<?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%">Matalonga, Leslie</style></author><author><style face="normal" font="default" size="100%">Bravo, Miren</style></author><author><style face="normal" font="default" size="100%">Serra-Peinado, Carla</style></author><author><style face="normal" font="default" size="100%">García-Pelegrí, Elisabeth</style></author><author><style face="normal" font="default" size="100%">Ugarteburu, Olatz</style></author><author><style face="normal" font="default" size="100%">Vidal, Silvia</style></author><author><style face="normal" font="default" size="100%">Llambrich, Maria</style></author><author><style face="normal" font="default" size="100%">Quintana, Ester</style></author><author><style face="normal" font="default" size="100%">Fuster-Jorge, Pedro</style></author><author><style face="normal" font="default" size="100%">Gonzalez-Bravo, Maria Nieves</style></author><author><style face="normal" font="default" size="100%">Beltran, Sergi</style></author><author><style face="normal" font="default" size="100%">Dopazo, Joaquin</style></author><author><style face="normal" font="default" size="100%">Garcia-Garcia, Francisco</style></author><author><style face="normal" font="default" size="100%">Foulquier, François</style></author><author><style face="normal" font="default" size="100%">Matthijs, Gert</style></author><author><style face="normal" font="default" size="100%">Mills, Philippa</style></author><author><style face="normal" font="default" size="100%">Ribes, Antonia</style></author><author><style face="normal" font="default" size="100%">Egea, Gustavo</style></author><author><style face="normal" font="default" size="100%">Briones, Paz</style></author><author><style face="normal" font="default" size="100%">Tort, Frederic</style></author><author><style face="normal" font="default" size="100%">Girós, Marisa</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mutations in TRAPPC11 are associated with a congenital disorder of glycosylation.</style></title><secondary-title><style face="normal" font="default" size="100%">Hum Mutat</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Hum Mutat</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Abnormalities, Multiple</style></keyword><keyword><style  face="normal" font="default" size="100%">Alleles</style></keyword><keyword><style  face="normal" font="default" size="100%">Amino Acid Substitution</style></keyword><keyword><style  face="normal" font="default" size="100%">Brain</style></keyword><keyword><style  face="normal" font="default" size="100%">Congenital Disorders of Glycosylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Genotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</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%">mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Phenotype</style></keyword><keyword><style  face="normal" font="default" size="100%">Vesicular Transport Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Whole Genome Sequencing</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2017 Feb</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">38</style></volume><pages><style face="normal" font="default" size="100%">148-151</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Congenital disorders of glycosylation (CDG) are a heterogeneous and rapidly growing group of diseases caused by abnormal glycosylation of proteins and/or lipids. Mutations in genes involved in the homeostasis of the endoplasmic reticulum (ER), the Golgi apparatus (GA), and the vesicular trafficking from the ER to the ER-Golgi intermediate compartment (ERGIC) have been found to be associated with CDG. Here, we report a patient with defects in both N- and O-glycosylation combined with a delayed vesicular transport in the GA due to mutations in TRAPPC11, a subunit of the TRAPPIII complex. TRAPPIII is implicated in the anterograde transport from the ER to the ERGIC as well as in the vesicle export from the GA. This report expands the spectrum of genetic alterations associated with CDG, providing new insights for the diagnosis and the understanding of the physiopathological mechanisms underlying glycosylation disorders.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">https://www.ncbi.nlm.nih.gov/pubmed/27862579?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%">Lucariello, Mario</style></author><author><style face="normal" font="default" size="100%">Vidal, Enrique</style></author><author><style face="normal" font="default" size="100%">Vidal, Silvia</style></author><author><style face="normal" font="default" size="100%">Saez, Mauricio</style></author><author><style face="normal" font="default" size="100%">Roa, Laura</style></author><author><style face="normal" font="default" size="100%">Huertas, Dori</style></author><author><style face="normal" font="default" size="100%">Pineda, Mercè</style></author><author><style face="normal" font="default" size="100%">Dalfó, Esther</style></author><author><style face="normal" font="default" size="100%">Dopazo, Joaquin</style></author><author><style face="normal" font="default" size="100%">Jurado, Paola</style></author><author><style face="normal" font="default" size="100%">Armstrong, Judith</style></author><author><style face="normal" font="default" size="100%">Esteller, Manel</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Whole exome sequencing of Rett syndrome-like patients reveals the mutational diversity of the clinical phenotype.</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%">Adolescent</style></keyword><keyword><style  face="normal" font="default" size="100%">Adult</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Caenorhabditis elegans</style></keyword><keyword><style  face="normal" font="default" size="100%">Carrier Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Cycle Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Child</style></keyword><keyword><style  face="normal" font="default" size="100%">Child, Preschool</style></keyword><keyword><style  face="normal" font="default" size="100%">DNA Mutational Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Exome</style></keyword><keyword><style  face="normal" font="default" size="100%">Female</style></keyword><keyword><style  face="normal" font="default" size="100%">Forkhead Transcription Factors</style></keyword><keyword><style  face="normal" font="default" size="100%">Genetic Variation</style></keyword><keyword><style  face="normal" font="default" size="100%">High-Throughput Nucleotide Sequencing</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Methyl-CpG-Binding Protein 2</style></keyword><keyword><style  face="normal" font="default" size="100%">mutation</style></keyword><keyword><style  face="normal" font="default" size="100%">Nerve Tissue Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Serine-Threonine Kinases</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Nicotinic</style></keyword><keyword><style  face="normal" font="default" size="100%">Rett Syndrome</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2016</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2016 12</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">135</style></volume><pages><style face="normal" font="default" size="100%">1343-1354</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Classical Rett syndrome (RTT) is a neurodevelopmental disorder where most of cases carry MECP2 mutations. Atypical RTT variants involve mutations in CDKL5 and FOXG1. However, a subset of RTT patients remains that do not carry any mutation in the described genes. Whole exome sequencing was carried out in a cohort of 21 female probands with clinical features overlapping with those of RTT, but without mutations in the customarily studied genes. Candidates were functionally validated by assessing the appearance of a neurological phenotype in Caenorhabditis elegans upon disruption of the corresponding ortholog gene. We detected pathogenic variants that accounted for the RTT-like phenotype in 14 (66.6 %) patients. Five patients were carriers of mutations in genes already known to be associated with other syndromic neurodevelopmental disorders. We determined that the other patients harbored mutations in genes that have not previously been linked to RTT or other neurodevelopmental syndromes, such as the ankyrin repeat containing protein ANKRD31 or the neuronal acetylcholine receptor subunit alpha-5 (CHRNA5). Furthermore, worm assays demonstrated that mutations in the studied candidate genes caused locomotion defects. Our findings indicate that mutations in a variety of genes contribute to the development of RTT-like phenotypes.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">12</style></issue><custom1><style face="normal" font="default" size="100%">https://www.ncbi.nlm.nih.gov/pubmed/27541642?dopt=Abstract</style></custom1></record></records></xml>