Salvatore Carbonetto

TL;DR: Examining a subset of these mRNAs and their encoded proteins in brain tissue from Fmr1 knockout mice, it is observed that some of these cargoes as well as the proteins they encode show discrete changes in abundance and/or differential subcellular distribution, consistent with spatially selective regulation of multiple biological pathways by FMRP.

TL;DR: Dystroglycan-alpha is an agrin-binding protein and part of a dystrophin-receptor complex involved in AChR aggregation, which is shown to be calcium dependent and inhibited by monoclonal antibody IIH6 against dystrog-alpha, heparin, and laminin, but not by fibronectin.

TL;DR: Two de novo mutations (R1117X and R536W) were identified in two families, one being found in three affected brothers, suggesting germline mosaicism.

TL;DR: This study used differentiating embryoid bodies derived from mouse embryonic stem cells null for γ1-laminin, β1-integrin and α/β-dystroglycan to dissect the contributions of laminin domains and interacting receptors to this process.

TL;DR: These protein microsequence data support the data of Ibraghimov-Beskrovnaya et al., which suggest that the dystroglycan precursor is processed into 120/156- and 43-kDa proteins, and suggest a revision in the position of the proposed cleavage site of the precursor.