S
Susana G. Rossi
Researcher at University of Miami
Publications - 22
Citations - 1724
Susana G. Rossi is an academic researcher from University of Miami. The author has contributed to research in topics: Acetylcholinesterase & Neuromuscular junction. The author has an hindex of 17, co-authored 22 publications receiving 1623 citations.
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Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging
TL;DR: The preservation of muscle integrity and function in MCK-PGC-1α animals resulted in significantly improved whole-body health; both the loss of bone mineral density and the increase of systemic chronic inflammation, observed during normal aging, were prevented.
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Absence of α-Syntrophin Leads to Structurally Aberrant Neuromuscular Synapses Deficient in Utrophin
Marvin E. Adams,Neal R. Kramarcy,Stuart P. Krall,Susana G. Rossi,Richard L. Rotundo,Robert Sealock,Stanley C. Froehner +6 more
TL;DR: The α-syn−/− mice showed no evidence of myopathy, despite reduced levels of α-dystrobrevin−2. as discussed by the authors showed that α-syntrophin null mice have shallow nerve gutters, abnormal distributions of acetylcholine receptors, and postjunctional folds that are generally less organized and have fewer openings to the synaptic cleft than controls.
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The Dystroglycan Complex Is Necessary for Stabilization of Acetylcholine Receptor Clusters at Neuromuscular Junctions and Formation of the Synaptic Basement Membrane
TL;DR: It is shown that myotubes differentiated from dystroglycan−/− embryonic stem cells are responsive to agrin, but produce acetylcholine receptor (AChR) clusters which are two to three times larger in area, about half as dense, and significantly less stable than those on dystoglycan+/+ myot tubes.
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Absence of acetylcholinesterase at the neuromuscular junctions of perlecan-null mice.
TL;DR: Perlecan, a multifunctional heparan sulfate proteoglycan concentrated at the NMJ, is the unique acceptor molecule for collagen-tailed AChE at sites of nerve–muscle contact and is the principal mechanism for localizing A cholinesterase to the synaptic basal lamina.
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Biglycan is an extracellular MuSK binding protein important for synapse stability
Alison R. Amenta,Hilliary Creely,Mary Lynn Mercado,Hiroki Hagiwara,Beth A. McKechnie,Beatrice E. Lechner,Susana G. Rossi,Qiang Wang,Rick T. Owens,Emilio Marrero,Lin Mei,Werner Hoch,Marian F. Young,David J. McQuillan,Richard L. Rotundo,Justin R. Fallon +15 more
TL;DR: Results indicate that biglycan is an extracellular ligand for MuSK that is important for synapse stability, and that previously occupied presynaptic and postsynaptic territory has been vacated.