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Edwin S. Lennox

MRC Laboratory of Molecular Biology

Publishes on Monoclonal and Polyclonal Antibodies Research, Glycosylation and Glycoproteins Research, Protein purification and stability. 35 papers and 1.2k citations.

35Publications
1.2kTotal Citations

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Top publicationsby citations

Distribution of Saccharide Residues on Membrane Fragments from a Myeloma-Cell Homogenate: Its Implications for Membrane Biogenesis
Hiroshi Hirano, Brenda Parkhouse, Garth L. Nicolson et al.|Proceedings of the National Academy of Sciences|1972
Cited by 182Open Access

Ferritin conjugates of two plant agglutinins, concanavalin A and ricin, have been used as specific electron microscopic stains for covalently-bound saccharide residues on membrane fragments from a myeloma-cell homogenate. The results indicate that different saccharide residues are uniformly localized to a single surface of each membrane fragment. In particular, the ferritin-concanavalin A conjugate binds exclusively to the cisternal side of membrane fragments of the rough endoplasmic reticulum. If it is postulated that the biogenesis of eukaryotic plasma membranes involves an assembly-line process from precursor intracellular membranes, these observed asymmetric distributions of saccharides on cell membranes can be explained.

Intracellular transport and secretion of an immunoglobulin light chain
Cited by 84

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIntracellular transport and secretion of an immunoglobulin light chainPaul M. Knopf, Yong Sung Choi, and Edwin S. LennoxCite this: Biochemistry 1971, 10, 4, 668–679Publication Date (Print):February 16, 1971Publication History Published online1 May 2002Published inissue 16 February 1971https://pubs.acs.org/doi/10.1021/bi00780a019https://doi.org/10.1021/bi00780a019research-articleACS PublicationsRequest reuse permissionsArticle Views50Altmetric-Citations57LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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Giuseppe Attardi, Melvin Cohn, Kengo Horibata et al.|Bacteriological Reviews|1959
Cited by 76Open Access

The title of this symposium implies a similarity which is not obvious between the cellular responses to virus infection and to antigenic stimulation. In fact, no analogy between these two types of cellular response is apparent either from a consideration of the natures of the stimuli, a specific nucleotide sequence on the one hand and almost any foreign chemical configuration on the other, or from an examination of the products of the response, identical units in the case of the virus and complementary antibody units in the case of the antigen.

Photo-Affinity Labeling of Specific Acetylcholine-Binding Sites on Membranes
Hansruedi Kiefer, Jon Lindstrom, Edwin S. Lennox et al.|Proceedings of the National Academy of Sciences|1970
Cited by 71Open Access

Acetylcholinesterase of intact red blood cell membranes and the acetylcholine receptor at the neuromuscular junction of whole-frog sartorius muscle have been irreversibly inactivated by photo-affinity labeling with two quaternary ammonium aryl azides. The inactivation requires that the azides, at the time of their photolytic conversion to highly reactive nitrenes, are reversibly bound to the specific acetylcholine-binding sites.