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Alonzo H. Ross

Researcher at Worcester Foundation for Biomedical Research

Publications -  59
Citations -  3773

Alonzo H. Ross is an academic researcher from Worcester Foundation for Biomedical Research. The author has contributed to research in topics: Nerve growth factor & Receptor. The author has an hindex of 29, co-authored 59 publications receiving 3741 citations. Previous affiliations of Alonzo H. Ross include Aichi Medical University & Wistar Institute.

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Gene transfer and molecular cloning of the human NGF receptor

TL;DR: Affinity cross-linking, metabolic labeling and immunoprecipitation, and equilibrium binding with 125I-labeled NGF revealed that this NGF receptor had the same size and binding characteristics as the receptor from human melanoma cells and rat PC12 cells.
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Characterization of nerve growth factor receptor in neural crest tumors using monoclonal antibodies

TL;DR: The NGF receptor was visualized by immunoperoxidase staining in tissue sections of human nevi, melanomas, neurofibromas, a pheochromocytoma, and peripheral nerves as mentioned in this paper.
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Molecular Cloning and Characterization of an Antigen Associated with Early Stages of Melanoma Tumor Progression

TL;DR: Southern blot analysis revealed no amplification or rearrangement of the ME491 gene in the human melanoma cell lines tested, including both high and low expressors of this antigen.
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Binding of an antagonistic monoclonal antibody to an intact and fragmented EGF-receptor polypeptide☆

TL;DR: The results of antibody binding studies indicate that the epitope is closely linked to the EGF binding active site, and is common to both high- and low-affinity EGF-receptors.
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Anti-idiotype immunization of cancer patients: modulation of the immune response.

TL;DR: Thirty patients with advanced colorectal carcinoma were treated with alum-precipitated polyclonal goat anti-idiotypic antibodies to monoclonal anti-CRC antibody CO17-1A in doses between 0.5 and 4 mg per injection, and all patients developed anti-anti-identical antibodies (Ab3) with binding specificities on the surfaces of cultured tumor cells similar to the specificity of Ab1.