{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,25]],"date-time":"2026-07-25T17:33:52Z","timestamp":1785000832349,"version":"3.55.0"},"reference-count":35,"publisher":"Elsevier BV","issue":"4","license":[{"start":{"date-parts":[[2021,7,1]],"date-time":"2021-07-01T00:00:00Z","timestamp":1625097600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,7,1]],"date-time":"2021-07-01T00:00:00Z","timestamp":1625097600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,11,23]],"date-time":"2023-11-23T00:00:00Z","timestamp":1700697600000},"content-version":"vor","delay-in-days":875,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"name":"University of Johannesburg research fund"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Cell Stress and Chaperones"],"published-print":{"date-parts":[[2021,7]]},"DOI":"10.1007\/s12192-021-01212-6","type":"journal-article","created":{"date-parts":[[2021,5,22]],"date-time":"2021-05-22T20:02:12Z","timestamp":1621713732000},"page":"685-693","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":20,"title":["Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1"],"prefix":"10.1016","volume":"26","author":[{"given":"Nicolaas","family":"Salomane","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ofentse J.","family":"Pooe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mthokozisi B.C.","family":"Simelane","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1007\/s12192-021-01212-6_bb0010","doi-asserted-by":"crossref","unstructured":"Alhazmi HA (2019) FT-IR spectroscopy for the identification of binding sites and measurements of the binding interactions of important metal ions with bovine serum albumin. Sci Pharm. https:\/\/doi.org\/10.3390\/scipharm87010005","DOI":"10.3390\/scipharm87010005"},{"key":"10.1007\/s12192-021-01212-6_bb0015","doi-asserted-by":"crossref","unstructured":"Ayeni G, Pooe OJ, Singh M et al (2019) Cytotoxic and antioxidant activities of selected South African medicinal plants. Pharmacogn J:11. https:\/\/doi.org\/10.5530\/PJ.2019.11.234","DOI":"10.5530\/pj.2019.11.234"},{"key":"10.1007\/s12192-021-01212-6_bb0020","doi-asserted-by":"crossref","unstructured":"Bekono BD, Ntie-Kang F, Ongu\u00e9n\u00e9 PA, et al (2020) The potential of anti-malarial compounds derived from African medicinal plants: a review of pharmacological evaluations from 2013 to 2019. Malar. J.","DOI":"10.1186\/s12936-020-03231-7"},{"key":"10.1007\/s12192-021-01212-6_bb0025","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1016\/j.biocel.2007.02.011","article-title":"The Hsp40 proteins of Plasmodium falciparum and other apicomplexa: regulating chaperone power in the parasite and the host","volume":"39","author":"Botha","year":"2007","journal-title":"Int J Biochem Cell Biol"},{"key":"10.1007\/s12192-021-01212-6_bb0030","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1089\/ars.2009.3074","article-title":"Cellular stress responses, the hormesis paradigm, and vitagenes: novel targets for therapeutic intervention in neurodegenerative disorders","volume":"13","author":"Calabrese","year":"2010","journal-title":"Antioxidants Redox Signal"},{"key":"10.1007\/s12192-021-01212-6_bb0035","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.mam.2011.10.007","article-title":"Hormesis, cellular stress response and vitagenes as critical determinants in aging and longevity","volume":"32","author":"Calabrese","year":"2011","journal-title":"Mol Aspects Med"},{"key":"10.1007\/s12192-021-01212-6_bb0040","doi-asserted-by":"crossref","first-page":"112176","DOI":"10.1016\/j.jep.2019.112176","article-title":"A review of the traditional use of southern African medicinal plants for the treatment of malaria","volume":"245","author":"Cock","year":"2019","journal-title":"J Ethnopharmacol"},{"key":"10.1007\/s12192-021-01212-6_bb0045","doi-asserted-by":"crossref","first-page":"295","DOI":"10.3390\/biom9070295","article-title":"Partners in mischief: functional networks of heat shock proteins of Plasmodium falciparum and their influence on parasite virulence","volume":"9","author":"Daniyan","year":"2019","journal-title":"Biomolecules"},{"key":"10.1007\/s12192-021-01212-6_bb0050","doi-asserted-by":"crossref","first-page":"2729","DOI":"10.1016\/j.jmb.2019.05.026","article-title":"Intermolecular interactions between Hsp90 and Hsp70","volume":"431","author":"Doyle","year":"2019","journal-title":"J Mol Biol"},{"key":"10.1007\/s12192-021-01212-6_bb0055","doi-asserted-by":"crossref","unstructured":"Hands JR, Clemens G, Stables R et al (2016) Brain tumour differentiation: rapid stratified serum diagnostics via attenuated total reflection Fourier-transform infrared spectroscopy. J Neurooncol. https:\/\/doi.org\/10.1007\/s11060-016-2060-x","DOI":"10.1007\/s11060-016-2060-x"},{"key":"10.1007\/s12192-021-01212-6_bb0060","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1038\/nrm2941","article-title":"The HSP70 chaperone machinery: J proteins as drivers of functional specificity","volume":"11","author":"Kampinga","year":"2010","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.1007\/s12192-021-01212-6_bb0065","doi-asserted-by":"crossref","first-page":"113330","DOI":"10.1016\/j.ejmech.2021.113330","article-title":"European Journal of Medicinal Chemistry Design and synthesis of quinoline-pyrimidine inspired hybrids as potential plasmodial inhibitors","volume":"217","author":"Kayamba","year":"2021","journal-title":"Eur J Med Chem"},{"key":"10.1007\/s12192-021-01212-6_bb0070","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1111\/j.1745-7270.2007.00320.x","article-title":"Fourier transform infrared spectroscopic analysis of protein secondary structures","volume":"39","author":"Kong","year":"2007","journal-title":"Acta Biochim Biophys Sin (Shanghai)"},{"key":"10.1007\/s12192-021-01212-6_bb0075","doi-asserted-by":"crossref","unstructured":"Kyaw A, Maung-U K, Toe T (1985) Determination of inorganic phosphate with molybdate and Triton X-100 without reduction. Anal Biochem. https:\/\/doi.org\/10.1016\/0003-2697(85)90354-9","DOI":"10.1016\/0003-2697(85)90354-9"},{"key":"10.1007\/s12192-021-01212-6_bb0080","doi-asserted-by":"crossref","unstructured":"Litvinov RI, Faizullin DA, Zuev YF, Weisel JW (2012) The \u03b1-helix to \u03b2-sheet transition in stretched and compressed hydrated fibrin clots. Biophys J. https:\/\/doi.org\/10.1016\/j.bpj.2012.07.046","DOI":"10.1016\/j.bpj.2012.07.046"},{"key":"10.1007\/s12192-021-01212-6_bb0085","doi-asserted-by":"crossref","unstructured":"Mabate B, Zininga T, Ramatsui L et al (2018) Structural and biochemical characterization of Plasmodium falciparum Hsp70-x reveals functional versatility of its C-terminal EEVN motif. Proteins Struct Funct Bioinforma. https:\/\/doi.org\/10.1002\/prot.25600","DOI":"10.1002\/prot.25600"},{"key":"10.1007\/s12192-021-01212-6_bb0090","doi-asserted-by":"crossref","first-page":"3235","DOI":"10.2147\/DDDT.S257494","article-title":"Potential impact of the multi-target drug approach in the treatment of some complex diseases","volume":"14","author":"Makhoba","year":"2020","journal-title":"Drug Des Devel Ther"},{"key":"10.1007\/s12192-021-01212-6_bb0095","doi-asserted-by":"crossref","unstructured":"Matambo TS, Odunuga OO, Boshoff A, Blatch GL (2004) Overproduction, purification, and characterization of the Plasmodium falciparum heat shock protein 70. Protein Expr Purif. https:\/\/doi.org\/10.1016\/j.pep.2003.09.010","DOI":"10.1016\/j.pep.2003.09.010"},{"key":"10.1007\/s12192-021-01212-6_bb0100","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.arr.2007.08.007","article-title":"Hormesis defined","volume":"7","author":"Mattson","year":"2008","journal-title":"Ageing Res Rev"},{"key":"10.1007\/s12192-021-01212-6_bb0105","doi-asserted-by":"crossref","unstructured":"Miller DJ, Fort PE (2018) Heat shock proteins regulatory role in neurodevelopment. Front. Neurosci.","DOI":"10.3389\/fnins.2018.00821"},{"key":"10.1007\/s12192-021-01212-6_bb0110","doi-asserted-by":"crossref","unstructured":"Misra G, Ramachandran R (2009) Hsp70-1 from Plasmodium falciparum: protein stability, domain analysis and chaperone activity. Biophys Chem. https:\/\/doi.org\/10.1016\/j.bpc.2009.03.006","DOI":"10.1016\/j.bpc.2009.03.006"},{"key":"10.1007\/s12192-021-01212-6_bb0115","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s12936-018-2439-6","article-title":"Isolation, characterization, and biological evaluation of a potent anti-malarial drimane sesquiterpene from Warburgia salutaris stem bark","volume":"17","author":"Nyaba","year":"2018","journal-title":"Malar J"},{"key":"10.1007\/s12192-021-01212-6_bb0120","doi-asserted-by":"crossref","unstructured":"Opoku F, Govender PP, Pooe OJ, Simelane MBC (2019) Evaluating iso-mukaadial acetate and ursolic acid acetate as plasmodium falciparum hypoxanthineguanine-xanthine phosphoribosyltransferase inhibitors. Biomolecules. https:\/\/doi.org\/10.3390\/biom9120861","DOI":"10.3390\/biom9120861"},{"key":"10.1007\/s12192-021-01212-6_bb0125","doi-asserted-by":"crossref","first-page":"503","DOI":"10.2174\/0929866524666170214141909","article-title":"Plasmodium falciparum heat shock protein 70 lacks immune modulatory activity","volume":"24","author":"Pooe","year":"2017","journal-title":"Protein Pept Lett"},{"key":"10.1007\/s12192-021-01212-6_bb0130","doi-asserted-by":"crossref","first-page":"34","DOI":"10.3389\/fmolb.2015.00034","article-title":"Plasmodial HSP70s are functionally adapted to the malaria parasite life cycle","volume":"2","author":"Przyborski","year":"2015","journal-title":"Front Mol Biosci"},{"key":"10.1007\/s12192-021-01212-6_bb0135","doi-asserted-by":"crossref","unstructured":"Shonhai A (2014) The role of Hsp70s in the development and pathogenicity of plasmodium species. In: Heat Shock Proteins of Malaria","DOI":"10.1007\/978-94-007-7438-4_3"},{"key":"10.1007\/s12192-021-01212-6_bb0140","doi-asserted-by":"crossref","unstructured":"Shonhai A, Boshoff A, Blatch GL (2007) The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum. Protein Sci. https:\/\/doi.org\/10.1110\/ps.072918107","DOI":"10.1110\/ps.072918107"},{"key":"10.1007\/s12192-021-01212-6_bb0145","doi-asserted-by":"crossref","unstructured":"Shonhai A, Botha M, de Beer T et al (2008) Structure-function study of a Plasmodium falciparum Hsp70 using three dimensional modelling and in vitro analyses. Protein Pept Lett. https:\/\/doi.org\/10.2174\/092986608786071067","DOI":"10.2174\/092986608786071067"},{"key":"10.1007\/s12192-021-01212-6_bb0150","doi-asserted-by":"crossref","first-page":"12313","DOI":"10.3390\/molecules181012313","article-title":"Anti-plasmodial activity of some zulu medicinal plants and of some triterpenes isolated from them","volume":"18","author":"Simelane","year":"2013","journal-title":"Molecules"},{"key":"10.1007\/s12192-021-01212-6_bb0155","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/antiox9090824","article-title":"Anti-inflammatory and anti-oxidant activity of hidrox\u00ae in rotenone-induced Parkinson\u2019s disease in mice","volume":"9","author":"Siracusa","year":"2020","journal-title":"Antioxidants"},{"key":"10.1007\/s12192-021-01212-6_bb0160","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.pep.2011.01.005","article-title":"Co-expression of the Plasmodium falciparum molecular chaperone, PfHsp70, improves the heterologous production of the antimalarial drug target GTP cyclohydrolase I, PfGCHI","volume":"77","author":"Stephens","year":"2011","journal-title":"Protein Expr Purif"},{"key":"10.1007\/s12192-021-01212-6_bb0165","doi-asserted-by":"crossref","first-page":"5661","DOI":"10.1074\/jbc.M111.275057","article-title":"Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity","volume":"287","author":"Xu","year":"2012","journal-title":"J Biol Chem"},{"key":"10.1007\/s12192-021-01212-6_bb0170","doi-asserted-by":"crossref","first-page":"208","DOI":"10.3844\/ajbbsp.2014.208.210","article-title":"Are heat shock proteins druggable candidates?","volume":"10","author":"Zininga","year":"2014","journal-title":"Am J Biochem Biotechnol"},{"key":"10.1007\/s12192-021-01212-6_bb0175","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0135326","article-title":"Plasmodium falciparum hop (PfHop) interacts with the Hsp70 chaperone in a nucleotide-dependent fashion and exhibits ligand selectivity","volume":"10","author":"Zininga","year":"2015","journal-title":"PLoS One"},{"key":"10.1007\/s12192-021-01212-6_bb0180","doi-asserted-by":"crossref","unstructured":"Zininga T, Pooe OJ, Makhado PB et al (2017) Polymyxin B inhibits the chaperone activity of Plasmodium falciparum Hsp70. Cell Stress Chaperones. https:\/\/doi.org\/10.1007\/s12192-017-0797-6","DOI":"10.1007\/s12192-017-0797-6"}],"container-title":["Cell Stress and Chaperones"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12192-021-01212-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12192-021-01212-6\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1355814523004029?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1355814523004029?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12192-021-01212-6.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T01:17:49Z","timestamp":1761182269000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1355814523004029"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,7]]},"references-count":35,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2021,7]]}},"alternative-id":["S1355814523004029"],"URL":"https:\/\/doi.org\/10.1007\/s12192-021-01212-6","relation":{},"ISSN":["1355-8145"],"issn-type":[{"value":"1355-8145","type":"print"}],"subject":[],"published":{"date-parts":[[2021,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Iso-mukaadial acetate and ursolic acid acetate inhibit the chaperone activity of Plasmodium falciparum heat shock protein 70-1","name":"articletitle","label":"Article Title"},{"value":"Cell Stress and Chaperones","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1007\/s12192-021-01212-6","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2021 THE AUTHOR(S). Published by Elsevier Inc on behalf of Cell Stress Society International","name":"copyright","label":"Copyright"}]}}