000130342 001__ 130342
000130342 005__ 20240731103330.0
000130342 0247_ $$2doi$$a10.1186/s13104-023-06491-z
000130342 0248_ $$2sideral$$a136558
000130342 037__ $$aART-2023-136558
000130342 041__ $$aeng
000130342 100__ $$aMoreno-Gázquez, Inmaculada
000130342 245__ $$aTargeted sequencing of selected functional genes in patients with wild-type transthyretin amyloidosis
000130342 260__ $$c2023
000130342 5060_ $$aAccess copy available to the general public$$fUnrestricted
000130342 5203_ $$aObjective: Wild-type transthyretin (ATTRwt) amyloidosis is caused by the misfolding and deposition of the transthyretin protein (TTR) in the absence of mutations in the TTR gene. Studies regarding the variant form of ATTR amyloidosis (ATTRv) suggest that the presence of single-nucleotide polymorphisms (SNP) in genes other than the TTR, may influence the development of the disease. However, other genetic factors involved in the aetiopathogenesis of ATTRwt are currently unknown. This work investigates the presence of sequence variants in genes selected for their possible impact on ATTRwt amyloidosis. To do so, targeted sequencing of 84 protein-coding genes was performed in a cohort of 27 patients diagnosed with ATTRwt.
Results: After applying quality and frequency filtering criteria, 72 rare or novel genetic variants were found. Subsequent classification according to the ACMG-AMP criteria resulted in 17 variants classified as of uncertain significance in 14 different genes. To our knowledge, this is the first report associating novel gene variants with ATTRwt amyloidosis. In conclusion, this study provides potential insights into the aetiopathogenesis of ATTRwt amyloidosis by linking novel coding-gene variants with the occurrence of the disease.
000130342 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000130342 592__ $$a0.486$$b2023
000130342 593__ $$aBiochemistry, Genetics and Molecular Biology (miscellaneous)$$c2023$$dQ2
000130342 593__ $$aMedicine (miscellaneous)$$c2023$$dQ3
000130342 594__ $$a3.6$$b2023
000130342 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000130342 700__ $$0(orcid)0000-0001-8655-9267$$aPérez-Palacios, Raquel$$uUniversidad de Zaragoza
000130342 700__ $$aAbengochea-Quílez, Lucia$$uUniversidad de Zaragoza
000130342 700__ $$aLahuerta Pueyo, Carmen
000130342 700__ $$aRoteta Unceta Barrenechea, Ana
000130342 700__ $$0(orcid)0000-0003-3501-0121$$aAndrés Gracia, Alejandro$$uUniversidad de Zaragoza
000130342 700__ $$0(orcid)0000-0002-1774-6488$$aAibar Arregui, Miguel Angel
000130342 700__ $$0(orcid)0000-0002-1817-4549$$aMenao Guillén, Sebastián$$uUniversidad de Zaragoza
000130342 7102_ $$11011$$2770$$aUniversidad de Zaragoza$$bDpto. Microb.Ped.Radio.Sal.Pú.$$cÁrea Radiol. y Medicina Física
000130342 7102_ $$11001$$2025$$aUniversidad de Zaragoza$$bDpto. Anatom.,Embri.Genét.Ani.$$cÁrea Anatom.Anatom.Patológ.Com
000130342 7102_ $$15005$$2555$$aUniversidad de Zaragoza$$bDpto. Ing.Quím.Tecnol.Med.Amb.$$cÁrea Ingeniería Química
000130342 7102_ $$11002$$2807$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Toxicología
000130342 773__ $$g16 (2023), 249 [8 pp.]$$pBMC Res. Notes$$tBBMC research notes$$x1756-0500
000130342 8564_ $$s1069878$$uhttps://zaguan.unizar.es/record/130342/files/texto_completo.pdf$$yVersión publicada
000130342 8564_ $$s2427462$$uhttps://zaguan.unizar.es/record/130342/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000130342 909CO $$ooai:zaguan.unizar.es:130342$$particulos$$pdriver
000130342 951__ $$a2024-07-31-09:46:11
000130342 980__ $$aARTICLE