{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,18]],"date-time":"2025-12-18T09:22:56Z","timestamp":1766049776243,"version":"3.40.3"},"publisher-location":"Cham","reference-count":72,"publisher":"Springer International Publishing","isbn-type":[{"type":"print","value":"9783030783969"},{"type":"electronic","value":"9783030783976"}],"license":[{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2021,1,1]],"date-time":"2021-01-01T00:00:00Z","timestamp":1609459200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021]]},"DOI":"10.1007\/978-3-030-78397-6_5","type":"book-chapter","created":{"date-parts":[[2021,9,26]],"date-time":"2021-09-26T20:08:45Z","timestamp":1632686925000},"page":"125-139","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Role of Hsp90 in Plasmodium falciparum Malaria"],"prefix":"10.1007","author":[{"given":"Dea","family":"Shahinas","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Dylan R.","family":"Pillai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2021,9,27]]},"reference":[{"issue":"2","key":"5_CR1","doi-asserted-by":"publisher","first-page":"85","DOI":"10.1016\/j.molbiopara.2007.01.009","volume":"153","author":"P Acharya","year":"2007","unstructured":"Acharya P, Kumar R, Tatu U (2007) Chaperoning a cellular upheaval in malaria: heat shock proteins in Plasmodium falciparum. Mol Biochem Parasitol 153(2):85\u201394. https:\/\/doi.org\/10.1016\/j.molbiopara.2007.01.009","journal-title":"Mol Biochem Parasitol"},{"issue":"Pt 1","key":"5_CR2","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1042\/bj3150307","volume":"315","author":"I Ansorge","year":"1996","unstructured":"Ansorge I, Benting J, Bhakdi S, Lingelbach K (1996) Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O. Biochem J 315(Pt 1):307\u2013314. https:\/\/doi.org\/10.1042\/bj3150307","journal-title":"Biochem J"},{"issue":"6","key":"5_CR3","doi-asserted-by":"publisher","first-page":"3902","DOI":"10.1074\/jbc.M110513200","volume":"277","author":"G Banumathy","year":"2002","unstructured":"Banumathy G, Singh V, Tatu U (2002) Host chaperones are recruited in membrane-bound complexes by Plasmodium falciparum. J Biol Chem 277(6):3902\u20133912. https:\/\/doi.org\/10.1074\/jbc.M110513200","journal-title":"J Biol Chem"},{"issue":"20","key":"5_CR4","doi-asserted-by":"publisher","first-page":"18336","DOI":"10.1074\/jbc.M211309200","volume":"278","author":"G Banumathy","year":"2003","unstructured":"Banumathy G, Singh V, Pavithra SR, Tatu U (2003) Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes. J Biol Chem 278(20):18336\u201318345. https:\/\/doi.org\/10.1074\/jbc.M211309200","journal-title":"J Biol Chem"},{"issue":"1","key":"5_CR5","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1186\/s12936-016-1625-7","volume":"15","author":"AG Bayih","year":"2016","unstructured":"Bayih AG, Folefoc A, Mohon AN, Eagon S, Anderson M, Pillai DR (2016) In vitro and in vivo anti-malarial activity of novel harmine-analog heat shock protein 90 inhibitors: a possible partner for artemisinin. Malar J 15(1):579. https:\/\/doi.org\/10.1186\/s12936-016-1625-7","journal-title":"Malar J"},{"issue":"6623","key":"5_CR6","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1038\/386414a0","volume":"386","author":"A Bergerat","year":"1997","unstructured":"Bergerat A, de Massy B, Gadelle D, Varoutas PC, Nicolas A, Forterre P (1997) An atypical topoisomerase II from archaea with implications for meiotic recombination. Nature 386(6623):414\u2013417. https:\/\/doi.org\/10.1038\/386414a0","journal-title":"Nature"},{"issue":"1","key":"5_CR7","doi-asserted-by":"publisher","first-page":"157","DOI":"10.1016\/0166-6851(94)90105-8","volume":"67","author":"S Bonnefoy","year":"1994","unstructured":"Bonnefoy S, Attal G, Langsley G, Tekaia F, Mercereau-Puijalon O (1994) Molecular characterization of the heat shock protein 90 gene of the human malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 67(1):157\u2013170. https:\/\/doi.org\/10.1016\/0166-6851(94)90105-8","journal-title":"Mol Biochem Parasitol"},{"issue":"9","key":"5_CR8","doi-asserted-by":"publisher","first-page":"3919","DOI":"10.1128\/mcb.9.9.3919","volume":"9","author":"KA Borkovich","year":"1989","unstructured":"Borkovich KA, Farrelly FW, Finkelstein DB, Taulien J, Lindquist S (1989) hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures. Mol Cell Biol 9(9):3919\u20133930. https:\/\/doi.org\/10.1128\/mcb.9.9.3919","journal-title":"Mol Cell Biol"},{"issue":"10","key":"5_CR9","doi-asserted-by":"publisher","first-page":"1675","DOI":"10.1007\/s00018-010-0275-0","volume":"67","author":"CS Chua","year":"2010","unstructured":"Chua CS, Low H, Goo KS, Sim TS (2010) Characterization of Plasmodium falciparum co-chaperone p23: its intrinsic chaperone activity and interaction with Hsp90. Cell Mol Life Sci 67(10):1675\u20131686. https:\/\/doi.org\/10.1007\/s00018-010-0275-0","journal-title":"Cell Mol Life Sci"},{"issue":"9","key":"5_CR10","doi-asserted-by":"publisher","first-page":"1177","DOI":"10.1017\/S0031182013002084","volume":"141","author":"CS Chua","year":"2014","unstructured":"Chua CS, Low H, Sim TS (2014) Co-chaperones of Hsp90 in Plasmodium falciparum and their concerted roles in cellular regulation. Parasitology 141(9):1177\u20131191. https:\/\/doi.org\/10.1017\/S0031182013002084","journal-title":"Parasitology"},{"issue":"13","key":"5_CR11","doi-asserted-by":"publisher","first-page":"2738","DOI":"10.1002\/prot.22799","volume":"78","author":"KD Corbett","year":"2010","unstructured":"Corbett KD, Berger JM (2010) Structure of the ATP-binding domain of Plasmodium falciparum Hsp90. Proteins 78(13):2738\u20132744. https:\/\/doi.org\/10.1002\/prot.22799","journal-title":"Proteins"},{"key":"5_CR12","doi-asserted-by":"publisher","first-page":"11901","DOI":"10.1038\/ncomms11901","volume":"7","author":"VC Corey","year":"2016","unstructured":"Corey VC, Lukens AK, Istvan ES, Lee MCS, Franco V, Magistrado P, Coburn-Flynn O, Sakata-Kato T, Fuchs O, Gnadig NF, Goldgof G, Linares M, Gomez-Lorenzo MG, De Cozar C, Lafuente-Monasterio MJ, Prats S, Meister S, Tanaseichuk O, Wree M, Zhou Y, Willis PA, Gamo FJ, Goldberg DE, Fidock DA, Wirth DF, Winzeler EA (2016) A broad analysis of resistance development in the malaria parasite. Nat Commun 7:11901. https:\/\/doi.org\/10.1038\/ncomms11901","journal-title":"Nat Commun"},{"key":"5_CR13","doi-asserted-by":"publisher","first-page":"193","DOI":"10.1016\/s0091-679x(08)61852-x","volume":"45","author":"I Crandall","year":"1994","unstructured":"Crandall I, Sherman IW (1994) Cytoadherence and the Plasmodium falciparum-infected erythrocyte. Methods Cell Biol 45:193\u2013210. https:\/\/doi.org\/10.1016\/s0091-679x(08)61852-x","journal-title":"Methods Cell Biol"},{"issue":"2","key":"5_CR14","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1016\/s0163-7258(98)00013-8","volume":"79","author":"P Csermely","year":"1998","unstructured":"Csermely P, Schnaider T, Soti C, Prohaszka Z, Nardai G (1998) The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol Ther 79(2):129\u2013168. https:\/\/doi.org\/10.1016\/s0163-7258(98)00013-8","journal-title":"Pharmacol Ther"},{"issue":"7","key":"5_CR15","doi-asserted-by":"publisher","first-page":"1027","DOI":"10.1016\/0092-8674(94)90442-1","volume":"77","author":"T Cutforth","year":"1994","unstructured":"Cutforth T, Rubin GM (1994) Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor tyrosine kinase in Drosophila. Cell 77(7):1027\u20131036. https:\/\/doi.org\/10.1016\/0092-8674(94)90442-1","journal-title":"Cell"},{"issue":"6","key":"5_CR16","doi-asserted-by":"publisher","first-page":"627","DOI":"10.1016\/j.ijpara.2005.01.007","volume":"35","author":"E Devaney","year":"2005","unstructured":"Devaney E, O'Neill K, Harnett W, Whitesell L, Kinnaird JH (2005) Hsp90 is essential in the filarial nematode Brugia pahangi. Int J Parasitol 35(6):627\u2013636. https:\/\/doi.org\/10.1016\/j.ijpara.2005.01.007","journal-title":"Int J Parasitol"},{"key":"5_CR17","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1186\/1471-2180-1-31","volume":"1","author":"S Dobson","year":"2001","unstructured":"Dobson S, Kar B, Kumar R, Adams B, Barik S (2001) A novel tetratricopeptide repeat (TPR) containing PP5 serine\/threonine protein phosphatase in the malaria parasite, Plasmodium falciparum. BMC Microbiol 1:31. https:\/\/doi.org\/10.1186\/1471-2180-1-31","journal-title":"BMC Microbiol"},{"issue":"34","key":"5_CR18","doi-asserted-by":"publisher","first-page":"30438","DOI":"10.1074\/jbc.M503761200","volume":"280","author":"DE Dollins","year":"2005","unstructured":"Dollins DE, Immormino RM, Gewirth DT (2005) Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change. J Biol Chem 280(34):30438\u201330447. https:\/\/doi.org\/10.1074\/jbc.M503761200","journal-title":"J Biol Chem"},{"issue":"1","key":"5_CR19","doi-asserted-by":"publisher","first-page":"24","DOI":"10.1016\/s0968-0004(99)01503-0","volume":"25","author":"R Dutta","year":"2000","unstructured":"Dutta R, Inouye M (2000) GHKL, an emergent ATPase\/kinase superfamily. Trends Biochem Sci 25(1):24\u201328. https:\/\/doi.org\/10.1016\/s0968-0004(99)01503-0","journal-title":"Trends Biochem Sci"},{"issue":"8","key":"5_CR20","doi-asserted-by":"publisher","first-page":"1559","DOI":"10.1091\/mbc.8.8.1559","volume":"8","author":"DK Eggers","year":"1997","unstructured":"Eggers DK, Welch WJ, Hansen WJ (1997) Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cells. Mol Biol Cell 8(8):1559\u20131573. https:\/\/doi.org\/10.1091\/mbc.8.8.1559","journal-title":"Mol Biol Cell"},{"issue":"6","key":"5_CR21","doi-asserted-by":"publisher","first-page":"2109","DOI":"10.1074\/jbc.REV118.002806","volume":"294","author":"O Genest","year":"2019","unstructured":"Genest O, Wickner S, Doyle SM (2019) Hsp90 and Hsp70 chaperones: collaborators in protein remodeling. J Biol Chem 294(6):2109\u20132120. https:\/\/doi.org\/10.1074\/jbc.REV118.002806","journal-title":"J Biol Chem"},{"issue":"2","key":"5_CR22","doi-asserted-by":"publisher","first-page":"191","DOI":"10.1007\/s12192-011-0299-x","volume":"17","author":"GW Gitau","year":"2012","unstructured":"Gitau GW, Mandal P, Blatch GL, Przyborski J, Shonhai A (2012) Characterisation of the Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop). Cell Stress Chaperones 17(2):191\u2013202. https:\/\/doi.org\/10.1007\/s12192-011-0299-x","journal-title":"Cell Stress Chaperones"},{"issue":"11","key":"5_CR23","doi-asserted-by":"publisher","first-page":"5307","DOI":"10.1128\/IAI.66.11.5307-5313.1998","volume":"66","author":"F Goulhen","year":"1998","unstructured":"Goulhen F, Hafezi A, Uitto VJ, Hinode D, Nakamura R, Grenier D, Mayrand D (1998) Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans. Infect Immun 66(11):5307\u20135313. https:\/\/doi.org\/10.1128\/IAI.66.11.5307-5313.1998","journal-title":"Infect Immun"},{"issue":"12","key":"5_CR24","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0015770","volume":"5","author":"I Grad","year":"2010","unstructured":"Grad I, Cederroth CR, Walicki J, Grey C, Barluenga S, Winssinger N, De Massy B, Nef S, Picard D (2010) The molecular chaperone Hsp90alpha is required for meiotic progression of spermatocytes beyond pachytene in the mouse. PLoS One 5(12):e15770. https:\/\/doi.org\/10.1371\/journal.pone.0015770","journal-title":"PLoS One"},{"issue":"6","key":"5_CR25","doi-asserted-by":"publisher","first-page":"1635","DOI":"10.1016\/j.celrep.2019.07.019","volume":"28","author":"C Hillier","year":"2019","unstructured":"Hillier C, Pardo M, Yu L, Bushell E, Sanderson T, Metcalf T, Herd C, Anar B, Rayner JC, Billker O, Choudhary JS (2019) Landscape of the Plasmodium Interactome reveals both conserved and species-specific functionality. Cell Rep 28(6):1635\u20131647. e1635. https:\/\/doi.org\/10.1016\/j.celrep.2019.07.019","journal-title":"Cell Rep"},{"issue":"44","key":"5_CR26","doi-asserted-by":"publisher","first-page":"46162","DOI":"10.1074\/jbc.M405253200","volume":"279","author":"RM Immormino","year":"2004","unstructured":"Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT (2004) Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone. J Biol Chem 279(44):46162\u201346171. https:\/\/doi.org\/10.1074\/jbc.M405253200","journal-title":"J Biol Chem"},{"issue":"5","key":"5_CR27","doi-asserted-by":"publisher","first-page":"1033","DOI":"10.1016\/j.jmb.2009.03.071","volume":"388","author":"RM Immormino","year":"2009","unstructured":"Immormino RM, Metzger LE t, Reardon PN, Dollins DE, Blagg BS, Gewirth DT (2009) Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design. J Mol Biol 388(5):1033\u20131042. https:\/\/doi.org\/10.1016\/j.jmb.2009.03.071","journal-title":"J Mol Biol"},{"issue":"3","key":"5_CR28","doi-asserted-by":"publisher","first-page":"607","DOI":"10.1016\/j.bbamcr.2011.09.020","volume":"1823","author":"JL Johnson","year":"2012","unstructured":"Johnson JL (2012) Evolution and function of diverse Hsp90 homologs and cochaperone proteins. Biochim Biophys Acta 1823(3):607\u2013613. https:\/\/doi.org\/10.1016\/j.bbamcr.2011.09.020","journal-title":"Biochim Biophys Acta"},{"issue":"1","key":"5_CR29","doi-asserted-by":"publisher","first-page":"83","DOI":"10.1007\/s12192-008-0058-9","volume":"14","author":"JL Johnson","year":"2009","unstructured":"Johnson JL, Brown C (2009) Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms. Cell Stress Chaperones 14(1):83\u201394. https:\/\/doi.org\/10.1007\/s12192-008-0058-9","journal-title":"Cell Stress Chaperones"},{"issue":"Suppl 1","key":"5_CR30","doi-asserted-by":"publisher","first-page":"S35","DOI":"10.1097\/00004836-199800001-00007","volume":"27","author":"S Kamiya","year":"1998","unstructured":"Kamiya S, Yamaguchi H, Osaki T, Taguchi H (1998) A virulence factor of Helicobacter pylori: role of heat shock protein in mucosal inflammation after H. pylori infection. J Clin Gastroenterol 27(Suppl 1):S35\u2013S39. https:\/\/doi.org\/10.1097\/00004836-199800001-00007","journal-title":"J Clin Gastroenterol"},{"issue":"8","key":"5_CR31","doi-asserted-by":"publisher","first-page":"3180","DOI":"10.1128\/IAI.65.8.3180-3185.1997","volume":"65","author":"K Kaneda","year":"1997","unstructured":"Kaneda K, Masuzawa T, Yasugami K, Suzuki T, Suzuki Y, Yanagihara Y (1997) Glycosphingolipid-binding protein of Borrelia burgdorferi sensu lato. Infect Immun 65(8):3180\u20133185. https:\/\/doi.org\/10.1128\/IAI.65.8.3180-3185.1997","journal-title":"Infect Immun"},{"issue":"5","key":"5_CR32","doi-asserted-by":"publisher","first-page":"601","DOI":"10.1016\/j.molcel.2005.04.021","volume":"18","author":"JJ Kovacs","year":"2005","unstructured":"Kovacs JJ, Murphy PJ, Gaillard S, Zhao X, Wu JT, Nicchitta CV, Yoshida M, Toft DO, Pratt WB, Yao TP (2005) HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor. Mol Cell 18(5):601\u2013607. https:\/\/doi.org\/10.1016\/j.molcel.2005.04.021","journal-title":"Mol Cell"},{"issue":"2","key":"5_CR33","doi-asserted-by":"publisher","first-page":"229","DOI":"10.1017\/S0033583510000314","volume":"44","author":"KA Krukenberg","year":"2011","unstructured":"Krukenberg KA, Street TO, Lavery LA, Agard DA (2011) Conformational dynamics of the molecular chaperone Hsp90. Q Rev Biophys 44(2):229\u2013255. https:\/\/doi.org\/10.1017\/S0033583510000314","journal-title":"Q Rev Biophys"},{"issue":"2","key":"5_CR34","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1016\/j.molbiopara.2005.02.007","volume":"141","author":"R Kumar","year":"2005","unstructured":"Kumar R, Adams B, Musiyenko A, Shulyayeva O, Barik S (2005) The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity. Mol Biochem Parasitol 141(2):163\u2013173. https:\/\/doi.org\/10.1016\/j.molbiopara.2005.02.007","journal-title":"Mol Biochem Parasitol"},{"issue":"3","key":"5_CR35","doi-asserted-by":"publisher","first-page":"531","DOI":"10.1007\/s12038-007-0052-x","volume":"32","author":"R Kumar","year":"2007","unstructured":"Kumar R, Pavithra SR, Tatu U (2007) Three-dimensional structure of heat shock protein 90 from Plasmodium falciparum: molecular modelling approach to rational drug design against malaria. J Biosci 32(3):531\u2013536. https:\/\/doi.org\/10.1007\/s12038-007-0052-x","journal-title":"J Biosci"},{"issue":"1","key":"5_CR36","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1084\/jem.169.1.357","volume":"169","author":"D Kwiatkowski","year":"1989","unstructured":"Kwiatkowski D (1989) Febrile temperatures can synchronize the growth of Plasmodium falciparum in vitro. J Exp Med 169(1):357\u2013361. https:\/\/doi.org\/10.1084\/jem.169.1.357","journal-title":"J Exp Med"},{"issue":"7064","key":"5_CR37","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1038\/nature04104","volume":"438","author":"DJ LaCount","year":"2005","unstructured":"LaCount DJ, Vignali M, Chettier R, Phansalkar A, Bell R, Hesselberth JR, Schoenfeld LW, Ota I, Sahasrabudhe S, Kurschner C, Fields S, Hughes RE (2005) A protein interaction network of the malaria parasite Plasmodium falciparum. Nature 438(7064):103\u2013107. https:\/\/doi.org\/10.1038\/nature04104","journal-title":"Nature"},{"issue":"5","key":"5_CR38","doi-asserted-by":"publisher","first-page":"2431","DOI":"10.1016\/S0021-9258(19)81631-9","volume":"264","author":"SP Lees-Miller","year":"1989","unstructured":"Lees-Miller SP, Anderson CW (1989) Two human 90-kDa heat shock proteins are phosphorylated in vivo at conserved serines that are phosphorylated in vitro by casein kinase II. J Biol Chem 264(5):2431\u20132437. https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/2492519","journal-title":"J Biol Chem"},{"key":"5_CR39","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1101\/sqb.2009.74.043","volume":"74","author":"S Lindquist","year":"2009","unstructured":"Lindquist S (2009) Protein folding sculpting evolutionary change. Cold Spring Harb Symp Quant Biol 74:103\u2013108. https:\/\/doi.org\/10.1101\/sqb.2009.74.043","journal-title":"Cold Spring Harb Symp Quant Biol"},{"issue":"4","key":"5_CR40","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0226657","volume":"15","author":"S Makumire","year":"2020","unstructured":"Makumire S, Zininga T, Vahokoski J, Kursula I, Shonhai A (2020) Biophysical analysis of Plasmodium falciparum Hsp70-Hsp90 organising protein (PfHop) reveals a monomer that is characterised by folded segments connected by flexible linkers. PLoS One 15(4):e0226657. https:\/\/doi.org\/10.1371\/journal.pone.0226657","journal-title":"PLoS One"},{"issue":"2","key":"5_CR41","doi-asserted-by":"publisher","first-page":"350","DOI":"10.1002\/pmic.200700697","volume":"8","author":"MA Morales","year":"2008","unstructured":"Morales MA, Watanabe R, Laurent C, Lenormand P, Rousselle JC, Namane A, Spath GF (2008) Phosphoproteomic analysis of Leishmania donovani pro- and amastigote stages. Proteomics 8(2):350\u2013363. https:\/\/doi.org\/10.1002\/pmic.200700697","journal-title":"Proteomics"},{"issue":"18","key":"5_CR42","doi-asserted-by":"publisher","first-page":"8381","DOI":"10.1073\/pnas.0914768107","volume":"107","author":"MA Morales","year":"2010","unstructured":"Morales MA, Watanabe R, Dacher M, Chafey P, Osorio y Fortea J, Scott DA, Beverley SM, Ommen G, Clos J, Hem S, Lenormand P, Rousselle JC, Namane A, Spath GF (2010) Phosphoproteome dynamics reveal heat-shock protein complexes specific to the Leishmania donovani infectious stage. Proc Natl Acad Sci U S A 107(18):8381\u20138386. https:\/\/doi.org\/10.1073\/pnas.0914768107","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"5_CR43","doi-asserted-by":"publisher","first-page":"292","DOI":"10.1186\/s12936-017-1940-7","volume":"16","author":"C Murillo-Solano","year":"2017","unstructured":"Murillo-Solano C, Dong C, Sanchez CG, Pizarro JC (2017) Identification and characterization of the antiplasmodial activity of Hsp90 inhibitors. Malar J 16(1):292. https:\/\/doi.org\/10.1186\/s12936-017-1940-7","journal-title":"Malar J"},{"issue":"40","key":"5_CR44","doi-asserted-by":"publisher","first-page":"33792","DOI":"10.1074\/jbc.M506997200","volume":"280","author":"PJ Murphy","year":"2005","unstructured":"Murphy PJ, Morishima Y, Kovacs JJ, Yao TP, Pratt WB (2005) Regulation of the dynamics of hsp90 action on the glucocorticoid receptor by acetylation\/deacetylation of the chaperone. J Biol Chem 280(40):33792\u201333799. https:\/\/doi.org\/10.1074\/jbc.M506997200","journal-title":"J Biol Chem"},{"issue":"6","key":"5_CR45","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.chom.2008.10.011","volume":"4","author":"L Neckers","year":"2008","unstructured":"Neckers L, Tatu U (2008) Molecular chaperones in pathogen virulence: emerging new targets for therapy. Cell Host Microbe 4(6):519\u2013527. https:\/\/doi.org\/10.1016\/j.chom.2008.10.011","journal-title":"Cell Host Microbe"},{"issue":"5","key":"5_CR46","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1080\/00034989760923","volume":"91","author":"CI Newbold","year":"1997","unstructured":"Newbold CI, Craig AG, Kyes S, Berendt AR, Snow RW, Peshu N, Marsh K (1997) PfEMP1, polymorphism and pathogenesis. Ann Trop Med Parasitol 91(5):551\u2013557. https:\/\/doi.org\/10.1080\/00034989760923","journal-title":"Ann Trop Med Parasitol"},{"key":"5_CR47","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1186\/1475-2875-9-236","volume":"9","author":"R Pallavi","year":"2010","unstructured":"Pallavi R, Acharya P, Chandran S, Daily JP, Tatu U (2010a) Chaperone expression profiles correlate with distinct physiological states of Plasmodium falciparum in malaria patients. Malar J 9:236. https:\/\/doi.org\/10.1186\/1475-2875-9-236","journal-title":"Malar J"},{"issue":"49","key":"5_CR48","doi-asserted-by":"publisher","first-page":"37964","DOI":"10.1074\/jbc.M110.155317","volume":"285","author":"R Pallavi","year":"2010","unstructured":"Pallavi R, Roy N, Nageshan RK, Talukdar P, Pavithra SR, Reddy R, Venketesh S, Kumar R, Gupta AK, Singh RK, Yadav SC, Tatu U (2010b) Heat shock protein 90 as a drug target against protozoan infections: biochemical characterization of HSP90 from Plasmodium falciparum and Trypanosoma evansi and evaluation of its inhibitor as a candidate drug. J Biol Chem 285(49):37964\u201337975. https:\/\/doi.org\/10.1074\/jbc.M110.155317","journal-title":"J Biol Chem"},{"issue":"1\u20132","key":"5_CR49","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1023\/a:1006884306169","volume":"185","author":"M Park","year":"1998","unstructured":"Park M, Yong Kang C, Krishna P (1998) Brassica napus hsp90 can autophosphorylate and phosphorylate other protein substrates. Mol Cell Biochem 185(1\u20132):33\u201338. https:\/\/doi.org\/10.1023\/a:1006884306169","journal-title":"Mol Cell Biochem"},{"issue":"45","key":"5_CR50","doi-asserted-by":"publisher","first-page":"46692","DOI":"10.1074\/jbc.M409165200","volume":"279","author":"SR Pavithra","year":"2004","unstructured":"Pavithra SR, Banumathy G, Joy O, Singh V, Tatu U (2004) Recurrent fever promotes Plasmodium falciparum development in human erythrocytes. J Biol Chem 279(45):46692\u201346699. https:\/\/doi.org\/10.1074\/jbc.M409165200","journal-title":"J Biol Chem"},{"issue":"9","key":"5_CR51","doi-asserted-by":"publisher","first-page":"1701","DOI":"10.1371\/journal.pcbi.0030168","volume":"3","author":"SR Pavithra","year":"2007","unstructured":"Pavithra SR, Kumar R, Tatu U (2007) Systems analysis of chaperone networks in the malarial parasite Plasmodium falciparum. PLoS Comput Biol 3(9):1701\u20131715. https:\/\/doi.org\/10.1371\/journal.pcbi.0030168","journal-title":"PLoS Comput Biol"},{"issue":"5","key":"5_CR52","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1007057","volume":"14","author":"D Posfai","year":"2018","unstructured":"Posfai D, Sylvester K, Reddy A, Ganley JG, Wirth J, Cullen QE, Dave T, Kato N, Dave SS, Derbyshire ER (2018) Plasmodium parasite exploits host aquaporin-3 during liver stage malaria infection. PLoS Pathog 14(5):e1007057. https:\/\/doi.org\/10.1371\/journal.ppat.1007057","journal-title":"PLoS Pathog"},{"issue":"2","key":"5_CR53","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1177\/153537020322800201","volume":"228","author":"WB Pratt","year":"2003","unstructured":"Pratt WB, Toft DO (2003) Regulation of signaling protein function and trafficking by the hsp90\/hsp70-based chaperone machinery. Exp Biol Med (Maywood) 228(2):111\u2013133. https:\/\/doi.org\/10.1177\/153537020322800201","journal-title":"Exp Biol Med (Maywood)"},{"issue":"16","key":"5_CR54","doi-asserted-by":"publisher","first-page":"2439","DOI":"10.1042\/BCJ20160005","volume":"473","author":"C Prodromou","year":"2016","unstructured":"Prodromou C (2016) Mechanisms of Hsp90 regulation. Biochem J 473(16):2439\u20132452. https:\/\/doi.org\/10.1042\/BCJ20160005","journal-title":"Biochem J"},{"issue":"6889","key":"5_CR55","doi-asserted-by":"publisher","first-page":"618","DOI":"10.1038\/nature749","volume":"417","author":"C Queitsch","year":"2002","unstructured":"Queitsch C, Sangster TA, Lindquist S (2002) Hsp90 as a capacitor of phenotypic variation. Nature 417(6889):618\u2013624. https:\/\/doi.org\/10.1038\/nature749","journal-title":"Nature"},{"issue":"6709","key":"5_CR56","doi-asserted-by":"publisher","first-page":"336","DOI":"10.1038\/24550","volume":"396","author":"SL Rutherford","year":"1998","unstructured":"Rutherford SL, Lindquist S (1998) Hsp90 as a capacitor for morphological evolution. Nature 396(6709):336\u2013342. https:\/\/doi.org\/10.1038\/24550","journal-title":"Nature"},{"issue":"2","key":"5_CR57","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1016\/S0092-8674(00)80830-2","volume":"101","author":"C Scheufler","year":"2000","unstructured":"Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I (2000) Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell 101(2):199\u2013210. https:\/\/doi.org\/10.1016\/S0092-8674(00)80830-2","journal-title":"Cell"},{"issue":"6","key":"5_CR58","doi-asserted-by":"publisher","first-page":"1007","DOI":"10.1007\/s12551-019-00605-3","volume":"11","author":"TV Seraphim","year":"2019","unstructured":"Seraphim TV, Chakafana G, Shonhai A, Houry WA (2019) Plasmodium falciparum R2TP complex: driver of parasite Hsp90 function. Biophys Rev 11(6):1007\u20131015. https:\/\/doi.org\/10.1007\/s12551-019-00605-3","journal-title":"Biophys Rev"},{"issue":"9","key":"5_CR59","doi-asserted-by":"publisher","first-page":"3552","DOI":"10.1021\/jm901796s","volume":"53","author":"D Shahinas","year":"2010","unstructured":"Shahinas D, Liang M, Datti A, Pillai DR (2010) A repurposing strategy identifies novel synergistic inhibitors of Plasmodium falciparum heat shock protein 90. J Med Chem 53(9):3552\u20133557. https:\/\/doi.org\/10.1021\/jm901796s","journal-title":"J Med Chem"},{"issue":"8","key":"5_CR60","doi-asserted-by":"publisher","first-page":"4207","DOI":"10.1128\/AAC.00328-12","volume":"56","author":"D Shahinas","year":"2012","unstructured":"Shahinas D, Macmullin G, Benedict C, Crandall I, Pillai DR (2012) Harmine is a potent antimalarial targeting Hsp90 and synergizes with chloroquine and artemisinin. Antimicrob Agents Chemother 56(8):4207\u20134213. https:\/\/doi.org\/10.1128\/AAC.00328-12","journal-title":"Antimicrob Agents Chemother"},{"key":"5_CR61","doi-asserted-by":"publisher","first-page":"108468","DOI":"10.1016\/j.abb.2020.108468","volume":"690","author":"NSM Silva","year":"2020","unstructured":"Silva NSM, Torricillas MS, Minari K, Barbosa LRS, Seraphim TV, Borges JC (2020) Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Arch Biochem Biophys 690:108468. https:\/\/doi.org\/10.1016\/j.abb.2020.108468","journal-title":"Arch Biochem Biophys"},{"issue":"1\u20132","key":"5_CR62","doi-asserted-by":"publisher","first-page":"225","DOI":"10.1016\/0378-1119(94)90661-0","volume":"151","author":"XZ Su","year":"1994","unstructured":"Su XZ, Wellems TE (1994) Sequence, transcript characterization and polymorphisms of a Plasmodium falciparum gene belonging to the heat-shock protein (HSP) 90 family. Gene 151(1\u20132):225\u2013230. https:\/\/doi.org\/10.1016\/0378-1119(94)90661-0","journal-title":"Gene"},{"issue":"7","key":"5_CR63","doi-asserted-by":"publisher","first-page":"515","DOI":"10.1038\/nrm2918","volume":"11","author":"M Taipale","year":"2010","unstructured":"Taipale M, Jarosz DF, Lindquist S (2010) HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat Rev Mol Cell Biol 11(7):515\u2013528. https:\/\/doi.org\/10.1038\/nrm2918","journal-title":"Nat Rev Mol Cell Biol"},{"issue":"2","key":"5_CR64","doi-asserted-by":"publisher","first-page":"434","DOI":"10.1016\/j.cell.2014.05.039","volume":"158","author":"M Taipale","year":"2014","unstructured":"Taipale M, Tucker G, Peng J, Krykbaeva I, Lin ZY, Larsen B, Choi H, Berger B, Gingras AC, Lindquist S (2014) A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158(2):434\u2013448. https:\/\/doi.org\/10.1016\/j.cell.2014.05.039","journal-title":"Cell"},{"issue":"1","key":"5_CR65","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1242\/dev.127.1.1","volume":"127","author":"AK Voss","year":"2000","unstructured":"Voss AK, Thomas T, Gruss P (2000) Mice lacking HSP90beta fail to develop a placental labyrinth. Development 127(1):1\u201311. https:\/\/www.ncbi.nlm.nih.gov\/pubmed\/10654595","journal-title":"Development"},{"issue":"13","key":"5_CR66","doi-asserted-by":"publisher","first-page":"6344","DOI":"10.1021\/acs.jmedchem.6b00591","volume":"59","author":"T Wang","year":"2016","unstructured":"Wang T, M\u00e4ser P, Picard D (2016) Inhibition of Plasmodium falciparum Hsp90 contributes to the antimalarial activities of aminoalcohol-carbazoles. J Med Chem 59(13):6344\u20136352. https:\/\/doi.org\/10.1021\/acs.jmedchem.6b00591","journal-title":"J Med Chem"},{"issue":"12","key":"5_CR67","doi-asserted-by":"publisher","first-page":"2813","DOI":"10.1093\/emboj\/19.12.2813","volume":"19","author":"JG Waterkeyn","year":"2000","unstructured":"Waterkeyn JG, Wickham ME, Davern KM, Cooke BM, Coppel RL, Reeder JC, Culvenor JG, Waller RF, Cowman AF (2000) Targeted mutagenesis of Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) disrupts cytoadherence of malaria-infected red blood cells. EMBO J 19(12):2813\u20132823. https:\/\/doi.org\/10.1093\/emboj\/19.12.2813","journal-title":"EMBO J"},{"key":"5_CR68","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s10254-003-0021-1","volume":"151","author":"H Wegele","year":"2004","unstructured":"Wegele H, Muller L, Buchner J (2004) Hsp70 and Hsp90--a relay team for protein folding. Rev Physiol Biochem Pharmacol 151:1\u201344. https:\/\/doi.org\/10.1007\/s10254-003-0021-1","journal-title":"Rev Physiol Biochem Pharmacol"},{"issue":"1\u20132","key":"5_CR69","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1007\/s004300100074","volume":"190","author":"M Wiesgigl","year":"2001","unstructured":"Wiesgigl M, Clos J (2001) The heat shock protein 90 of Leishmania donovani. Med Microbiol Immunol 190(1\u20132):27\u201331. https:\/\/doi.org\/10.1007\/s004300100074","journal-title":"Med Microbiol Immunol"},{"key":"5_CR70","doi-asserted-by":"publisher","first-page":"199","DOI":"10.1002\/9780470515730.ch14","volume":"226","author":"MF Wiser","year":"1999","unstructured":"Wiser MF, Grab DJ, Lanners HN (1999a) An alternative secretory pathway in Plasmodium: more questions than answers. Novartis Found Symp 226:199\u2013211.; discussion 211-194. https:\/\/doi.org\/10.1002\/9780470515730.ch14","journal-title":"Novartis Found Symp"},{"issue":"5","key":"5_CR71","doi-asserted-by":"publisher","first-page":"194","DOI":"10.1016\/s0169-4758(99)01440-4","volume":"15","author":"MF Wiser","year":"1999","unstructured":"Wiser MF, Lanners HN, Bafford RA (1999b) Export of proteins via a novel secretory pathway. Parasitol Today 15(5):194\u2013198. https:\/\/doi.org\/10.1016\/s0169-4758(99)01440-4","journal-title":"Parasitol Today"},{"key":"5_CR72","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1146\/annurev.mi.48.100194.002313","volume":"48","author":"D Zilberstein","year":"1994","unstructured":"Zilberstein D, Shapira M (1994) The role of pH and temperature in the development of Leishmania parasites. Annu Rev Microbiol 48:449\u2013470. https:\/\/doi.org\/10.1146\/annurev.mi.48.100194.002313","journal-title":"Annu Rev Microbiol"}],"container-title":["Advances in Experimental Medicine and Biology","Heat Shock Proteins of Malaria"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/978-3-030-78397-6_5","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,9,26]],"date-time":"2021-09-26T20:17:40Z","timestamp":1632687460000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/978-3-030-78397-6_5"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021]]},"ISBN":["9783030783969","9783030783976"],"references-count":72,"URL":"https:\/\/doi.org\/10.1007\/978-3-030-78397-6_5","relation":{},"ISSN":["0065-2598","2214-8019"],"issn-type":[{"type":"print","value":"0065-2598"},{"type":"electronic","value":"2214-8019"}],"subject":[],"published":{"date-parts":[[2021]]},"assertion":[{"value":"27 September 2021","order":1,"name":"first_online","label":"First Online","group":{"name":"ChapterHistory","label":"Chapter History"}}]}}