The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Different biological properties of the two constituent peptide chains of ricin a toxic protein inhibiting protein synthesis
Abstract
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDifferent biological properties of the two constituent peptide chains of ricin a toxic protein inhibiting protein synthesisSjur Olsnes and Alexander PihlCite this: Biochemistry 1973, 12, 16, 3121–3126Publication Date (Print):July 1, 1973Publication History Published online1 May 2002Published inissue 1 July 1973https://pubs.acs.org/doi/10.1021/bi00740a028https://doi.org/10.1021/bi00740a028research-articleACS PublicationsRequest reuse permissionsArticle Views1035Altmetric-Citations364LEARN 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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Citations
Cites
Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 20,298
The interaction of Ricinus communis agglutinin with normal and tumor cell surfaces
Nicolson, G. L., & Blaustein, J. (1972) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(72)90109-5 · Cited by 514
Isolation and Properties of Abrin: a Toxic Protein Inhibiting Protein Synthesis
Olsnes, S., & Pihl, A. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb02823.x · Cited by 186
Self-citationReconstitution of Diphtheria Toxin from Two Nontoxic Cross-Reacting Mutant Proteins
Uchida, T., Pappenheimer, A. M., & Harper, A. A. (1972) · Science · doi:10.1126/science.175.4024.901 · Cited by 176
Ricin — a potent inhibitor of protein synthesis
Olsnes, S., & Pihl, A. (1972) · FEBS Letters · doi:10.1016/0014-5793(72)80098-x · Cited by 135
Self-citationISHIGURO, T., Funatsu, G., HAVASHI, K., et al. (1964) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a127930 · Cited by 111
Toxic proteins inhibiting protein synthesis
Olsnes, S. (1972) · Die Naturwissenschaften · doi:10.1007/bf00609814 · Cited by 35
Self-citationThe mechanism of the cytotoxicity of phytoagglutinin toward rat ascites tumor cells
Onozaki, K., Tomita, M., Sakurai, Y., et al. (1972) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(72)90675-4 · Cited by 27
Cited by
Structural determinants of Ricinus communis agglutinin and toxin specificity for oligosaccharides
Baenziger, J. U., & Fiete, D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83586-x · Cited by 476
Inhibitors of protein synthesis
Vazquez, D. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80689-7 · Cited by 414
Lambert, J. M., McIntyre, G., Gauthier, M. N., Zullo, D., Rao, V., Steeves, R. M., Goldmacher, V. S., & Blattler, W. A. (1991) · Biochemistry · doi:10.1021/bi00227a011 · Cited by 82
Metadata
- Authors
- Olsnes, S., & Pihl, A.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1973-07-01
- Volume
- 12
- Issue
- 16
- Pages
- 3121-3126
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2089598244
- Cited by
- 466
- References
- 8
- FWCI
- 6.84
- Type
- journal article
- Language
- en
- Open access
- closed
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