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Robert A. Lazzarini

Researcher at Icahn School of Medicine at Mount Sinai

Publications -  128
Citations -  10233

Robert A. Lazzarini is an academic researcher from Icahn School of Medicine at Mount Sinai. The author has contributed to research in topics: Vesicular stomatitis virus & RNA. The author has an hindex of 55, co-authored 128 publications receiving 10082 citations. Previous affiliations of Robert A. Lazzarini include National Institutes of Health & Hoffmann-La Roche.

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CNS Myelin and Sertoli Cell Tight Junction Strands Are Absent in Osp/Claudin-11 Null Mice

TL;DR: It is demonstrated that OSP is the mediator of parallel-array tight junction strands and distinguishes this protein from other intrinsic membrane proteins in tight junctions, providing direct evidence of the pivotal role of the claudin family in generating the paracellular physical barrier of tight junications necessary for spermatogenesis and normal CNS function.
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The glial cells missing-1 protein is essential for branching morphogenesis in the chorioallantoic placenta

TL;DR: These studies provide the earliest molecular insight into this aspect of placental development and show that Gcm1, encoding the transcription factor glial cells missing-1 (Gcm1), is expressed in small clusters of chorionic trophoblast cells at the flat Chorionic plate stage and at sites of chorioallantoic folding and extension when morphogenesis begins.
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Identification of the major multiphosphorylation site in mammalian neurofilaments.

TL;DR: A cross-reactive antigenic determinant shared by the peptides and the major NF phosphorylation site was shown to exist in neurofibrillary tangles of patients with Alzheimer disease as well as in two neuron-specific microtubule-associated proteins (MAPs)--i.e., MAP2 and tau.
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Emergence of three myelin proteins in oligodendrocytes cultured without neurons.

TL;DR: The sequential emergence, cytoplasmic location, and peak of expression of these three myelin proteins in vitro follow a pattern similar to that described in vivo and, therefore, are independent of continuous neuronal influences.
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An improved method for thin-layer chromatography of nucleotide mixtures containing32P-labeled orthophosphate

TL;DR: Developing poly(ethylene)imine cellulose thin layers with phosphate solutions gives improved resolution of complex mixtures of nucleotides and minimizes the tailing of highly radioactive orthophosphate present in the mixtures and thus facilitates chromatographic analysis of crude acid extracts of phosphate-labeled bacteria.