{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,10]],"date-time":"2026-09-10T15:48:22Z","timestamp":1789055302149,"version":"build-2803163510"},"reference-count":132,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2025,12,1]],"date-time":"2025-12-01T00:00:00Z","timestamp":1764547200000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["21775059"],"award-info":[{"award-number":["21775059"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22074057"],"award-info":[{"award-number":["22074057"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22305107"],"award-info":[{"award-number":["22305107"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004775","name":"Natural Science Foundation of Gansu Province","doi-asserted-by":"publisher","award":["20YF3FA025"],"award-info":[{"award-number":["20YF3FA025"]}],"id":[{"id":"10.13039\/501100004775","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004775","name":"Natural Science Foundation of Gansu Province","doi-asserted-by":"publisher","award":["18YF1NA004"],"award-info":[{"award-number":["18YF1NA004"]}],"id":[{"id":"10.13039\/501100004775","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2025,12]]},"DOI":"10.1016\/j.ijbiomac.2025.149116","type":"journal-article","created":{"date-parts":[[2025,11,20]],"date-time":"2025-11-20T16:36:12Z","timestamp":1763656572000},"page":"149116","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":1,"special_numbering":"P2","title":["Recombinant elastin for biomedical applications\u2014Advances in molecular design, expression platforms, and purification strategies: A review"],"prefix":"10.1016","volume":"334","author":[{"given":"Lijun","family":"Zhu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingjing","family":"Shi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fei","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xuehong","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiuxia","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianxi","family":"Xiao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ijbiomac.2025.149116_bb0005","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1042\/bst0190824","article-title":"Molecular biology and pathology of human elastin","volume":"19","author":"Uitto","year":"1991","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0010","doi-asserted-by":"crossref","first-page":"3796","DOI":"10.1021\/acsbiomaterials.1c00145","article-title":"Structure\u2013property relationships of elastin-like polypeptides: a review of experimental and computational studies","volume":"9","author":"L\u00f3pez Barreiro","year":"2023","journal-title":"ACS Biomater Sci. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0015","doi-asserted-by":"crossref","DOI":"10.1098\/rsfs.2013.0058","article-title":"The structure and micromechanics of elastic tissue","volume":"4","author":"Green","year":"2014","journal-title":"Interface Focus."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0020","doi-asserted-by":"crossref","DOI":"10.1017\/S0033583524000040","article-title":"Structural and physical basis for the elasticity of elastin","volume":"57","author":"Depenveiller","year":"2024","journal-title":"Q. Rev. Biophys."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0025","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1016\/j.bpj.2018.01.045","article-title":"Modeling the early stages of phase separation in disordered elastin-like proteins","volume":"114","author":"Zhang","year":"2018","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0030","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1016\/j.matbio.2019.07.005","article-title":"Elastin architecture","volume":"84","author":"Vindin","year":"2019","journal-title":"Matrix Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0035","doi-asserted-by":"crossref","first-page":"4024","DOI":"10.1111\/febs.15702","article-title":"Domains 12 to 16 of tropoelastin promote cell attachment and spreading through interactions with glycosaminoglycan and integrins alphaV and alpha5beta1","volume":"288","author":"Bochicchio","year":"2021","journal-title":"FEBS J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0040","doi-asserted-by":"crossref","DOI":"10.3389\/fbioe.2021.643110","article-title":"Tropoelastin and elastin assembly","volume":"9","author":"Ozsvar","year":"2021","journal-title":"Front. Bioeng. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0045","doi-asserted-by":"crossref","first-page":"28616","DOI":"10.1074\/jbc.M109.017525","article-title":"Cell adhesion to tropoelastin is mediated via the C-terminal GRKRK motif and integrin alphaVbeta3","volume":"284","author":"Bax","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0050","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1074\/jbc.M112.419929","article-title":"Interaction between the elastin peptide VGVAPG and human elastin binding protein*","volume":"288","author":"Blanchevoye","year":"2013","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0055","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/0014-5793(95)00641-L","article-title":"Stimulation of cell proliferation and autoregulation of elastin expression by elastin peptide VPGVG in cultured chick vascular smooth muscle cells","volume":"368","author":"Wachi","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0060","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1046\/j.0106-9543.2002.01573.x","article-title":"Tropoelastin expression is up-regulated during activation of hepatic stellate cells and in the livers of CCl(4)-cirrhotic rats","volume":"22","author":"Kanta","year":"2002","journal-title":"Liver"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0065","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1042\/bj2141023","article-title":"Desmosine and isodesmosine contents and elastase activity in normal and cirrhotic rat liver","volume":"214","author":"Velebn\u00fd","year":"1983","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0070","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.matbio.2019.07.004","article-title":"The role of elastin-derived peptides in human physiology and diseases","volume":"84","author":"Le Page","year":"2019","journal-title":"Matrix Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0075","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-3-030-48457-6_1","article-title":"Elastin in the tumor microenvironment","volume":"1272","author":"Wang","year":"2020","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0080","doi-asserted-by":"crossref","first-page":"5158","DOI":"10.1021\/acsabm.4c00135","article-title":"Self-assembled fibroblast growth factor nanoparticles as a therapeutic for oxidant-induced neuronal and skin cell injury","volume":"7","author":"Kumar","year":"2024","journal-title":"ACS Appl. Bio Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0085","doi-asserted-by":"crossref","first-page":"2938","DOI":"10.1021\/acs.biomac.0c00740","article-title":"Catechol-functionalized elastin-like polypeptides as tissue adhesives","volume":"21","author":"Desai","year":"2020","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0090","doi-asserted-by":"crossref","first-page":"6975","DOI":"10.1039\/D3TB00564J","article-title":"Biocompatible and bioactive hydrogels of recombinant fusion elastin with low transition temperature for improved healing of UV-irradiated skin","volume":"11","author":"Li","year":"2023","journal-title":"J. Mater. Chem. B"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0095","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.jbiotec.2025.02.010","article-title":"Efficiently scaled-up production of recombinant human elastin-like polypeptides using multiple optimization strategies","volume":"401","author":"Xiong","year":"2025","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0100","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1186\/s12951-023-02184-8","article-title":"The construction of elastin-like polypeptides and their applications in drug delivery system and tissue repair","volume":"21","author":"Guo","year":"2023","journal-title":"J. Nanobiotechnology."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0105","doi-asserted-by":"crossref","DOI":"10.1002\/anie.202300511","article-title":"Light-responsive elastin-like peptide-based targeted nanoparticles for enhanced spheroid penetration","volume":"62","author":"Le","year":"2023","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0110","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1146\/annurev-bioeng-092419-061127","article-title":"Elastin-like polypeptides for biomedical applications","volume":"22","author":"Varanko","year":"2020","journal-title":"Annu. Rev. Biomed. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0115","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.tibtech.2019.08.005","article-title":"Elastin biomaterials in dermal repair","volume":"38","author":"Wen","year":"2020","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0120","doi-asserted-by":"crossref","first-page":"2530","DOI":"10.1002\/adhm.201400781","article-title":"Fabricated elastin","volume":"4","author":"Yeo","year":"2015","journal-title":"Adv. Healthc. Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0125","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1046\/j.1432-1327.1998.2580001.x","article-title":"Biochemistry of tropoelastin","volume":"258","author":"Vrhovski","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0130","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1002\/(SICI)1097-0029(19970815)38:4<428::AID-JEMT10>3.0.CO;2-L","article-title":"Elastic fiber during development and aging","volume":"38","author":"Pasquali-Ronchetti","year":"1997","journal-title":"Microsc. Res. Tech."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0135","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.matbio.2018.01.005","article-title":"Elastin in lung development and disease pathogenesis","volume":"73","author":"Mecham","year":"2018","journal-title":"Matrix Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0140","doi-asserted-by":"crossref","first-page":"1572","DOI":"10.1007\/s10439-009-9724-z","article-title":"An experimental and theoretical study on the anisotropy of elastin network","volume":"37","author":"Zou","year":"2009","journal-title":"Ann. Biomed. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0145","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/1523-1747.ep12530093","article-title":"Biochemistry of the elastic fibers in normal connective tissues and its alterations in diseases","volume":"72","author":"Uitto","year":"1979","journal-title":"J. Invest. Dermatol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0150","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1038\/s41428-025-01028-6","article-title":"Self-assembled nanofibers and hydrogels of double-hydrophobic elastin-like polypeptides formed via coacervation","volume":"57","author":"Sugawara-Narutaki","year":"2025","journal-title":"Polym. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0155","doi-asserted-by":"crossref","first-page":"2477","DOI":"10.1016\/j.febslet.2015.08.029","article-title":"Elastin-like polypeptides as models of intrinsically disordered proteins","volume":"589","author":"Roberts","year":"2015","journal-title":"FEBS Lett."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0160","doi-asserted-by":"crossref","first-page":"197","DOI":"10.3109\/03008208709006976","article-title":"Structure of the 3\u2032 region of the human elastin gene: great abundance of Alu repetitive sequences and few coding sequences","volume":"16","author":"Indik","year":"1987","journal-title":"Connect. Tissue Res."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0165","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1002\/ajmg.1320340115","article-title":"Structure of the elastin gene and alternative splicing of elastin mRNA: implications for human disease","volume":"34","author":"Indik","year":"1989","journal-title":"Am. J. Med. Genet. A"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0170","doi-asserted-by":"crossref","first-page":"15107","DOI":"10.1074\/jbc.RA118.004322","article-title":"Elastin is heterogeneously cross-linked","volume":"293","author":"Schr\u00e4der","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0175","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1016\/j.str.2006.09.008","article-title":"Proline and glycine control protein self-organization into elastomeric or amyloid fibrils","volume":"14","author":"Rauscher","year":"2006","journal-title":"Structure"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0180","doi-asserted-by":"crossref","first-page":"1086","DOI":"10.1016\/S0006-3495(02)75468-4","article-title":"Solid-state 13C NMR reveals effects of temperature and Hydrationon elastin","volume":"82","author":"Perry","year":"2002","journal-title":"Biophys. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0185","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1002\/bip.10470","article-title":"13C CPMAS NMR studies of the elastin-like polypeptide (LGGVG)n","volume":"70","author":"Kumashiro","year":"2003","journal-title":"Biopolymers"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0190","doi-asserted-by":"crossref","first-page":"10057","DOI":"10.1074\/jbc.M113.533893","article-title":"Conformational transitions of the cross-linking domains of elastin during self-assembly","volume":"289","author":"Reichheld","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0195","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1111\/j.1432-1033.1997.00092.x","article-title":"Coacervation characteristics of recombinant human Tropoelastin","volume":"250","author":"Vrhovski","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0200","doi-asserted-by":"crossref","DOI":"10.1016\/j.colsurfb.2020.110776","article-title":"Glucose-induced structural changes and anomalous diffusion of elastin","volume":"188","author":"De","year":"2020","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0205","doi-asserted-by":"crossref","first-page":"7338","DOI":"10.1073\/pnas.1801205115","article-title":"Molecular model of human tropoelastin and implications of associated mutations","volume":"115","author":"Tarakanova","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0210","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.26526","article-title":"The liquid structure of elastin","volume":"6","author":"Rauscher","year":"2017","journal-title":"Elife"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0215","doi-asserted-by":"crossref","first-page":"4322","DOI":"10.1073\/pnas.1014280108","article-title":"Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity","volume":"108","author":"Baldock","year":"2011","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0220","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.addr.2012.06.009","article-title":"Tropoelastin \u2014 a multifaceted naturally smart material","volume":"65","author":"Mithieux","year":"2013","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0225","doi-asserted-by":"crossref","first-page":"1680","DOI":"10.1021\/bm034120l","article-title":"Mechanism for the phase transition of a genetically engineered elastin model peptide (VPGIG)40 in aqueous solution","volume":"4","author":"Yamaoka","year":"2003","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0230","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1042\/bj1280737","article-title":"The formation and stabilization of protein structure","volume":"128","author":"Anfinsen","year":"1972","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0235","doi-asserted-by":"crossref","first-page":"5064","DOI":"10.1021\/acsbiomaterials.1c00329","article-title":"De novo synthesis of elastin-like polypeptides (elps): an applied overview on the current experimental techniques","volume":"7","author":"Riziotis","year":"2021","journal-title":"ACS Biomater Sci. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0240","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.coche.2019.01.004","article-title":"Hierarchical assembly of elastin materials","volume":"24","author":"Wang","year":"2019","journal-title":"Curr. Opin. Chem. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0245","doi-asserted-by":"crossref","first-page":"2051","DOI":"10.1021\/acs.biomac.2c00053","article-title":"Injectable hydrogels of stimuli-responsive elastin and calmodulin-based triblock copolypeptides for controlled drug release","volume":"23","author":"Lee","year":"2022","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0250","doi-asserted-by":"crossref","first-page":"1954","DOI":"10.1007\/s11814-023-1473-4","article-title":"Thermoresponsive, dually cross-linked elastin-like-polypeptide (ELP) micelle hydrogel with recovery properties","volume":"40","author":"Choi","year":"2023","journal-title":"Korean J. Chem. Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0255","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.tibtech.2009.10.004","article-title":"Elastin-like polypeptides revolutionize recombinant protein expression and their biomedical application","volume":"28","author":"Floss","year":"2010","journal-title":"Trends Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0260","doi-asserted-by":"crossref","first-page":"334","DOI":"10.1016\/j.actbio.2024.01.014","article-title":"Contributions of collagen and elastin to elastic behaviours of tendon fascicle","volume":"176","author":"Ishizaki","year":"2024","journal-title":"Acta Biomater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0265","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1161\/CIRCRESAHA.122.321123","article-title":"Tropoelastin improves post-infarct cardiac function","volume":"132","author":"Hume","year":"2023","journal-title":"Circ. Res."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0270","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1002\/bip.22663","article-title":"Proline-poor hydrophobic domains modulate the assembly and material properties of polymeric elastin","volume":"103","author":"Muiznieks","year":"2015","journal-title":"Biopolymers"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0275","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1007\/s11064-019-02920-3","article-title":"Elastin-derived peptide VGVAPG affects production and secretion of testosterone in mouse astrocyte in vitro","volume":"45","author":"Szychowski","year":"2020","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0280","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1073\/pnas.84.4.995","article-title":"Effect of elastin peptides on ion fluxes in mononuclear cells, fibroblasts, and smooth muscle cells","volume":"84","author":"Jacob","year":"1987","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0285","doi-asserted-by":"crossref","first-page":"1100","DOI":"10.1016\/j.kint.2017.04.044","article-title":"Elastin insufficiency causes hypertension, structural defects and abnormal remodeling of renal vascular signaling","volume":"92","author":"Owens","year":"2017","journal-title":"Kidney Int."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0290","doi-asserted-by":"crossref","first-page":"1779","DOI":"10.1016\/S0735-1097(21)03135-1","article-title":"Selective deletion of elastin in smooth muscle cells identifies unique cell populations in neointima","volume":"77","author":"Lin","year":"2021","journal-title":"J. Am. Coll. Cardiol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0295","doi-asserted-by":"crossref","first-page":"1828","DOI":"10.1172\/JCI115204","article-title":"Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon","volume":"87","author":"Shapiro","year":"1991","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0300","doi-asserted-by":"crossref","first-page":"87","DOI":"10.1002\/jcp.20546","article-title":"Elastic fiber formation: a dynamic view of extracellular matrix assembly using timer reporters","volume":"207","author":"Kozel","year":"2006","journal-title":"J. Cell. Physiol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0305","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.matbio.2004.02.004","article-title":"Deposition of tropoelastin into the extracellular matrix requires a competent elastic fiber scaffold but not live cells","volume":"23","author":"Kozel","year":"2004","journal-title":"Matrix Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0310","doi-asserted-by":"crossref","first-page":"9989","DOI":"10.1021\/bi0610092","article-title":"Tropoelastin massively associates during coacervation to form quantized protein spheres","volume":"45","author":"Clarke","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0315","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.cis.2010.10.003","article-title":"Coacervation of tropoelastin","volume":"167","author":"Yeo","year":"2011","journal-title":"Adv. Colloid Interf. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0320","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1083\/jcb.40.2.366","article-title":"The elastic fiber. I. The separation and partial characterization of its macromolecular components","volume":"40","author":"Ross","year":"1969","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0325","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.biochi.2017.11.018","article-title":"Degradation of tropoelastin and skin elastin by neprilysin","volume":"146","author":"Mora Huertas","year":"2018","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0330","doi-asserted-by":"crossref","first-page":"1965","DOI":"10.1002\/hep.25567","article-title":"Elastin accumulation is regulated at the level of degradation by macrophage metalloelastase (MMP-12) during experimental liver fibrosis","volume":"55","author":"Pellicoro","year":"2012","journal-title":"Hepatology"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0335","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.biochi.2019.07.001","article-title":"MMP-14 degrades tropoelastin and elastin","volume":"165","author":"Miekus","year":"2019","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0340","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.biochi.2011.10.006","article-title":"The action of neutrophil serine proteases on elastin and its precursor","volume":"94","author":"Heinz","year":"2012","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0345","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1161\/01.ATV.0000134530.27208.41","article-title":"Lysosomal cysteine proteases in atherosclerosis","volume":"24","author":"Liu","year":"2004","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0350","doi-asserted-by":"crossref","first-page":"210","DOI":"10.7326\/0003-4819-55-2-210","article-title":"The collagen and elastin content of the lung in emphysema","volume":"55","author":"Pierce","year":"1961","journal-title":"Ann. Intern. Med."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0355","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1183\/13993003.01125-2016","article-title":"Age-dependent elastin degradation is enhanced in chronic obstructive pulmonary disease","volume":"48","author":"Huang","year":"2016","journal-title":"Eur. Respir. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0360","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/j.tcm.2012.12.004","article-title":"Elastin fragmentation and atherosclerosis progression: the elastokine concept","volume":"23","author":"Maurice","year":"2013","journal-title":"Trends Cardiovasc. Med."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0365","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1186\/s12885-020-6686-x","article-title":"Elastin is a key factor of tumor development in colorectal cancer","volume":"20","author":"Li","year":"2020","journal-title":"BMC Cancer"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0370","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0021-9150(79)90195-3","article-title":"Elastin--lipid interaction action in the arterial wall. Part 1. Extraction of elastin from human aortic intima","volume":"33","author":"Noma","year":"1979","journal-title":"Atherosclerosis"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0375","doi-asserted-by":"crossref","first-page":"6191","DOI":"10.1016\/S0021-9258(19)42239-4","article-title":"Isolation and characterization of cross-linked peptides from elastin","volume":"249","author":"Foster","year":"1974","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0380","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1038\/185320a0","article-title":"An elastin gel","volume":"185","author":"Grant","year":"1960","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0385","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1016\/j.biomaterials.2005.06.013","article-title":"Biocompatibility and remodeling potential of pure arterial elastin and collagen scaffolds","volume":"27","author":"Simionescu","year":"2006","journal-title":"Biomaterials"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0390","doi-asserted-by":"crossref","DOI":"10.1016\/j.jclepro.2019.118471","article-title":"Extraction of elastin from tannery wastes: a cleaner technology for tannery waste management","volume":"243","author":"Yoseph","year":"2020","journal-title":"J. Clean. Prod."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0395","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1002\/psc.2866","article-title":"High-molecular-weight poly(Gly-Val-Gly-Val-pro) synthesis through microwave irradiation","volume":"22","author":"Goto","year":"2016","journal-title":"J. Pept. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0400","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.colsurfb.2017.02.014","article-title":"Multi-scale characterization of thermoresponsive dendritic elastin-like peptides","volume":"153","author":"Zhou","year":"2017","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0405","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1016\/0003-9861(90)90521-Y","article-title":"Production of recombinant human tropoelastin: characterization and demonstration of immunologic and chemotactic activity","volume":"280","author":"Indik","year":"1990","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0410","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0378-1119(94)00848-M","article-title":"Total synthesis and expression in Escherichia coli of a gene encoding human tropoelastin","volume":"154","author":"Martin","year":"1995","journal-title":"Gene"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0415","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1021\/bp00016a012","article-title":"Production and purification of a recombinant elastomeric polypeptide, G-(VPGVG)19-VPGV, from Escherichia coli","volume":"8","author":"Mcpherson","year":"1992","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0420","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1006\/prep.1996.0008","article-title":"Product purification by reversible phase transition following Escherichia coli expression of genes encoding up to 251 repeats of the elastomeric pentapeptide GVGVP","volume":"7","author":"McPherson","year":"1996","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0425","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1021\/bp0503742","article-title":"Ultra-high expression of a thermally responsive recombinant fusion protein in E. Coli","volume":"22","author":"Chow","year":"2006","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0430","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2025.145936","article-title":"Process optimization and scale-up of high-efficient biosynthesis for recombinant collagen-elastin fusion protein","volume":"320","author":"Zhou","year":"2025","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0435","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1002\/btpr.717","article-title":"Secretion of elastin-like polypeptides with different transition temperatures by Pichia pastoris","volume":"28","author":"Schipperus","year":"2012","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0440","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1042\/BJ20060544","article-title":"Functional expression of a biologically active fragment of soluble gp130 as an ELP-fusion protein in transgenic plants: purification via inverse transition cycling","volume":"398","author":"Lin","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0445","doi-asserted-by":"crossref","first-page":"5245","DOI":"10.1039\/C9TB00821G","article-title":"Incorporation of short, charged peptide tags affects the temperature responsiveness of positively-charged elastin-like polypeptides","volume":"7","author":"Lin","year":"2019","journal-title":"J. Mater. Chem. B"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0450","doi-asserted-by":"crossref","DOI":"10.1016\/j.addr.2022.114541","article-title":"Cytokine conjugates to elastin-like polypeptides","volume":"190","author":"Gong","year":"2022","journal-title":"Adv. Drug Deliv. Rev."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0455","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.pep.2016.01.010","article-title":"Recombinant production and purification of short hydrophobic elastin-like polypeptides with low transition temperatures","volume":"121","author":"Bataille","year":"2016","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0460","doi-asserted-by":"crossref","first-page":"5265","DOI":"10.1021\/acs.biomac.3c00779","article-title":"Enhancement of aggregate formation through aromatic compound adsorption in elastin-like peptide (FPGVG)5 analogs","volume":"24","author":"Suyama","year":"2023","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0465","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1007\/s12257-024-00102-9","article-title":"Memristor device based on bioengineered elastin-like polypeptide and its bionanohybrid","volume":"29","author":"Lee","year":"2024","journal-title":"Biotechnol. Bioprocess Eng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0470","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.biomaterials.2015.07.041","article-title":"In vitro myogenesis induced by human recombinant elastin-like proteins","volume":"67","author":"D'Andrea","year":"2015","journal-title":"Biomaterials"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0475","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1016\/j.jbiotec.2019.04.010","article-title":"Production, purification and characterization of an elastin-like polypeptide containing the Ile-Lys-Val-ala-Val (IKVAV) peptide for tissue engineering applications","volume":"298","author":"Paiva dos Santos","year":"2019","journal-title":"J. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0480","doi-asserted-by":"crossref","DOI":"10.1088\/1758-5090\/ab10a5","article-title":"Use of proteolytic sequences with different cleavage kinetics as a way to generate hydrogels with preprogrammed cell-infiltration patterns imparted over their given 3D spatial structure","volume":"11","author":"Flora","year":"2019","journal-title":"Biofabrication"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0485","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1080\/00914037.2016.1217534","article-title":"Thermosensitive elastin-derived polypeptide hydrogels crosslinked by genipin","volume":"66","author":"Zhao","year":"2017","journal-title":"Int. J. Polym. Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0490","doi-asserted-by":"crossref","DOI":"10.1002\/mabi.202300203","article-title":"Fabrication of insoluble elastin by enzyme-free cross-linking","volume":"23","author":"Hedtke","year":"2023","journal-title":"Macromol. Biosci."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0495","doi-asserted-by":"crossref","first-page":"4814","DOI":"10.1002\/adfm.201501489","article-title":"A highly elastic and rapidly crosslinkable elastin-like polypeptide-based hydrogel for biomedical applications","volume":"25","author":"Zhang","year":"2015","journal-title":"Adv. Funct. Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0500","doi-asserted-by":"crossref","DOI":"10.1016\/j.cej.2022.135155","article-title":"Design of functional hydrogels using smart polymer based on elastin-like polypeptides","volume":"435","author":"Guo","year":"2022","journal-title":"Chem. Eng. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0505","doi-asserted-by":"crossref","first-page":"4149","DOI":"10.1021\/acs.biomac.0c00939","article-title":"Controlled production of elastin-like recombinamer polymer-based membranes at a liquid\u2013liquid interface by click chemistry","volume":"21","author":"Gonz\u00e1lez-P\u00e9rez","year":"2020","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0510","article-title":"\u201cIn-situ\u201d formation of elastin-like recombinamer hydrogels with tunable viscoelasticity through efficient one-pot process","volume":"25","author":"Misbah","year":"2024","journal-title":"Mater. Today Bio."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0515","doi-asserted-by":"crossref","first-page":"3678","DOI":"10.1021\/acs.biomac.2c00562","article-title":"Protein vesicles with pH-responsive disassembly","volume":"23","author":"Dautel","year":"2022","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0520","doi-asserted-by":"crossref","first-page":"7156","DOI":"10.1021\/acs.biomac.4c00751","article-title":"Exploring LCST- and UCST-like behavior of branched molecules bearing repeat units of elastin-like peptides as side components","volume":"25","author":"Tanaka","year":"2024","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0525","doi-asserted-by":"crossref","first-page":"24385","DOI":"10.1021\/acsami.1c00676","article-title":"Switchable self-assembly of elastin- and resilin-based block copolypeptides with converse phase transition behaviors","volume":"13","author":"Basheer","year":"2021","journal-title":"ACS Appl. Mater. Interfaces"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0530","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.jconrel.2018.03.015","article-title":"Fusion of fibroblast growth factor 21 to a thermally responsive biopolymer forms an injectable depot with sustained anti-diabetic action","volume":"277","author":"Gilroy","year":"2018","journal-title":"J. Control. Release"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0535","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1021\/acs.biomac.1c01251","article-title":"Intracellular dynamin elastin-like polypeptides assemble into rodlike, spherical, and reticular dynasomes","volume":"23","author":"Avila","year":"2022","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0540","doi-asserted-by":"crossref","first-page":"46733","DOI":"10.1021\/acsomega.3c09325","article-title":"Elastin-like recombinamers as a biotechnological platform for the development of cytokine-functionalized materials","volume":"9","author":"Gon\u00e7alves","year":"2024","journal-title":"ACS Omega."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0545","article-title":"Construction of a collagen-like protein based on elastin-like polypeptide fusion and evaluation of its performance in promoting wound healing","author":"Chen","year":"2023","journal-title":"Molecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0550","doi-asserted-by":"crossref","DOI":"10.21769\/BioProtoc.5342","article-title":"A novel protein purification approach using elastin-like polypeptides (ELP) with his-tag assistance","volume":"15","author":"Chae","year":"2025","journal-title":"Bio-protocol"},{"issue":"2","key":"10.1016\/j.ijbiomac.2025.149116_bb0555","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1360\/SSC-2022-0225","article-title":"A crosslinked hydrogel based on recombinant human elastin for rapid repair of photodamaged skin","volume":"53","author":"Li","year":"2023","journal-title":"Sci. Sin. Chim."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0560","doi-asserted-by":"crossref","first-page":"11698","DOI":"10.1021\/acs.iecr.9b00769","article-title":"Protein purification by ethanol-induced phase transitions of the elastin-like polypeptide (ELP)","volume":"58","author":"Mills","year":"2019","journal-title":"Ind. Eng. Chem. Res."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0565","doi-asserted-by":"crossref","first-page":"749","DOI":"10.3390\/nano14090749","article-title":"Characterization of a chimeric Resilin-elastin structural protein dedicated to 3D bioprinting as a bioink component","volume":"14","author":"Cecuda-Adamczewska","year":"2024","journal-title":"Nanomaterials"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0570","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1039\/C3PY00537B","article-title":"A quantitative recipe for engineering protein polymer nanoparticles","volume":"5","author":"Janib","year":"2014","journal-title":"Polym. Chem."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0575","doi-asserted-by":"crossref","first-page":"9231","DOI":"10.1016\/j.biomaterials.2011.06.010","article-title":"Recombinant exon-encoded resilins for elastomeric biomaterials","volume":"32","author":"Qin","year":"2011","journal-title":"Biomaterials"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0580","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1021\/bm101322m","article-title":"Elastin-like polypeptide based hydroxyapatite bionanocomposites","volume":"12","author":"Wang","year":"2011","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0585","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/1475-2859-12-21","article-title":"Batch production of a silk-elastin-like protein in E. Coli BL21(DE3): key parameters for optimisation","volume":"12","author":"Collins","year":"2013","journal-title":"Microb. Cell Factories"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0590","doi-asserted-by":"crossref","first-page":"1810","DOI":"10.1002\/btpr.208","article-title":"Expression of a recombinant elastin-like protein in pichia pastoris","volume":"25","author":"Sallach","year":"2009","journal-title":"Biotechnol. Prog."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0595","doi-asserted-by":"crossref","first-page":"2505","DOI":"10.1002\/bit.28158","article-title":"Synthesis of single-chain antibody fragment fused to the elastin-like polypeptide in Nicotiana benthamiana and its application in affinity precipitation of difficult to produce proteins","volume":"119","author":"Mar\u00edn Viegas","year":"2022","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0600","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.copbio.2019.10.006","article-title":"Proteases of Nicotiana benthamiana: an emerging battle for molecular farming","volume":"61","author":"Jutras","year":"2020","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0605","doi-asserted-by":"crossref","first-page":"27946","DOI":"10.1021\/acsomega.1c03821","article-title":"One-pot synthesis of multiple stimuli-responsive magnetic nanomaterials based on the biomineralization of elastin-like polypeptides","volume":"6","author":"Zhou","year":"2021","journal-title":"ACS Omega"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0610","doi-asserted-by":"crossref","first-page":"2475","DOI":"10.1021\/bm060507n","article-title":"Simultaneous phase transition of ELP tagged molecules and free ELP: an efficient and reversible capture system","volume":"7","author":"Ge","year":"2006","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0615","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1021\/acs.biomac.5b01604","article-title":"Effect of ELP sequence and fusion protein design on concentrated solution self-assembly","volume":"17","author":"Qin","year":"2016","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0620","first-page":"4242","article-title":"Construction and biological activity of metallothionein fused with ELP","volume":"40","author":"Liu","year":"2024","journal-title":"Sheng Wu Gong Cheng Xue Bao"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0625","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1039\/C8BM00124C","article-title":"Rapid and simple purification of elastin-like polypeptides directly from whole cells and cell lysates by organic solvent extraction","volume":"6","author":"VerHeul","year":"2018","journal-title":"Biomater. Sci."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0630","doi-asserted-by":"crossref","first-page":"1990","DOI":"10.1021\/acs.biomac.1c00096","article-title":"Development of a fast organic extraction\u2013precipitation method for improved purification of elastin-like polypeptides that is independent of sequence and molecular weight","volume":"22","author":"Sweet","year":"2021","journal-title":"Biomacromolecules"},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0635","article-title":"Bioinspired genetic and chemical engineering of protein hydrogels for programable multi-responsive actuation","volume":"13","author":"Ji","year":"2024","journal-title":"Adv. Healthc. Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0640","doi-asserted-by":"crossref","first-page":"1227","DOI":"10.1021\/acs.accounts.3c00694","article-title":"Self-assembled recombinant elastin and globular protein vesicles with tunable properties for diverse applications","volume":"57","author":"Gray","year":"2024","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0645","doi-asserted-by":"crossref","DOI":"10.1002\/adma.202003915","article-title":"Human-recombinant-elastin-based bioinks for 3D bioprinting of vascularized soft tissues","volume":"32","author":"Lee","year":"2020","journal-title":"Adv. Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0650","doi-asserted-by":"crossref","DOI":"10.1016\/j.eurpolymj.2019.109334","article-title":"Layer-by-layer biofabrication of coronary covered stents with clickable elastin-like recombinamers","volume":"121","author":"Fern\u00e1ndez-Colino","year":"2019","journal-title":"Eur. Polym. J."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0655","doi-asserted-by":"crossref","first-page":"6890","DOI":"10.1021\/acsanm.2c00889","article-title":"Graphene oxide\/elastin nanostructure-based membranes for bone regeneration","volume":"5","author":"Li","year":"2022","journal-title":"ACS Appl. Nano Mater."},{"key":"10.1016\/j.ijbiomac.2025.149116_bb0660","doi-asserted-by":"crossref","DOI":"10.1016\/j.ijbiomac.2025.145467","article-title":"Multipotent anti-aging recombinant human elastin: counteracting zebrafish caudal fin shrinkage and D-galactose-induced intrinsic skin aging in mice","volume":"319","author":"Zhu","year":"2025","journal-title":"Int. J. Biol. Macromol."}],"updated-by":[{"DOI":"10.1016\/j.ijbiomac.2025.149870","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2025,12,30]],"date-time":"2025-12-30T00:00:00Z","timestamp":1767052800000}},{"DOI":"10.1016\/j.ijbiomac.2025.149870","type":"erratum","label":"Erratum","source":"publisher","updated":{"date-parts":[[2026,1,1]],"date-time":"2026-01-01T00:00:00Z","timestamp":1767225600000}}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025096734?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813025096734?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,6,11]],"date-time":"2026-06-11T08:46:05Z","timestamp":1781167565000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813025096734"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12]]},"references-count":132,"alternative-id":["S0141813025096734"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.149116","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2025,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Recombinant elastin for biomedical applications\u2014Advances in molecular design, expression platforms, and purification strategies: A review","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2025.149116","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2025 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}],"article-number":"149116"}}