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Basil Rapoport
Researcher at University of California, San Francisco
Publications - 141
Citations - 6221
Basil Rapoport is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Thyroid peroxidase & Thyrotropin receptor. The author has an hindex of 42, co-authored 141 publications receiving 6162 citations. Previous affiliations of Basil Rapoport include United States Department of Veterans Affairs & Austrian Academy of Sciences.
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Journal ArticleDOI
Molecular cloning, sequence and functional expression of the cDNA for the human thyrotropin receptor
Yuji Nagayama,Keith D. Kaufman,Keith D. Kaufman,Pui Seto,Pui Seto,Basil Rapoport,Basil Rapoport +6 more
TL;DR: A human thyroid cDNA library with two synthetic oligonucleotides based on the reported amino acid sequence of the 3rd and 4th transmembrane domains of a putative human TSH receptor and related receptors generated a functional receptor, able to activate adenylate cyclase specifically in response to TSH stimulation.
Journal Article
Lack of promiscuity in autoantigen-specific H and L chain combinations as revealed by human H and L chain "roulette".
TL;DR: Individual H or L chains from a human autoantibody were used to search for other L or H chains that could form antigen-binding fragments, Fab, with the same specificity, raising the possibility that the L chain is critical in defining epitope specificity, even in the presence of completely different D regions and nonidentical VH regions.
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The thyrotropin receptor 25 years after its discovery: new insight after its molecular cloning.
Yuji Nagayama,Basil Rapoport +1 more
TL;DR: Understanding precisely how TSH interacts with and activates its receptor is closer to the goal of understanding precisely how the B cell, and ultimately T cell, epitopes on the TSH receptor that are recognized by the immune system.
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The molecular biology of thyroid peroxidase: cloning, expression and role as autoantigen in autoimmune thyroid disease.
TL;DR: Three of the four major thyroid-specific proteins have been cloned, namely thyroglobulin (TG), TPO (see below), and the TSH receptor (5–8), and molecular cloning of the thyroid iodide transporter may occur soon (9).
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An insertion in the human thyrotropin receptor critical for high affinity hormone binding.
TL;DR: This work has shown that the eight-amino acid tract near the amino terminus of the TSH receptor appears to be an important site of interaction for both TSH and TSI, and deletion or substitution of this region abolished these activities.