% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Martin:136803,
      author       = {Martin, Elodie and Schüle, Rebecca and Smets, Katrien and
                      Rastetter, Agnès and Boukhris, Amir and Loureiro, José L
                      and Gonzalez, Michael A and Mundwiller, Emeline and
                      Deconinck, Tine and Wessner, Marc and Jornea, Ludmila and
                      Oteyza, Andrés Caballero and Durr, Alexandra and Martin,
                      Jean-Jacques and Schöls, Ludger and Mhiri, Chokri and
                      Lamari, Foudil and Züchner, Stephan and De Jonghe, Peter
                      and Kabashi, Edor and Brice, Alexis and Stevanin, Giovanni},
      title        = {{L}oss of function of glucocerebrosidase {GBA}2 is
                      responsible for motor neuron defects in hereditary spastic
                      paraplegia.},
      journal      = {The American journal of human genetics},
      volume       = {92},
      number       = {2},
      issn         = {0002-9297},
      address      = {New York, NY},
      publisher    = {Elsevier},
      reportid     = {DZNE-2020-03125},
      pages        = {238-244},
      year         = {2013},
      abstract     = {Spastic paraplegia 46 refers to a locus mapped to
                      chromosome 9 that accounts for a complicated
                      autosomal-recessive form of hereditary spastic paraplegia
                      (HSP). With next-generation sequencing in three independent
                      families, we identified four different mutations in GBA2
                      (three truncating variants and one missense variant), which
                      were found to cosegregate with the disease and were absent
                      in controls. GBA2 encodes a microsomal nonlysosomal
                      glucosylceramidase that catalyzes the conversion of
                      glucosylceramide to free glucose and ceramide and the
                      hydrolysis of bile acid 3-O-glucosides. The missense variant
                      was also found at the homozygous state in a simplex subject
                      in whom no residual glucocerebrosidase activity of GBA2
                      could be evidenced in blood cells, opening the way to a
                      possible measurement of this enzyme activity in clinical
                      practice. The overall phenotype was a complex HSP with
                      mental impairment, cataract, and hypogonadism in males
                      associated with various degrees of corpus callosum and
                      cerebellar atrophy on brain imaging. Antisense morpholino
                      oligonucleotides targeting the zebrafish GBA2 orthologous
                      gene led to abnormal motor behavior and axonal
                      shortening/branching of motoneurons that were rescued by the
                      human wild-type mRNA but not by applying the same mRNA
                      containing the missense mutation. This study highlights the
                      role of ceramide metabolism in HSP pathology.},
      keywords     = {Adolescent / Adult / Aged / Animals / Brain: pathology /
                      Child / Child, Preschool / Family / Female / Humans / Infant
                      / Male / Middle Aged / Motor Neurons: pathology / Mutation:
                      genetics / Neuroimaging / Pedigree / Spastic Paraplegia,
                      Hereditary: enzymology / Spastic Paraplegia, Hereditary:
                      genetics / Young Adult / Zebrafish / Zebrafish Proteins:
                      genetics / beta-Glucosidase: genetics / Zebrafish Proteins
                      (NLM Chemicals) / beta-Glucosidase (NLM Chemicals) / GBA2
                      protein, human (NLM Chemicals) / GBA2 protein, zebrafish
                      (NLM Chemicals)},
      cin          = {AG Schöls},
      ddc          = {570},
      cid          = {I:(DE-2719)5000005},
      pnm          = {345 - Population Studies and Genetics (POF3-345)},
      pid          = {G:(DE-HGF)POF3-345},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23332916},
      pmc          = {pmc:PMC3567271},
      doi          = {10.1016/j.ajhg.2012.11.021},
      url          = {https://pub.dzne.de/record/136803},
}