{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T15:26:32Z","timestamp":1787498792824,"version":"build-2736575974"},"reference-count":56,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2024,11,22]],"date-time":"2024-11-22T00:00:00Z","timestamp":1732233600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100006769","name":"Russian Science Foundation","doi-asserted-by":"publisher","award":["23-15-00472"],"award-info":[{"award-number":["23-15-00472"]}],"id":[{"id":"10.13039\/501100006769","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nanomaterials"],"abstract":"<jats:p>Anti-cancer targeted therapy is a promising approach. However, the identification of target molecules over-expressed in a wide range of tumors remains a significant challenge. The aim of this study was to analyze the expression of cell membrane-exposed heat shock protein 70 kDa (mHSP70) on different tumor cells and to develop a nanoscale delivery system based on a monoclonal antibody (mAb) that recognizes mHSP70 and uses chitosan core\u2013shell nanoparticles (NPs). Several types of tumor cells (breast, pancreas, colon, prostate cancers, and some lymphomas) expressed mHSP70 as was determined by flow cytometry and confocal microscopy both in 2D and 3D cultures. Core NPs were formed by chitosan (C) conjugated to allocolchicinoid, which was used as a model drug (D). mAbs (A) targeting mHSP70 were complexed with succinylchitosan and used as NP shells forming final CAD-NPs. These NPs were characterized by size, charge, and functional activity. CAD-NPs were shown to have additional toxicity in comparison with CD-NPs in mHSP7-positive cells. Taken collectively, this study shows that mAb to mHSP70 can be used as a targeting vector in antitumor therapy.<\/jats:p>","DOI":"10.3390\/nano14231873","type":"journal-article","created":{"date-parts":[[2024,11,22]],"date-time":"2024-11-22T06:41:48Z","timestamp":1732257708000},"page":"1873","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Core\u2013Shell Chitosan Particles Targeting Membrane-Bound Heat Shock Protein 70 for Cancer Therapy"],"prefix":"10.3390","volume":"14","author":[{"given":"Elena V.","family":"Svirshchevskaya","sequence":"first","affiliation":[{"name":"Laboratory of Cell Interactions, Department of Immunology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentina V.","family":"Kostenko","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Interactions, Department of Immunology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8996-2905","authenticated-orcid":false,"given":"Anna A.","family":"Boyko","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Interactions, Department of Immunology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8539-2239","authenticated-orcid":false,"given":"Maxim","family":"Shevtsov","sequence":"additional","affiliation":[{"name":"Department of Radiation Oncology, Klinikum Rechts der Isar, Technical University of Munich, 81675 Munich, Germany"},{"name":"Laboratory of Biomedical Nanotechnologies, Institute of Cytology of the Russian Academy of Sciences (RAS), 194064 St. Petersburg, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6083-6588","authenticated-orcid":false,"given":"Roman V.","family":"Kholodenko","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Interactions, Department of Immunology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria V.","family":"Grechikhina","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Interactions, Department of Immunology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5640-2696","authenticated-orcid":false,"given":"Iuliia A.","family":"Gracheva","sequence":"additional","affiliation":[{"name":"Department of Organic Chemistry, Nizhni Novgorod State University, 603950 Nizhni Novgorod, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexey Yu.","family":"Fedorov","sequence":"additional","affiliation":[{"name":"Department of Organic Chemistry, Nizhni Novgorod State University, 603950 Nizhni Novgorod, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexander M.","family":"Sapozhnikov","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Interactions, Department of Immunology, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, 117997 Moscow, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,11,22]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1007\/s10555-011-9282-3","article-title":"Modulation of tumor immunity by therapeutic monoclonal antibodies","volume":"30","author":"Teillaud","year":"2011","journal-title":"Cancer Metastasis Rev."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"17240","DOI":"10.3402\/nano.v3i0.17240","article-title":"Detection of biomarkers using recombinant antibodies coupled to nanostructured platforms","volume":"3","author":"Kierny","year":"2012","journal-title":"Nano Rev."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.ymeth.2007.06.006","article-title":"Heat shock protein 70 (Hsp70): Membrane location, export and immunological relevance","volume":"43","author":"Multhoff","year":"2007","journal-title":"Methods"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1073\/pnas.1016065108","article-title":"Targeting membrane heat-shock protein 70 (Hsp70) on tumors by cmHsp70.1 antibody","volume":"108","author":"Stangl","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1007\/s12192-021-01228-y","article-title":"The interaction of heat shock proteins with cellular membranes: A historical perspective","volume":"26","author":"Hightower","year":"2021","journal-title":"Cell Stress Chaperones"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"19233","DOI":"10.1038\/s41598-023-46131-x","article-title":"A new look at Hsp70 activity in phosphatidylserine-enriched membranes: Chaperone-induced quasi-interdigitated lipid phase","volume":"6","author":"Tagaeva","year":"2023","journal-title":"Sci. Rep."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Makky, A., Czajor, J., Konovalov, O., Zhakhov, A., Ischenko, A., Behl, A., Singh, S., Abuillan, W., and Shevtsov, M. (2023). X-ray reflectivity study of the heat shock protein Hsp70 interaction with an artificial cell membrane model. Sci. Rep., 13.","DOI":"10.1038\/s41598-023-46066-3"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1007\/s12192-018-0879-0","article-title":"Molecular AFM imaging of Hsp70-1A association with dipalmitoyl phosphatidylserine reveals membrane blebbing in the presence of cholesterol","volume":"23","author":"Lamprecht","year":"2018","journal-title":"Cell Stress Chaperones"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.bbagen.2008.10.005","article-title":"Binding of Silurus asotus lectin to Gb3 on Raji cells causes disappearance of membrane-bound form of HSP70","volume":"1790","author":"Sugawara","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Gehrmann, M., Liebisch, G., Schmitz, G., Anderson, R., Steinem, C., De Maio, A., Pockley, G., and Multhoff, G. (2008). Tumor-specific Hsp70 plasma membrane localization is enabled by the glycosphingolipid Gb3. PLoS ONE, 3.","DOI":"10.1371\/journal.pone.0001925"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1038\/s41580-019-0133-3","article-title":"The Hsp70 chaperone network","volume":"20","author":"Rosenzweig","year":"2019","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_12","doi-asserted-by":"crossref","unstructured":"Joshi, P., Garg, S., Mani, S., Shoaib, R., Jakhar, K., Almuqdadi, H.T.A., Sonar, S., Marothia, M., Behl, A., and Biswas, S. (2024). Targeting host inducible-heat shock protein 70 with PES-Cl is a promising antiviral strategy against SARS-CoV-2 infection and pathogenesis. Int. J. Biol. Macromol., 279.","DOI":"10.1016\/j.ijbiomac.2024.135069"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"109918","DOI":"10.1016\/j.isci.2024.109918","article-title":"Targeting PfProhibitin 2-Hu-Hsp70A1A complex as a unique approach towards malaria vaccine development","volume":"7","author":"Marothia","year":"2024","journal-title":"iScience"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Breuninger, S., Stangl, S., Werner, C., Sievert, W., Lobinger, D., Foulds, G.A., Wagner, S., Pickhard, A., Piontek, G., and Kokowski, K. (2018). Membrane Hsp70-A Novel Target for the Isolation of Circulating Tumor Cells After Epithelial-to-Mesenchymal Transition. Front. Oncol., 8.","DOI":"10.3389\/fonc.2018.00497"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0165-2478(00)00256-X","article-title":"Splenic murine cytotoxic cells recognize surface HSP70 on culture-adapted EL-4 lymphoma cells","volume":"74","author":"Ponomarev","year":"2000","journal-title":"Immunol. Lett."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1017\/S1462399401003556","article-title":"Heat shock proteins in health and disease: Therapeutic targets or therapeutic agents?","volume":"3","author":"Pockley","year":"2001","journal-title":"Expert Rev. Mol. Med."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1152\/ajpcell.00364.2003","article-title":"Cytokine function of heat shock proteins","volume":"286","author":"Tsan","year":"2004","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1080\/02656730902902001","article-title":"Activation of natural killer cells by heat shock protein 70","volume":"25","author":"Multhoff","year":"2009","journal-title":"Int. J. Hyperthermia."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1038\/nri749","article-title":"Roles of heat-shock proteins in innate and adaptive immunity","volume":"2","author":"Srivastava","year":"2002","journal-title":"Nat. Rev. Immunol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1126\/science.1071059","article-title":"The danger model: A renewed sense of self","volume":"296","author":"Matzinger","year":"2002","journal-title":"Science"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1111\/j.1399-0039.2004.00299.x","article-title":"The heat-shock protein receptors: Some answers and more questions","volume":"64","author":"Binder","year":"2004","journal-title":"Tissue Antigens"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1038\/nri1593","article-title":"Heat-shock proteins induce T-cell regulation of chronic inflammation","volume":"5","author":"Prakken","year":"2005","journal-title":"Nat. Rev. Immunol."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1379\/1466-1268(2002)007<0017:HSPIAP>2.0.CO;2","article-title":"Heat shock protein 70 is a potent activator of the human complement system","volume":"7","author":"Singh","year":"2002","journal-title":"Cell Stress Chaperones"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"1636","DOI":"10.1096\/fj.04-2088com","article-title":"Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability","volume":"18","author":"Arispe","year":"2004","journal-title":"FASEB J."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"6268","DOI":"10.1158\/0008-5472.CAN-18-0707","article-title":"Preclinical Evaluation of the Hsp70 Peptide Tracer TPP-PEG24-DFO [89Zr] for Tumor-Specific PET\/CT Imaging","volume":"78","author":"Stangl","year":"2018","journal-title":"Cancer Res."},{"key":"ref_26","first-page":"203","article-title":"Functional characterization of chitin and chitosan","volume":"3","author":"Aranaz","year":"2009","journal-title":"Curr. Chem. Biol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"4532","DOI":"10.1016\/j.ijbiomac.2020.09.042","article-title":"Chitosan: Structural modification, biological activity and application","volume":"164","author":"Wang","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1177\/0885328208091562","article-title":"Review paper: Chitosan derivatives as promising materials for controlled drug delivery","volume":"23","author":"Prabaharan","year":"2008","journal-title":"J. Biomater. Appl."},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Tang, W., Wang, J., Hou, H., Li, Y., Wang, J., Fu, J., Lu, L., Gao, D., Liu, Z., and Zhao, F. (2023). Review: Application of chitosan and its derivatives in medical materials. Int. J. Biol. Macromol., 240.","DOI":"10.1016\/j.ijbiomac.2023.124398"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"571","DOI":"10.4172\/2161-0444.1000401","article-title":"Antitumor Activity of Furanoallocolchicinoid-Chitosan Conjugate","volume":"6","author":"Svirshchevskaya","year":"2016","journal-title":"Med. Chem."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Hawash, M. (2022). Recent Advances of Tubulin Inhibitors Targeting the Colchicine Binding Site for Cancer Therapy. Biomolecules, 12.","DOI":"10.3390\/biom12121843"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"116543","DOI":"10.1016\/j.ejmech.2024.116543","article-title":"Dual-target inhibitors of colchicine binding site for cancer treatment","volume":"274","author":"Lu","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1103","DOI":"10.1158\/1535-7163.MCT-21-0899","article-title":"Colchicine-Binding Site Agent CH-2-77 as a Potent Tubulin Inhibitor Suppressing Triple-Negative Breast Cancer","volume":"21","author":"Deng","year":"2022","journal-title":"Mol. Cancer Ther."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1134\/S0003683818010118","article-title":"Study of the protective activity of chitosan hydrolyzate against septoria leaf blotch of wheat and brown spot of tobacco","volume":"54","author":"Shagdarova","year":"2018","journal-title":"Appl. Biochem. Microbiol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/S0008-6215(00)84614-5","article-title":"Preparation of partially N-succinylated chitosans and their cross-linked gels","volume":"88","author":"Yamaguchi","year":"1981","journal-title":"Carbohydr. Res."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Herdiana, Y., Wathoni, N., Shamsuddin, S., Joni, I.M., and Muchtaridi, M. (2021). Chitosan-Based Nanoparticles of Targeted Drug Delivery System in Breast Cancer Treatment. Polymers, 13.","DOI":"10.3390\/polym13111717"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"e202200127","DOI":"10.1002\/cmdc.202200127","article-title":"Biphasic Dose-Dependent G0\/G1 and G2\/M Cell-Cycle Arrest by Synthetic 2,3-Arylpyridylindole Derivatives in A549 Lung Cancer Cells","volume":"17","author":"Chaiputtanapun","year":"2022","journal-title":"ChemMedChem"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1084\/jem.20011097","article-title":"Antitumor monoclonal antibodies enhance cross-presentation ofcCellular antigens and the generation of myeloma-specific killer T cells by dendritic cells","volume":"195","author":"Dhodapkar","year":"2002","journal-title":"J. Exp. Med."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"8373","DOI":"10.2147\/IJN.S472433","article-title":"Chitosan nanoparticles for targeted cancer therapy: A review of stimuli-responsive, passive, and active targeting strategies","volume":"19","author":"Alkhudhair","year":"2024","journal-title":"Int. J. Nanomed."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Sachdeva, B., Sachdeva, P., Negi, A., Ghosh, S., Han, S., Dewanjee, S., Jha, S.K., Bhaskar, R., Sinha, J.K., and Paiva-Santos, A.C. (2023). Chitosan nanoparticles-based cancer drug delivery: Application and challenges. Mar. Drugs, 21.","DOI":"10.3390\/md21040211"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1080\/21691401.2017.1423494","article-title":"Chitosan nanoparticles triggered the induction of ROS-mediated cytoprotective autophagy in cancer cells","volume":"46","author":"Wang","year":"2018","journal-title":"Artif. Cells Nanomed. Biotechnol."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1080\/21691401.2019.1577876","article-title":"Chitosan nanoparticles induced the antitumor effect in hepatocellular carcinoma cells by regulating ROS-mediated mitochondrial damage and endoplasmic reticulum stress","volume":"47","author":"Jiang","year":"2019","journal-title":"Artif. Cells Nanomed. Biotechnol."},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Sun, Y., and Davis, E. (2021). Nanoplatforms for targeted stimuli-responsive drug delivery: A review of platform materials and stimuli-responsive release and targeting mechanisms. Nanomaterials, 11.","DOI":"10.3390\/nano11030746"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Rahim, M.A., Jan, N., Khan, S., Shah, H., Madni, A., Khan, A., Jabar, A., Khan, S., Elhissi, A., and Hussain, Z. (2021). Recent advancements in stimuli responsive drug delivery platforms for active and passive cancer targeting. Cancers, 13.","DOI":"10.3390\/cancers13040670"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.jconrel.2011.03.027","article-title":"Comparative study of photosensitizer loaded and conjugated glycol chitosan nanoparticles for cancer therapy","volume":"152","author":"Lee","year":"2011","journal-title":"J. Control Release"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1022","DOI":"10.1021\/bc300012g","article-title":"Iodinated photosensitizing chitosan: Self-assembly into tumor-homing nanoparticles with enhanced singlet oxygen generation","volume":"23","author":"Lim","year":"2012","journal-title":"Bioconjug. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.ijpharm.2013.06.035","article-title":"Ursodeoxycholic acid-conjugated chitosan for photodynamic treatment of HuCC-T1 human cholangiocarcinoma cells","volume":"454","author":"Lee","year":"2013","journal-title":"Int. J. Pharm."},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Al-Nemrawi, N., Hameedat, F., Al-Husein, B., and Nimrawi, S. (2022). Photolytic controlled release formulation of methotrexate loaded in Chitosan\/TiO2 nanoparticles for breast cancer. Pharmaceuticals, 15.","DOI":"10.3390\/ph15020149"},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Choi, Y., Han, H., Jeon, S., Yoon, H.Y., Kim, H., Kwon, I.C., and Kim, K. (2020). Deep tumor penetration of doxorubicin-loaded glycol chitosan nanoparticles using high-intensity focused ultrasound. Pharmaceutics, 12.","DOI":"10.3390\/pharmaceutics12100974"},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"Yoon, K., Jung, S., Ryu, J., Park, H.J., Oh, H.K., and Kook, M.S. (2023). Redox-sensitive delivery of doxorubicin from nanoparticles of poly(ethylene glycol)-chitosan copolymer for treatment of drug-resistant oral cancer cells. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms241813704"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/j.ijbiomac.2017.02.030","article-title":"Enhanced apoptotic and anticancer potential of paclitaxel loaded biodegradable nanoparticles based on chitosan","volume":"98","author":"Gupta","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Lazer, L.M., Kesavan, Y., Gor, R., Ramachandran, I., Pathak, S., Narayan, S., Anbalagan, M., and Ramalingam, S. (2022). Targeting colon cancer stem cells using novel doublecortin like kinase 1 antibody functionalized folic acid conjugated hesperetin encapsulated chitosan nanoparticles. Colloids Surf. B Biointerfaces, 217.","DOI":"10.1016\/j.colsurfb.2022.112612"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1016\/j.colsurfb.2018.10.007","article-title":"Trastuzumab decorated TPGS-g-chitosan nanoparticles for targeted breast cancer therapy","volume":"173","author":"Kumar","year":"2019","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"2025","DOI":"10.1158\/2767-9764.CRC-24-0094","article-title":"Membrane-bound heat shock protein mHsp70 is required for migration and invasion of brain tumors","volume":"4","author":"Shevtsov","year":"2024","journal-title":"Cancer Res. Commun."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Kimm, M.A., Shevtsov, M., Werner, C., Sievert, W., Zhiyuan, W., Schoppe, O., Menze, B.H., Rummeny, E.J., Proksa, R., and Bystrova, O. (2020). Gold Nanoparticle Mediated Multi-Modal CT Imaging of Hsp70 Membrane-Positive Tumors. Cancers, 12.","DOI":"10.3390\/cancers12051331"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Du, S., Liu, Y., Yuan, Y., Wang, Y., Chen, Y., Wang, S., and Chi, Y. (2022). Advances in the study of HSP70 inhibitors to enhance the sensitivity of tumor cells to radiotherapy. Front. Cell Dev. Biol., 10.","DOI":"10.3389\/fcell.2022.942828"}],"container-title":["Nanomaterials"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2079-4991\/14\/23\/1873\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:37:31Z","timestamp":1760114251000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2079-4991\/14\/23\/1873"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,11,22]]},"references-count":56,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2024,12]]}},"alternative-id":["nano14231873"],"URL":"https:\/\/doi.org\/10.3390\/nano14231873","relation":{},"ISSN":["2079-4991"],"issn-type":[{"value":"2079-4991","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,11,22]]}}}