (2014) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-014-9764-x · Cited by 65
Loss of lysophosphatidylcholine acyltransferase 1 leads to photoreceptor degeneration in rd11 mice
Friedman, J. S., Chang, B., Krauth, D. S., López, I., Waseem, N. H., Hurd, R. E., Feathers, K. L., Branham, K. E. H., Shaw, M., Thomas, G. E., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002897107 · Cited by 65
The Clinical Effect of Homozygous ABCA4 Alleles in 18 Patients
Fujinami, K., Sergouniotis, P. I., Davidson, A. E., Mackay, D. S., Tsunoda, K., Tsubota, K., Robson, A. G., Holder, G. E., Moore, A. T., Michaelides, M., et al. (2013) · Ophthalmology · doi:10.1016/j.ophtha.2013.04.016 · Cited by 60
Deducing the pathogenic contribution of recessive ABCA4 alleles in an outbred population
Schindler, E. I., Nylen, E. L., Ko, A. C., Affatigato, L. M., Heggen, A. C., Wang, K., Sheffield, V. C., & Stone, E. M. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq284 · Cited by 58
Zangerl, B., Wickström, K., Slavik, J., Lindauer, S. J., Ahonen, S., Schelling, C., Lohi, H., Guziewicz, K. E., & Aguirre, G. K. (2010) · PubMed Central · Cited by 54
ATP binding cassette systems: structures, mechanisms, and functions
Licht, A., & Schneider, E. (2011) · Open Life Sciences · doi:10.2478/s11535-011-0054-4 · Cited by 54
Kubota, R., Birch, D. G., Gregory, J. K., & Koester, J. M. (2020) · British Journal of Ophthalmology · doi:10.1136/bjophthalmol-2020-317712 · Cited by 53
Li, J., Cai, X., Xia, Q., Yao, K., Chen, J., Zhang, Y., Naranmandura, H., Liu, X., & Wu, Y. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu223 · Cited by 53
Sterols and sphingolipids: Dynamic duo or partners in crime?
Gulati, S., Liu, Y., Munkacsi, A. B., Wilcox, L. J., & Sturley, S. L. (2010) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.03.003 · Cited by 56
Taubitz, T., Tschulakow, A., Валерьевна, Т. М., Illing, B., Fang, Y., Biesemeier, A., Julien, S., & Schraermeyer, U. (2018) · PeerJ · doi:10.7717/peerj.5215 · Cited by 51
García‐Cazorla, À., Mochel, F., Lamari, F., & Saudubray, J. (2014) · Journal of Inherited Metabolic Disease · doi:10.1007/s10545-014-9776-6 · Cited by 51
Molecular components affecting ocular carotenoid and retinoid homeostasis
von Lintig, J., Moon, J., & Babino, D. (2021) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2020.100864 · Cited by 50
Update on viral gene therapy clinical trials for retinal diseases
Cheng, S.-Y., & Punzo, C. (2022) · Human Gene Therapy · doi:10.1089/hum.2022.159 · Cited by 49
Sabirzhanova, I. B., Lopes‐Pacheco, M., Rapino, D., Grover, R., Handa, J. T., Guggino, W. B., & Cebotaru, L. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.647685 · Cited by 48
Molday, L. L., Wahl, D. J., Šarunic, M. V., & Molday, R. S. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx400 · Cited by 48
Self-citationSun, H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2011.06.010 · Cited by 47
Gene Therapy of Inherited Retinal Degenerations: Prospects and Challenges
Trapani, I., Banfi, S., Simonelli, F., Surace, E. M., & Auricchio, A. (2015) · Human Gene Therapy · doi:10.1089/hum.2015.030 · Cited by 46
Quantifying the Rate of Ellipsoid Zone Loss in Stargardt Disease
Cai, C. X., Light, J. G., & Handa, J. T. (2017) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2017.10.032 · Cited by 47
Posttranslational Modifications of the Photoreceptor-Specific ABC Transporter ABCA4
Tsybovsky, Y., Wang, B., Quazi, F., Molday, R. S., & Palczewski, K. (2011) · Biochemistry · doi:10.1021/bi200774w · Cited by 39
Self-citationCell-autonomous lipid-handling defects in Stargardt iPSC-derived retinal pigment epithelium cells
Farnoodian, M., Bose, D., Khristov, V., Susaimanickam, P. J., Maddileti, S., Mariappan, I., Abu-Asab, M. S., Campos, M. M., Villasmil, R., Wan, Q., et al. (2022) · Stem Cell Reports · doi:10.1016/j.stemcr.2022.10.001 · Cited by 38
Osada, H., Toda, E., Homma, K., Mendoza, N. A. G., Nagai, N., Ogawa, M., Negishi, K., Arita, M., Tsubota, K., & Ozawa, Y. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03741-5 · Cited by 36
Association of ABCA4 and MAFB with non‐syndromic cleft lip with or without cleft palate
Yuan, Q., Blanton, S. H., & Hecht, J. T. (2011) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.33940 · Cited by 37
ABCA4 Gene Screening in a Chinese Cohort With Stargardt Disease: Identification of 37 Novel Variants
Hu, F., Li, J., Gao, F., Qi, Y.-H., Xu, P., Zhang, Y.-J., Wang, D., Wang, L.-S., Li, W. S., Wang, M., et al. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00773 · Cited by 36
Weiss, J. N., & Levy, S. (2021) · Medicines · doi:10.3390/medicines8020010 · Cited by 33
Trezza, A., Bernini, A., Langella, A., Ascher, D. B., Pires, D. E. V., Sodi, A., Passerini, I., Pelo, E., Rizzo, S., Niccolai, N., et al. (2017) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.17-22158 · Cited by 32
Zhang, L., Zhou, Y., Xia, Q., Chen, Y., & Li, J. (2020) · Toxicology Letters · doi:10.1016/j.toxlet.2020.01.005 · Cited by 30
Watson, A., & Lako, M. (2022) · Journal of Anatomy · doi:10.1111/joa.13768 · Cited by 32
Peripapillary Dark Choroid Ring as a Helpful Diagnostic Sign in Advanced Stargardt Disease
Jayasundera, T., Rhoades, W. R., Branham, K. E. H., Niziol, L. M., Musch, D. C., & Heckenlively, J. R. (2010) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2009.11.005 · Cited by 30
OCTA-Based Identification of Different Vascular Patterns in Stargardt Disease
Arrigo, A., Romano, F., Aragona, E., Nunzio, C. D., Sperti, A., Bandello, F. M., & Parodi, M. B. (2019) · Translational Vision Science & Technology · doi:10.1167/tvst.8.6.26 · Cited by 29
Structural Features of the ATP-Binding Cassette (ABC) Transporter ABCA3
Paolini, A., Baldassarre, A., Gaudio, I. D., & Masotti, A. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160819631 · Cited by 29
Outcome of ABCA4 microarray screening in routine clinical practice.
Ernest, P. J. G., Boon, C. J. F., Klevering, B. J., Hoefsloot, L. H., & Hoyng, C. B. (2009) · PubMed Central · Cited by 29
Potential Therapeutic Agents Against Retinal Diseases Caused by Aberrant Metabolism of Retinoids
Liu, X., Chen, J., Liu, Z., Li, J., Yao, K., & Wu, Y. (2016) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-18429 · Cited by 30
Biswas, E. E., Kurpad, D. S., Joshi, K., & Biswas, S. B. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.112896 · Cited by 28
Sasaki, K., Tachikawa, M., Uchida, Y., Hirano, S., Kadowaki, F., Watanabe, M., Ohtsuki, S., & Terasaki, T. (2018) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.7b00679 · Cited by 27
Liu, Q., Sabirzhanova, I. B., Bergbower, E. A. S., Yanda, M. K., Guggino, W. G., & Cebotaru, L. (2019) · Cellular Physiology and Biochemistry · doi:10.33594/000000146 · Cited by 25
Battu, R., Verma, A., Hariharan, R., Krishna, S., Kiran, R. P., Jacob, J., Ganapathy, A., Ramprasad, V. L., Kumaramanickavel, G., Jeyabalan, N., et al. (2015) · BioMed Research International · doi:10.1155/2015/940864 · Cited by 25
The lipid translocase, ABCA4: seeing is believing
Pollock, N. L., & Callaghan, R. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08169.x · Cited by 22
Variants in the ABCA4 gene in a Brazilian population with Stargardt disease.
Salles, M. V., Motta, F. L., Martin, R. P., Filippelli-Silva, R., da Silva, E. D., Varela, P., Costa, K. A., Chiang, J., Pesquero, J. B., & Sallum, J. M. F. (2018) · Europe PMC (PubMed Central) · Cited by 22
Retina and RPE lipid profile changes linked with ABCA4 associated Stargardt's maculopathy
Farnoodian, M., Bose, D., Barone, F., Nelson, L. M., Boyle, M. P., Jun, B., Do, K., Gordon, W. C., Kautzmann, M.-A. I., Perera, R. M., et al. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108482 · Cited by 25
Vitamin A aldehyde-taurine adduct and the visual cycle
Kim, H. J., Zhao, J., & Sparrow, J. R. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005714117 · Cited by 22
Li, J., Zhang, Y., Cai, X., Xia, Q., Chen, J., Liao, Y., Liu, Z., & Wu, Y. (2016) · Toxicology · doi:10.1016/j.tox.2016.10.005 · Cited by 20
Zhong, M., & Molday, R. S. (2010) · Methods in molecular biology · doi:10.1007/978-1-60327-325-1_9 · Cited by 21
Self-citationClinical and genetic analyses reveal novel pathogenic ABCA4 mutations in Stargardt disease families
Lin, B., Cai, X., Zheng, Z., Huang, X., Liu, X., Qu, J., & Jin, Z. (2016) · Scientific Reports · doi:10.1038/srep35414 · Cited by 20
Fain, G. (2019) · doi:10.1093/oso/9780198835028.001.0001 · Cited by 22
Wright, J., Muench, S. P., Goldman, A., & Baker, A. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180146 · Cited by 25
Identification of novel pathogenic ABCA4 variants in a Han Chinese family with Stargardt disease
Qin, X., Cao, Y., Xu, H., Guo, Y., Yang, Z., Lu, C., Yuan, L., & Deng, H. (2018) · Bioscience Reports · doi:10.1042/bsr20180872 · Cited by 18
Nanoparticle‐motivated gene delivery for ophthalmic application
Mitra, R. N., Zheng, M., & Han, Z. (2015) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1356 · Cited by 18
The ABCs of Stargardt disease: the latest advances in precision medicine
Zaydon, Y. A., & Tsang, S. H. (2024) · Cell & Bioscience · doi:10.1186/s13578-024-01272-y · Cited by 20
Sung, Y.-C., Yang, C., Yang, C., Lin, C., Huang, D.-S., Huang, Y.-S., Hu, F., Chen, P., & Chen, T. (2020) · Genes · doi:10.3390/genes11121421 · Cited by 15
Clinical and genetic characteristics of Stargardt disease in a large Western China cohort: Report 1
Liu, X., Meng, X., Yang, L., Long, Y., Fujinami‐Yokokawa, Y., Ren, J., Kurihara, T., Tsubota, K., Tsunoda, K., Fujinami, K., et al. (2020) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.31838 · Cited by 15
Foveal sparing in patients with Japanese Stargardt’s disease and good visual acuity
Nakao, T., Tsujikawa, M., Sawa, M., Gomi, F., & Nishida, K. (2012) · Japanese Journal of Ophthalmology · doi:10.1007/s10384-012-0172-1 · Cited by 15
Engfer, Z. J., Lewandowski, D., Dong, Z., Palczewska, G., Zhang, J., Kordecka, K., Płaczkiewicz, J., Panas, D., Foik, A. T., Tabaka, M., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2314698120 · Cited by 13
Hamano, F., Kuribayashi, H., Iwagawa, T., Tsuhako, A., Nagata, K., Sagara, H., Shimizu, T., Shindou, H., & Watanabe, S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100303 · Cited by 16
Stargardt’s Disease: Molecular Pathogenesis and Current Therapeutic Landscape
Dayma, K., Rajanala, K., & Upadhyay, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26147006 · Cited by 14
Corradi, Z., Khan, M., Hitti‐Malin, R. J., Mishra, K., Whelan, L., Cornelis, S. S., Hoyng, C. B., Kämpjärvi, K., Klaver, C. C. W., Lišková, P., et al. (2023) · Human Genetics and Genomics Advances · doi:10.1016/j.xhgg.2023.100237 · Cited by 13
Huang, D., Thompson, J. A., Charng, J., Chelva, E. S., McLenachan, S., Chen, S., Zhang, D., McLaren, T. L., Lamey, T. M., Constable, I. J., et al. (2020) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.1259 · Cited by 13
New Prospects for Retinal Pigment Epithelium Transplantation
Gullapalli, V. K., & Zarbin, M. A. (2022) · Asia-Pacific Journal of Ophthalmology · doi:10.1097/apo.0000000000000521 · Cited by 13
Sajovic, J., Meglič, A., Volk, M., Maver, A., Jarc-Vidmar, M., Hawlina, M., & Fakin, A. (2023) · Genes · doi:10.3390/genes14020291 · Cited by 12
Gurramkonda, V. B., Syed, A. H., Murthy, J., Chaubey, G., & Bhaskar, L. V. (2015) · International Journal of Pediatric Otorhinolaryngology · doi:10.1016/j.ijporl.2015.10.055 · Cited by 12
Membrane transporters and the diseases corresponding to functional defects
Lai, Y. (2013) · Elsevier eBooks · doi:10.1533/9781908818287.1 · Cited by 13
Metadata
- Authors
- Molday, R. S., Zhong, M., & Quazi, F.
- Affiliations
- University of British Columbia (CA)
- Corresponding author
- Molday, Robert S.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
- Publisher
- Elsevier BV
- Published
- 2009-07
- Volume
- 1791
- Issue
- 7
- Pages
- 573-583
- ISSN
- 1388-1981 (ISSN-L)
- PMC
- PMC2746242
- OpenAlex
- W2031287535
- Cited by
- 182
- References
- 131
- Citations by year
- 2026: 5 · 2025: 7 · 2024: 7 · 2023: 6 · 2022: 11 · 2021: 11 · 2020: 13 · 2019: 22 · 2018: 15 · 2017: 8 · 2016: 9 · 2015: 11 · 2014: 5 · 2013: 7 · 2012: 11
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Macula Vision Research Foundation
- National Eye Institute (EY02422, R01EY002422)
- Topics
- Health Sciences › Medicine › Ophthalmology › Retinal Development and Disorders
- Health Sciences › Medicine › Ophthalmology › Retinal Diseases and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Keywords
- ABCA4, ABC transporters, lipid transport, photoreceptors, retinal degeneration, cone-rod dystrophy, retinitis pigmentosa, ABCA4 mutations
- MeSH terms
- Amino Acid Sequence, Animals, Biological Transport, Humans, Macular Degeneration, Molecular Sequence Data, Mice, Knockout, ATP-Binding Cassette Transporters, Lipid Metabolism, Mice
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
