Retinal biomarkers and pharmacological targets for Hermansky-Pudlak syndrome 7.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
04 03 2020
04 03 2020
Historique:
received:
08
09
2019
accepted:
19
02
2020
entrez:
6
3
2020
pubmed:
7
3
2020
medline:
27
11
2020
Statut:
epublish
Résumé
Deletion of dystrobrevin binding protein 1 has been linked to Hermansky-Pudlak syndrome type 7 (HPS-7), a rare disease characterized by oculocutaneous albinism and retinal dysfunction. We studied dysbindin-1 null mutant mice (Dys
Identifiants
pubmed: 32132582
doi: 10.1038/s41598-020-60931-5
pii: 10.1038/s41598-020-60931-5
pmc: PMC7055265
doi:
Substances chimiques
MicroRNAs
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3972Références
Ghiani, C. A. et al. The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth. Molecular psychiatry 15(115), 204–215 (2010).
doi: 10.1038/mp.2009.58
Mullin, A. P. et al. Gene dosage in the dysbindin schizophrenia susceptibility network differentially affect synaptic function and plasticity. The Journal of neuroscience: the official journal of the Society for Neuroscience 35, 325–338 (2015).
doi: 10.1523/JNEUROSCI.3542-14.2015
Benson, M. A., Newey, S. E., Martin-Rendon, E., Hawkes, R. & Blake, D. J. Dysbindin, a novel coiled-coil-containing protein that interacts with the dystrobrevins in muscle and brain. The Journal of biological chemistry 276, 24232–24241 (2001).
pubmed: 11316798
doi: 10.1074/jbc.M010418200
Iijima, S. et al. Immunohistochemical detection of dysbindin at the astroglial endfeet around the capillaries of mouse brain. Journal of molecular histology 40, 117–121 (2009).
pubmed: 19495999
doi: 10.1007/s10735-009-9221-6
Shao, L. et al. Schizophrenia susceptibility gene dysbindin regulates glutamatergic and dopaminergic functions via distinctive mechanisms in Drosophila. Proceedings of the National Academy of Sciences of the United States of America 108, 18831–18836 (2011).
pubmed: 22049342
pmcid: 3219129
doi: 10.1073/pnas.1114569108
Donohoe, G. et al. Early visual processing deficits in dysbindin-associated schizophrenia. Biological psychiatry 63, 484–489 (2008).
pubmed: 17945199
doi: 10.1016/j.biopsych.2007.07.022
Li, W. et al. Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1). Nature genetics 35, 84–89 (2003).
pubmed: 12923531
pmcid: 2860733
doi: 10.1038/ng1229
Bryan, M. M. et al. Clinical and molecular phenotyping of a child with Hermansky-Pudlak syndrome-7, an uncommon genetic type of HPS. Molecular genetics and metabolism 120, 378–383 (2017).
pubmed: 28259707
pmcid: 5395203
doi: 10.1016/j.ymgme.2017.02.007
Orphanet. Hermansky-Pudlak syndrome. available at: https://www.orpha.net/consor/cgi-bin/OC_Exp.php?lng=EN&Expert=79430 .
Bahadori, R. et al. The zebrafish fade out mutant: A novel genetic model for Hermansky-Pudlak syndrome. Investigative Ophthalmology and Visual Science, https://doi.org/10.1167/iovs.05-1596 (2006).
doi: 10.1167/iovs.05-1596
F, P. et al. Dysbindin-1 modulates prefrontal cortical activity and schizophrenia-like behaviors via dopamine/D2 pathways. in Molecular Psychiatry, https://doi.org/10.1038/mp.2010.106 (2012).
pubmed: 20956979
pmcid: 3388848
doi: 10.1038/mp.2010.106
Fagadau, W. R., Heinemann, M. H. & Cotlier, E. Hermansky-Pudlak syndrome: albinism with lipofuscin storage. International Ophthalmology, https://doi.org/10.1007/BF00139585 (1981).
pubmed: 7298260
doi: 10.1007/BF00139585
Krill, A. E. The electroretinogram and electro-oculogram: clinical applications. Investigative ophthalmology 9, 600–617 (1970).
pubmed: 5311620
Mechelli, A. et al. Dysbindin modulates brain function during visual processing in children. NeuroImage 49, 817–822 (2010).
pubmed: 19631276
doi: 10.1016/j.neuroimage.2009.07.030
Straub, R. E. et al. Genetic variation in the 6p22.3 gene DTNBP1, the human ortholog of the mouse dysbindin gene, is associated with schizophrenia. American journal of human genetics 71, 337–348 (2002).
pubmed: 12098102
pmcid: 379166
doi: 10.1086/341750
Ji, Y. et al. Role of dysbindin in dopamine receptor trafficking and cortical GABA function. Proceedings of the National Academy of Sciences of the United States of America 106, 19593–19598 (2009).
pubmed: 19887632
pmcid: 2780743
doi: 10.1073/pnas.0904289106
Papaleo, F., Lipska, B. K. & Weinberger, D. R. Mouse models of genetic effects on cognition: relevance to schizophrenia. Neuropharmacology 62, 1204–1220 (2012).
pubmed: 21557953
doi: 10.1016/j.neuropharm.2011.04.025
Savage, J. E. et al. Genome-wide association meta-analysis in 269,867 individuals identifies new genetic and functional links to intelligence. Nature genetics 50, 912–919 (2018).
pubmed: 29942086
pmcid: 6411041
doi: 10.1038/s41588-018-0152-6
Scheggia, D. et al. Variations in Dysbindin-1 are associated with cognitive response to antipsychotic drug treatment. Nature communications 9, 2265 (2018).
pubmed: 29891954
pmcid: 5995960
doi: 10.1038/s41467-018-04711-w
Leggio, G. M. et al. The epistatic interaction between the dopamine D3 receptor and dysbindin-1 modulates higher-order cognitive functions in mice and humans. Molecular Psychiatry, https://doi.org/10.1038/s41380-019-0511-4 (2019).
De Groef, L. & Cordeiro, M. F. Is the Eye an Extension of the Brain in Central Nervous System Disease? Journal of ocular pharmacology and therapeutics: the official journal of the Association for Ocular Pharmacology and Therapeutics 34, 129–133 (2018).
doi: 10.1089/jop.2016.0180
Kutzbach, B., Summers, C. G., Holleschau, A. M., King, R. A. & MacDonald, J. T. The prevalence of attention-deficit/hyperactivity disorder among persons with albinism. Journal of child neurology 22, 1342–1347 (2007).
pubmed: 18174549
doi: 10.1177/0883073807307078
pmcid: 18174549
Saadeh, R., Lisi, E. C., Batista, D. A. S., McIntosh, I. & Hoover-Fong, J. E. Albinism and developmental delay: the need to test for 15q11-q13 deletion. Pediatric neurology 37, 299–302 (2007).
pubmed: 17903679
pmcid: 2128718
doi: 10.1016/j.pediatrneurol.2007.06.024
Liu, T. et al. A MicroRNA Profile in Fmr1 Knockout Mice Reveals MicroRNA Expression Alterations with Possible Roles in Fragile X Syndrome. Molecular neurobiology 51, 1053–1063 (2015).
pubmed: 24906954
doi: 10.1007/s12035-014-8770-1
pmcid: 24906954
Ma, A. J. et al. Associations of CXCL16, miR-146a and miR-146b in atherosclerotic apolipoprotein E-knockout mice. Molecular Medicine Reports, https://doi.org/10.3892/mmr.2018.9270 (2018).
Ham, S., Kim, T. K., Lee, S., Tang, Y. P. & Im, H. I. MicroRNA Profiling in Aging Brain of PSEN1/PSEN2 Double Knockout Mice. Molecular Neurobiology, https://doi.org/10.1007/s12035-017-0753-6 (2018).
pubmed: 28879407
doi: 10.1007/s12035-017-0753-6
pmcid: 28879407
Takao, A. et al. Generation of PTEN-knockout (−/−) murine prostate cancer cells using the CRISPR/Cas9 system and comprehensive gene expression profiling. Oncology Reports, https://doi.org/10.3892/or.2018.6683 (2018).
de Ronde, M. W. J., Ruijter, J. M., Moerland, P. D., Creemers, E. E. & Pinto-Sietsma, S.-J. Study Design and qPCR Data Analysis Guidelines for Reliable Circulating miRNA Biomarker Experiments: A Review. Clinical chemistry, https://doi.org/10.1373/clinchem.2017.285288 (2018).
pubmed: 29903876
doi: 10.1373/clinchem.2017.285288
pmcid: 29903876
Vlachos, I. S. et al. DIANA-miRPath v3.0: deciphering microRNA function with experimental support. Nucleic acids research 43, W460–6 (2015).
pubmed: 25977294
pmcid: 4489228
doi: 10.1093/nar/gkv403
Riffo-Campos, A. L. et al. Tools for Sequence-Based miRNA Target Prediction: What to Choose? International Journal of Molecular Sciences 17, (2016).
pmcid: 5187787
doi: 10.3390/ijms17121987
pubmed: 5187787
Tang, T. T.-T. et al. Dysbindin regulates hippocampal LTP by controlling NMDA receptor surface expression. Proceedings of the National Academy of Sciences, https://doi.org/10.1073/pnas.0910499106 (2009).
doi: 10.1073/pnas.0910499106
Marley, A. & von Zastrow, M. Dysbindin promotes the post-endocytic sorting of G protein-coupled receptors to lysosomes. PloS one 5, e9325 (2010).
pubmed: 20174469
pmcid: 2824829
doi: 10.1371/journal.pone.0009325
Tropea, D., Hardingham, N., Millar, K. & Fox, K. Mechanisms underlying the role of DISC1 in synaptic plasticity. The Journal of physiology 596, 2747–2771 (2018).
pubmed: 30008190
pmcid: 6046077
doi: 10.1113/JP274330
Yang, W., Zhu, C., Shen, Y. & Xu, Q. The pathogenic mechanism of dysbindin-1B toxic aggregation: BLOC-1 and intercellular vesicle trafficking. Neuroscience 333, 78–91 (2016).
pubmed: 27421225
doi: 10.1016/j.neuroscience.2016.07.008
Kang, H. Role of MicroRNAs in TGF-beta Signaling Pathway-Mediated Pulmonary Fibrosis. International journal of molecular sciences 18, (2017).
pmcid: 5751130
doi: 10.3390/ijms18122527
pubmed: 5751130
Herrmann, R. et al. Rod vision is controlled by dopamine-dependent sensitization of rod bipolar cells by GABA. Neuron 72, 101–110 (2011).
pubmed: 21982372
pmcid: 3197016
doi: 10.1016/j.neuron.2011.07.030
Travis, A. M., Heflin, S. J., Hirano, A. A., Brecha, N. C. & Arshavsky, V. Y. Dopamine-Dependent Sensitization of Rod Bipolar Cells by GABA Is Conveyed through Wide-Field Amacrine Cells. The Journal of neuroscience: the official journal of the Society for Neuroscience 38, 723–732 (2018).
doi: 10.1523/JNEUROSCI.1994-17.2017
Balogh, Z., Benedek, G. & Keri, S. Retinal dysfunctions in schizophrenia. Progress in neuro-psychopharmacology & biological psychiatry 32, 297–300 (2008).
doi: 10.1016/j.pnpbp.2007.08.024
Hebert, M. et al. Retinal response to light in young nonaffected offspring at high genetic risk of neuropsychiatric brain disorders. Biological psychiatry 67, 270–274 (2010).
pubmed: 19833322
doi: 10.1016/j.biopsych.2009.08.016
Huang, Y.-W. A., Ruiz, C. R., Eyler, E. C. H., Lin, K. & Meffert, M. K. Dual regulation of miRNA biogenesis generates target specificity in neurotrophin-induced protein synthesis. Cell 148, 933–946 (2012).
pubmed: 22385959
pmcid: 4074528
doi: 10.1016/j.cell.2012.01.036
Harris, D. A., Kim, K., Nakahara, K., Vasquez-Doorman, C. & Carthew, R. W. Cargo sorting to lysosome-related organelles regulates siRNA-mediated gene silencing. The Journal of cell biology 194, 77–87 (2011).
pubmed: 21746852
pmcid: 3135410
doi: 10.1083/jcb.201102021
Schneider, D. J. et al. Cadherin-11 contributes to pulmonary fibrosis: potential role in TGF-beta production and epithelial to mesenchymal transition. FASEB journal: official publication of the Federation of American Societies for Experimental Biology 26, 503–512 (2012).
doi: 10.1096/fj.11-186098
Agassandian, M. et al. VCAM-1 is a TGF-beta1 inducible gene upregulated in idiopathic pulmonary fibrosis. Cellular signalling 27, 2467–2473 (2015).
pubmed: 26386411
pmcid: 4684430
doi: 10.1016/j.cellsig.2015.09.003
Margadant, C. & Sonnenberg, A. Integrin-TGF-beta crosstalk in fibrosis, cancer and wound healing. EMBO reports 11, 97–105 (2010).
pubmed: 20075988
pmcid: 2828749
doi: 10.1038/embor.2009.276
Huang, C. et al. MicroRNA-101 attenuates pulmonary fibrosis by inhibiting fibroblast proliferation and activation. The Journal of biological chemistry 292, 16420–16439 (2017).
pubmed: 28726637
pmcid: 5633105
doi: 10.1074/jbc.M117.805747
Das, S. et al. MicroRNA-326 regulates profibrotic functions of transforming growth factor-beta in pulmonary fibrosis. American journal of respiratory cell and molecular biology 50, 882–892 (2014).
pubmed: 24279830
pmcid: 4068942
doi: 10.1165/rcmb.2013-0195OC
Braunger, B. M. et al. TGF-β signaling protects retinal neurons from programmed cell death during the development of the mammalian eye. Journal of Neuroscience, https://doi.org/10.1523/JNEUROSCI.0991-13.2013 (2013).
pubmed: 23986258
doi: 10.1523/JNEUROSCI.0991-13.2013
Ren, J. Q. & Li, L. A circadian clock regulates the process of ERG b- and d-wave dominance transition in dark-adapted zebrafish. Vision Research, https://doi.org/10.1016/j.visres.2004.03.022 (2004).
pubmed: 15183681
doi: 10.1016/j.visres.2004.03.022
Rojas, A., Padidam, M., Cress, D. & Grady, W. M. TGF-beta receptor levels regulate the specificity of signaling pathway activation and biological effects of TGF-beta. Biochimica et biophysica acta 1793, 1165–1173 (2009).
pubmed: 19339207
pmcid: 2700179
doi: 10.1016/j.bbamcr.2009.02.001
Moretto, E., Murru, L., Martano, G., Sassone, J. & Passafaro, M. Glutamatergic synapses in neurodevelopmental disorders. Progress in neuro-psychopharmacology & biological psychiatry 84, 328–342 (2018).
doi: 10.1016/j.pnpbp.2017.09.014
Gokhale, A. et al. The N-ethylmaleimide-sensitive factor and dysbindin interact to modulate synaptic plasticity. The Journal of neuroscience: the official journal of the Society for Neuroscience 35, 7643–7653 (2015).
doi: 10.1523/JNEUROSCI.4724-14.2015
Millar, J. K. et al. Disruption of two novel genes by a translocation co-segregating with schizophrenia. Human molecular genetics 9, 1415–1423 (2000).
pubmed: 10814723
doi: 10.1093/hmg/9.9.1415
pmcid: 10814723
Bradshaw, N. J. & Porteous, D. J. DISC1-binding proteins in neural development, signalling and schizophrenia. Neuropharmacology 62, 1230–1241 (2012).
pubmed: 21195721
pmcid: 3275753
doi: 10.1016/j.neuropharm.2010.12.027
Greenhill, S. D. et al. NEURODEVELOPMENT. Adult cortical plasticity depends on an early postnatal critical period. Science (New York, N.Y.) 349, 424–427 (2015).
doi: 10.1126/science.aaa8481
Lee, S.-A. et al. Disrupted-in-schizophrenia 1 (DISC1) regulates dysbindin function by enhancing its stability. The Journal of biological chemistry 290, 7087–7096 (2015).
pubmed: 25635053
pmcid: 4358130
doi: 10.1074/jbc.M114.614750
Wei, H. P., Yao, Y. Y., Zhang, R. W., Zhao, X. F. & Du, J. L. Activity-induced long-term potentiation of excitatory synapses in developing zebrafish retina in vivo. Neuron, https://doi.org/10.1016/j.neuron.2012.05.031 (2012).
pubmed: 22884331
doi: 10.1016/j.neuron.2012.05.031
Carr, G. V., Jenkins, K. A., Weinberger, D. R. & Papaleo, F. Loss of dysbindin-1 in mice impairs reward-based operant learning by increasing impulsive and compulsive behavior. Behavioural brain research 241, 173–184 (2013).
pubmed: 23261874
doi: 10.1016/j.bbr.2012.12.021
Cox, M. M. et al. Neurobehavioral abnormalities in the dysbindin-1 mutant, sandy, on a C57BL/6J genetic background. Genes, brain, and behavior 8, 390–397 (2009).
pubmed: 19220483
pmcid: 2774142
doi: 10.1111/j.1601-183X.2009.00477.x
Dickman, D. K. & Davis, G. W. The schizophrenia susceptibility gene dysbindin controls synaptic homeostasis. Science (New York, N.Y.) 326, 1127–1130 (2009).
doi: 10.1126/science.1179685
Leggio, G. M., Bucolo, C., Platania, C. B. M., Salomone, S. & Drago, F. Current drug treatments targeting dopamine D3 receptor. Pharmacology and Therapeutics, 165 (2016).
Kumamoto, N. et al. Hyperactivation of midbrain dopaminergic system in schizophrenia could be attributed to the down-regulation of dysbindin. Biochemical and biophysical research communications 345, 904–909 (2006).
pubmed: 16701550
doi: 10.1016/j.bbrc.2006.04.163
pmcid: 16701550
Pflug, R., Nelson, R., Huber, S. & Reitsamer, H. Modulation of horizontal cell function by dopaminergic ligands in mammalian retina. Vision Research, https://doi.org/10.1016/j.visres.2008.03.004 (2008).
pubmed: 18440579
pmcid: 5244834
doi: 10.1016/j.visres.2008.03.004
Zhang, D.-Q., Zhou, T.-R. & McMahon, D. G. Functional Heterogeneity of Retinal Dopaminergic Neurons Underlying Their Multiple Roles in Vision. Journal of Neuroscience, https://doi.org/10.1523/JNEUROSCI.4478-06.2007 (2007).
pubmed: 17234601
doi: 10.1523/JNEUROSCI.4478-06.2007
pmcid: 17234601
Kim, M. K. et al. Dopamine Deficiency Mediates Early Rod-Driven Inner Retinal Dysfunction in Diabetic Mice. Investigative ophthalmology & visual science 59, 572–581 (2018).
doi: 10.1167/iovs.17-22692
Jensen, R. J. Effects of Antipsychotic Drugs Haloperidol and Clozapine on Visual Responses of Retinal Ganglion Cells in a Rat Model of Retinitis Pigmentosa. Journal of ocular pharmacology and therapeutics: the official journal of the Association for Ocular Pharmacology and Therapeutics 32, 685–690 (2016).
doi: 10.1089/jop.2016.0102
Popova, E., Kostov, M. & Kupenova, P. Effects of dopamine D1 receptor blockade on the ERG b- and d-waves during blockade of ionotropic GABA receptors. Eye and vision (London, England) 3, 32 (2016).
doi: 10.1186/s40662-016-0064-4
Popova, E. & Kupenova, P. Effects of dopamine receptor blockade on the intensity-response function of ERG b- and d-waves in dark adapted eyes. Vision Research, https://doi.org/10.1016/j.visres.2013.06.004 (2013).
pubmed: 23810982
doi: 10.1016/j.visres.2013.06.004
pmcid: 23810982
Wachtmeister, L. Oscillatory potentials in the retina: What do they reveal. Progress in Retinal and Eye Research, https://doi.org/10.1016/S1350-9462(98)00006-8 (1998).
pubmed: 9777648
doi: 10.1016/S1350-9462(98)00006-8
pmcid: 9777648
Iizuka, Y., Sei, Y., Weinberger, D. R. & Straub, R. E. Evidence That the BLOC-1 Protein Dysbindin Modulates Dopamine D2 Receptor Internalization and Signaling But Not D1 Internalization. Journal of Neuroscience, https://doi.org/10.1523/JNEUROSCI.1689-07.2007 (2007).
pubmed: 17989303
doi: 10.1523/JNEUROSCI.1689-07.2007
pmcid: 17989303
Liu, C. et al. MirSNP, a database of polymorphisms altering miRNA target sites, identifies miRNA-related SNPs in GWAS SNPs and eQTLs. BMC genomics 13, 661 (2012).
pubmed: 23173617
pmcid: 3582533
doi: 10.1186/1471-2164-13-661
Betel, D., Wilson, M., Gabow, A., Marks, D. S. & Sander, C. The microRNA.org resource: targets and expression. Nucleic acids research 36, D149–53 (2008).
pubmed: 18158296
doi: 10.1093/nar/gkm995
Wang, L. & Lyerla, T. Histochemical and cellular changes accompanying the appearance of lung fibrosis in an experimental mouse model for Hermansky Pudlak syndrome. Histochemistry and cell biology 134, 205–213 (2010).
pubmed: 20603711
pmcid: 2909458
doi: 10.1007/s00418-010-0724-8
Tech, K. & Gershon, T. R. Energy metabolism in neurodevelopment and medulloblastoma. Translational pediatrics 4, 12–19 (2015).
pubmed: 26835355
pmcid: 4729065
Mita, T. et al. Docosahexaenoic Acid Promotes Axon Outgrowth by Translational Regulation of Tau and Collapsin Response Mediator Protein 2 Expression. The Journal of biological chemistry 291, 4955–4965 (2016).
pubmed: 26763232
pmcid: 4777833
doi: 10.1074/jbc.M115.693499
Ando, H., Ichihashi, M. & Hearing, V. J. Role of the ubiquitin proteasome system in regulating skin pigmentation. International journal of molecular sciences 10, 4428–4434 (2009).
pubmed: 20057953
pmcid: 2790116
doi: 10.3390/ijms10104428
Stenina, M. A., Krivov, L. I., Voevodin, D. A. & Yarygin, V. N. Phenotypic differences between mdx black mice and mdx albino mice. Comparison of cytokine levels in the blood. Bulletin of experimental biology and medicine 155, 376–379 (2013).
pubmed: 24137608
doi: 10.1007/s10517-013-2158-5
Fei, E. et al. Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related protein, regulates synapsin I expression. The Journal of biological chemistry 285, 38630–38640 (2010).
pubmed: 20921223
pmcid: 2992295
doi: 10.1074/jbc.M110.107912
Ryder, P. V. et al. The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky-Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIalpha. Molecular biology of the cell 24, 2269–2284 (2013).
pubmed: 23676666
pmcid: 3708732
doi: 10.1091/mbc.e13-02-0088
Palmisano, I. et al. The ocular albinism type 1 protein, an intracellular G protein-coupled receptor, regulates melanosome transport in pigment cells. Human molecular genetics 17, 3487–3501 (2008).
pubmed: 18697795
pmcid: 2572695
doi: 10.1093/hmg/ddn241
Kanehisa, M., Sato, Y., Furumichi, M., Morishima, K. & Tanabe, M. New approach for understanding genome variations in KEGG. Nucleic Acids Research, https://doi.org/10.1093/nar/gky962 (2019).
pmcid: 6324070
doi: 10.1093/nar/gky962
pubmed: 6324070
Tea, M., Michael, M. Z., Brereton, H. M. & Williams, K. A. Stability of small non-coding RNA reference gene expression in the rat retina during exposure to cyclic hyperoxia. Molecular vision 19, 501–508 (2013).
pubmed: 23441123
pmcid: 3580969
Mi, Q.-S. et al. Identification of mouse serum miRNA endogenous references by global gene expression profiles. PloS one 7, e31278 (2012).
pubmed: 22348064
pmcid: 3277497
doi: 10.1371/journal.pone.0031278
Castorina, A. et al. Neurofibromin and amyloid precursor protein expression in dopamine D3 receptor knock-out mice brains. Neurochemical Research, https://doi.org/10.1007/s11064-010-0359-0 (2011).
pubmed: 21170735
doi: 10.1007/s11064-010-0359-0
Rueden, C. T. et al. ImageJ2: ImageJ for the next generation of scientific image data. BMC Bioinformatics, https://doi.org/10.1186/s12859-017-1934-z (2017).
Robson, J. G., Saszik, S. M., Ahmed, J. & Frishman, L. J. Rod and cone contributions to the a-wave of the electroretinogram of the macaque. Journal of Physiology, https://doi.org/10.1113/jphysiol.2002.030304 (2003).
pubmed: 12562933
pmcid: 2342654
doi: 10.1113/jphysiol.2002.030304