{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,3]],"date-time":"2025-11-03T09:01:24Z","timestamp":1762160484527},"reference-count":40,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2006,4,1]],"date-time":"2006-04-01T00:00:00Z","timestamp":1143849600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2006,4]]},"DOI":"10.1016\/j.bbrc.2006.02.055","type":"journal-article","created":{"date-parts":[[2006,2,21]],"date-time":"2006-02-21T12:14:56Z","timestamp":1140524096000},"page":"1014-1021","source":"Crossref","is-referenced-by-count":10,"title":["Cloning and partial characterization of Entamoeba histolytica PTPases"],"prefix":"10.1016","volume":"342","author":[{"given":"Sara Elisa","family":"Herrera-Rodr\u00edguez","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lidia","family":"Bayl\u00f3n-Pacheco","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patricia","family":"Talam\u00e1s-Rohana","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 Luis","family":"Rosales-Encina","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2006.02.055_bib1","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1093\/clinids\/8.2.228","article-title":"Problems in recognition and diagnosis of amebiasis: estimation of global magnitude and mortality","volume":"8","author":"Walsh","year":"1986","journal-title":"Rev. Infect. Dis."},{"key":"10.1016\/j.bbrc.2006.02.055_bib2","series-title":"Amebiasis: Human Infection by Entamoeba histolytica","first-page":"93","article-title":"Prevalence of Entamoeba histolytica infection","author":"Walsh","year":"1988"},{"key":"10.1016\/j.bbrc.2006.02.055_bib3","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/S0140-6736(03)12830-9","article-title":"Amoebiasis","volume":"361","author":"Stanley","year":"2003","journal-title":"The Lancet"},{"key":"10.1016\/j.bbrc.2006.02.055_bib4","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1080\/00034983.1989.11812341","article-title":"Evidence for selection of virulent sub-populations of Entamoeba histolytica by cholesterol","volume":"83","author":"Katiyar","year":"1989","journal-title":"Ann. Trop. Med. Parasitol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib5","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1111\/j.1550-7408.1989.tb02716.x","article-title":"Secretion of acid phosphatase by axenic Entamoeba histolytica NIH-200 and properties of the extracellular enzyme","volume":"36","author":"Agrawal","year":"1989","journal-title":"J. Protozool."},{"key":"10.1016\/j.bbrc.2006.02.055_bib6","first-page":"182","article-title":"Membrane acid phosphatase (MAP) from Entamoeba histolytica","volume":"28","author":"Anaya-Ruiz","year":"1997","journal-title":"Arch. Med. Res."},{"key":"10.1016\/j.bbrc.2006.02.055_bib7","first-page":"184","article-title":"Secreted Entamoeba histolytica acid phosphatase (SAP)","volume":"28","author":"Aguirre-Garc\u00eda","year":"1997","journal-title":"Arch. Med. Res."},{"key":"10.1016\/j.bbrc.2006.02.055_bib8","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1016\/S0020-7519(00)00032-1","article-title":"Purification and properties of an acid phosphatase from Entamoeba histolytica HM-1:IMSS","volume":"30","author":"Aguirre-Garc\u00eda","year":"2000","journal-title":"Int. J. Parasitol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib9","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1017\/S0031182002002767","article-title":"Membrane-bound acid phosphatase (MAP) from Entamoeba histolytica has phosphotyrosine phosphatase activity and disrupts the actin cytoskeleton of host cells","volume":"126","author":"Aguirre-Garc\u00eda","year":"2003","journal-title":"Parasitology"},{"key":"10.1016\/j.bbrc.2006.02.055_bib10","doi-asserted-by":"crossref","first-page":"663","DOI":"10.1016\/S0020-7519(03)00029-8","article-title":"An ecto-protein tyrosine phosphatase of Entamoeba histolytica induces cellular detachment by disruption of actin filaments in HeLa cells","volume":"33","author":"Anaya-Ruiz","year":"2003","journal-title":"Int. J. Parasitol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib11","first-page":"63","article-title":"Great expectations: protein tyrosine phosphatases in cell regulation","volume":"1114","author":"Brautigan","year":"1992","journal-title":"Biochim. Biophys. Acta."},{"key":"10.1016\/j.bbrc.2006.02.055_bib12","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1146\/annurev.pharmtox.42.083001.144616","article-title":"Protein tyrosine phosphatases: structure and function, substrate specificity, and inhibitor development","volume":"42","author":"Zhang","year":"2002","journal-title":"Ann. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib13","doi-asserted-by":"crossref","first-page":"17026","DOI":"10.1016\/S0021-9258(19)47335-3","article-title":"Evidence for protein\u2013tyrosine phosphatase catalysis proceeding via a cysteine-phosphate intermediate","volume":"266","author":"Guan","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2006.02.055_bib14","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1126\/science.1650499","article-title":"Protein tyrosine phosphatases: a diverse family of intracellular and transmembrane enzymes","volume":"253","author":"Fischer","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.bbrc.2006.02.055_bib15","doi-asserted-by":"crossref","first-page":"31323","DOI":"10.1016\/S0021-9258(18)31694-6","article-title":"Protein\u2013tyrosine phosphatases","volume":"269","author":"Stone","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2006.02.055_bib16","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1016\/0968-0004(94)90274-7","article-title":"\u2019Zip codes\u2019 direct intracellular protein tyrosine phosphatases to the correct cellular \u2019address\u2019","volume":"19","author":"Mauro","year":"1994","journal-title":"Trends. Biochem. Sci."},{"key":"10.1016\/j.bbrc.2006.02.055_bib17","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1016\/0035-9203(78)90144-X","article-title":"A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba","volume":"72","author":"Diamond","year":"1978","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.bbrc.2006.02.055_bib18","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.exppara.2004.04.006","article-title":"Entamoeba histolytica: ultrastructure of trophozoites recovered from experimental liver lesions","volume":"107","author":"Ch\u00e1vez-Mungu\u00eda","year":"2004","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib19","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1046\/j.1365-2958.2002.02941.x","article-title":"Differential gene expression in Entamoeba histolytica isolated from amoebic liver abscess","volume":"44","author":"Bruchhaus","year":"2002","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib20","doi-asserted-by":"crossref","first-page":"6565","DOI":"10.1093\/nar\/19.23.6565","article-title":"Automated assembly of protein blocks for database searching","volume":"19","author":"Henikoff","year":"1991","journal-title":"Nucleic Acids. Res."},{"key":"10.1016\/j.bbrc.2006.02.055_bib21","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1017\/S0031182004005086","article-title":"A single step duplex PCR to distinguish Entamoeba histolytica from Entamoeba dispar","volume":"128","author":"Freitas","year":"2004","journal-title":"Parasitology"},{"key":"10.1016\/j.bbrc.2006.02.055_bib22","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/0378-1119(88)90005-4","article-title":"Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase","volume":"67","author":"Smith","year":"1988","journal-title":"Gene"},{"key":"10.1016\/j.bbrc.2006.02.055_bib23","doi-asserted-by":"crossref","first-page":"23759","DOI":"10.1016\/S0021-9258(18)35903-9","article-title":"Expression, purification, and physicochemical characterization of a recombinant Yersinia protein tyrosine phosphatase","volume":"267","author":"Zhang","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2006.02.055_bib24","doi-asserted-by":"crossref","first-page":"6408","DOI":"10.1128\/MCB.16.11.6408","article-title":"Identification of p130cas as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST","volume":"16","author":"Garton","year":"1996","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib25","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2006.02.055_bib26","doi-asserted-by":"crossref","first-page":"4350","DOI":"10.1073\/pnas.76.9.4350","article-title":"Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications","volume":"76","author":"Towbin","year":"1979","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.bbrc.2006.02.055_bib27","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/S0014-4894(03)00062-6","article-title":"Entamoeba histolytica: a \u03b21 integrin-like fibronectin receptor assembles a signaling complex similar to those of mammalian cells","volume":"103","author":"Flores-Robles","year":"2003","journal-title":"Exp. Parasitol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib28","doi-asserted-by":"crossref","first-page":"7117","DOI":"10.1128\/MCB.21.21.7117-7136.2001","article-title":"Structural and evolutionary relationships among protein tyrosine phosphatase domains","volume":"21","author":"Andersen","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib29","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1096\/fj.02-1212rev","article-title":"A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage","volume":"18","author":"Andersen","year":"2004","journal-title":"FASEB J."},{"key":"10.1016\/j.bbrc.2006.02.055_bib30","doi-asserted-by":"crossref","first-page":"5484","DOI":"10.1074\/jbc.273.10.5484","article-title":"Altering the nucleophile specificity of a protein\u2013tyrosine phosphatase-catalyzed reaction. Probing the function of the invariant glutamine residues","volume":"273","author":"Zhao","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2006.02.055_bib31","doi-asserted-by":"crossref","first-page":"2431","DOI":"10.1128\/MCB.16.5.2431","article-title":"Multiple roles of the novel protein tyrosine phosphatase PTP3 during Dictyostelium growth and development","volume":"16","author":"Gamper","year":"1996","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib32","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1105\/tpc.10.5.849","article-title":"Molecular characterization of a protein tyrosine phosphatase encoded by a stress-responsive gene in Arabidopsis","volume":"10","author":"Xu","year":"1998","journal-title":"Plant Cell"},{"key":"10.1016\/j.bbrc.2006.02.055_bib33","doi-asserted-by":"crossref","first-page":"6731","DOI":"10.1016\/S0021-9258(18)68703-4","article-title":"Characterization of the major protein\u2013tyrosine-phosphatase of human placenta","volume":"263","author":"Tonks","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2006.02.055_bib34","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0092-8674(91)90582-J","article-title":"The cdc25 protein contains an intrinsic phosphatase activity","volume":"67","author":"Dunphy","year":"1991","journal-title":"Cell"},{"key":"10.1016\/j.bbrc.2006.02.055_bib35","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1128\/jb.178.1.136-142.1996","article-title":"Cloning, purification, and properties of a phosphotyrosine protein phosphatase from Streptomyces coelicolor A3(2)","volume":"178","author":"Li","year":"1996","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib36","doi-asserted-by":"crossref","first-page":"22680","DOI":"10.1016\/S0021-9258(18)41581-5","article-title":"Cloning and functional expression of a Dictyostelium discoideum protein tyrosine phosphatase","volume":"268","author":"Ramalingam","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbrc.2006.02.055_bib37","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.1096\/fj.02-0740com","article-title":"Novel genes modulated by FSH in normal and immortalized FSH-responsive cells: new insights into the mechanism of FSH action","volume":"17","author":"Sasson","year":"2003","journal-title":"FASEB J."},{"key":"10.1016\/j.bbrc.2006.02.055_bib38","doi-asserted-by":"crossref","first-page":"3752","DOI":"10.1128\/MCB.14.6.3752","article-title":"PRL-1, a unique nuclear protein tyrosine phosphatase, affects cell growth","volume":"14","author":"Diamond","year":"1994","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.bbrc.2006.02.055_bib39","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/359644a0","article-title":"Oxidative stress and heat shock induce a human gene encoding a protein\u2013tyrosine phosphatase","volume":"359","author":"Keyse","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.bbrc.2006.02.055_bib40","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1677\/joe.1.06069","article-title":"Protein tyrosine phosphatases and signalling","volume":"185","author":"Stoker","year":"2005","journal-title":"J. Endocrinol."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X06003500?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X06003500?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,7,24]],"date-time":"2021-07-24T04:55:47Z","timestamp":1627102547000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X06003500"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,4]]},"references-count":40,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2006,4]]}},"alternative-id":["S0006291X06003500"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2006.02.055","relation":{},"ISSN":["0006-291X"],"issn-type":[{"value":"0006-291X","type":"print"}],"subject":[],"published":{"date-parts":[[2006,4]]}}}