{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,6,17]],"date-time":"2024-06-17T17:24:34Z","timestamp":1718645074100},"reference-count":57,"publisher":"Public Library of Science (PLoS)","issue":"8","license":[{"start":{"date-parts":[[2011,8,22]],"date-time":"2011-08-22T00:00:00Z","timestamp":1313971200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0023692","type":"journal-article","created":{"date-parts":[[2011,8,24]],"date-time":"2011-08-24T17:20:09Z","timestamp":1314206409000},"page":"e23692","update-policy":"http:\/\/dx.doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":7,"title":["Modulation of Toxin Stability by 4-Phenylbutyric Acid and Negatively Charged Phospholipids"],"prefix":"10.1371","volume":"6","author":[{"given":"Supriyo","family":"Ray","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael","family":"Taylor","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mansfield","family":"Burlingame","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Suren A.","family":"Tatulian","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ken","family":"Teter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2011,8,22]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1146\/annurev.cellbio.18.011502.142107","article-title":"Membrane traffic exploited by protein toxins.","volume":"18","author":"K Sandvig","year":"2002","journal-title":"Annu Rev Cell Dev Biol"},{"key":"ref2","first-page":"149","article-title":"Entry of protein toxins into mammalian cells by crossing the endoplasmic reticulum membrane: co-opting basic mechanisms of endoplasmic reticulum-associated degradation.","volume":"300","author":"JM Lord","year":"2005","journal-title":"Curr Top Microbiol Immunol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1042\/BJ20040742","article-title":"Protein disulphide-isomerase reduces ricin to its A and B chains in the endoplasmic reticulum.","volume":"383","author":"RA Spooner","year":"2004","journal-title":"Biochem J"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1006\/jmbi.1996.0277","article-title":"Crystal structure of the pertussis toxin-ATP complex: a molecular sensor.","volume":"258","author":"B Hazes","year":"1996","journal-title":"J Mol Biol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/S0014-5793(96)01447-0","article-title":"Reduction of protein disulfide bonds in an oxidizing environment. The disulfide bridge of cholera toxin A-subunit is reduced in the endoplasmic reticulum.","volume":"401","author":"I Majoul","year":"1997","journal-title":"FEBS Lett"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"4591","DOI":"10.1016\/S0021-9258(19)67333-3","article-title":"Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line.","volume":"272","author":"PA Orlandi","year":"1997","journal-title":"J Biol Chem"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1016\/S0092-8674(01)00289-6","article-title":"Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin.","volume":"104","author":"B Tsai","year":"2001","journal-title":"Cell"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1042\/BJ20061890","article-title":"The protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation).","volume":"404","author":"JL Brodsky","year":"2007","journal-title":"Biochem J"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"3405","DOI":"10.1021\/bi011580v","article-title":"The low lysine content of ricin A chain reduces the risk of proteolytic degradation after translocation from the endoplasmic reticulum to the cytosol.","volume":"41","author":"ED Deeks","year":"2002","journal-title":"Biochemistry"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"11051","DOI":"10.1021\/bi971383p","article-title":"Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells.","volume":"36","author":"B Hazes","year":"1997","journal-title":"Biochemistry"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1222","DOI":"10.1093\/embo-reports\/kvf239","article-title":"Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation.","volume":"3","author":"C Rodighiero","year":"2002","journal-title":"EMBO Rep"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"2946","DOI":"10.1128\/IAI.02011-06","article-title":"Evading the proteasome: absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation.","volume":"75","author":"ZE Worthington","year":"2007","journal-title":"Infect Immun"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"13734","DOI":"10.1021\/bi061175+","article-title":"The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome.","volume":"45","author":"AH Pande","year":"2006","journal-title":"Biochemistry"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1016\/j.jmb.2007.10.025","article-title":"Conformational instability of the cholera toxin A1 polypeptide.","volume":"374","author":"AH Pande","year":"2007","journal-title":"J Mol Biol"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"748","DOI":"10.1016\/j.jmb.2007.12.075","article-title":"Order-disorder-order transitions mediate the activation of cholera toxin.","volume":"377","author":"RS Ampapathi","year":"2008","journal-title":"J Mol Biol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"9263","DOI":"10.1074\/jbc.275.13.9263","article-title":"Ribosome-mediated folding of partially unfolded ricin A-chain.","volume":"275","author":"RH Argent","year":"2000","journal-title":"J Biol Chem"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1093\/protein\/gzh043","article-title":"Finding a new vaccine in the ricin protein fold.","volume":"17","author":"MA Olson","year":"2004","journal-title":"Protein Eng Des Sel"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1002\/jps.20675","article-title":"A rapid, three-step process for the preformulation of a recombinant ricin toxin A-chain vaccine.","volume":"96","author":"LJ Peek","year":"2007","journal-title":"J Pharm Sci"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"2836","DOI":"10.1021\/bi012012i","article-title":"Binding of ricin A-chain to negatively charged phospholipid vesicles leads to protein structural changes and destabilizes the lipid bilayer.","volume":"41","author":"PJ Day","year":"2002","journal-title":"Biochemistry"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"10232","DOI":"10.1074\/jbc.M808387200","article-title":"Ricin A chain insertion into endoplasmic reticulum membranes is triggered by a temperature increase to 37 {degrees}C.","volume":"284","author":"PU Mayerhofer","year":"2009","journal-title":"J Biol Chem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1111\/j.1432-1033.1995.tb20831.x","article-title":"Point mutations in the hydrophobic C-terminal region of ricin A chain indicate that Pro250 plays a key role in membrane translocation.","volume":"232","author":"JC Simpson","year":"1995","journal-title":"Eur J Biochem"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"23310","DOI":"10.1074\/jbc.M414193200","article-title":"A role for the protease-sensitive loop region of Shiga-like toxin 1 in the retrotranslocation of its A1 domain from the endoplasmic reticulum lumen.","volume":"280","author":"P LaPointe","year":"2005","journal-title":"J Biol Chem"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"15865","DOI":"10.1021\/bi970944+","article-title":"Orientation in lipid bilayers of a synthetic peptide representing the C-terminus of the A1 domain of shiga toxin. A polarized ATR-FTIR study.","volume":"36","author":"A Menikh","year":"1997","journal-title":"Biochemistry"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"9325","DOI":"10.1021\/bi960177z","article-title":"Insertion and orientation of a synthetic peptide representing the C-terminus of the A1 domain of Shiga toxin into phospholipid membranes.","volume":"35","author":"MT Saleh","year":"1996","journal-title":"Biochemistry"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"5252","DOI":"10.1128\/IAI.66.11.5252-5259.1998","article-title":"Disruption of an internal membrane-spanning region in Shiga toxin 1 reduces cytotoxicity.","volume":"66","author":"ML Suhan","year":"1998","journal-title":"Infect Immun"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"12010","DOI":"10.1016\/S0021-9258(19)50301-5","article-title":"Brefeldin A blocks the response of cultured cells to cholera toxin. Implications for intracellular trafficking in toxin action.","volume":"268","author":"PA Orlandi","year":"1993","journal-title":"J Biol Chem"},{"key":"ref27","first-page":"G548","article-title":"Signal transduction by cholera toxin: processing in vesicular compartments does not require acidification.","volume":"269","author":"WI Lencer","year":"1995","journal-title":"Am J Physiol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/0014-4827(90)90137-Y","article-title":"Increased cytotoxicity of ricin in a putative Golgi-defective mutant of Chinese hamster ovary cell.","volume":"190","author":"T Yoshida","year":"1990","journal-title":"Exp Cell Res"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"787","DOI":"10.3390\/toxins3070787","article-title":"Ricin trafficking in plant and mammalian cells.","volume":"3","author":"JM Lord","year":"2011","journal-title":"Toxins"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"310","DOI":"10.3390\/toxins2030310","article-title":"Cholera toxin: an intracellular journey into the cytosol by way of the endoplasmic reticulum.","volume":"2","author":"NLB Wernick","year":"2010","journal-title":"Toxins"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1016\/S0076-6879(00)27301-1","article-title":"Studying organelle physiology with fusion protein-targeted avidin and fluorescent biotin conjugates.","volume":"327","author":"MM Wu","year":"2000","journal-title":"Methods Enzymol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"2997","DOI":"10.1073\/pnas.95.6.2997","article-title":"Noninvasive measurement of the pH of the endoplasmic reticulum at rest and during calcium release.","volume":"95","author":"JH Kim","year":"1998","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1021\/bi00406a035","article-title":"Thermal stability and intersubunit interactions of cholera toxin in solution and in association with its cell-surface receptor ganglioside GM1.","volume":"27","author":"B Goins","year":"1988","journal-title":"Biochemistry"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"7300","DOI":"10.1021\/jf061199n","article-title":"Thermal Inactivation of Ricin Using Infant Formula as a Food Matrix.","volume":"54","author":"LS Jackson","year":"2006","journal-title":"J Agric Food Chem"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1016\/j.jmb.2009.09.013","article-title":"Stabilization of the tertiary structure of the cholera toxin A1 subunit inhibits toxin dislocation and cellular intoxication.","volume":"393","author":"S Massey","year":"2009","journal-title":"J Mol Biol"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"8839","DOI":"10.1021\/bi101201c","article-title":"Contribution of subdomain structure to the thermal stability of the cholera toxin A1 subunit.","volume":"49","author":"T Banerjee","year":"2010","journal-title":"Biochemistry"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1083\/jcb.122.6.1231","article-title":"The End2 mutation in CHO cells slows the exit of transferrin receptors from the recycling compartment but bulk membrane recycling is unaffected.","volume":"122","author":"JF Presley","year":"1993","journal-title":"J Cell Biol"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1001\/jama.294.18.2342","article-title":"Ricin poisoning: a comprehensive review.","volume":"294","author":"J Audi","year":"2005","journal-title":"JAMA"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/0014-5793(87)80759-7","article-title":"Expression of ricin A chain in <italic>Escherichia coli<\/italic>.","volume":"216","author":"M O'Hare","year":"1987","journal-title":"FEBS Lett"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"4837","DOI":"10.1016\/S0021-9258(18)68862-3","article-title":"Expression of soluble and fully functional ricin A chain in <italic>Escherichia coli<\/italic> is temperature-sensitive.","volume":"263","author":"M Piatak","year":"1988","journal-title":"J Biol Chem"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1002\/jps.10296","article-title":"Thermal stability of vaccines.","volume":"92","author":"DT Brandau","year":"2003","journal-title":"J Pharm Sci"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1002\/prot.22933","article-title":"Introduction of a disulfide bond leads to stabilization and crystallization of a ricin immunogen.","volume":"79","author":"JR Compton","year":"2010","journal-title":"Proteins"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"4775","DOI":"10.1016\/j.vaccine.2005.04.037","article-title":"Preclinical toxicity and efficacy testing of RiVax, a recombinant protein vaccine against ricin.","volume":"23","author":"JE Smallshaw","year":"2005","journal-title":"Vaccine"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"2268","DOI":"10.1073\/pnas.0510893103","article-title":"A pilot clinical trial of a recombinant ricin vaccine in normal humans.","volume":"103","author":"ES Vitetta","year":"2006","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.1016\/j.vaccine.2009.12.081","article-title":"A lyophilized formulation of RiVax, a recombinant ricin subunit vaccine, retains immunogenicity.","volume":"28","author":"JE Smallshaw","year":"2010","journal-title":"Vaccine"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1056\/NEJM199609193351204","article-title":"Long-term treatment of girls with ornithine transcarbamylase deficiency.","volume":"335","author":"NE Maestri","year":"1996","journal-title":"N Engl J Med"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"e18825","DOI":"10.1371\/journal.pone.0018825","article-title":"A therapeutic chemical chaperone inhibits cholera intoxication and unfolding\/translocation of the cholera toxin A1 subunit.","volume":"6","author":"M Taylor","year":"2011","journal-title":"PLoS ONE"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/S0958-1669(97)80157-7","article-title":"Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors.","volume":"8","author":"DG Myszka","year":"1997","journal-title":"Curr Opin Biotechnol"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/978-1-61779-102-4_5","article-title":"A Cell-Based Fluorescent Assay to Detect the Activity of Shiga Toxin and Other Toxins that Inhibit Protein Synthesis.","volume":"739","author":"S Massey","year":"2011","journal-title":"Methods Mol Biol"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1128\/AEM.02230-08","article-title":"Novel cell-based method to detect Shiga toxin 2 from <italic>Escherichia coli<\/italic> O157:H7 and inhibitors of toxin activity.","volume":"75","author":"B Quinones","year":"2009","journal-title":"Appl Environ Microbiol"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/0301-4622(88)80036-X","article-title":"Circular dichroism of isolated ricin A- and B-chains.","volume":"31","author":"EJ Wawrzynczak","year":"1988","journal-title":"Biophys Chem"},{"key":"ref52","first-page":"601","article-title":"Circular dichroism of peptides and proteins., in <italic>Circular Dichroism: Principles and Applications<\/italic>","author":"N Sreerama","year":"2000"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1002\/prot.340100308","article-title":"Crystallographic refinement of ricin to 2.5 A.","volume":"10","author":"E Rutenber","year":"1991","journal-title":"Proteins"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1042\/bj2190935","article-title":"Dimethyl sulphoxide protects cells against polypeptide toxins and poliovirus.","volume":"219","author":"K Sandvig","year":"1984","journal-title":"Biochem J"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1111\/j.1462-5822.2005.00520.x","article-title":"Cellular internalization of cytolethal distending toxin: a new end to a known pathway.","volume":"7","author":"L Guerra","year":"2005","journal-title":"Cell Microbiol"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.bbamcr.2008.11.017","article-title":"A novel mode of translocation for cytolethal distending toxin.","volume":"1793","author":"L Guerra","year":"2009","journal-title":"Biochim Biophys Acta"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1203\/00006450-200212000-00004","article-title":"Chemical chaperones: a pharmacological strategy for disorders of protein folding and trafficking.","volume":"52","author":"DH Perlmutter","year":"2002","journal-title":"Pediatr Res"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0023692","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,12,1]],"date-time":"2021-12-01T16:46:27Z","timestamp":1638377187000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0023692"}},"subtitle":[],"editor":[{"given":"Michel R.","family":"Popoff","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2011,8,22]]},"references-count":57,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2011,8,22]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0023692","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,8,22]]}}}