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dc.contributor.authorSiggs, Owen Men_US
dc.contributor.authorSouzeau, Emmanuelleen_US
dc.contributor.authorCraig, Jamie Een_US
dc.date.accessioned2019-01-04T05:25:53Z
dc.date.available2019-01-04T05:25:53Z
dc.date.issued2019-01-02
dc.identifier.citationSiggs, O. M., Souzeau, E., & Craig, J. E. (2019). Loss of ciliary zonule protein hydroxylation and lens stability as a predicted consequence of biallelic ASPH variation. Ophthalmic Genetics, 1–5. https:// doi.org/10.1080/13816810.2018.1561904en_US
dc.identifier.urihttps://doi.org/10.1080/13816810.2018.1561904
dc.identifier.urihttp://hdl.handle.net/2328/38796
dc.descriptionThis author accepted manuscript is made available following 12 month embargo from date of publication (January 2019) in accordance with the publisher’s archiving policy “This is an Accepted Manuscript of an article published by Taylor & Francis in Ophthalmic Genetics on 2 January 2019, available online: http://www.tandfonline.com/10.1080/13816810.2018.1561904”en_US
dc.description.abstractPurpose: Stability of the crystalline lens requires formation of microfibril bundles and their higher-order structures of ciliary zonules. Trauma, malformation, or degeneration of the ciliary zonules can lead to dislocation or displacement of the lens, which in turn can cause transient or permanent loss of visual acuity. The purpose of this study was to identify the predicted substrates of ASPH, a 2-oxoglutarate- and Fe2+-dependent hydroxylase, which may account for the lens instability phenotype of ASPH-associated syndromes. Methods: A single proband of European ancestry with spherophakia and high myopia was subjected to exome sequencing. Proteins containing the ASPH hydroxylation motif were identified within the SwissProt protein database. Results: We identified 105 putative substrates of ASPH-mediated hydroxylation in the human proteome, of which two (FBN1 and LTBP2) are associated with inherited ectopia lentis syndromes, and are essential for microfibril and ciliary zonule development. Conclusion: Our results implicate ASPH-mediated hydroxylation in the formation of FBN1/LTBP2 microfibril bundles and competent ciliary zonules.en_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Groupen_US
dc.relationhttp://purl.org/au-research/grants/nhmrc/1116360en_US
dc.relationhttp://purl.org/au-research/grants/nhmrc/1107098en_US
dc.rights© 2019 Taylor & Francis Group, LLCen_US
dc.subjectTraboulsi syndromeen_US
dc.subjectASPHen_US
dc.subjectLTBP2en_US
dc.subjectFBN1en_US
dc.subjectectopia lentisen_US
dc.titleLoss of ciliary zonule protein hydroxylation and lens stability as a predicted consequence of biallelic ASPH variationen_US
dc.typeArticleen_US
dc.relation.grantnumberNHMRC/1116360en_US
dc.relation.grantnumberNHMRC/1107098en_US
dc.identifier.doihttps://doi.org/10.1080/13816810.2018.1561904en_US
dc.rights.holderTaylor & Francis Group, LLCen_US
dc.rights.licenseIn Copyright
local.contributor.authorOrcidLookupSiggs, Owen M: https://orcid.org/0000-0003-2840-4851en_US
local.contributor.authorOrcidLookupSouzeau, Emmanuelle: https://orcid.org/0000-0002-2015-6577en_US
local.contributor.authorOrcidLookupCraig, Jamie E: https://orcid.org/0000-0001-9955-9696en_US


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