<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bonaglia, Maria Clara</style></author><author><style face="normal" font="default" size="100%">Kurtas, Nehir Edibe</style></author><author><style face="normal" font="default" size="100%">Errichiello, Edoardo</style></author><author><style face="normal" font="default" size="100%">Bertuzzo, Sara</style></author><author><style face="normal" font="default" size="100%">Beri, Silvana</style></author><author><style face="normal" font="default" size="100%">Mehrjouy, Mana M</style></author><author><style face="normal" font="default" size="100%">Provenzano, Aldesia</style></author><author><style face="normal" font="default" size="100%">Vergani, Debora</style></author><author><style face="normal" font="default" size="100%">Pecile, Vanna</style></author><author><style face="normal" font="default" size="100%">Novara, Francesca</style></author><author><style face="normal" font="default" size="100%">Reho, Paolo</style></author><author><style face="normal" font="default" size="100%">Di Giacomo, Marilena Carmela</style></author><author><style face="normal" font="default" size="100%">Discepoli, Giancarlo</style></author><author><style face="normal" font="default" size="100%">Giorda, Roberto</style></author><author><style face="normal" font="default" size="100%">Aldred, Micheala A</style></author><author><style face="normal" font="default" size="100%">Santos-Rebouças, Cíntia Barros</style></author><author><style face="normal" font="default" size="100%">Goncalves, Andressa Pereira</style></author><author><style face="normal" font="default" size="100%">Abuelo, Diane N</style></author><author><style face="normal" font="default" size="100%">Giglio, Sabrina</style></author><author><style face="normal" font="default" size="100%">Ricca, Ivana</style></author><author><style face="normal" font="default" size="100%">Franchi, Fabrizia</style></author><author><style face="normal" font="default" size="100%">Patsalis, Philippos</style></author><author><style face="normal" font="default" size="100%">Sismani, Carolina</style></author><author><style face="normal" font="default" size="100%">Morí, María Angeles</style></author><author><style face="normal" font="default" size="100%">Nevado, Julián</style></author><author><style face="normal" font="default" size="100%">Tommerup, Niels</style></author><author><style face="normal" font="default" size="100%">Zuffardi, Orsetta</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">De novo unbalanced translocations have a complex history/aetiology.</style></title><secondary-title><style face="normal" font="default" size="100%">Hum Genet</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Hum. Genet.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">DNA End-Joining Repair</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Meiosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Recombinational DNA Repair</style></keyword><keyword><style  face="normal" font="default" size="100%">Translocation, Genetic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2018 Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">137</style></volume><pages><style face="normal" font="default" size="100%">817-829</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We investigated 52 cases of de novo unbalanced translocations, consisting in a terminally deleted or inverted-duplicated deleted (inv-dup del) 46th chromosome to which the distal portion of another chromosome or its opposite end was transposed. Array CGH, whole-genome sequencing, qPCR, FISH, and trio genotyping were applied. A biparental origin of the deletion and duplication was detected in 6 cases, whereas in 46, both imbalances have the same parental origin. Moreover, the duplicated region was of maternal origin in more than half of the cases, with 25% of them showing two maternal and one paternal haplotype. In all these cases, maternal age was increased. These findings indicate that the primary driver for the occurrence of the de novo unbalanced translocations is a maternal meiotic non-disjunction, followed by partial trisomy rescue of the supernumerary chromosome present in the trisomic zygote. In contrast, asymmetric breakage of a dicentric chromosome, originated either at the meiosis or postzygotically, in which the two resulting chromosomes, one being deleted and the other one inv-dup del, are repaired by telomere capture, appears at the basis of all inv-dup del translocations. Notably, this mechanism also fits with the origin of some simple translocations in which the duplicated region was of paternal origin. In all cases, the signature at the translocation junctions was that of non-homologous end joining (NHEJ) rather than non-allelic homologous recombination (NAHR). Our data imply that there is no risk of recurrence in the following pregnancies for any of the de novo unbalanced translocations we discuss here.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">10</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/30276538?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Ghezzi, Daniele</style></author><author><style face="normal" font="default" size="100%">Sevrioukova, Irina</style></author><author><style face="normal" font="default" size="100%">Invernizzi, Federica</style></author><author><style face="normal" font="default" size="100%">Lamperti, Costanza</style></author><author><style face="normal" font="default" size="100%">Mora, Marina</style></author><author><style face="normal" font="default" size="100%">d'Adamo, Pio</style></author><author><style face="normal" font="default" size="100%">Novara, Francesca</style></author><author><style face="normal" font="default" size="100%">Zuffardi, Orsetta</style></author><author><style face="normal" font="default" size="100%">Uziel, Graziella</style></author><author><style face="normal" font="default" size="100%">Zeviani, Massimo</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Severe X-linked mitochondrial encephalomyopathy associated with a mutation in apoptosis-inducing factor.</style></title><secondary-title><style face="normal" font="default" size="100%">Am J Hum Genet</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Am. J. Hum. Genet.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Apoptosis</style></keyword><keyword><style  face="normal" font="default" size="100%">Apoptosis Inducing Factor</style></keyword><keyword><style  face="normal" font="default" size="100%">Caspase 3</style></keyword><keyword><style  face="normal" font="default" size="100%">Computer Simulation</style></keyword><keyword><style  face="normal" font="default" size="100%">Dietary Supplements</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Primers</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA, Mitochondrial</style></keyword><keyword><style  face="normal" font="default" size="100%">Electron Transport</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Fibroblasts</style></keyword><keyword><style  face="normal" font="default" size="100%">Flavin-Adenine Dinucleotide</style></keyword><keyword><style  face="normal" font="default" size="100%">Genes, X-Linked</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">In Situ Nick-End Labeling</style></keyword><keyword><style  face="normal" font="default" size="100%">Infant, Newborn</style></keyword><keyword><style  face="normal" font="default" size="100%">Magnetic Resonance Imaging</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mitochondrial Encephalomyopathies</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle, Skeletal</style></keyword><keyword><style  face="normal" font="default" size="100%">Mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Nervous System Diseases</style></keyword><keyword><style  face="normal" font="default" size="100%">Pedigree</style></keyword><keyword><style  face="normal" font="default" size="100%">Poly(ADP-ribose) Polymerases</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Conformation</style></keyword><keyword><style  face="normal" font="default" size="100%">Riboflavin</style></keyword><keyword><style  face="normal" font="default" size="100%">Staurosporine</style></keyword><keyword><style  face="normal" font="default" size="100%">Twins, Monozygotic</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2010</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2010 Apr 9</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">86</style></volume><pages><style face="normal" font="default" size="100%">639-49</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;We investigated two male infant patients who were given a diagnosis of progressive mitochondrial encephalomyopathy on the basis of clinical, biochemical, and morphological features. These patients were born from monozygotic twin sisters and unrelated fathers, suggesting an X-linked trait. Fibroblasts from both showed reduction of respiratory chain (RC) cIII and cIV, but not of cI activities. We found a disease-segregating mutation in the X-linked AIFM1 gene, encoding the Apoptosis-Inducing Factor (AIF) mitochondrion-associated 1 precursor that deletes arginine 201 (R201 del). Under normal conditions, mature AIF is a FAD-dependent NADH oxidase of unknown function and is targeted to the mitochondrial intermembrane space (this form is called AIF(mit)). Upon apoptogenic stimuli, a soluble form (AIF(sol)) is released by proteolytic cleavage and migrates to the nucleus, where it induces &quot;parthanatos,&quot; i.e., caspase-independent fragmentation of chromosomal DNA. In vitro, the AIF(R201 del) mutation decreases stability of both AIF(mit) and AIF(sol) and increases the AIF(sol) DNA binding affinity, a prerequisite for nuclear apoptosis. In AIF(R201 del) fibroblasts, staurosporine-induced parthanatos was markedly increased, whereas re-expression of AIF(wt) induced recovery of RC activities. Numerous TUNEL-positive, caspase 3-negative nuclei were visualized in patient #1's muscle, again indicating markedly increased parthanatos in the AIF(R201 del) critical tissues. We conclude that AIF(R201 del) is an unstable mutant variant associated with increased parthanatos-linked cell death. Our data suggest a role for AIF in RC integrity and mtDNA maintenance, at least in some tissues. Interestingly, riboflavin supplementation was associated with prolonged improvement of patient #1's neurological conditions, as well as correction of RC defects in mutant fibroblasts, suggesting that stabilization of the FAD binding in AIF(mit) is beneficial.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/20362274?dopt=Abstract</style></custom1></record></records></xml>