{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2024,8,7]],"date-time":"2024-08-07T17:54:14Z","timestamp":1723053254386},"reference-count":55,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2015,3,12]],"date-time":"2015-03-12T00:00:00Z","timestamp":1426118400000},"content-version":"vor","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.0120692","type":"journal-article","created":{"date-parts":[[2015,3,12]],"date-time":"2015-03-12T17:48:36Z","timestamp":1426182516000},"page":"e0120692","update-policy":"http:\/\/dx.doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":9,"title":["On the Role of Protein Disulfide Isomerase in the Retrograde Cell Transport of Secreted Phospholipases A2"],"prefix":"10.1371","volume":"10","author":[{"given":"Jernej","family":"Ober\u010dkal","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lidija","family":"Kova\u010di\u010d","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jernej","family":"\u0160ribar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Adrijana","family":"Leonardi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Klemen","family":"Dolinar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anja","family":"Pucer Jane\u017e","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Igor","family":"Kri\u017eaj","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2015,3,12]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1021\/cr990139w","article-title":"Interfacial enzymology: the secreted phospholipase A<sub>2<\/sub> paradigm","volume":"101","author":"OG Berg","year":"2001","journal-title":"Chem Rev"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.plipres.2010.12.001","article-title":"Recent progress in phospholipase A<sub>2<\/sub> research: from cells to animals to humans","volume":"50","author":"M Murakami","year":"2011","journal-title":"Prog Lipid Res"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/j.bbalip.2006.04.002","article-title":"Analysis of expression of secreted phospholipases A<sub>2<\/sub> in mouse tissues at protein and mRNA levels","volume":"1761","author":"LI Eerola","year":"2006","journal-title":"Biochim Biophys Acta"},{"key":"ref4","first-page":"678","article-title":"Secreted phospholipases A<sub>2<\/sub>\u2014not just enzymes","volume":"58","author":"J \u0160ribar","year":"2011","journal-title":"Acta Chim Slov"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/j.biochi.2010.03.015","article-title":"Emerging roles of secreted phospholipase A<sub>2<\/sub> enzymes: lessons from transgenic and knockout mice","volume":"92","author":"M Murakami","year":"2010","journal-title":"Biochimie"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.biochi.2012.09.007","article-title":"Emerging roles of secreted phospholipase A<sub>2<\/sub> enzymes: an update","volume":"95","author":"M Murakami","year":"2013","journal-title":"Biochimie"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.biochi.2014.09.023","article-title":"Secreted phospholipases A<sub>2<\/sub> in cancer: diverse mechanisms of action","volume":"107","author":"V Brglez","year":"2014","journal-title":"Biochimie"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"1201","DOI":"10.2174\/0929866521666140819122624","article-title":"Roles of secreted phospholipases A<sub>2<\/sub> in the mammalian immune system","volume":"21","author":"I Kri\u017eaj","year":"2014","journal-title":"Protein Pept Lett"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"985","DOI":"10.1242\/jcs.111.7.985","article-title":"Nuclear location of PLA<sub>2<\/sub>-I in proliferative cells","volume":"111","author":"JM Fayard","year":"1998","journal-title":"J Cell Sci"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"37860","DOI":"10.1074\/jbc.M303855200","article-title":"Rat brain cortex mitochondria release group II secretory phospholipase A<sub>2<\/sub> under reduced membrane potential","volume":"279","author":"L Macchioni","year":"2004","journal-title":"J Biol Chem"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1345","DOI":"10.1016\/j.bbalip.2007.08.007","article-title":"The presence of a secretory phospholipase A<sub>2<\/sub> in the nuclei of neuronal and glial cells of rat brain cortex","volume":"1771","author":"V Nardicchi","year":"2007","journal-title":"Biochim Biophys Acta"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"48059","DOI":"10.1074\/jbc.M305904200","article-title":"Localization of group V phospholipase A<sub>2<\/sub> in caveolin-enriched granules in activated P388D1 macrophage-like cells","volume":"278","author":"MA Balboa","year":"2003","journal-title":"J Biol Chem"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.toxicon.2011.06.009","article-title":"Ammodytoxin: a window into understanding presynaptic toxicity of secreted phospholipases A<sub>2<\/sub> and more","volume":"58","author":"I Kri\u017eaj","year":"2011","journal-title":"Toxicon"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/j.bbamcr.2008.01.011","article-title":"A presynaptically toxic secreted phospholipase A<sub>2<\/sub> is internalized into motoneuron-like cells where it is rapidly translocated into the cytosol","volume":"1783","author":"Z Jenko Pra\u017enikar","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1016\/j.expneurol.2009.07.017","article-title":"Ultrastructural evidence for the uptake of a neurotoxic snake venom phospholipase A<sub>2<\/sub> into mammalian motor nerve terminals","volume":"219","author":"U Logonder","year":"2009","journal-title":"Exp Neurol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/j.bbrc.2005.02.036","article-title":"Protein disulphide isomerase binds ammodytoxin strongly: possible implications for toxin trafficking","volume":"329","author":"J \u0160ribar","year":"2005","journal-title":"Biochem Biophys Res Commun"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.bbamcr.2007.11.010","article-title":"The human PDI family: versatility packed into a single fold","volume":"1783","author":"C Appenzeller-Herzog","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1038\/nrm780","article-title":"Retro-translocation of proteins from the endoplasmic reticulum into the cytosol","volume":"3","author":"B Tsai","year":"2002","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1016\/j.tibs.2003.10.002","article-title":"The intracellular voyage of cholera toxin: going retro","volume":"28","author":"WI Lencer","year":"2003","journal-title":"Trends Biochem Sci"},{"key":"ref20","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":"ref21","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":"ref22","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1007\/s00418-013-1111-z","article-title":"Retrograde transport of protein toxins through the Golgi apparatus","volume":"140","author":"K Sandvig","year":"2013","journal-title":"Histochem Cell Biol"},{"key":"ref23","first-page":"443","article-title":"Basic proteins of <italic>Vipera ammodytes<\/italic> venom\u2014studies of structure and function","volume":"82","author":"F Guben\u0161ek","year":"1980","journal-title":"Period Biol"},{"key":"ref24","first-page":"229","article-title":"Assaying phospholipase A<sub>2<\/sub> activity","volume":"284","author":"CC Leslie","year":"2004","journal-title":"Methods Mol Biol"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"48535","DOI":"10.1074\/jbc.M205855200","article-title":"Interfacial kinetic and binding properties of the complete set of human and mouse groups I, II, V, X, and XII secreted phospholipases A<sub>2<\/sub>","volume":"277","author":"AG Singer","year":"2002","journal-title":"J Biol Chem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.cell.2005.10.044","article-title":"The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites","volume":"124","author":"G Tian","year":"2006","journal-title":"Cell"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"2424","DOI":"10.1073\/pnas.73.7.2424","article-title":"Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor","volume":"73","author":"LA Greene","year":"1976","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/j.bioorg.2006.12.002","article-title":"A new photoprobe for studying biological activities of secreted phospholipases A<sub>2<\/sub>","volume":"35","author":"L Kova\u010di\u010d","year":"2007","journal-title":"Bioorg Chem"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1093\/protein\/gzq019","article-title":"Structural basis of the significant calmodulin-induced increase in the enzymatic activity of secreted phospholipases A<sub>2<\/sub>","volume":"23","author":"L Kova\u010di\u010d","year":"2010","journal-title":"Protein Eng Des Sel"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/0003-2697(84)90782-6","article-title":"A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids","volume":"138","author":"D Wessel","year":"1984","journal-title":"Anal Biochem"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1038\/nmeth.2089","article-title":"NIH Image to ImageJ: 25 years of image analysis","volume":"9","author":"CA Schneider","year":"2012","journal-title":"Nat Methods"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1111\/j.1365-2818.2006.01706.x","article-title":"A guided tour into subcellular colocalization analysis in light microscopy","volume":"224","author":"S Bolte","year":"2006","journal-title":"J Microsc"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.jsb.2009.10.010","article-title":"Comparative structural studies of two natural isoforms of ammodytoxin, phospholipases A<sub>2<\/sub> from <italic>Vipera ammodytes ammodytes<\/italic> which differ in neurotoxicity and anticoagulant activity","volume":"169","author":"FA Saul","year":"2010","journal-title":"J Struct Biol"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1002\/prot.20569","article-title":"Docking essential dynamics eigenstructures","volume":"60","author":"D Mustard","year":"2005","journal-title":"Proteins"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"5933","DOI":"10.1021\/jp027815+","article-title":"Polarizable atomic multipole water model for molecular mechanics simulation","volume":"107","author":"P Ren","year":"2003","journal-title":"J Phys Chem B"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1002\/(SICI)1096-987X(20000130)21:2<86::AID-JCC2>3.0.CO;2-G","article-title":"All-atom empirical force field for nucleic acids: I. Parameter optimization based on small molecule and condensed phase macromolecular target data","volume":"21","author":"N Foloppe","year":"2000","journal-title":"J Comput Chem"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"1731","DOI":"10.1021\/ja026939x","article-title":"HADDOCK: A protein-protein docking approach based on biochemical or biophysical information","volume":"125","author":"C Dominguez","year":"2003","journal-title":"J Am Chem Soc"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1038\/nprot.2010.32","article-title":"The HADDOCK web server for data-driven biomolecular docking","volume":"5","author":"SJ De Vries","year":"2010","journal-title":"Nat Protoc"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"1784","DOI":"10.1074\/mcp.M000051-MCP201","article-title":"Building macromolecular assemblies by information-driven docking: introducing the HADDOCK multibody docking server","volume":"9","author":"E Karaca","year":"2010","journal-title":"Mol Cell Proteomics"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0003-2697(89)90022-5","article-title":"A sensitive and continuous fluorometric assay for phospholipase A<sub>2<\/sub> using pyrene-labeled phospholipids in the presence of serum albumin","volume":"177","author":"F Radvanyi","year":"1989","journal-title":"Anal Biochem"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1042\/BJ20050417","article-title":"Ammodytoxin, a secretory phospholipase A<sub>2<\/sub>, inhibits G<sub>2<\/sub> cell cycle arrest in yeast <italic>Saccharomyces cerevisiae<\/italic>","volume":"391","author":"U Petrovi\u010d","year":"2005","journal-title":"Biochem J"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"981","DOI":"10.1016\/j.bbrc.2004.09.144","article-title":"Ammodytoxin, a neurotoxic secreted phospholipase A<sub>2<\/sub>, can act in the cytosol of the nerve cell","volume":"324","author":"U Petrovi\u010d","year":"2004","journal-title":"Biochem Biophys Res Commun"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1046\/j.0953-816x.2001.01699.x","article-title":"Beta-bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization","volume":"14","author":"M Herkert","year":"2001","journal-title":"Eur J Neurosci"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"2339","DOI":"10.1046\/j.1471-4159.1995.64052339.x","article-title":"Novel reticular calcium binding protein is purified on taipoxin columns","volume":"64","author":"D Dodds","year":"1995","journal-title":"J Neurochem"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1006\/bbrc.1997.7416","article-title":"Purification and partial amino acid sequence of a novel protein of the reticulocalbin family","volume":"239","author":"MJ Hseu","year":"1997","journal-title":"Biochem Biophys Res Commun"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1006\/jmbi.1997.1504","article-title":"The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency","volume":"276","author":"NJ Darby","year":"1998","journal-title":"J Mol Biol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1093\/emboj\/18.1.65","article-title":"The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide","volume":"18","author":"P Koivunen","year":"1999","journal-title":"EMBO J"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"3924","DOI":"10.1111\/j.1742-4658.2010.07793.x","article-title":"A structural overview of the PDI family of proteins","volume":"277","author":"G Kozlov","year":"2010","journal-title":"FEBS J"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"12535","DOI":"10.1021\/bi051024r","article-title":"Ammodytoxins, potent presynaptic neurotoxins, are also highly efficient phospholipase A<sub>2<\/sub> enzymes","volume":"44","author":"T Petan","year":"2005","journal-title":"Biochemistry"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"12493","DOI":"10.1074\/jbc.C100048200","article-title":"A high affinity acceptor for phospholipase A<sub>2<\/sub> with neurotoxic activity is a calmodulin","volume":"276","author":"J \u0160ribar","year":"2001","journal-title":"J Biol Chem"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"13045","DOI":"10.1074\/jbc.M808352200","article-title":"Generating an unfoldase from thioredoxin-like domains","volume":"284","author":"ML Forster","year":"2009","journal-title":"J Biol Chem"},{"key":"ref52","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":"ref53","doi-asserted-by":"crossref","first-page":"22090","DOI":"10.1074\/jbc.M111.237966","article-title":"Protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit","volume":"286","author":"M Taylor","year":"2011","journal-title":"J Biol Chem"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"36479","DOI":"10.1074\/jbc.M205399200","article-title":"Group V phospholipase A<sub>2<\/sub> induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A<sub>2<\/sub>","volume":"277","author":"YJ Kim","year":"2002","journal-title":"J Biol Chem"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"5034","DOI":"10.1074\/jbc.M708844200","article-title":"A catalytically independent physiological function for human acute phase protein group IIA phospholipase A<sub>2<\/sub>: cellular uptake facilitates cell debris removal","volume":"283","author":"CN Birts","year":"2008","journal-title":"J Biol Chem"}],"container-title":["PLOS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0120692","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,5,2]],"date-time":"2022-05-02T07:52:24Z","timestamp":1651477944000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0120692"}},"subtitle":[],"editor":[{"given":"Bruno","family":"Lomonte","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2015,3,12]]},"references-count":55,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2015,3,12]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0120692","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,3,12]]}}}