{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,2]],"date-time":"2025-07-02T04:30:16Z","timestamp":1751430616070,"version":"3.37.3"},"reference-count":36,"publisher":"Springer Science and Business Media LLC","issue":"2","license":[{"start":{"date-parts":[[2024,5,27]],"date-time":"2024-05-27T00:00:00Z","timestamp":1716768000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2024,5,27]],"date-time":"2024-05-27T00:00:00Z","timestamp":1716768000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/100000057","name":"National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["1R16GM145575-01"],"award-info":[{"award-number":["1R16GM145575-01"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell Biochem Biophys"],"published-print":{"date-parts":[[2024,6]]},"DOI":"10.1007\/s12013-024-01293-x","type":"journal-article","created":{"date-parts":[[2024,5,27]],"date-time":"2024-05-27T18:02:23Z","timestamp":1716832943000},"page":"1389-1395","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Screening Carbon Nano Materials for Preventing Amyloid Protein Aggregation by Adopting a Facile Method"],"prefix":"10.1007","volume":"82","author":[{"given":"Daisy L.","family":"Wilson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ana","family":"Carreon","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sampath","family":"Chinnam","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hamidreza","family":"Sharifan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jyoti","family":"Ahlawat","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2194-5228","authenticated-orcid":false,"given":"Mahesh","family":"Narayan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2024,5,27]]},"reference":[{"issue":"6","key":"1293_CR1","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1016\/j.cocis.2012.08.001","volume":"17","author":"J Adamcik","year":"2012","unstructured":"Adamcik, J., & Mezzenga, R. (2012). Study of amyloid fibrils via atomic force microscopy. Current Opinion in Colloid & Interface Science, 17(6), 369\u2013376. https:\/\/doi.org\/10.1016\/j.cocis.2012.08.001.","journal-title":"Current Opinion in Colloid & Interface Science"},{"issue":"7","key":"1293_CR2","doi-asserted-by":"publisher","first-page":"1405","DOI":"10.1016\/j.bbapap.2010.04.001","volume":"1804","author":"M Biancalana","year":"2010","unstructured":"Biancalana, M., & Koide, S. (2010). Molecular mechanism of Thioflavin-T binding to amyloid fibrils. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1804(7), 1405\u20131412. https:\/\/doi.org\/10.1016\/j.bbapap.2010.04.001.","journal-title":"Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"},{"issue":"7","key":"1293_CR3","doi-asserted-by":"publisher","first-page":"1095","DOI":"10.1016\/j.str.2016.05.002","volume":"24","author":"S Chan","year":"2016","unstructured":"Chan, S., Yau, J., Ing, C., Liu, K., Farber, P., Won, A., Bhandari, V., Kara-Yacoubian, N., Seraphim, T., Chakrabarti, N., Kay, L., Yip, C., Pom\u00e8s, R., Sharpe, S., & Houry, W. (2016). Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone. Structure, 24(7), 1095\u20131109. https:\/\/doi.org\/10.1016\/j.str.2016.05.002.","journal-title":"Structure"},{"key":"1293_CR4","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1016\/j.sbi.2014.12.004","volume":"30","author":"AJ Doig","year":"2015","unstructured":"Doig, A. J., & Derreumaux, P. (2015). Inhibition of protein aggregation and amyloid formation by small molecules. Current Opinion in Structural Biology, 30, 50\u201356. https:\/\/doi.org\/10.1016\/j.sbi.2014.12.004.","journal-title":"Current Opinion in Structural Biology"},{"key":"1293_CR5","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1016\/j.sbi.2019.05.003","volume":"58","author":"AW Fitzpatrick","year":"2019","unstructured":"Fitzpatrick, A. W., & Saibil, H. R. (2019). Cryo-EM of amyloid fibrils and cellular aggregates. Current Opinion in Structural Biology, 58, 34\u201342. https:\/\/doi.org\/10.1016\/j.sbi.2019.05.003.","journal-title":"Current Opinion in Structural Biology"},{"issue":"3","key":"1293_CR6","doi-asserted-by":"publisher","first-page":"2423","DOI":"10.1021\/acsanm.0c02792","volume":"4","author":"ED Guerrero","year":"2021","unstructured":"Guerrero, E. D., Lopez-Velazquez, A. M., Ahlawat, J., & Narayan, M. (2021). Carbon Quantum Dots for Treatment of Amyloid Disorders. ACS Applied Nano Materials, 4(3), 2423\u20132433. https:\/\/doi.org\/10.1021\/acsanm.0c02792.","journal-title":"ACS Applied Nano Materials"},{"issue":"13","key":"1293_CR7","doi-asserted-by":"publisher","first-page":"8648","DOI":"10.1073\/pnas.132098999","volume":"99","author":"JH Ippel","year":"2002","unstructured":"Ippel, J. H., Olofsson, A., Schleucher, J., Lundgren, E., & Wijmenga, S. S. (2002). Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy. Proceedings of the National Academy of Sciences, 99(13), 8648\u20138653. https:\/\/doi.org\/10.1073\/pnas.132098999.","journal-title":"Proceedings of the National Academy of Sciences"},{"issue":"9 Jun","key":"1293_CR8","doi-asserted-by":"publisher","first-page":"1919","DOI":"10.1002\/pro.4144","volume":"30","author":"Rahamtullah","year":"2021","unstructured":"Rahamtullah, & Mishra, R. (2021). Nicking and fragmentation are responsible for \u03b1\u2010lactalbumin amyloid fibril formation at acidic PH and elevated temperature. Protein Science, 30(9 Jun), 1919\u20131934. https:\/\/doi.org\/10.1002\/pro.4144. Accessed 4 Feb. 2024.","journal-title":"Protein Science"},{"issue":"4","key":"1293_CR9","doi-asserted-by":"publisher","first-page":"532","DOI":"10.1002\/ana.22615","volume":"70","author":"M Jucker","year":"2011","unstructured":"Jucker, M., & Walker, L. C. (2011). Pathogenic protein seeding in alzheimer disease and other neurodegenerative disorders. Annals of Neurology, 70(4), 532\u2013540. https:\/\/doi.org\/10.1002\/ana.22615.","journal-title":"Annals of Neurology"},{"issue":"9","key":"1293_CR10","doi-asserted-by":"publisher","first-page":"812","DOI":"10.1038\/s41565-018-0179-y","volume":"13","author":"D Kim","year":"2018","unstructured":"Kim, D., Yoo, J. M., Hwang, H., Lee, J., Lee, S. H., Yun, S. P., Park, M. J., Lee, M., Choi, S., Kwon, S. H., Lee, S., Kwon, S. H., Kim, S., Park, Y. J., Kinoshita, M., Lee, Y. H., Shin, S., Paik, S. R., Lee, S. J., & Ko, H. S. (2018). Graphene quantum dots prevent \u03b1-synucleinopathy in Parkinson\u2019s disease. Nature Nanotechnology, 13(9), 812\u2013818. https:\/\/doi.org\/10.1038\/s41565-018-0179-y.","journal-title":"Nature Nanotechnology"},{"issue":"5259","key":"1293_CR11","doi-asserted-by":"publisher","first-page":"680","DOI":"10.1038\/227680a0","volume":"227","author":"UK Laemmli","year":"1970","unstructured":"Laemmli, U. K. (1970). Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature, 227(5259), 680\u2013685. https:\/\/doi.org\/10.1038\/227680a0.","journal-title":"Nature"},{"issue":"2","key":"1293_CR12","doi-asserted-by":"publisher","first-page":"655","DOI":"10.1016\/0003-2697(78)90792-3","volume":"86","author":"LC Lane","year":"1978","unstructured":"Lane, L. C. (1978). A simple method for stabilizing protein-sulfhydryl groups during SDS-gel electrophoresis. Analytical Biochemistry, 86(2), 655\u2013664. https:\/\/doi.org\/10.1016\/0003-2697(78)90792-3.","journal-title":"Analytical Biochemistry"},{"issue":"22","key":"1293_CR13","doi-asserted-by":"publisher","first-page":"4846","DOI":"10.1021\/bi900394b","volume":"48","author":"A Loksztejn","year":"2009","unstructured":"Loksztejn, A., & Dzwolak, W. (2009). Noncooperative dimethyl sulfoxide-induced dissection of insulin fibrils: Toward soluble building blocks of amyloid. Biochemistry, 48(22), 4846\u20134851. https:\/\/doi.org\/10.1021\/bi900394b.","journal-title":"Biochemistry"},{"issue":"23","key":"1293_CR14","doi-asserted-by":"publisher","first-page":"7322","DOI":"10.1039\/c2nr31657a","volume":"4","author":"M Mahmoudi","year":"2012","unstructured":"Mahmoudi, M., Akhavan, O., Ghavami, M., Rezaee, F., & Ghiasi, S. M. A. (2012). Graphene oxide strongly inhibits amyloid beta fibrillation. Nanoscale, 4(23), 7322 https:\/\/doi.org\/10.1039\/c2nr31657a.","journal-title":"Nanoscale"},{"issue":"1","key":"1293_CR15","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1073\/pnas.222681699","volume":"100","author":"G Bitan","year":"2003","unstructured":"Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2003). Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways. Proceedings of the National Academy of Sciences of the United States of America, 100(1), 330\u2013335. https:\/\/doi.org\/10.1073\/pnas.222681699.","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"issue":"6","key":"1293_CR16","doi-asserted-by":"publisher","first-page":"357","DOI":"10.1021\/ar000214l","volume":"37","author":"G Bitan","year":"2004","unstructured":"Bitan, G., & Teplow, D. B. (2004). Rapid photochemical cross-linkinga new tool for studies of metastable, amyloidogenic protein assemblies. Accounts of Chemical Research, 37(6), 357\u2013364. https:\/\/doi.org\/10.1021\/ar000214l.","journal-title":"Accounts of Chemical Research"},{"key":"1293_CR17","doi-asserted-by":"publisher","unstructured":"Pujol-Pina, R., Vilapriny\u00f3-Pascual, S., Mazzucato, R., Arcella, A., Vilaseca, M., Orozco, M., & Carulla, N. (2015). SDS-PAGE analysis of A\u03b2 oligomers is disserving research into Alzheimer\u00b4s disease: appealing for ESI-IM-MS. Scientific Reports, 5(1). https:\/\/doi.org\/10.1038\/srep14809.","DOI":"10.1038\/srep14809"},{"issue":"5","key":"1293_CR18","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1002\/bmb.20321","volume":"37","author":"J Markwell","year":"2009","unstructured":"Markwell, J. (2009). Fundamental laboratory approaches for biochemistry and biotechnology, 2nd edition. Biochemistry and Molecular Biology Education, 37(5), 317\u2013318. https:\/\/doi.org\/10.1002\/bmb.20321.","journal-title":"Biochemistry and Molecular Biology Education"},{"key":"1293_CR19","doi-asserted-by":"publisher","unstructured":"Morris, K. L., & Serpell, L. C. (2012). X-ray fibre diffraction studies of amyloid fibrils. Methods in Molecular Biology, 121\u2013135. https:\/\/doi.org\/10.1007\/978-1-61779-551-0_9.","DOI":"10.1007\/978-1-61779-551-0_9"},{"issue":"41","key":"1293_CR20","doi-asserted-by":"publisher","first-page":"10481","DOI":"10.1073\/pnas.1804198115","volume":"115","author":"J Pujols","year":"2018","unstructured":"Pujols, J., Pe\u00f1a-D\u00edaz, S., L\u00e1zaro, D. F., Peccati, F., Pinheiro, F., Gonz\u00e1lez, D., Carija, A., Navarro, S., Conde-Gim\u00e9nez, M., Garc\u00eda, J., Guardiola, S., Giralt, E., Salvatella, X., Sancho, J., Sodupe, M., Outeiro, T. F., Dalf\u00f3, E., & Ventura, S. (2018). Small molecule inhibits \u03b1-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons. Proceedings of the National Academy of Sciences, 115(41), 10481\u201310486. https:\/\/doi.org\/10.1073\/pnas.1804198115.","journal-title":"Proceedings of the National Academy of Sciences"},{"key":"1293_CR21","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1016\/j.ebiom.2016.03.035","volume":"6","author":"U Sengupta","year":"2016","unstructured":"Sengupta, U., Nilson, A. N., & Kayed, R. (2016). The role of amyloid-\u03b2 oligomers in toxicity, propagation, and immunotherapy. EBioMedicine, 6, 42\u201349. https:\/\/doi.org\/10.1016\/j.ebiom.2016.03.035.","journal-title":"EBioMedicine"},{"issue":"6","key":"1293_CR22","doi-asserted-by":"publisher","first-page":"2741","DOI":"10.1021\/acschemneuro.8b00650","volume":"10","author":"P Singh","year":"2019","unstructured":"Singh, P., & Bhat, R. (2019). Binding of noradrenaline to native and intermediate states during the fibrillation of \u03b1-synuclein leads to the formation of stable and structured cytotoxic species. ACS Chemical Neuroscience, 10(6), 2741\u20132755. https:\/\/doi.org\/10.1021\/acschemneuro.8b00650.","journal-title":"ACS Chemical Neuroscience"},{"issue":"9","key":"1293_CR23","doi-asserted-by":"publisher","first-page":"3911","DOI":"10.1021\/acschemneuro.9b00445","volume":"10","author":"S Sreenivasan","year":"2019","unstructured":"Sreenivasan, S., & Narayan, M. (2019). Learnings from protein folding projected onto amyloid misfolding. ACS Chemical Neuroscience, 10(9), 3911\u20133913. https:\/\/doi.org\/10.1021\/acschemneuro.9b00445.","journal-title":"ACS Chemical Neuroscience"},{"issue":"8","key":"1293_CR24","doi-asserted-by":"publisher","first-page":"3343","DOI":"10.1021\/acschemneuro.9b00353","volume":"10","author":"S Sreeprasad","year":"2019","unstructured":"Sreeprasad, S., & Narayan, M. (2019). Nanoscopic portrait of an amyloidogenic pathway visualized through tip-enhanced Raman spectroscopy. ACS Chemical Neuroscience, 10(8), 3343\u20133345. https:\/\/doi.org\/10.1021\/acschemneuro.9b00353.","journal-title":"ACS Chemical Neuroscience"},{"issue":"4","key":"1293_CR25","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1007\/s12551-016-0218-6","volume":"8","author":"J Stetefeld","year":"2016","unstructured":"Stetefeld, J., McKenna, S. A., & Patel, T. R. (2016). Dynamic light scattering: a practical guide and applications in biomedical sciences. Biophysical Reviews, 8(4), 409\u2013427. https:\/\/doi.org\/10.1007\/s12551-016-0218-6.","journal-title":"Biophysical Reviews"},{"issue":"1","key":"1293_CR26","doi-asserted-by":"publisher","first-page":"e54541","DOI":"10.1371\/journal.pone.0054541","volume":"8","author":"AM Streets","year":"2013","unstructured":"Streets, A. M., Sourigues, Y., Kopito, R. R., Melki, R., & Quake, S. R. (2013). Simultaneous measurement of amyloid fibril formation by dynamic light scattering and fluorescence reveals complex aggregation kinetics. PLoS ONE, 8(1), e54541 https:\/\/doi.org\/10.1371\/journal.pone.0054541.","journal-title":"PLoS ONE"},{"key":"1293_CR27","doi-asserted-by":"publisher","DOI":"10.1016\/j.phrs.2021.105661","volume":"169","author":"L Subedi","year":"2021","unstructured":"Subedi, L., & Gaire, B. P. (2021). Tanshinone IIA: A phytochemical as a promising drug candidate for neurodegenerative diseases. Pharmacological Research, 169, 105661 https:\/\/doi.org\/10.1016\/j.phrs.2021.105661.","journal-title":"Pharmacological Research"},{"issue":"1","key":"1293_CR28","doi-asserted-by":"publisher","first-page":"279","DOI":"10.1146\/annurev-physchem-032210-103539","volume":"62","author":"R Tycko","year":"2011","unstructured":"Tycko, R. (2011). Solid-state NMR studies of amyloid fibril structure. Annual Review of Physical Chemistry, 62(1), 279\u2013299. https:\/\/doi.org\/10.1146\/annurev-physchem-032210-103539.","journal-title":"Annual Review of Physical Chemistry"},{"issue":"4","key":"1293_CR29","doi-asserted-by":"publisher","first-page":"1362","DOI":"10.1021\/bm0498979","volume":"5","author":"BA Vernaglia","year":"2004","unstructured":"Vernaglia, B. A., Huang, J., & Clark, E. D. (2004). Guanidine hydrochloride can induce amyloid fibril formation from Hen Egg-white lysozyme. Biomacromolecules, 5(4), 1362\u20131370. https:\/\/doi.org\/10.1021\/bm0498979.","journal-title":"Biomacromolecules"},{"issue":"42","key":"1293_CR30","doi-asserted-by":"publisher","first-page":"19995","DOI":"10.1039\/c8nr07180b","volume":"10","author":"M Wang","year":"2018","unstructured":"Wang, M., Sun, Y., Cao, X., Peng, G., Javed, I., Kakinen, A., Davis, T. P., Lin, S., Liu, J., Ding, F., & Ke, P. C. (2018). Graphene quantum dots against human IAPP aggregation and toxicity in vivo. Nanoscale, 10(42), 19995\u201320006. https:\/\/doi.org\/10.1039\/c8nr07180b.","journal-title":"Nanoscale"},{"issue":"12","key":"1293_CR31","doi-asserted-by":"publisher","first-page":"4287","DOI":"10.3390\/ijms21124287","volume":"21","author":"T Watanabe-Nakayama","year":"2020","unstructured":"Watanabe-Nakayama, T., Sahoo, B. R., Ramamoorthy, A., & Ono, K. (2020). High-speed atomic force microscopy reveals the structural dynamics of the amyloid-\u03b2 and amylin aggregation pathways. International Journal of Molecular Sciences, 21(12), 4287 https:\/\/doi.org\/10.3390\/ijms21124287.","journal-title":"International Journal of Molecular Sciences"},{"key":"1293_CR32","doi-asserted-by":"publisher","unstructured":"Kumar, J., Varela\u2010Ramirez, A., & Narayan, M. (2024). Development of novel carbon\u2010based biomedical platforms for intervention in xenotoxicant\u2010induced Parkinson\u2019s disease onset. BMEMat, e12072. https:\/\/doi.org\/10.1002\/bmm2.12072.","DOI":"10.1002\/bmm2.12072"},{"key":"1293_CR33","doi-asserted-by":"publisher","unstructured":"Kumar, J., Delgado, S. A., Sarma, H., & Narayan, M. (2023). Caffeic acid recarbonization: A green chemistry, sustainable carbon nano material platform to intervene in neurodegeneration induced by emerging contaminants. Environmental Research, 237, 116932. https:\/\/doi.org\/10.1016\/j.envres.2023.116932.","DOI":"10.1016\/j.envres.2023.116932"},{"key":"1293_CR34","doi-asserted-by":"publisher","unstructured":"Henriquez, G., Ahlawat, J., Fairman, R., & Narayan, M. (2022). Citric acid-derived carbon quantum dots attenuate paraquat-induced neuronal compromise in vitro and in vivo. ACS Chemical Neuroscience, 13(16), 2399\u20132409. https:\/\/doi.org\/10.1021\/acschemneuro.2c00099.","DOI":"10.1021\/acschemneuro.2c00099"},{"key":"1293_CR35","doi-asserted-by":"publisher","unstructured":"Ahlawat, J., Henriquez, G., Varela-Ramirez, A., Fairman, R., & Narayan, M. (2022). Gelatin-derived carbon quantum dots mitigate herbicide-induced neurotoxic effects in vitro and in vivo. Biomaterials Advances, 137, 212837. https:\/\/doi.org\/10.1016\/j.bioadv.2022.212837.","DOI":"10.1016\/j.bioadv.2022.212837"},{"key":"1293_CR36","doi-asserted-by":"publisher","unstructured":"Asil, S. M., & Narayan, M. (2024). Molecular interactions between gelatin-derived carbon quantum dots and Apo-myoglobin: Implications for carbon nanomaterial frameworks. International Journal of Biological Macromolecules, 130416. https:\/\/doi.org\/10.1016\/j.ijbiomac.2024.130416.","DOI":"10.1016\/j.ijbiomac.2024.130416"}],"container-title":["Cell Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12013-024-01293-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s12013-024-01293-x\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s12013-024-01293-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,8,24]],"date-time":"2024-08-24T06:24:57Z","timestamp":1724480697000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s12013-024-01293-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,5,27]]},"references-count":36,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2024,6]]}},"alternative-id":["1293"],"URL":"https:\/\/doi.org\/10.1007\/s12013-024-01293-x","relation":{},"ISSN":["1085-9195","1559-0283"],"issn-type":[{"type":"print","value":"1085-9195"},{"type":"electronic","value":"1559-0283"}],"subject":[],"published":{"date-parts":[[2024,5,27]]},"assertion":[{"value":"24 April 2024","order":1,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 May 2024","order":2,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with ethical standards"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of interest"}}]}}