Keyword search (4,163 papers available)

"Stanga D" Authored Publications:

Title Authors PubMed ID
1 A Spike-Accum bioconjugate protein vaccine confers potent SARS-CoV-2-specific immunity Pierre Bikorimana J; Caveney NA; El-Hachem N; Mandl GA; Capobianco JA; Stanga D; Abusarah J; Hancock MA; Farah R; Gonçalves MP; Falzarano D; Liao M; Hamonic G; Liu Q; Beaudoin S; Talbot S; Rafei M; 41054531
CNSR
2 Publisher Correction: Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein. Milev MP; Stanga D; Schänzer A; Nascimento A; Saint-Dic D; Ortez C; Natera-de Benito D; Barrios DG; Colomer J; Badosa C; Jou C; Gallano P; Gonzalez-Quereda L; Töpf A; Johnson K; Straub V; Hahn A; Sacher M; Jimenez-Mallebrera C; 33173071
BIOLOGY
3 TRAPPing a neurological disorder: from yeast to humans. Lipatova Z, Van Bergen N, Stanga D, Sacher M, Christodoulou J, Segev N 32116085
BIOLOGY
4 Deficiencies in vesicular transport mediated by TRAPPC4 are associated with severe syndromic intellectual disability. Van Bergen NJ, Guo Y, Al-Deri N, Lipatova Z, Stanga D, Zhao S, Murtazina R, Gyurkovska V, Pehlivan D, Mitani T, Gezdirici A, Antony J, Collins F, Willis MJH, Coban Akdemir ZH, Liu P, Punetha J, Hunter JV, Jhangiani SN, Fatih JM, Rosenfeld JA, Posey JE, Gibbs RA, Karaca E, Massey S, Ranasinghe TG, Sleiman P, Troedson C, Lupski JR, Sacher M, Segev N, Hakonarson H, Christodoulou J 31794024
BIOLOGY
5 Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein. Milev MP, Stanga D, Schänzer A, Nascimento A, Saint-Dic D, Ortez C, Benito DN, Barrios DG, Colomer J, Badosa C, Jou C, Gallano P, Gonzalez-Quereda L, Töpf A, Johnson K, Straub V, Hahn A, Sacher M, Jimenez-Mallebrera C 31575891
BIOLOGY
6 Bi-allelic mutations in TRAPPC2L result in a neurodevelopmental disorder and have an impact on RAB11 in fibroblasts. Milev MP, Graziano C, Karall D, Kuper WFE, Al-Deri N, Cordelli DM, Haack TB, Danhauser K, Iuso A, Palombo F, Pippucci T, Prokisch H, Saint-Dic D, Seri M, Stanga D, Cenacchi G, van Gassen KLI, Zschocke J, Fauth C, Mayr JA, Sacher M, van Hasselt PM 30120216
BIOLOGY
7 TRAPPC11 functions in autophagy by recruiting ATG2B-WIPI4/WDR45 to preautophagosomal membranes. Stanga D, Zhao Q, Milev MP, Saint-Dic D, Jimenez-Mallebrera C, Sacher M 30843302
CONCORDIA

 

Title:Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein.
Authors:Milev MPStanga DSchänzer ANascimento ASaint-Dic DOrtez CBenito DNBarrios DGColomer JBadosa CJou CGallano PGonzalez-Quereda LTöpf AJohnson KStraub VHahn ASacher MJimenez-Mallebrera C
Link:https://www.ncbi.nlm.nih.gov/pubmed/31575891?dopt=Abstract
DOI:10.1038/s41598-019-50415-6
Publication:Scientific reports
Keywords:
PMID:31575891 Category:Sci Rep Date Added:2019-10-03
Dept Affiliation: BIOLOGY
1 Concordia University, Department of Biology, Montreal, Quebec, Canada.
2 Institute of Neuropathology, Justus Liebig University Giessen, Giessen, Germany.
3 Neuromuscular Unit, Neuropaediatrics Department, Hospital Sant Joan de Déu, Institut de Recerca Sant Joan de Déu, Barcelona, Spain.
4 U705 and U703 Center for Biomedical Research on Rare Diseases (CIBERER), Instituto de Salud Carlos III, Madrid, Spain.
5 Servicio de Pediatría, Hospital Universitario Nuestra Señora de Candelaria, Santa Cruz de Tenerife, Spain.
6 Pathology Department and Biobank, Hospital Sant Joan de Déu, Institut de Recerca Sant Joan de Déu, Barcelona, Spain.
7 Servicio de Genética, Hospital de la Santa Creu i Sant Pau, Barcelona, Spain.
8 The John Walton Muscular Dystrophy Research Centre, Institute of Genetic Medicine, Newcastle University and Newcastle Hospitals NHS Foundation Trust, Newcastle-upon-Tyne, UK.
9 Institute of Cellular Medicine, Newcastle University, Newcastle-upon-Tyne, UK.
10 Department of Child Neurology, Justus Liebig University Giessen, Giessen, Germany. Andreas.Hahn@paediat.med.uni-giessen.de.
11 Concordia University, Department of Biology, Montreal, Quebec, Canada. michael.sacher@concordia.ca.
12 McGill University, Department of Anatomy and Cell Biology, Montreal, Quebec, Canada. michael.sacher@concordia.ca.
13 Neuromuscular Unit, Neuropaediatrics Department, Hospital Sant Joan de Déu, Institut de Recerca Sant Joan de Déu, Barcelona, Spain. cjimenezm@fsjd.org.
14 U705 and U703 Center for Biomedical Research on Rare Diseases (CIBERER), Instituto de Salud Carlos III, Madrid, Spain. cjimenezm@fsjd.org.

Description:

Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein.

Sci Rep. 2019 Oct 01;9(1):14036

Authors: Milev MP, Stanga D, Schänzer A, Nascimento A, Saint-Dic D, Ortez C, Benito DN, Barrios DG, Colomer J, Badosa C, Jou C, Gallano P, Gonzalez-Quereda L, Töpf A, Johnson K, Straub V, Hahn A, Sacher M, Jimenez-Mallebrera C

Abstract

TRAPPC11 was identified as a component of the TRAPP III complex that functions in membrane trafficking and autophagy. Variants in TRAPPC11 have been reported to be associated with a broad spectrum of phenotypes but all affected individuals display muscular pathology. Identifying additional variants will further our understanding of the clinical spectrum of phenotypes and will reveal regions of the protein critical for its functions. Here we report three individuals from unrelated families that have bi-allellic TRAPPC11 variants. Subject 1 harbors a compound heterozygous variant (c.1287?+?5G?>?A and c.3379_3380insT). The former variant results in a partial deletion of the foie gras domain (p.Ala372_Ser429del), while the latter variant results in a frame-shift and extension at the carboxy terminus (p.Asp1127Valfs*47). Subjects 2 and 3 both harbour a homozygous missense variant (c.2938G?>?A; p.Gly980Arg). Fibroblasts from all three subjects displayed membrane trafficking defects manifested as delayed endoplasmic reticulum (ER)-to-Golgi transport and/or a delay in protein exit from the Golgi. All three individuals also show a defect in glycosylation of an ER-resident glycoprotein. However, only the compound heterozygous subject displayed an autophagic flux defect. Collectively, our characterization of these individuals with bi-allelic TRAPPC11 variants highlights the functional importance of the carboxy-terminal portion of the protein.

PMID: 31575891 [PubMed - in process]





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