L
Lee J. Martin
Researcher at Johns Hopkins University School of Medicine
Publications - 254
Citations - 26446
Lee J. Martin is an academic researcher from Johns Hopkins University School of Medicine. The author has contributed to research in topics: Neurodegeneration & Glutamate receptor. The author has an hindex of 80, co-authored 252 publications receiving 25183 citations. Previous affiliations of Lee J. Martin include University of Mainz & University of California, San Francisco.
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Journal ArticleDOI
Localization of neuronal and glial glutamate transporters
Jeffrey D. Rothstein,Lee J. Martin,Allan I. Levey,Margaret Dykes-Hoberg,Lin Jin,David Wu,Norman Nash,Ralph W. Kuncl +7 more
TL;DR: The cellular and subcellular distributions of the glutamate transporter subtypes EAAC1, GLT-1, and GLAST in the rat CNS were demonstrated using anti-peptide antibodies that recognize the C-terminal domains of each transporter.
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Selective loss of glial glutamate transporter GLT-1 in amyotrophic lateral sclerosis.
TL;DR: Developing C‐terminal, antioligopeptide antibodies that were specific for each glutamate transporter subtype found that GLT‐1 immunoreactive protein was severely decreased in ALS, both in motor cortex (71% decrease compared with control) and in spinal cord.
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Decreased Glutamate Transport by the Brain and Spinal Cord in Amyotrophic Lateral Sclerosis
TL;DR: ALS is associated with a defect in high-affinity glutamate transport that has disease, region, and chemical specificity and could lead to neurotoxic levels of extracellular glutamate and thus be pathogenic in ALS.
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Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death.
Toshio Ohshima,Jerrold M. Ward,Chang Goo Huh,Glenn Longenecker,Veeranna,Harish C. Pant,Roscoe O. Brady,Lee J. Martin,Ashok B. Kulkarni +8 more
TL;DR: Cdk5(-/-) mice exhibit unique lesions in the central nervous system associated with perinatal mortality and also suggest that Cdk5 may play critical roles in neuronal cytoskeleton structure and organization.
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Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport.
Edward H. Koo,Sangram S. Sisodia,David R. Archer,Lee J. Martin,Andreas Weidemann,Konrad Beyreuther,Peter Fischer,Colin L. Masters,Donald L. Price +8 more
TL;DR: It is suggested that APP is synthesized in neurons and delivered to dystrophic nerve endings, where subsequent alterations of local processing of APP result in deposits of brain amyloid.