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Sha Mi

Researcher at Biogen Idec

Publications -  82
Citations -  6333

Sha Mi is an academic researcher from Biogen Idec. The author has contributed to research in topics: Oligodendrocyte & Oligodendrocyte differentiation. The author has an hindex of 27, co-authored 80 publications receiving 5890 citations. Previous affiliations of Sha Mi include Genetics Institute, Inc..

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Syncytin is a captive retroviral envelope protein involved in human placental morphogenesis.

TL;DR: It is shown that expression of recombinant syncytin in a wide variety of cell types induces the formation of giant syncytia, and that fusion of a human trophoblastic cell line expressing endogenousSyncytin can be inhibited by an anti-syncytin antiserum, and thus may be important in human placental morphogenesis.
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LINGO-1 is a component of the Nogo-66 receptor/p75 signaling complex.

TL;DR: In non-neuronal cells, coexpression of human NgR1, p75 and LINGO-1 conferred responsiveness to oligodendrocyte myelin glycoprotein, as measured by RhoA activation, which suggests that Lingo-1 has an important role in CNS biology.
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LINGO-1 negatively regulates myelination by oligodendrocytes.

TL;DR: The ability to recapitulate CNS myelination in vitro using LINGO-1 antagonists and the in vivo effects seen in the LINGo-1 knockout indicate that Lingo-1 signaling may be critical for CNSMyelination.
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LINGO-1 antagonist promotes spinal cord remyelination and axonal integrity in MOG-induced experimental autoimmune encephalomyelitis

TL;DR: Antagonism of LINGO-1 or its pathway is a promising approach for the treatment of demyelinating diseases of the CNS by reflected biologically by improved axonal integrity, as confirmed by magnetic resonance diffusion tensor imaging, and by newly formed myelin sheaths, as determined by electron microscopy.
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TAJ/TROY, an Orphan TNF Receptor Family Member, Binds Nogo-66 Receptor 1 and Regulates Axonal Regeneration

TL;DR: It is shown that an orphan receptor in the TNF family called TAJ, broadly expressed in postnatal and adult neurons, binds to NgR1 and can replace p75 in the p75/NgR1/LINGO-1 complex to activate RhoA in the presence of myelin inhibitors.