{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T02:46:25Z","timestamp":1790822785558,"version":"4.1.0"},"reference-count":130,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T00:00:00Z","timestamp":1675209600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,12,16]],"date-time":"2022-12-16T00:00:00Z","timestamp":1671148800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000268","name":"BBSRC","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000268","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000289","name":"Cancer Research UK","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000289","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["mcponline.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular & Cellular Proteomics"],"published-print":{"date-parts":[[2023,2]]},"DOI":"10.1016\/j.mcpro.2022.100485","type":"journal-article","created":{"date-parts":[[2022,12,19]],"date-time":"2022-12-19T20:17:26Z","timestamp":1671481046000},"page":"100485","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":7,"title":["Native Size-Exclusion Chromatography\u2013Based Mass Spectrometry Reveals New Components of the Early Heat Shock Protein 90 Inhibition Response Among Limited Global Changes"],"prefix":"10.1016","volume":"22","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1952-259X","authenticated-orcid":false,"given":"Rahul S.","family":"Samant","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8311-8685","authenticated-orcid":false,"given":"Silvia","family":"Batista","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8579-2267","authenticated-orcid":false,"given":"Mark","family":"Larance","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1441-4162","authenticated-orcid":false,"given":"Bugra","family":"Ozer","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1744-6071","authenticated-orcid":false,"given":"Christopher I.","family":"Milton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2601-238X","authenticated-orcid":false,"given":"Isabell","family":"Bludau","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6197-6694","authenticated-orcid":false,"given":"Estelle","family":"Wu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0975-1121","authenticated-orcid":false,"given":"Laura","family":"Biggins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5006-3507","authenticated-orcid":false,"given":"Simon","family":"Andrews","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8061-6678","authenticated-orcid":false,"given":"Alexia","family":"Hervieu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7032-0227","authenticated-orcid":false,"given":"Harvey E.","family":"Johnston","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3367-2519","authenticated-orcid":false,"given":"Bissan","family":"Al-Lazikhani","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6204-6045","authenticated-orcid":false,"given":"Angus I.","family":"Lamond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9342-1290","authenticated-orcid":false,"given":"Paul A.","family":"Clarke","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1659-3034","authenticated-orcid":false,"given":"Paul","family":"Workman","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.mcpro.2022.100485_bib1","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1146\/annurev-cancerbio-030518-055533","article-title":"HSP90: enabler of cancer adaptation","volume":"3","author":"Jaeger","year":"2019","journal-title":"Annu. Rev. Cancer Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib2","article-title":"Linking hsp90\u2019s role as an evolutionary capacitator to the development of cancer","volume":"28","author":"Lacey","year":"2021","journal-title":"Cancer Treat. Res. Commun."},{"key":"10.1016\/j.mcpro.2022.100485_bib3","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1007\/978-3-030-40204-4_11","article-title":"Reflections and outlook on targeting HSP90, HSP70 and HSF1 in cancer: a personal perspective","volume":"1243","author":"Workman","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib4","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1007\/978-1-4939-7477-1_29","article-title":"Clinical evaluation and biomarker profiling of Hsp90 inhibitors","volume":"1709","author":"Yuno","year":"2018","journal-title":"Met. Mol. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib5","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.1158\/1541-7786.MCR-15-0234","article-title":"Maximizing the therapeutic potential of HSP90 inhibitors","volume":"13","author":"Butler","year":"2015","journal-title":"Mol. Cancer Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib6","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.chembiol.2020.10.005","article-title":"HSP90 inhibition enhances cancer immunotherapy by modulating the surface expression of multiple immune checkpoint proteins","volume":"28","author":"Zavareh","year":"2021","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib7","doi-asserted-by":"crossref","first-page":"11524","DOI":"10.1200\/JCO.2021.39.15_suppl.11524","volume":"39","author":"Honma","year":"2021","journal-title":"J.\u00a0Clin. Oncol."},{"key":"10.1016\/j.mcpro.2022.100485_bib8","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1007\/s40265-022-01764-6","article-title":"Pimitespib: first approval","volume":"82","author":"Hoy","year":"2022","journal-title":"Drugs"},{"key":"10.1016\/j.mcpro.2022.100485_bib9","doi-asserted-by":"crossref","first-page":"3269","DOI":"10.1007\/s00705-017-3511-1","article-title":"HSP90: a promising broad-spectrum antiviral drug target","volume":"162","author":"Wang","year":"2017","journal-title":"Arch. Virol."},{"key":"10.1016\/j.mcpro.2022.100485_bib10","doi-asserted-by":"crossref","DOI":"10.1016\/j.isci.2021.103412","article-title":"Oral Hsp90 inhibitor SNX-5422 attenuates SARS-CoV-2 replication and dampens inflammation in airway cells","volume":"24","author":"Goswami","year":"2021","journal-title":"iScience"},{"key":"10.1016\/j.mcpro.2022.100485_bib11","doi-asserted-by":"crossref","first-page":"1048","DOI":"10.1080\/15384101.2018.1475828","article-title":"Hsp90 inhibitors as senolytic drugs to extend healthy aging","volume":"17","author":"Fuhrmann-Stroissnigg","year":"2018","journal-title":"Cell Cycle"},{"key":"10.1016\/j.mcpro.2022.100485_bib12","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.celrep.2019.03.044","article-title":"Transcriptomics-based screening identifies pharmacological inhibition of Hsp90 as a means to defer aging","volume":"27","author":"Janssens","year":"2019","journal-title":"Cell Rep."},{"key":"10.1016\/j.mcpro.2022.100485_bib13","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1021\/cb600224w","article-title":"Tumor selectivity of Hsp90 inhibitors: The explanation remains elusive","volume":"1","author":"Chiosis","year":"2006","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib14","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.molmed.2003.12.005","article-title":"Altered states: selectively drugging the Hsp90 cancer chaperone","volume":"10","author":"Workman","year":"2004","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.mcpro.2022.100485_bib15","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nature01913","article-title":"A\u00a0high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors","volume":"425","author":"Kamal","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.mcpro.2022.100485_bib16","doi-asserted-by":"crossref","first-page":"2162","DOI":"10.1074\/jbc.REV118.002811","article-title":"Chaperome heterogeneity and its implications for cancer study and treatment","volume":"294","author":"Wang","year":"2019","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.mcpro.2022.100485_bib17","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.coisb.2019.03.008","article-title":"Proteostasis network deregulation signatures as biomarkers for pharmacological disease intervention","volume":"15","author":"Brehme","year":"2019","journal-title":"Curr. Opin. Sys Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib18","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.1080\/14789450.2017.1389649","article-title":"Proteomic interrogation of HSP90 and insights for medical research","volume":"14","author":"Weidenauer","year":"2017","journal-title":"Exp. Rev. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib19","doi-asserted-by":"crossref","first-page":"3239","DOI":"10.1158\/0008-5472.CAN-06-2968","article-title":"Gene and protein expression profiling of human ovarian cancer cells treated with the heat shock protein 90 inhibitor 17-allylamino-17-demethoxygeldanamycin","volume":"67","author":"Maloney","year":"2007","journal-title":"Cancer Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib20","doi-asserted-by":"crossref","first-page":"2603","DOI":"10.1002\/pmic.200700108","article-title":"Proteome-wide changes induced by the Hsp90 inhibitor, geldanamycin in anaplastic large cell lymphoma cells","volume":"7","author":"Schumacher","year":"2007","journal-title":"Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib21","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.014654","article-title":"Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response","volume":"11","author":"Sharma","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib22","doi-asserted-by":"crossref","first-page":"3697","DOI":"10.1021\/pr400321x","article-title":"The anticancer drug AUY922 generates a proteomics fingerprint that is highly conserved among structurally diverse Hsp90 inhibitors","volume":"12","author":"Voruganti","year":"2013","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib23","doi-asserted-by":"crossref","DOI":"10.1074\/mcp.M111.016675","article-title":"Systematic identification of the HSP90 candidate regulated proteome","volume":"11","author":"Wu","year":"2012","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib24","doi-asserted-by":"crossref","first-page":"674","DOI":"10.1016\/j.bbamcr.2011.09.001","article-title":"The role of Hsp90 in protein complex assembly","volume":"1823","author":"Makhnevych","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.mcpro.2022.100485_bib25","doi-asserted-by":"crossref","first-page":"2422","DOI":"10.1073\/pnas.1912897117","article-title":"Widespread remodeling of proteome solubility in response to different protein homeostasis stresses","volume":"117","author":"Sui","year":"2020","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.mcpro.2022.100485_bib26","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1038\/nature19807","article-title":"The epichaperome is an integrated chaperome network that facilitates tumour survival","volume":"538","author":"Rodina","year":"2016","journal-title":"Nature"},{"key":"10.1016\/j.mcpro.2022.100485_bib27","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.cell.2012.06.047","article-title":"Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition","volume":"150","author":"Taipale","year":"2012","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib28","doi-asserted-by":"crossref","first-page":"e8438","DOI":"10.15252\/msb.20188438","article-title":"Complex-centric proteome profiling by SEC-SWATH-MS","volume":"15","author":"Heusel","year":"2019","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib29","doi-asserted-by":"crossref","first-page":"3851","DOI":"10.1074\/mcp.M113.032367","article-title":"Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics","volume":"12","author":"Kirkwood","year":"2013","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1074\/mcp.R119.001803","article-title":"Next-generation interactomics: considerations for the use of Co-elution to measure protein interaction networks","volume":"19","author":"Salas","year":"2020","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib31","doi-asserted-by":"crossref","first-page":"6834","DOI":"10.1073\/pnas.1322412111","article-title":"E3 ubiquitin ligase Cullin-5 modulates multiple molecular and cellular responses to heat shock protein 90 inhibition in human cancer cells","volume":"111","author":"Samant","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.mcpro.2022.100485_bib32","doi-asserted-by":"crossref","first-page":"2476","DOI":"10.1074\/mcp.O115.055467","article-title":"Global membrane protein interactome analysis using in vivo crosslinking and mass spectrometry-based protein correlation profiling","volume":"15","author":"Larance","year":"2016","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib33","doi-asserted-by":"crossref","first-page":"2513","DOI":"10.1074\/mcp.M113.031591","article-title":"Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ","volume":"13","author":"Cox","year":"2014","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib34","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1038\/bjc.1998.59","article-title":"In vitro circumvention of cisplatin resistance by the novel sterically hindered platinum complex AMD473","volume":"77","author":"Holford","year":"1998","journal-title":"Br. J. Cancer"},{"key":"10.1016\/j.mcpro.2022.100485_bib35","doi-asserted-by":"crossref","first-page":"D543","DOI":"10.1093\/nar\/gkab1038","article-title":"The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences","volume":"50","author":"Perez-Riverol","year":"2022","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib36","doi-asserted-by":"crossref","first-page":"1367","DOI":"10.1038\/nbt.1511","article-title":"MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification","volume":"26","author":"Cox","year":"2008","journal-title":"Nat. Biotechnol."},{"key":"10.1016\/j.mcpro.2022.100485_bib37","doi-asserted-by":"crossref","first-page":"2938","DOI":"10.1093\/bioinformatics\/btx364","article-title":"UpSetR: an R package for the visualization of intersecting sets and their properties","volume":"33","author":"Conway","year":"2017","journal-title":"Bioinformatics"},{"key":"10.1016\/j.mcpro.2022.100485_bib38","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1111\/2041-210X.13384","article-title":"metan: an R package for multi-environment trial analysis","volume":"11","author":"Olivoto","year":"2020","journal-title":"Met. Ecol. Evol."},{"key":"10.1016\/j.mcpro.2022.100485_bib39","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1038\/nprot.2017.147","article-title":"Proteome-wide identification of ubiquitin interactions using UbIA-MS","volume":"13","author":"Zhang","year":"2018","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.mcpro.2022.100485_bib40","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1186\/s12859-018-2533-3","article-title":"GOnet: a tool for interactive gene ontology analysis","volume":"19","author":"Pomaznoy","year":"2018","journal-title":"BMC Bioinform."},{"key":"10.1016\/j.mcpro.2022.100485_bib41","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1038\/s41592-021-01107-5","article-title":"PCprophet: a framework for protein complex prediction and differential analysis using proteomic data","volume":"18","author":"Fossati","year":"2021","journal-title":"Nat. Met."},{"key":"10.1016\/j.mcpro.2022.100485_bib42","article-title":"Rapid profiling of protein complex re-organization in perturbed systems","author":"Bludau","year":"2022","journal-title":"bioRxiv"},{"key":"10.1016\/j.mcpro.2022.100485_bib43","doi-asserted-by":"crossref","first-page":"2301","DOI":"10.1038\/nprot.2016.136","article-title":"The MaxQuant computational platform for mass spectrometry-based shotgun proteomics","volume":"11","author":"Tyanova","year":"2016","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.mcpro.2022.100485_bib44","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0080425","article-title":"Dynamic impacts of the inhibition of the molecular chaperone Hsp90 on the T-cell proteome have implications for anti-cancer therapy","volume":"8","author":"Fierro-Monti","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.mcpro.2022.100485_bib45","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/j.jprot.2015.02.020","article-title":"Hsp90 inhibition induces both protein-specific and global changes in the ubiquitinome","volume":"120","author":"Quadroni","year":"2015","journal-title":"J.\u00a0Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib46","doi-asserted-by":"crossref","first-page":"260","DOI":"10.1016\/j.cell.2018.02.030","article-title":"Multiplexed proteome dynamics profiling reveals\u00a0mechanisms controlling protein homeostasis","volume":"173","author":"Savitski","year":"2018","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib47","first-page":"3312","article-title":"Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents","volume":"6","author":"Bagatell","year":"2000","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib48","doi-asserted-by":"crossref","first-page":"5815","DOI":"10.3390\/ijms20225815","article-title":"HSF1Base: a comprehensive database of HSF1 (heat shock factor 1) target genes","volume":"20","author":"Kovacs","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.mcpro.2022.100485_bib49","doi-asserted-by":"crossref","DOI":"10.1016\/j.yexcr.2020.112246","article-title":"Hsf1 on a leash - controlling the heat shock response by chaperone titration","volume":"396","author":"Masser","year":"2020","journal-title":"Exp. Cell Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib50","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1007\/978-3-030-40204-4_3","article-title":"Regulation of Hsf1 and the heat shock response","volume":"1243","author":"Pincus","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib51","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1186\/1471-2407-11-468","article-title":"Development and characterization of a novel C-terminal inhibitor of Hsp90 in androgen dependent and independent prostate cancer cells","volume":"11","author":"Eskew","year":"2011","journal-title":"BMC Cancer"},{"key":"10.1016\/j.mcpro.2022.100485_bib52","doi-asserted-by":"crossref","first-page":"15100","DOI":"10.1074\/jbc.M109.094698","article-title":"Biochemical and biophysical characterization of the Mg2+-induced 90-kDa heat shock protein oligomers","volume":"285","author":"Moullintraffort","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.mcpro.2022.100485_bib53","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/j.cels.2020.01.001","article-title":"A global screen for assembly state changes of the mitotic proteome by SEC-SWATH-MS","volume":"10","author":"Heusel","year":"2020","journal-title":"Cell Syst."},{"key":"10.1016\/j.mcpro.2022.100485_bib54","doi-asserted-by":"crossref","first-page":"7113","DOI":"10.7314\/APJCP.2014.15.17.7113","article-title":"Comparison of inhibitory effects of 17-AAG nanoparticles and free 17-AAG on HSP90 gene expression in breast cancer","volume":"15","author":"Ghalhar","year":"2014","journal-title":"Asian Pac. J. Cancer Prev."},{"key":"10.1016\/j.mcpro.2022.100485_bib55","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1186\/1471-2407-10-481","article-title":"17-Allylamino-17-demethoxygeldanamycin induces downregulation of critical Hsp90 protein clients and results in cell cycle arrest\u00a0and apoptosis of human urinary bladder cancer cells","volume":"10","author":"Karkoulis","year":"2010","journal-title":"BMC Cancer"},{"key":"10.1016\/j.mcpro.2022.100485_bib56","doi-asserted-by":"crossref","first-page":"3613","DOI":"10.1038\/s41467-019-11552-8","article-title":"HSP90 inhibitors stimulate DNAJB4 protein expression through a mechanism involving N(6)-methyladenosine","volume":"10","author":"Miao","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mcpro.2022.100485_bib57","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1038\/nrm.2017.20","article-title":"The HSP90 chaperone machinery","volume":"18","author":"Schopf","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib58","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.molcel.2011.12.031","article-title":"Conformational switching of the molecular chaperone Hsp90 via regulated phosphorylation","volume":"45","author":"Soroka","year":"2012","journal-title":"Mol. Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib59","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1016\/j.molcel.2008.07.021","article-title":"Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37","volume":"31","author":"Vaughan","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib60","doi-asserted-by":"crossref","first-page":"D497","DOI":"10.1093\/nar\/gkp914","article-title":"Corum: the comprehensive resource of mammalian protein complexes--2009","volume":"38","author":"Ruepp","year":"2010","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib61","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1074\/mcp.M112.024547","article-title":"Global subcellular characterization of protein degradation using quantitative proteomics","volume":"12","author":"Larance","year":"2013","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib62","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/j.cell.2019.03.012","article-title":"The chaperonin TRiC\/CCT associates with Prefoldin through a conserved electrostatic interface essential for cellular proteostasis","volume":"177","author":"Gestaut","year":"2019","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib63","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1146\/annurev-biochem-062917-011931","article-title":"Structure and function of the 26S proteasome","volume":"87","author":"Bard","year":"2018","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.mcpro.2022.100485_bib64","doi-asserted-by":"crossref","first-page":"4023","DOI":"10.1016\/j.febslet.2008.10.053","article-title":"HSP90 is required for TAK1 stability but not for its activation in the pro-inflammatory signaling pathway","volume":"582","author":"Liu","year":"2008","journal-title":"FEBS Lett."},{"key":"10.1016\/j.mcpro.2022.100485_bib65","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.molimm.2008.07.019","article-title":"Heat shock protein 90 (Hsp90) regulates the stability of transforming growth factor beta-activated kinase 1 (TAK1) in interleukin-1beta-induced cell signaling","volume":"46","author":"Shi","year":"2009","journal-title":"Mol. Immunol."},{"key":"10.1016\/j.mcpro.2022.100485_bib66","doi-asserted-by":"crossref","first-page":"5364","DOI":"10.1093\/emboj\/cdf531","article-title":"Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes","volume":"21","author":"Lange","year":"2002","journal-title":"EMBO J."},{"key":"10.1016\/j.mcpro.2022.100485_bib67","doi-asserted-by":"crossref","first-page":"4684","DOI":"10.1111\/j.1742-4658.2005.04884.x","article-title":"A\u00a0client-binding site of Cdc37","volume":"272","author":"Terasawa","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.mcpro.2022.100485_bib68","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1158\/1535-7163.MCT-16-0848","article-title":"Inhibition of Hsp90 suppresses PI3K\/AKT\/mTOR signaling and has antitumor activity in burkitt lymphoma","volume":"16","author":"Giulino-Roth","year":"2017","journal-title":"Mol. Cancer Ther."},{"key":"10.1016\/j.mcpro.2022.100485_bib69","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1038\/nchembio.670","article-title":"Affinity-based proteomics reveal cancer-specific networks coordinated by Hsp90","volume":"7","author":"Moulick","year":"2011","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib70","doi-asserted-by":"crossref","DOI":"10.1016\/j.lfs.2020.118000","article-title":"Hsp90 inhibitor gedunin causes apoptosis in A549 lung cancer cells by disrupting Hsp90:Beclin-1:Bcl-2 interaction and downregulating autophagy","volume":"256","author":"Hasan","year":"2020","journal-title":"Life Sci."},{"key":"10.1016\/j.mcpro.2022.100485_bib71","doi-asserted-by":"crossref","first-page":"2700","DOI":"10.1096\/fj.10-167676","article-title":"Functional interaction of heat shock protein 90 and Beclin 1 modulates Toll-like receptor-mediated autophagy","volume":"25","author":"Xu","year":"2011","journal-title":"FASEB J."},{"key":"10.1016\/j.mcpro.2022.100485_bib72","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/j.tcb.2004.04.001","article-title":"LKB1 tumor suppressor protein: PARtaker in cell polarity","volume":"14","author":"Baas","year":"2004","journal-title":"Trends Cell Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib73","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.bbamcr.2013.11.013","article-title":"Hsp90 activity is necessary to acquire a proper neuronal polarization","volume":"1843","author":"Benitez","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.mcpro.2022.100485_bib74","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1111\/j.1398-9219.2004.00197.x","article-title":"Fractionation and characterization of kinesin II species in vertebrate brain","volume":"5","author":"Berezuk","year":"2004","journal-title":"Traffic"},{"key":"10.1016\/j.mcpro.2022.100485_bib75","doi-asserted-by":"crossref","first-page":"4133","DOI":"10.1038\/sj.onc.1209461","article-title":"17-AAG, an Hsp90 inhibitor, causes kinetochore defects: a novel mechanism by which 17-AAG inhibits cell proliferation","volume":"25","author":"Niikura","year":"2006","journal-title":"Oncogene"},{"key":"10.1016\/j.mcpro.2022.100485_bib76","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1083\/jcb.200910036","article-title":"Hsp90-Sgt1 and Skp1 target human Mis12 complexes to ensure efficient formation of kinetochore-microtubule binding sites","volume":"189","author":"Davies","year":"2010","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib77","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.cell.2014.06.016","article-title":"Polo-like kinase 1 licenses CENP-A deposition at centromeres","volume":"158","author":"McKinley","year":"2014","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib78","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1080\/15384101.2017.1325039","article-title":"SGT1-HSP90 complex is required for CENP-A deposition at centromeres","volume":"16","author":"Niikura","year":"2017","journal-title":"Cell Cycle"},{"key":"10.1016\/j.mcpro.2022.100485_bib79","doi-asserted-by":"crossref","first-page":"D605","DOI":"10.1093\/nar\/gkaa1074","article-title":"The STRING database in 2021: customizable protein-protein networks, and functional characterization of user-uploaded gene\/measurement sets","volume":"49","author":"Szklarczyk","year":"2021","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib80","doi-asserted-by":"crossref","first-page":"D1074","DOI":"10.1093\/nar\/gkaa1059","article-title":"canSAR: update to the cancer translational research and drug discovery knowledgebase","volume":"49","author":"Mitsopoulos","year":"2021","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib81","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1093\/nar\/30.7.1575","article-title":"An efficient algorithm for large-scale detection of protein families","volume":"30","author":"Enright","year":"2002","journal-title":"Nucl. Acids Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib82","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1007\/s00018-020-03605-9","article-title":"Anillin is an emerging regulator of tumorigenesis, acting as a cortical cytoskeletal scaffold and a nuclear modulator of cancer cell differentiation","volume":"78","author":"Naydenov","year":"2021","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.mcpro.2022.100485_bib83","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1111\/1759-7714.13135","article-title":"Overexpression of ANLN in lung adenocarcinoma is associated with metastasis","volume":"10","author":"Xu","year":"2019","journal-title":"Thorac. Cancer"},{"key":"10.1016\/j.mcpro.2022.100485_bib84","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.18632\/aging.101510","article-title":"Anillin is required for tumor growth and regulated by miR-15a\/miR-16-1 in HBV-related hepatocellular carcinoma","volume":"10","author":"Lian","year":"2018","journal-title":"Aging (Albany NY)"},{"key":"10.1016\/j.mcpro.2022.100485_bib85","doi-asserted-by":"crossref","first-page":"459","DOI":"10.3233\/CBM-160585","article-title":"Overexpression of Anillin (ANLN) is correlated with colorectal cancer progression and poor prognosis","volume":"16","author":"Wang","year":"2016","journal-title":"Cancer Biomark."},{"key":"10.1016\/j.mcpro.2022.100485_bib86","doi-asserted-by":"crossref","first-page":"1421","DOI":"10.1053\/j.gastro.2017.12.013","article-title":"Knockdown of anillin actin binding protein blocks cytokinesis in Hepatocytes and reduces liver tumor development in mice without affecting regeneration","volume":"154","author":"Zhang","year":"2018","journal-title":"Gastroenterology"},{"key":"10.1016\/j.mcpro.2022.100485_bib87","doi-asserted-by":"crossref","first-page":"847","DOI":"10.3389\/fphar.2018.00847","article-title":"UBE2C is a potential biomarker of intestinal-type gastric cancer with chromosomal instability","volume":"9","author":"Zhang","year":"2018","journal-title":"Front. Pharmacol."},{"key":"10.1016\/j.mcpro.2022.100485_bib88","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.3390\/cancers12061600","article-title":"Role of anillin in tumour: from a prognostic biomarker to a novel target","volume":"12","author":"Tuan","year":"2020","journal-title":"Cancers (Basel)"},{"key":"10.1016\/j.mcpro.2022.100485_bib89","doi-asserted-by":"crossref","first-page":"3118","DOI":"10.1038\/s41388-022-02274-1","article-title":"Targeting\u00a0anillin inhibits tumorigenesis and tumor growth in hepatocellular carcinoma via impairing cytokinesis fidelity","volume":"41","author":"Chen","year":"2022","journal-title":"Oncogene"},{"key":"10.1016\/j.mcpro.2022.100485_bib90","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.bbrc.2006.04.104","article-title":"F1F0-ATP synthase functions as a co-chaperone of Hsp90-substrate protein complexes","volume":"345","author":"Papathanassiu","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.mcpro.2022.100485_bib91","doi-asserted-by":"crossref","first-page":"976","DOI":"10.1021\/cb400906e","article-title":"Cruentaren A binds F1F0 ATP synthase to modulate the Hsp90 protein folding machinery","volume":"9","author":"Hall","year":"2014","journal-title":"ACS Chem. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib92","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1038\/nature04670","article-title":"Global landscape of protein complexes in the yeast Saccharomyces cerevisiae","volume":"440","author":"Krogan","year":"2006","journal-title":"Nature"},{"key":"10.1016\/j.mcpro.2022.100485_bib93","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.cell.2007.07.036","article-title":"Diverse cellular functions of the Hsp90 molecular chaperone uncovered using systems approaches","volume":"131","author":"McClellan","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib94","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1186\/s12915-021-01179-x","article-title":"An HSP90 cochaperone Ids2 maintains the stability of mitochondrial DNA and ATP synthase","volume":"19","author":"Jiang","year":"2021","journal-title":"BMC Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib95","first-page":"A891","article-title":"Human mitochondrial NAD-specific isocitrate dehrydrogenase 3 and subunits: cloning, tissue specific expression and functional analyses of the recombinant proteins","volume":"11","author":"Huh","year":"1997","journal-title":"FASEB J."},{"key":"10.1016\/j.mcpro.2022.100485_bib96","doi-asserted-by":"crossref","first-page":"14361","DOI":"10.1074\/jbc.M512613200","article-title":"Hsp90 recognizes a common surface on client kinases","volume":"281","author":"Citri","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.mcpro.2022.100485_bib97","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1016\/j.bbamcr.2011.08.013","article-title":"Approaches for defining the Hsp90-dependent proteome","volume":"1823","author":"Hartson","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.mcpro.2022.100485_bib98","doi-asserted-by":"crossref","first-page":"1301","DOI":"10.4161\/cc.19722","article-title":"The expanding\u00a0proteome of the molecular chaperone HSP90","volume":"11","author":"Samant","year":"2012","journal-title":"Cell Cycle"},{"key":"10.1016\/j.mcpro.2022.100485_bib99","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1038\/nsmb.3305","article-title":"Importance of cycle timing for the function of the molecular chaperone Hsp90","volume":"23","author":"Zierer","year":"2016","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib100","doi-asserted-by":"crossref","first-page":"6780","DOI":"10.1158\/1078-0432.CCR-05-0997","article-title":"The septin-binding protein anillin is overexpressed in diverse human tumors","volume":"11","author":"Hall","year":"2005","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib101","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/j.semcdb.2010.08.002","article-title":"The myriad roles of Anillin during cytokinesis","volume":"21","author":"Piekny","year":"2010","journal-title":"Semin. Cell Dev. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib102","doi-asserted-by":"crossref","first-page":"eaaw4543","DOI":"10.1126\/sciadv.aaw4543","article-title":"Cancer-associated mutation and beyond: the emerging biology of isocitrate dehydrogenases in human disease","volume":"5","author":"Tommasini-Ghelfi","year":"2019","journal-title":"Sci. Adv."},{"key":"10.1016\/j.mcpro.2022.100485_bib103","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.aat0456","article-title":"IDH3alpha regulates one-carbon metabolism in glioblastoma","volume":"5","author":"May","year":"2019","journal-title":"Sci. Adv."},{"key":"10.1016\/j.mcpro.2022.100485_bib104","doi-asserted-by":"crossref","first-page":"4758","DOI":"10.1038\/onc.2014.411","article-title":"Aberrant IDH3alpha expression promotes malignant tumor growth by inducing HIF-1-mediated metabolic reprogramming and angiogenesis","volume":"34","author":"Zeng","year":"2015","journal-title":"Oncogene"},{"key":"10.1016\/j.mcpro.2022.100485_bib105","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1016\/j.celrep.2015.02.006","article-title":"Metabolic reprogramming of cancer-associated fibroblasts by IDH3alpha downregulation","volume":"10","author":"Zhang","year":"2015","journal-title":"Cell Rep."},{"key":"10.1016\/j.mcpro.2022.100485_bib106","doi-asserted-by":"crossref","first-page":"646","DOI":"10.1016\/j.cell.2011.02.013","article-title":"Hallmarks of cancer: the next generation","volume":"144","author":"Hanahan","year":"2011","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib107","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.exger.2018.12.018","article-title":"The age-related changes and differences in energy metabolism and glutamate-glutamine recycling in the d-gal-induced and naturally occurring senescent astrocytes in\u00a0vitro","volume":"118","author":"Cao","year":"2019","journal-title":"Exp. Gerontol."},{"key":"10.1016\/j.mcpro.2022.100485_bib108","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.cell.2007.08.028","article-title":"Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network","volume":"131","author":"Kang","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib109","doi-asserted-by":"crossref","first-page":"988","DOI":"10.1016\/j.cmet.2013.04.019","article-title":"The mitochondrial chaperone TRAP1 promotes neoplastic\u00a0growth by inhibiting succinate dehydrogenase","volume":"17","author":"Sciacovelli","year":"2013","journal-title":"Cell Metab."},{"key":"10.1016\/j.mcpro.2022.100485_bib110","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/S0092-8674(02)01250-3","article-title":"Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70","volume":"112","author":"Young","year":"2003","journal-title":"Cell"},{"key":"10.1016\/j.mcpro.2022.100485_bib111","doi-asserted-by":"crossref","first-page":"33313","DOI":"10.1074\/jbc.M605250200","article-title":"Hsp90 functions in the targeting and outer membrane translocation steps of Tom70-mediated mitochondrial import","volume":"281","author":"Fan","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.mcpro.2022.100485_bib112","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1534\/g3.113.005777","article-title":"The genomic and transcriptomic landscape of a HeLa cell line","volume":"3","author":"Landry","year":"2013","journal-title":"G3 (Bethesda)"},{"key":"10.1016\/j.mcpro.2022.100485_bib113","doi-asserted-by":"crossref","first-page":"4767","DOI":"10.1038\/ncomms5767","article-title":"Genome dynamics of the human embryonic kidney 293 lineage in response to cell biology manipulations","volume":"5","author":"Lin","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mcpro.2022.100485_bib114","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1038\/s41598-021-81279-4","article-title":"A\u00a0comparative study of evaluating missing value imputation methods in label-free proteomics","volume":"11","author":"Jin","year":"2021","journal-title":"Sci. Rep."},{"key":"10.1016\/j.mcpro.2022.100485_bib115","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1021\/pr501138h","article-title":"Review, evaluation, and discussion of\u00a0the challenges of missing value imputation for mass spectrometry-based label-free global proteomics","volume":"14","author":"Webb-Robertson","year":"2015","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib116","doi-asserted-by":"crossref","first-page":"2494","DOI":"10.1021\/acsomega.0c04030","article-title":"Benchmarking quantitative performance in label-free proteomics","volume":"6","author":"Dowell","year":"2021","journal-title":"ACS Omega"},{"key":"10.1016\/j.mcpro.2022.100485_bib117","doi-asserted-by":"crossref","DOI":"10.15252\/msb.20178126","article-title":"Data-independent acquisition-based SWATH-MS for quantitative proteomics: a tutorial","volume":"14","author":"Ludwig","year":"2018","journal-title":"Mol. Syst. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib118","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1021\/acs.jproteome.8b00898","article-title":"Comparison of protein quantification in a complex background by DIA and TMT workflows with fixed instrument time","volume":"18","author":"Muntel","year":"2019","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib119","doi-asserted-by":"crossref","first-page":"1934","DOI":"10.1021\/acs.jproteome.8b00016","article-title":"Proteome-wide evaluation of two common protein quantification methods","volume":"17","author":"O'Connell","year":"2018","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib120","doi-asserted-by":"crossref","first-page":"926","DOI":"10.1021\/acs.jproteome.9b00701","article-title":"Systematic comparison of label-free, SILAC, and TMT techniques to study early adaption toward inhibition of EGFR signaling in the colorectal cancer cell line DiFi","volume":"19","author":"Stepath","year":"2020","journal-title":"J.\u00a0Proteome Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib121","doi-asserted-by":"crossref","first-page":"1876","DOI":"10.1074\/mcp.RA120.002154","article-title":"Analytical guidelines for co-fractionation mass spectrometry obtained through global profiling of gold standard Saccharomyces cerevisiae protein complexes","volume":"19","author":"Pang","year":"2020","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.mcpro.2022.100485_bib122","doi-asserted-by":"crossref","first-page":"5117","DOI":"10.1016\/j.csbj.2021.08.042","article-title":"PROMISed: a novel web-based tool to facilitate analysis and visualization of the molecular interaction networks from co-fractionation mass spectrometry (CF-MS) experiments","volume":"19","author":"Schlossarek","year":"2021","journal-title":"Comput. Struct. Biotechnol. J."},{"key":"10.1016\/j.mcpro.2022.100485_bib123","doi-asserted-by":"crossref","first-page":"1446","DOI":"10.1016\/j.apsb.2020.11.015","article-title":"The disruption of protein-protein interactions with co-chaperones and client substrates as a strategy towards Hsp90 inhibition","volume":"11","author":"Serwetnyk","year":"2021","journal-title":"Acta Pharm. Sin. B"},{"key":"10.1016\/j.mcpro.2022.100485_bib124","doi-asserted-by":"crossref","first-page":"2702","DOI":"10.2174\/092986708786242895","article-title":"Novobiocin and additional inhibitors of the Hsp90 C-terminal nucleotide-binding pocket","volume":"15","author":"Donnelly","year":"2008","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.mcpro.2022.100485_bib125","doi-asserted-by":"crossref","first-page":"1446","DOI":"10.1016\/j.chembiol.2021.03.016","article-title":"Discovery of a covalent inhibitor of heat shock protein 90 with antitumor activity that blocks the co-chaperone binding via C-terminal modification","volume":"28","author":"Li","year":"2021","journal-title":"Cell Chem. Biol."},{"key":"10.1016\/j.mcpro.2022.100485_bib126","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2021.105523","article-title":"Tubocapsenolide A targets C-terminal cysteine residues of HSP90 to exert the anti-tumor effect","volume":"166","author":"Zhu","year":"2021","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.mcpro.2022.100485_bib127","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1038\/s41467-017-02013-1","article-title":"Structure-guided design of an Hsp90beta N-terminal isoform-selective inhibitor","volume":"9","author":"Khandelwal","year":"2018","journal-title":"Nat. Commun."},{"key":"10.1016\/j.mcpro.2022.100485_bib128","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/s12276-019-0360-x","article-title":"Unleashing the full potential of Hsp90 inhibitors as cancer therapeutics through simultaneous inactivation of Hsp90, Grp94, and TRAP1","volume":"52","author":"Park","year":"2020","journal-title":"Exp. Mol. Med."},{"key":"10.1016\/j.mcpro.2022.100485_bib129","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2020.107531","article-title":"Rational design of allosteric and selective inhibitors of the molecular chaperone TRAP1","volume":"31","author":"Sanchez-Martin","year":"2020","journal-title":"Cell Rep."},{"key":"10.1016\/j.mcpro.2022.100485_bib130","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-017-18344-4","article-title":"Isoform-selective Hsp90 inhibition rescues model of hereditary open-angle glaucoma","volume":"7","author":"Stothert","year":"2017","journal-title":"Sci. Rep."}],"container-title":["Molecular & Cellular Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947622002936?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1535947622002936?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,27]],"date-time":"2025-10-27T01:10:18Z","timestamp":1761527418000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1535947622002936"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,2]]},"references-count":130,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2023,2]]}},"alternative-id":["S1535947622002936"],"URL":"https:\/\/doi.org\/10.1016\/j.mcpro.2022.100485","relation":{},"ISSN":["1535-9476"],"issn-type":[{"value":"1535-9476","type":"print"}],"subject":[],"published":{"date-parts":[[2023,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Native Size-Exclusion Chromatography\u2013Based Mass Spectrometry Reveals New Components of the Early Heat Shock Protein 90 Inhibition Response Among Limited Global Changes","name":"articletitle","label":"Article Title"},{"value":"Molecular & Cellular Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.mcpro.2022.100485","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2022 THE AUTHORS. Published by Elsevier Inc on behalf of American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}],"article-number":"100485"}}