{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T07:41:02Z","timestamp":1793778062035,"version":"4.6.1"},"reference-count":68,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,2,1]],"date-time":"2021-02-01T00:00:00Z","timestamp":1612137600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100007741","name":"University of Hyderabad","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100007741","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100006755","name":"School of Life Sciences, Arizona State University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100006755","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","award":["ECRA\/2018\/1640"],"award-info":[{"award-number":["ECRA\/2018\/1640"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","award":["IFA16-LSBM-170"],"award-info":[{"award-number":["IFA16-LSBM-170"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001843","name":"Science and Engineering Research Board","doi-asserted-by":"publisher","award":["ECR\/2017\/002023"],"award-info":[{"award-number":["ECR\/2017\/002023"]}],"id":[{"id":"10.13039\/501100001843","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001409","name":"Department of Science and Technology, Ministry of Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001409","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"published-print":{"date-parts":[[2021,2]]},"DOI":"10.1016\/j.bbamcr.2020.118898","type":"journal-article","created":{"date-parts":[[2020,11,3]],"date-time":"2020-11-03T23:22:23Z","timestamp":1604445743000},"page":"118898","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"title":["Molecular chaperone function of stress inducible Hsp70 is critical for intracellular multiplication of Toxoplasma gondii"],"prefix":"10.1016","volume":"1868","author":[{"given":"Pallabi","family":"Mitra","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Abhijit S.","family":"Deshmukh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chinmayee","family":"Choudhury","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbamcr.2020.118898_bb0005","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1126\/science.1094717","article-title":"Intracellular parasite invasion strategies","volume":"304","author":"Sibley","year":"2004","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0010","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1016\/S0140-6736(04)16412-X","article-title":"Toxoplasmosis","volume":"363","author":"Montoya","year":"2004","journal-title":"Lancet"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0015","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1111\/acps.12423","article-title":"Beyond the association. Toxoplasma gondii in schizophrenia, bipolar disorder, and addiction: systematic review and meta-analysis","volume":"132","author":"Sutterland","year":"2015","journal-title":"Acta Psychiatr. Scand."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0020","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1093\/cid\/ciw655","article-title":"Latent toxoplasma infection and higher toxoplasma gondii immunoglobulin G levels are associated with worse neurocognitive functioning in HIV-infected adults","volume":"63","author":"Bharti","year":"2016","journal-title":"Clin. Infect. Dis."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0025","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.cca.2019.08.015","article-title":"Heat shock proteins in infection","volume":"498","author":"Bolhassani","year":"2019","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0030","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1007\/s00018-004-4464-6","article-title":"Hsp70 chaperones: cellular functions and molecular mechanism","volume":"62","author":"Mayer","year":"2005","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0035","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.2174\/156802606777811997","article-title":"Hsp70 molecular chaperones: emerging roles in human disease and identification of small molecule modulators","volume":"6","author":"Brodsky","year":"2006","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0040","doi-asserted-by":"crossref","first-page":"2592","DOI":"10.4161\/cc.5.22.3448","article-title":"Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties","volume":"5","author":"Garrido","year":"2006","journal-title":"Cell Cycle"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0045","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/S0074-7696(06)54003-3","article-title":"Hsp70 chaperone as a survival factor in cell pathology","volume":"254","author":"Guzhova","year":"2006","journal-title":"Int. Rev. Cytol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0050","doi-asserted-by":"crossref","first-page":"4191","DOI":"10.1158\/0008-5472.CAN-05-3778","article-title":"Heat shock protein 70 neutralization exerts potent antitumor effects in animal models of colon cancer and melanoma","volume":"66","author":"Schmitt","year":"2006","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0055","doi-asserted-by":"crossref","first-page":"3758","DOI":"10.1016\/j.febslet.2007.05.040","article-title":"Inhibitors of the heat shock response: biology and pharmacology","volume":"581","author":"Powers","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0060","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.chom.2008.10.011","article-title":"Molecular chaperones in pathogen virulence: emerging new targets for therapy","volume":"4","author":"Neckers","year":"2008","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0065","doi-asserted-by":"crossref","DOI":"10.3390\/ijms20235930","article-title":"Small molecule inhibitors targeting the heat shock protein system of human obligate protozoan parasites","volume":"20","author":"Zininga","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0070","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1007\/s00438-005-1150-9","article-title":"Plasmodium falciparum heat shock protein 70 is able to suppress the thermosensitivity of an Escherichia coli DnaK mutant strain","volume":"274","author":"Shonhai","year":"2005","journal-title":"Mol. Geneti. Genomics"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0075","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0020047","article-title":"Expression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast","volume":"6","author":"Bell","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0080","doi-asserted-by":"crossref","first-page":"958","DOI":"10.4049\/jimmunol.169.2.958","article-title":"Heat shock protein 70 is a potential virulence factor in murine toxoplasma infection via immunomodulation of host NF-kappa B and nitric oxide","volume":"169","author":"Dobbin","year":"2002","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0085","doi-asserted-by":"crossref","first-page":"2193","DOI":"10.4049\/jimmunol.167.4.2193","article-title":"Toxoplasma gondii tachyzoites inhibit proinflammatory cytokine induction in infected macrophages by preventing nuclear translocation of the transcription factor NF-kappa B","volume":"167","author":"Butcher","year":"2001","journal-title":"J. Immunol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0090","doi-asserted-by":"crossref","first-page":"D391","DOI":"10.2741\/Weiss","article-title":"The development and biology of bradyzoites of Toxoplasma gondii","volume":"5","author":"Weiss","year":"2000","journal-title":"Front. Biosci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0095","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1128\/IAI.01115-07","article-title":"Modulation of the host cell proteome by the intracellular apicomplexan parasite Toxoplasma gondii","volume":"76","author":"Nelson","year":"2008","journal-title":"Infect. Immun."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0100","doi-asserted-by":"crossref","first-page":"a006734","DOI":"10.1101\/cshperspect.a006734","article-title":"Integration of clearance mechanisms: the proteasome and autophagy","volume":"2","author":"Wong","year":"2010","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0105","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/j.ab.2007.12.009","article-title":"Identification of small molecules that modify the protein folding activity of heat shock protein 70","volume":"374","author":"Wisen","year":"2008","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0110","doi-asserted-by":"crossref","DOI":"10.3390\/cells9030587","article-title":"HSP70 multi-functionality in cancer","volume":"9","author":"Albakova","year":"2020","journal-title":"Cells"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0115","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.molcel.2009.09.023","article-title":"A small molecule inhibitor of inducible heat shock protein 70","volume":"36","author":"Leu","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0120","doi-asserted-by":"crossref","first-page":"936","DOI":"10.1158\/1541-7786.MCR-11-0019","article-title":"HSP70 inhibition by the small-molecule 2-phenylethynesulfonamide impairs protein clearance pathways in tumor cells","volume":"9","author":"Leu","year":"2011","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0125","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1016\/j.bbagrm.2018.02.004","article-title":"Cdk-related kinase 9 regulates RNA polymerase II mediated transcription in Toxoplasma gondii","volume":"1861","author":"Deshmukh","year":"2018","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0130","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.bbagrm.2019.01.003","article-title":"Characterization of Toxoplasma gondii Spt5 like transcription elongation factor","volume":"1862","author":"Mitra","year":"2019","journal-title":"Biochim. Biophys. Acta Gene Regul. Mech."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0135","doi-asserted-by":"crossref","first-page":"35288","DOI":"10.1038\/srep35288","article-title":"Cdk7 mediates RPB1-driven mRNA synthesis in Toxoplasma gondii","volume":"6","author":"Deshmukh","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0140","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1003809","article-title":"Toxoplasma gondii-induced activation of EGFR prevents autophagy protein-mediated killing of the parasite","volume":"9","author":"Muniz-Feliciano","year":"2013","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0145","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1006\/jmbi.1993.1626","article-title":"Comparative protein modelling by satisfaction of spatial restraints","volume":"234","author":"Sali","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0150","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1002\/pro.663","article-title":"Biochemical and structural studies on the high affinity of Hsp70 for ADP","volume":"8","author":"Arakawa","year":"2011","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0155","article-title":"Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate","volume":"9","author":"Zhang","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0160","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nmeth.3213","article-title":"The I-TASSER Suite: protein structure and function prediction","volume":"12","author":"Yang","year":"2015","journal-title":"Nat. Methods"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0165","doi-asserted-by":"crossref","first-page":"184109","DOI":"10.1063\/1.2191489","article-title":"The midpoint method for parallelization of particle simulations","volume":"124","author":"Bowers","year":"2006","journal-title":"J. Chem. Phys."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0170","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1002\/pro.3289","article-title":"PDBsum: structural summaries of PDB entries","volume":"27","author":"Laskowski","year":"2018","journal-title":"Protein Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0175","series-title":"Schr\u00f6dinger Release 2019-2: LigPrep, Schr\u00f6dinger, LLC, New York, NY","year":"2019"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0180","series-title":"Schr\u00f6dinger Release 2019-2: Glide, Schr\u00f6dinger, LLC, New York, NY","year":"2019"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0185","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1038\/nchembio809","article-title":"Small-molecule inhibitor of p53 binding to mitochondria protects mice from gamma radiation","volume":"2","author":"Strom","year":"2006","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0190","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1158\/0008-5472.CAN-10-1443","article-title":"Peptides and aptamers targeting HSP70: a novel approach for anticancer chemotherapy","volume":"71","author":"Rerole","year":"2011","journal-title":"Cancer Res."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0195","doi-asserted-by":"crossref","first-page":"3702","DOI":"10.1016\/j.febslet.2007.05.039","article-title":"The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions","volume":"581","author":"Daugaard","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0200","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1379\/1466-1268(2003)008<0309:MFROHF>2.0.CO;2","article-title":"Mechanisms for regulation of Hsp70 function by Hsp40","volume":"8","author":"Fan","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0205","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1379\/1466-1268(2003)008<0303:CALBTC>2.0.CO;2","article-title":"CHIP: a link between the chaperone and proteasome systems","volume":"8","author":"McDonough","year":"2003","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0210","doi-asserted-by":"crossref","first-page":"66","DOI":"10.4161\/auto.1.2.1738","article-title":"Does autophagy contribute to cell death?","volume":"1","author":"Debnath","year":"2005","journal-title":"Autophagy"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0215","doi-asserted-by":"crossref","first-page":"1","DOI":"10.4161\/auto.1.1.1270","article-title":"Maturation of autophagic vacuoles in Mammalian cells","volume":"1","author":"Eskelinen","year":"2005","journal-title":"Autophagy"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0220","first-page":"62079","article-title":"Signaling, polyubiquitination, trafficking, and inclusions: sequestosome 1\/p62\u2019s role in neurodegenerative disease","volume":"2006","author":"Wooten","year":"2006","journal-title":"J. Biomed. Biotechnol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0225","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.tibs.2006.12.002","article-title":"Signal integration and diversification through the p62 scaffold protein","volume":"32","author":"Moscat","year":"2007","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0230","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1083\/jcb.200507002","article-title":"p62\/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death","volume":"171","author":"Bjorkoy","year":"2005","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0235","doi-asserted-by":"crossref","first-page":"24131","DOI":"10.1074\/jbc.M702824200","article-title":"p62\/SQSTM1 binds directly to Atg8\/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy","volume":"282","author":"Pankiv","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0240","doi-asserted-by":"crossref","first-page":"5029","DOI":"10.1016\/j.febslet.2005.08.010","article-title":"Evidence for p62 aggregate formation: role in cell survival","volume":"579","author":"Paine","year":"2005","journal-title":"FEBS Lett."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0245","doi-asserted-by":"crossref","first-page":"2685","DOI":"10.1242\/jcs.026005","article-title":"The N-terminus and Phe52 residue of LC3 recruit p62\/SQSTM1 into autophagosomes","volume":"121","author":"Shvets","year":"2008","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0250","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1158\/1541-7786.MCR-12-0547-T","article-title":"A modified HSP70 inhibitor shows broad activity as an anticancer agent","volume":"11","author":"Balaburski","year":"2013","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0255","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1016\/j.ijbiomac.2011.12.012","article-title":"Toxoplasma gondii Sis1-like J-domain protein is a cytosolic chaperone associated to HSP90\/HSP70 complex","volume":"50","author":"Figueras","year":"2012","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0260","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1099\/vir.0.83414-0","article-title":"Epstein-Barr virus nuclear antigen (EBNA) 3A induces the expression of and interacts with a subset of chaperones and co-chaperones","volume":"89","author":"Young","year":"2008","journal-title":"J. Gen. Virol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0265","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1005274","article-title":"Hsp70 isoforms are essential for the formation of Kaposi\u2019s sarcoma-associated herpesvirus replication and transcription compartments","volume":"11","author":"Baquero-Perez","year":"2015","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0270","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1002\/hep.23766","article-title":"Small molecular compounds that inhibit hepatitis C virus replication through destabilizing heat shock cognate 70 messenger RNA","volume":"52","author":"Peng","year":"2010","journal-title":"Hepatology"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0275","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1002\/(SICI)1097-010X(199809\/10)282:1\/2<261::AID-JEZ28>3.0.CO;2-V","article-title":"HSP70-2 heat-shock protein of mouse spermatogenic cells","volume":"282","author":"Eddy","year":"1998","journal-title":"J. Exp. Zool."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0280","doi-asserted-by":"crossref","DOI":"10.1371\/annotation\/5a7961d9-a7ea-4b10-9b48-5b106c405b02","article-title":"Functional analysis of Hsp70 inhibitors","volume":"8","author":"Schlecht","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0285","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/s41419-018-0779-3","article-title":"The Hsp70 inhibitor 2-phenylethynesulfonamide inhibits replication and carcinogenicity of Epstein-Barr virus by inhibiting the molecular chaperone function of Hsp70","volume":"9","author":"Wang","year":"2018","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0290","doi-asserted-by":"crossref","first-page":"1694","DOI":"10.1074\/jbc.M807890200","article-title":"Host cell autophagy is induced by Toxoplasma gondii and contributes to parasite growth","volume":"284","author":"Wang","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0295","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1016\/j.immuni.2007.07.004","article-title":"Innate and adaptive immunity through autophagy","volume":"27","author":"Schmid","year":"2007","journal-title":"Immunity"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0300","doi-asserted-by":"crossref","first-page":"117","DOI":"10.4161\/auto.3618","article-title":"Autophagy limits Listeria monocytogenes intracellular growth in the early phase of primary infection","volume":"3","author":"Py","year":"2007","journal-title":"Autophagy"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0305","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1126\/science.1152725","article-title":"Identification of host proteins required for HIV infection through a functional genomic screen","volume":"319","author":"Brass","year":"2008","journal-title":"Science"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0310","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.0030156","article-title":"Subversion of cellular autophagosomal machinery by RNA viruses","volume":"3","author":"Jackson","year":"2005","journal-title":"PLoS Biol."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0315","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1242\/jcs.02934","article-title":"Toxoplasma gondii triggers Gi-dependent PI 3-kinase signaling required for inhibition of host cell apoptosis","volume":"119","author":"Kim","year":"2006","journal-title":"J. Cell Sci."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0320","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1038\/nature08710","article-title":"Hsp70 stabilizes lysosomes and reverts Niemann-Pick disease-associated lysosomal pathology","volume":"463","author":"Kirkegaard","year":"2010","journal-title":"Nature"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0325","doi-asserted-by":"crossref","DOI":"10.1038\/cddis.2013.263","article-title":"HSP70 inhibition by 2-phenylethynesulfonamide induces lysosomal cathepsin D release and immunogenic cell death in primary effusion lymphoma","volume":"4","author":"Granato","year":"2013","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0330","doi-asserted-by":"crossref","first-page":"6602","DOI":"10.1074\/jbc.M110.151324","article-title":"Lucanthone is a novel inhibitor of autophagy that induces cathepsin D-mediated apoptosis","volume":"286","author":"Carew","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamcr.2020.118898_bb0335","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.cell.2006.01.056","article-title":"Toxoplasma gondii sequesters lysosomes from mammalian hosts in the vacuolar space","volume":"125","author":"Coppens","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.bbamcr.2020.118898_bb0340","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.molcel.2009.01.021","article-title":"Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates","volume":"33","author":"Korolchuk","year":"2009","journal-title":"Mol. Cell"}],"container-title":["Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488920302561?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0167488920302561?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,5,12]],"date-time":"2026-05-12T23:19:43Z","timestamp":1778627983000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0167488920302561"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,2]]},"references-count":68,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2021,2]]}},"alternative-id":["S0167488920302561"],"URL":"https:\/\/doi.org\/10.1016\/j.bbamcr.2020.118898","relation":{},"ISSN":["0167-4889"],"issn-type":[{"value":"0167-4889","type":"print"}],"subject":[],"published":{"date-parts":[[2021,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Molecular chaperone function of stress inducible Hsp70 is critical for intracellular multiplication of Toxoplasma gondii","name":"articletitle","label":"Article Title"},{"value":"Biochimica et Biophysica Acta (BBA) - Molecular Cell Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbamcr.2020.118898","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"118898"}}