{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,9]],"date-time":"2026-08-09T04:41:52Z","timestamp":1786250512848,"version":"build-2736575974"},"reference-count":153,"publisher":"MDPI AG","issue":"16","license":[{"start":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T00:00:00Z","timestamp":1786060800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100003725","name":"National Research Foundation of Korea","doi-asserted-by":"crossref","award":["RS-2024-00344799"],"award-info":[{"award-number":["RS-2024-00344799"]}],"id":[{"id":"10.13039\/501100003725","id-type":"DOI","asserted-by":"crossref"}]},{"award":["RS-2024-00344799"],"award-info":[{"award-number":["RS-2024-00344799"]}],"id":[{"id":"https:\/\/ror.org\/013aysd81","id-type":"ROR","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003716","name":"Korea Basic Science Institute","doi-asserted-by":"publisher","award":["RS-2024-00402577"],"award-info":[{"award-number":["RS-2024-00402577"]}],"id":[{"id":"10.13039\/501100003716","id-type":"DOI","asserted-by":"publisher"}]},{"award":["RS-2024-00402577"],"award-info":[{"award-number":["RS-2024-00402577"]}],"id":[{"id":"https:\/\/ror.org\/0417sdw47","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Int. J. Mol. Sci.","IJMS"],"abstract":"<jats:p>Intracellular retinoid-binding proteins, including cellular retinol-binding proteins (CRBPs) and cellular retinoic acid-binding proteins (CRABPs), belong to the intracellular lipid-binding protein (iLBP) family, whereas cellular retinaldehyde-binding protein (CRALBP) is a structurally distinct retinoid-binding protein belonging to the CRAL-TRIO protein family and functions as an active regulator of retinoid trafficking, metabolism, and signaling. Although these proteins are directly implicated in inherited retinal dystrophies, retinoid-dependent cancers, and neurodegenerative diseases, they have received comparatively little attention as pharmacological targets relative to the extracellular carrier Retinol-Binding Protein 4 (RBP4). High-resolution structural studies, including atomic-resolution X-ray co-crystal structures of protein\u2013ligand complexes, have defined the binding pocket architecture of each protein and established a basis for structure-guided drug discovery. This review critically evaluates the druggability of CRBP, CRALBP, and CRABP by integrating structural, biochemical, and pharmacological evidence. We discuss known small-molecule modulators, including the first-in-class CRBP1 inhibitor abn-CBD and next-generation non-retinoid scaffolds, alongside gene therapy strategies targeting CRALBP deficiency. We further address the selectivity challenges inherent to the conserved iLBP fold and identify future directions for the development of isoform-selective therapeutics for retinal degeneration, oncology, and neurodegeneration.<\/jats:p>","DOI":"10.3390\/ijms27167096","type":"journal-article","created":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T16:00:43Z","timestamp":1786118443000},"page":"7096","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Intracellular Retinoid-Binding Proteins (CRBP, CRALBP, CRABP) as Emerging Drug Targets in Retinal Disease"],"prefix":"10.3390","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0009-0009-0618-7834","authenticated-orcid":false,"given":"Laxmi","family":"Regmi Bagale","sequence":"first","affiliation":[{"name":"College of Pharmacy, Keimyung University, 1095 Dalgubeol-daero, Dalseo-gu, Daegu 42601, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7363-4053","authenticated-orcid":false,"given":"Hye Jin","family":"Kim","sequence":"additional","affiliation":[{"name":"College of Pharmacy, Keimyung University, 1095 Dalgubeol-daero, Dalseo-gu, Daegu 42601, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,8,7]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1126\/science.162.3850.230","article-title":"Molecular basis of visual excitation","volume":"162","author":"Wald","year":"1968","journal-title":"Science"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1126\/science.289.5480.739","article-title":"Crystal structure of rhodopsin: A G protein-coupled receptor","volume":"289","author":"Palczewski","year":"2000","journal-title":"Science"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/S0896-6273(00)80845-4","article-title":"The evolution and physiology of human color vision: Insights from molecular genetic studies of visual pigments","volume":"24","author":"Nathans","year":"1999","journal-title":"Neuron"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1021\/cr400107q","article-title":"Chemistry of the Retinoid (Visual) Cycle","volume":"114","author":"Kiser","year":"2014","journal-title":"Chem. 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