{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T20:51:50Z","timestamp":1791406310480,"version":"4.3.3"},"reference-count":67,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81373318"],"award-info":[{"award-number":["81373318"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Acta Biomaterialia"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.actbio.2026.01.051","type":"journal-article","created":{"date-parts":[[2026,1,28]],"date-time":"2026-01-28T16:49:52Z","timestamp":1769618992000},"page":"678-690","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Sulfatase-responsive phase-separating peptide coacervates target stress granules to reverse sorafenib resistance in hepatocellular carcinoma"],"prefix":"10.1016","volume":"213","author":[{"given":"Chenhui","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Weishu","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yutong","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuqing","family":"Yang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luomeng","family":"Qian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fangyu","family":"Cao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Quanhong","family":"Han","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhilin","family":"Yu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8923-1993","authenticated-orcid":false,"given":"Sihe","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"3","key":"10.1016\/j.actbio.2026.01.051_bib0001","doi-asserted-by":"crossref","first-page":"209","DOI":"10.3322\/caac.21660","article-title":"Global Cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries","volume":"71","author":"Sung","year":"2021","journal-title":"Cancer J. Clin."},{"issue":"4","key":"10.1016\/j.actbio.2026.01.051_bib0002","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1056\/NEJMoa0708857","article-title":"Sorafenib in advanced hepatocellular carcinoma","volume":"359","author":"Llovet","year":"2008","journal-title":"N. Engl. J. Med."},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0003","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1038\/s41392-020-0187-x","article-title":"The mechanisms of sorafenib resistance in hepatocellular carcinoma: theoretical basis and therapeutic aspects","volume":"5","author":"Tang","year":"2020","journal-title":"Signal Transduct. Target. Ther."},{"issue":"12","key":"10.1016\/j.actbio.2026.01.051_bib0004","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1016\/j.trecan.2023.08.005","article-title":"Stress granules and hormetic adaptation of cancer","volume":"9","author":"Redding","year":"2023","journal-title":"Trend. Cancer."},{"issue":"14","key":"10.1016\/j.actbio.2026.01.051_bib0005","doi-asserted-by":"crossref","first-page":"9036","DOI":"10.1021\/acs.chemrev.2c00608","article-title":"A new phase of networking: the molecular composition and regulatory dynamics of mammalian stress granules","volume":"123","author":"Millar","year":"2023","journal-title":"Chem. Rev."},{"issue":"41","key":"10.1016\/j.actbio.2026.01.051_bib0006","doi-asserted-by":"crossref","first-page":"43927","DOI":"10.18632\/oncotarget.5980","article-title":"Sorafenib, a multikinase inhibitor, induces formation of stress granules in hepatocarcinoma cells","volume":"6","author":"Adjibade","year":"2015","journal-title":"Oncotarget"},{"issue":"7","key":"10.1016\/j.actbio.2026.01.051_bib0007","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1038\/s43018-024-00886-y","article-title":"Stress granules shape metabolic reprogramming and drug resistance","volume":"6","author":"Zhong","year":"2025","journal-title":"Nat. Cancer"},{"key":"10.1016\/j.actbio.2026.01.051_bib0008","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2020.105143","article-title":"Targeting stress granules: a novel therapeutic strategy for human diseases","volume":"161","author":"Wang","year":"2020","journal-title":"Pharmacol. Res."},{"issue":"28","key":"10.1016\/j.actbio.2026.01.051_bib0009","doi-asserted-by":"crossref","DOI":"10.1002\/adma.202420399","article-title":"In Situ liquid-liquid phase separation of peptides into droplets targeting membraneless organelles for enhanced cancer chemotherapy","volume":"37","author":"Wang","year":"2025","journal-title":"Adv. Mater. Weinheim."},{"issue":"9","key":"10.1016\/j.actbio.2026.01.051_bib0010","doi-asserted-by":"crossref","first-page":"2134","DOI":"10.3390\/molecules29092134","article-title":"Stress granule core protein-derived peptides inhibit assembly of Stress granules and improve sorafenib sensitivity in cancer cells","volume":"29","author":"Li","year":"2024","journal-title":"Molecules"},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0011","doi-asserted-by":"crossref","first-page":"2365","DOI":"10.1038\/s41467-025-57539-6","article-title":"Suppression of stress granule formation is a vulnerability imposed by mutant p53","volume":"16","author":"Thoenen","year":"2025","journal-title":"Nat Commun."},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0012","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1038\/s41420-024-02161-6","article-title":"Metal-polyphenol-network coated R612F nanoparticles reduce drug resistance in hepatocellular carcinoma by inhibiting stress granules","volume":"10","author":"Zhou","year":"2024","journal-title":"Cell Death Discov."},{"key":"10.1016\/j.actbio.2026.01.051_bib0013","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2022.106548","article-title":"G3BP2: structure and function","volume":"186","author":"Jin","year":"2022","journal-title":"Pharmacol. Res."},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0014","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/gtc.12023","article-title":"Both G3BP1 and G3BP2 contribute to stress granule formation","volume":"18","author":"Matsuki","year":"2013","journal-title":"Genes Cell."},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0015","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.cell.2020.03.046","article-title":"G3BP1 Is a tunable switch that triggers phase separation to assemble stress granules","volume":"181","author":"Yang","year":"2020","journal-title":"Cell"},{"issue":"5","key":"10.1016\/j.actbio.2026.01.051_bib0016","doi-asserted-by":"crossref","first-page":"1033","DOI":"10.1073\/pnas.1525387114","article-title":"Stress granule-associated protein G3BP2 regulates breast tumor initiation","volume":"114","author":"Gupta","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"5","key":"10.1016\/j.actbio.2026.01.051_bib0017","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1023\/A:1021737413055","article-title":"The expression of Ras-GTPase activating protein SH3 domain-binding proteins, G3BPs, in human breast cancers","volume":"34","author":"French","year":"2002","journal-title":"Histochem. J."},{"issue":"25","key":"10.1016\/j.actbio.2026.01.051_bib0018","doi-asserted-by":"crossref","first-page":"3433","DOI":"10.1038\/s41388-022-02352-4","article-title":"RIOK1 mediates p53 degradation and radioresistance in colorectal cancer through phosphorylation of G3BP2","volume":"41","author":"Chen","year":"2022","journal-title":"Oncogene"},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0019","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1186\/s13018-022-03181-7","article-title":"EBF1-mediated up-regulation of lncRNA FGD5-AS1 facilitates osteosarcoma progression by regulating miR-124-3p\/G3BP2 axis as a ceRNA","volume":"17","author":"Shuang","year":"2022","journal-title":"J. Orthop. Surg. Res."},{"issue":"9","key":"10.1016\/j.actbio.2026.01.051_bib0020","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.3390\/cancers12092690","article-title":"FOXD1 Repression potentiates radiation effectiveness by downregulating G3BP2 expression and promoting the activation of TXNIP-related pathways in oral cancer","volume":"12","author":"Lin","year":"2020","journal-title":"Cancers"},{"issue":"5","key":"10.1016\/j.actbio.2026.01.051_bib0021","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1038\/ncb3157","article-title":"Matrix stiffness drives epithelial-mesenchymal transition and tumour metastasis through a TWIST1-G3BP2 mechanotransduction pathway","volume":"17","author":"Wei","year":"2015","journal-title":"Nat. Cell Biol."},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0022","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1004659","article-title":"Viral and cellular proteins containing FGDF motifs bind G3BP to block stress granule formation","volume":"11","author":"Panas","year":"2015","journal-title":"PLoS Pathog."},{"issue":"7","key":"10.1016\/j.actbio.2026.01.051_bib0023","doi-asserted-by":"crossref","DOI":"10.1098\/rsob.160078","article-title":"Combined structural, biochemical and cellular evidence demonstrates that both FGDF motifs in alphavirus nsP3 are required for efficient replication","volume":"6","author":"Schulte","year":"2016","journal-title":"Open Biol."},{"issue":"10","key":"10.1016\/j.actbio.2026.01.051_bib0024","doi-asserted-by":"crossref","first-page":"1967","DOI":"10.1016\/j.cub.2023.04.012","article-title":"Stress granule formation inhibits stress-induced apoptosis by selectively sequestering executioner caspases","volume":"33","author":"Fujikawa","year":"2023","journal-title":"Curr. Biol."},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0025","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/s41392-021-00678-1","article-title":"Liquid-liquid phase separation in human health and diseases","volume":"6","author":"Wang","year":"2021","journal-title":"Signal Transduct. Target. Ther."},{"issue":"42","key":"10.1016\/j.actbio.2026.01.051_bib0026","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202307045","article-title":"Photo-responsive phase-separating fluorescent molecules for intracellular protein delivery","volume":"62","author":"Bao","year":"2023","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"11","key":"10.1016\/j.actbio.2026.01.051_bib0027","doi-asserted-by":"crossref","first-page":"1046","DOI":"10.1038\/s41557-021-00788-x","article-title":"A short peptide synthon for liquid-liquid phase separation","volume":"13","author":"Abbas","year":"2021","journal-title":"Nat Chem."},{"issue":"38","key":"10.1016\/j.actbio.2026.01.051_bib0028","article-title":"Regulation of peptide liquid-liquid phase separation by aromatic amino acid composition","volume":"20","author":"Netzer","year":"2024","journal-title":"Small"},{"issue":"3","key":"10.1016\/j.actbio.2026.01.051_bib0029","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1038\/s41557-021-00854-4","article-title":"Phase-separating peptides for direct cytosolic delivery and redox-activated release of macromolecular therapeutics","volume":"14","author":"Sun","year":"2022","journal-title":"Nat Chem."},{"issue":"24","key":"10.1016\/j.actbio.2026.01.051_bib0030","doi-asserted-by":"crossref","first-page":"11725","DOI":"10.1039\/D3CS01066J","article-title":"Recent advances in peptide macrocyclization strategies","volume":"53","author":"Fang","year":"2024","journal-title":"Chem. Soc. Rev."},{"issue":"19","key":"10.1016\/j.actbio.2026.01.051_bib0031","doi-asserted-by":"crossref","first-page":"27697","DOI":"10.1021\/acsami.5c04775","article-title":"Peptide coacervates: formation, mechanism, and biological applications","volume":"17","author":"Yuan","year":"2025","journal-title":"ACS Appl. Mater. Interfac."},{"issue":"24","key":"10.1016\/j.actbio.2026.01.051_bib0032","doi-asserted-by":"crossref","first-page":"34951","DOI":"10.1021\/acsami.5c00048","article-title":"Polyphosphate- and antioxidant peptide-based coacervate delivers miRNA","volume":"17","author":"Wang","year":"2025","journal-title":"ACS Appl. Mater Interfac."},{"issue":"11","key":"10.1016\/j.actbio.2026.01.051_bib0033","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1038\/s41551-024-01254-y","article-title":"In situ formation of biomolecular condensates as intracellular drug reservoirs for augmenting chemotherapy","volume":"8","author":"Liang","year":"2024","journal-title":"Nat. Biomed.l Eng."},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0034","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1210\/er.2004-0003","article-title":"Steroid sulfatase: molecular biology, regulation, and inhibition","volume":"26","author":"Reed","year":"2005","journal-title":"Endocr. Rev."},{"issue":"43","key":"10.1016\/j.actbio.2026.01.051_bib0035","doi-asserted-by":"crossref","first-page":"5736","DOI":"10.1002\/anie.200300632","article-title":"Sulfatases: structure, mechanism, biological activity, inhibition, and synthetic utility","volume":"43","author":"Hanson","year":"2004","journal-title":"Angew. Chem. Int. Ed. Engl."},{"issue":"15","key":"10.1016\/j.actbio.2026.01.051_bib0036","doi-asserted-by":"crossref","first-page":"10753","DOI":"10.1021\/jacs.4c00826","article-title":"Sulfatase-induced In situ formulation of antineoplastic supra-PROTACs","volume":"146","author":"Chen","year":"2024","journal-title":"J. Am. Chem. Soc."},{"issue":"34","key":"10.1016\/j.actbio.2026.01.051_bib0037","doi-asserted-by":"crossref","DOI":"10.1002\/adma.202202913","article-title":"Peptide-based coacervate-core vesicles with semipermeable membranes","volume":"34","author":"Abbas","year":"2022","journal-title":"Adv. Mater. Weinheim."},{"issue":"6478","key":"10.1016\/j.actbio.2026.01.051_bib0038","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1126\/science.aaw8653","article-title":"Valence and patterning of aromatic residues determine the phase behavior of prion-like domains","volume":"367","author":"Martin","year":"2020","journal-title":"Science"},{"issue":"7","key":"10.1016\/j.actbio.2026.01.051_bib0039","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1038\/s43018-025-00984-5","article-title":"RIOK1 phase separation restricts PTEN translation via stress granules activating tumor growth in hepatocellular carcinoma","volume":"6","author":"Meng","year":"2025","journal-title":"Nat. Cancer"},{"issue":"11","key":"10.1016\/j.actbio.2026.01.051_bib0040","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1038\/ncb1791","article-title":"Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways","volume":"10","author":"Arimoto","year":"2008","journal-title":"Nat. Cell Biol."},{"key":"10.1016\/j.actbio.2026.01.051_bib0041","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms10252","article-title":"TIA1 oxidation inhibits stress granule assembly and sensitizes cells to stress-induced apoptosis","volume":"7","author":"Arimoto-Matsuzaki","year":"2016","journal-title":"Nat Commun."},{"issue":"35","key":"10.1016\/j.actbio.2026.01.051_bib0042","doi-asserted-by":"crossref","first-page":"5223","DOI":"10.3748\/wjg.v26.i35.5223","article-title":"Stress granules in colorectal cancer: current knowledge and potential therapeutic applications","volume":"26","author":"Legrand","year":"2020","journal-title":"World J. Gastroenterol."},{"issue":"7","key":"10.1016\/j.actbio.2026.01.051_bib0043","doi-asserted-by":"crossref","first-page":"1803","DOI":"10.1016\/j.cell.2016.11.035","article-title":"Mutant KRAS enhances tumor cell fitness by upregulating stress granules","volume":"167","author":"Grabocka","year":"2016","journal-title":"Cell"},{"issue":"23","key":"10.1016\/j.actbio.2026.01.051_bib0044","doi-asserted-by":"crossref","first-page":"3727","DOI":"10.4161\/15384101.2014.965013","article-title":"Downregulation of BRCA1 protein in BCR-ABL1 leukemia cells depends on stress-triggered TIAR-mediated suppression of translation","volume":"13","author":"Podszywalow-Bartnicka","year":"2014","journal-title":"Cell. Cycle"},{"issue":"6497","key":"10.1016\/j.actbio.2026.01.051_bib0045","doi-asserted-by":"crossref","first-page":"1386","DOI":"10.1126\/science.aaz4427","article-title":"Partitioning of cancer therapeutics in nuclear condensates","volume":"368","author":"Klein","year":"2020","journal-title":"Science"},{"issue":"8","key":"10.1016\/j.actbio.2026.01.051_bib0046","doi-asserted-by":"crossref","first-page":"698","DOI":"10.2174\/1568009617666170427104356","article-title":"Epithelial-to-mesenchymal transition: a mediator of sorafenib resistance in advanced hepatocellular carcinoma","volume":"17","author":"Mir","year":"2017","journal-title":"Curr. Cancer Drug Targ."},{"issue":"4","key":"10.1016\/j.actbio.2026.01.051_bib0047","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1038\/s41388-021-02073-0","article-title":"G3BP2 regulated by the lncRNA LINC01554 facilitates esophageal squamous cell carcinoma metastasis through stabilizing HDGF transcript","volume":"41","author":"Zheng","year":"2022","journal-title":"Oncogene"},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0048","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.bbrc.2015.09.123","article-title":"Crystal structure of the G3BP2 NTF2-like domain in complex with a canonical FGDF motif peptide","volume":"467","author":"Kristensen","year":"2015","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"9","key":"10.1016\/j.actbio.2026.01.051_bib0049","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1089\/dna.2015.2957","article-title":"FGDF motif regulation of stress granule formation","volume":"34","author":"McInerney","year":"2015","journal-title":"DNA Cell Biol."},{"issue":"7","key":"10.1016\/j.actbio.2026.01.051_bib0050","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1007\/s11427-020-1702-x","article-title":"Liquid-liquid phase separation in biology: mechanisms, physiological functions and human diseases","volume":"63","author":"Zhang","year":"2020","journal-title":"Sci. China Life Sci."},{"issue":"1","key":"10.1016\/j.actbio.2026.01.051_bib0051","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/febs.15765","article-title":"Aberrant phase separation and cancer","volume":"289","author":"Taniue","year":"2022","journal-title":"FEBS J."},{"issue":"6357","key":"10.1016\/j.actbio.2026.01.051_bib0052","doi-asserted-by":"crossref","first-page":"eaaf4382","DOI":"10.1126\/science.aaf4382","article-title":"Liquid phase condensation in cell physiology and disease","volume":"357","author":"Shin","year":"2017","journal-title":"Science"},{"issue":"6","key":"10.1016\/j.actbio.2026.01.051_bib0053","doi-asserted-by":"crossref","first-page":"3690","DOI":"10.1039\/D0CS00307G","article-title":"Peptide-based coacervates as biomimetic protocells","volume":"50","author":"Abbas","year":"2021","journal-title":"Chem Soc Rev."},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0054","doi-asserted-by":"crossref","DOI":"10.1002\/cbic.202400773","article-title":"Peptides for liquid-liquid phase separation: an emerging biomaterial","volume":"26","author":"Wang","year":"2025","journal-title":"Chembiochem"},{"issue":"3","key":"10.1016\/j.actbio.2026.01.051_bib0055","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202308083","article-title":"Identification of small molecule inhibitors of G3BP-driven stress granule formation","volume":"223","author":"Freibaum","year":"2024","journal-title":"J. Cell Biol."},{"issue":"3","key":"10.1016\/j.actbio.2026.01.051_bib0056","doi-asserted-by":"crossref","first-page":"380","DOI":"10.1021\/ci900404p","article-title":"Structure-based design of peptides against G3BP with cytotoxicity on tumor cells","volume":"50","author":"Cui","year":"2010","journal-title":"J. Chem. Inf. Model."},{"issue":"4","key":"10.1016\/j.actbio.2026.01.051_bib0057","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.3892\/mmr.2013.1343","article-title":"Growth inhibition effect of peptide P110 plus cisplatin on various cancer cells and xenotransplanted tumors in mice","volume":"7","author":"Li","year":"2013","journal-title":"Mol. Med. Rep."},{"issue":"10","key":"10.1016\/j.actbio.2026.01.051_bib0058","doi-asserted-by":"crossref","first-page":"1848","DOI":"10.1111\/j.1349-7006.2012.02361.x","article-title":"GAP161 targets and downregulates G3BP to suppress cell growth and potentiate cisplaitin-mediated cytotoxicity to colon carcinoma HCT116 cells","volume":"103","author":"Zhang","year":"2012","journal-title":"Cancer Sci."},{"issue":"55","key":"10.1016\/j.actbio.2026.01.051_bib0059","doi-asserted-by":"crossref","first-page":"8971","DOI":"10.1038\/sj.onc.1207999","article-title":"A RasGAP-derived cell permeable peptide potently enhances genotoxin-induced cytotoxicity in tumor cells","volume":"23","author":"Michod","year":"2004","journal-title":"Oncogene"},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0060","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.apsb.2014.02.004","article-title":"RasGAP-derived peptide GAP159 enhances cisplatin-induced cytotoxicity and apoptosis in HCT116 cells","volume":"4","author":"Zhang","year":"2014","journal-title":"Acta Pharm. Sin. B"},{"issue":"24","key":"10.1016\/j.actbio.2026.01.051_bib0061","doi-asserted-by":"crossref","first-page":"11519","DOI":"10.1021\/acs.chemrev.8b00038","article-title":"Biomolecular assemblies: moving from observation to predictive design","volume":"118","author":"Wilson","year":"2018","journal-title":"Chem. Rev."},{"key":"10.1016\/j.actbio.2026.01.051_bib0062","first-page":"244","article-title":"Smart coacervate microdroplets: biomimetic design, material innovations, and emerging applications in biomacromolecule delivery","volume":"52","author":"Ding","year":"2025","journal-title":"Bioact. Mater."},{"issue":"18","key":"10.1016\/j.actbio.2026.01.051_bib0063","doi-asserted-by":"crossref","first-page":"7235","DOI":"10.1021\/jacs.8b07727","article-title":"Endogenous reactive oxygen species-triggered morphology transformation for enhanced cooperative interaction with mitochondria","volume":"141","author":"Cheng","year":"2019","journal-title":"J. Am. Chem. Soc."},{"issue":"34","key":"10.1016\/j.actbio.2026.01.051_bib0064","doi-asserted-by":"crossref","first-page":"24177","DOI":"10.1021\/jacs.4c10309","article-title":"In vivo self-sorting of peptides via In situ assembly evolution","volume":"146","author":"Liu","year":"2024","journal-title":"J. Am. Chem. Soc."},{"issue":"2","key":"10.1016\/j.actbio.2026.01.051_bib0065","doi-asserted-by":"crossref","first-page":"770","DOI":"10.1021\/ja510156v","article-title":"Cancer cell death induced by the intracellular self-assembly of an enzyme-responsive supramolecular gelator","volume":"137","author":"Tanaka","year":"2015","journal-title":"J. Am. Chem. Soc."},{"issue":"9","key":"10.1016\/j.actbio.2026.01.051_bib0066","doi-asserted-by":"crossref","first-page":"5547","DOI":"10.1021\/acs.biomac.5c01019","article-title":"Liquid-Liquid phase separation of peptide-based biomacromolecules: mechanisms, responsive factors, and biomedical applications","volume":"26","author":"Zhang","year":"2025","journal-title":"Biomacromolecules"},{"issue":"17","key":"10.1016\/j.actbio.2026.01.051_bib0067","doi-asserted-by":"crossref","first-page":"16597","DOI":"10.1021\/acsnano.3c02669","article-title":"Redox-responsive phase-separating peptide as a universal delivery vehicle for CRISPR\/Cas9 genome editing machinery","volume":"17","author":"Sun","year":"2023","journal-title":"ACS Nano"}],"container-title":["Acta Biomaterialia"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1742706126000681?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1742706126000681?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T20:02:36Z","timestamp":1791403356000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1742706126000681"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":67,"alternative-id":["S1742706126000681"],"URL":"https:\/\/doi.org\/10.1016\/j.actbio.2026.01.051","relation":{},"ISSN":["1742-7061"],"issn-type":[{"value":"1742-7061","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Sulfatase-responsive phase-separating peptide coacervates target stress granules to reverse sorafenib resistance in hepatocellular carcinoma","name":"articletitle","label":"Article Title"},{"value":"Acta Biomaterialia","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.actbio.2026.01.051","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Acta Materialia Inc. Published by Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}