Literature DB >> 15302520

The history of ricin, abrin and related toxins.

Sjur Olsnes1.   

Abstract

Ricin, abrin and related plant toxins have played interesting and important roles in the history of clinical medicine and biomedical research. The use of these proteins in medical treatment since ancient times is reviewed. Later the proteins played important roles in the early days of immunological research and some of the fundamental principles of immunology were discovered with toxic proteins of this group. During the last three decades the mechanism of action of the toxins was elucidated. This led to a major effort to target the toxins to malignant cells. Ricin has been used in bioterrorism. Recently, the toxins have played important roles as experimental models to elucidate the intracellular trafficking of endocytosed proteins.

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Year:  2004        PMID: 15302520     DOI: 10.1016/j.toxicon.2004.05.003

Source DB:  PubMed          Journal:  Toxicon        ISSN: 0041-0101            Impact factor:   3.033


  76 in total

1.  Bivalent carbohydrate binding is required for biological activity of Clitocybe nebularis lectin (CNL), the N,N'-diacetyllactosediamine (GalNAcβ1-4GlcNAc, LacdiNAc)-specific lectin from basidiomycete C. nebularis.

Authors:  Jure Pohleven; Miha Renko; Špela Magister; David F Smith; Markus Künzler; Borut Štrukelj; Dušan Turk; Janko Kos; Jerica Sabotič
Journal:  J Biol Chem       Date:  2012-02-01       Impact factor: 5.157

2.  Folding domains within the ricin toxin A subunit as targets of protective antibodies.

Authors:  Joanne M O'Hara; Lori M Neal; Elizabeth A McCarthy; Jane A Kasten-Jolly; Robert N Brey; Nicholas J Mantis
Journal:  Vaccine       Date:  2010-08-18       Impact factor: 3.641

3.  A neutralizing antibody to the a chain of abrin inhibits abrin toxicity both in vitro and in vivo.

Authors:  Kalpana Surendranath; Anjali A Karande
Journal:  Clin Vaccine Immunol       Date:  2008-03-19

4.  Structural insights into the neutralization mechanism of monoclonal antibody 6C2 against ricin.

Authors:  Yuwei Zhu; Jianxin Dai; Tiancheng Zhang; Xu Li; Pengfei Fang; Huajing Wang; Yongliang Jiang; Xiaojie Yu; Tian Xia; Liwen Niu; Yajun Guo; Maikun Teng
Journal:  J Biol Chem       Date:  2013-07-12       Impact factor: 5.157

Review 5.  The relevance of higher plants in lead compound discovery programs.

Authors:  A Douglas Kinghorn; Li Pan; Joshua N Fletcher; Heebyung Chai
Journal:  J Nat Prod       Date:  2011-06-08       Impact factor: 4.050

6.  Truncated abrin A chain expressed in Escherichia coli: a promising vaccine candidate.

Authors:  Tao Zhang; Lin Kang; Shan Gao; Hao Yang; Wenwen Xin; Junhong Wang; Maowen Guo; Jinglin Wang
Journal:  Hum Vaccin Immunother       Date:  2014-11-17       Impact factor: 3.452

7.  Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization.

Authors:  Kimberly J Hassett; Megan C Cousins; Lilia A Rabia; Chrystal M Chadwick; Joanne M O'Hara; Pradyot Nandi; Robert N Brey; Nicholas J Mantis; John F Carpenter; Theodore W Randolph
Journal:  Eur J Pharm Biopharm       Date:  2013-04-10       Impact factor: 5.571

Review 8.  Targeting ricin to the ribosome.

Authors:  Kerrie L May; Qing Yan; Nilgun E Tumer
Journal:  Toxicon       Date:  2013-02-20       Impact factor: 3.033

9.  Crystallization and preliminary X-ray diffraction data analysis of stenodactylin, a highly toxic type 2 ribosome-inactivating protein from Adenia stenodactyla.

Authors:  Giovanna Tosi; Simona Fermani; Giuseppe Falini; Letizia Polito; Massimo Bortolotti; Andrea Bolognesi
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-12-25

10.  The P1/P2 proteins of the human ribosomal stalk are required for ribosome binding and depurination by ricin in human cells.

Authors:  Kerrie L May; Xiao-Ping Li; Francisco Martínez-Azorín; Juan P G Ballesta; Przemysław Grela; Marek Tchórzewski; Nilgun E Tumer
Journal:  FEBS J       Date:  2012-09-11       Impact factor: 5.542

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