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Lin Mei

Researcher at Case Western Reserve University

Publications -  266
Citations -  18002

Lin Mei is an academic researcher from Case Western Reserve University. The author has contributed to research in topics: Neuromuscular junction & Agrin. The author has an hindex of 69, co-authored 245 publications receiving 15903 citations. Previous affiliations of Lin Mei include University of Arizona & Chinese Academy of Sciences.

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Journal ArticleDOI

The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein

TL;DR: It is shown that PABPN1 interacts with and is stabilized by heat shock protein 90 (HSP90) and a potential therapeutic application of the HSP90 inhibitor 17-AAG for the treatment of OPMD is suggested.
Book ChapterDOI

Morphological Analysis of Neuromuscular Junctions by Immunofluorescent Staining of Whole-Mount Mouse Diaphragms

TL;DR: The immunofluorescent staining of whole-mount neonatal mouse diaphragms is described to study the morphological patterns of the neuromuscular junction by using of presynaptic neuronal marker-neurofilament and synaptophysin antibodies.
Journal ArticleDOI

Myosin X Interaction with KIF13B, a Crucial Pathway for Netrin-1-Induced Axonal Development.

TL;DR: Netrin-1 increases Myosin X (Myo X) interaction with KIF13B, and thus promotes axonal delivery of Myo X and axon initiation and contralateral branching in developing cerebral neurons, revealing unrecognized functions and mechanisms underlying Netrin- 1 regulation of axon development.
Journal ArticleDOI

pHluorin-BACE1-mCherry Acts as a Reporter for the Intracellular Distribution of Active BACE1 In Vitro and In Vivo

TL;DR: P pHluorin-BACE1-mCherry fusion protein may serve as a useful tool for visualizing active/inactive BACE1 in culture and in vivo, and (pro)renin receptor (PRR), a subunit of the v-ATPase complex, regulates pHLUorin’s fluorescence and Bace1 activity in pHluorbase expressing cells.
Journal ArticleDOI

PRRT2 frameshift mutation reduces its mRNA stability resulting loss of function in paroxysmal kinesigenic dyskinesia

TL;DR: These studies suggest that PRRT2 frameshift mutation leads to the loss of function by affecting its mRNA stability, a mechanism that is different from haploinsufficiency due to dysfunctional protein or gain of function caused by truncated protein.