Associated Papers
A scalable approach to resolving variants of uncertain significance.
Tejura M et al.
Biorxiv : the Preprint Server for Biology, 2026
Restoring Sight: The Journey of AIPL1 from Discovery to Therapy.
Galieva A et al.
International Journal of Molecular Sciences, 2025
The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation.
Boehm AN et al.
The Journal of Biological Chemistry, 2020
AIPL1: A specialized chaperone for the phototransduction effector.
Yadav RP et al.
Cellular Signalling, 2017
The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6.
Sacristan-Reviriego A et al.
Human Molecular Genetics, 2017
Sources of discordance among germ-line variant classifications in ClinVar.
Yang S et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 2017
Aryl Hydrocarbon Receptor-interacting Protein-like 1 Is an Obligate Chaperone of Phosphodiesterase 6 and Is Assisted by the γ-Subunit of Its Client.
Gopalakrishna KN et al.
The Journal of Biological Chemistry, 2016
The Leber congenital amaurosis protein AIPL1 and EB proteins co-localize at the photoreceptor cilium.
Hidalgo-de-Quintana J et al.
Plos One, 2015
Genome-wide association and linkage analyses localize a progressive retinal atrophy locus in Persian cats.
Alhaddad H et al.
Mammalian Genome : Official Journal of the International Mammalian Genome Society, 2014
Interaction of aryl hydrocarbon receptor-interacting protein-like 1 with the farnesyl moiety.
Majumder A et al.
The Journal of Biological Chemistry, 2013
Structural studies on AIPL1 and its functional interactions with NUB1 to identify key interacting residues in LCA4.
Muthukumaran S et al.
Journal of Ocular Biology, Diseases, and Informatics, 2012
The inherited blindness protein AIPL1 regulates the ubiquitin-like FAT10 pathway.
Bett JS et al.
Plos One, 2012
Residual electroretinograms in young Leber congenital amaurosis patients with mutations of AIPL1.
Pennesi ME et al.
Investigative Ophthalmology & Visual Science, 2011
The Leber congenital amaurosis protein AIPL1 functions as part of a chaperone heterocomplex.
Hidalgo-de-Quintana J et al.
Investigative Ophthalmology & Visual Science, 2008
Leber congenital amaurosis: genes, proteins and disease mechanisms.
den Hollander AI et al.
Progress in Retinal and Eye Research, 2008
Leber congenital amaurosis - a model for efficient genetic testing of heterogeneous disorders: LXIV Edward Jackson Memorial Lecture.
Stone EM
American Journal of Ophthalmology, 2007
The Leber congenital amaurosis protein AIPL1 modulates the nuclear translocation of NUB1 and suppresses inclusion formation by NUB1 fragments.
van der Spuy J et al.
The Journal of Biological Chemistry, 2004
Purification, characterisation and intracellular localisation of aryl hydrocarbon interacting protein-like 1 (AIPL1) and effects of mutations associated with inherited retinal dystrophies.
Gallon VA et al.
Biochimica Et Biophysica Acta, 2004
Abolished interaction of NUB1 with mutant AIPL1 involved in Leber congenital amaurosis.
Kanaya K et al.
Biochemical and Biophysical Research Communications, 2004
The inherited blindness associated protein AIPL1 interacts with the cell cycle regulator protein NUB1.
Akey DT et al.
Human Molecular Genetics, 2002
Prevalence of mutations causing retinitis pigmentosa and other inherited retinopathies.
Sohocki MM et al.
Human Mutation, 2001
Mutations in a new photoreceptor-pineal gene on 17p cause Leber congenital amaurosis.
Sohocki MM et al.
Nature Genetics, 2000