{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T09:53:53Z","timestamp":1792662833586,"version":"4.5.0"},"reference-count":53,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"11","funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["EB000768"],"award-info":[{"award-number":["EB000768"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81671725"],"award-info":[{"award-number":["81671725"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Sci. Adv."],"published-print":{"date-parts":[[2018,11,2]]},"abstract":"<jats:p>Misfolded proteins in amyloid plaques in transgenic Alzheimer\u2019s disease mouse brains are visualized directly without labeling.<\/jats:p>","DOI":"10.1126\/sciadv.aat7715","type":"journal-article","created":{"date-parts":[[2018,11,16]],"date-time":"2018-11-16T14:16:52Z","timestamp":1542377812000},"source":"Crossref","is-referenced-by-count":187,"title":["Label-free imaging of amyloid plaques in Alzheimer\u2019s disease with stimulated Raman scattering microscopy"],"prefix":"10.1126","volume":"4","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9066-4008","authenticated-orcid":true,"given":"Minbiao","family":"Ji","sequence":"first","affiliation":[{"name":"State Key Laboratory of Surface Physics and Department of Physics, Multiscale Research Institute of Complex Systems, Human Phenome Institute, Key Laboratory of Micro and Nano Photonics Structures (Ministry of Education), Fudan University, Shanghai 200433, China."},{"name":"Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michal","family":"Arbel","sequence":"additional","affiliation":[{"name":"Alzheimer\u2019s Disease Research Laboratory, Department of Neurology, MassGeneral Institute for Neurodegenerative Disease, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lili","family":"Zhang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Surface Physics and Department of Physics, Multiscale Research Institute of Complex Systems, Human Phenome Institute, Key Laboratory of Micro and Nano Photonics Structures (Ministry of Education), Fudan University, Shanghai 200433, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian W.","family":"Freudiger","sequence":"additional","affiliation":[{"name":"Invenio Imaging Inc., Santa Clara, CA 95051, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven S.","family":"Hou","sequence":"additional","affiliation":[{"name":"Alzheimer\u2019s Disease Research Laboratory, Department of Neurology, MassGeneral Institute for Neurodegenerative Disease, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7228-5397","authenticated-orcid":true,"given":"Dongdong","family":"Lin","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Surface Physics and Department of Physics, Multiscale Research Institute of Complex Systems, Human Phenome Institute, Key Laboratory of Micro and Nano Photonics Structures (Ministry of Education), Fudan University, Shanghai 200433, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinju","family":"Yang","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Surface Physics and Department of Physics, Multiscale Research Institute of Complex Systems, Human Phenome Institute, Key Laboratory of Micro and Nano Photonics Structures (Ministry of Education), Fudan University, Shanghai 200433, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian J.","family":"Bacskai","sequence":"additional","affiliation":[{"name":"Alzheimer\u2019s Disease Research Laboratory, Department of Neurology, MassGeneral Institute for Neurodegenerative Disease, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"X. Sunney","family":"Xie","sequence":"additional","affiliation":[{"name":"Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_3_2_2_2","first-page":"3","article-title":"About a peculiar disease of the cerebral cortex. By Alois Alzheimer, 1907 (Translated by L. Jarvik and H. Greenson)","volume":"1","author":"Jarvik L.","year":"1987","unstructured":"L. Jarvik, H. Greenson, About a peculiar disease of the cerebral cortex. By Alois Alzheimer, 1907 (Translated by L. Jarvik and H. Greenson). Alzheimer Dis. Assoc. Disord. 1, 3\u20138 (1987).","journal-title":"Alzheimer Dis. Assoc. Disord."},{"key":"e_1_3_2_3_2","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/0092-8674(89)90093-7","article-title":"Amyloid \u03b2 protein precursor and the pathogenesis of Alzheimer\u2019s disease","volume":"58","author":"Selkoe D. J.","year":"1989","unstructured":"D. J. Selkoe, Amyloid \u03b2 protein precursor and the pathogenesis of Alzheimer\u2019s disease. Cell 58, 611\u2013612 (1989).","journal-title":"Cell"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.2001.81.2.741"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2012.02.022"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.75.101304.123901"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.6801762"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nm1066"},{"key":"e_1_3_2_9_2","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1146\/annurev.genom.7.080505.115737","article-title":"Protein misfolding and human disease","volume":"7","author":"Gregersen N.","year":"2006","unstructured":"N. Gregersen, P. Bross, S. Vang, J. H. Christensen, Protein misfolding and human disease. Annu. Rev. Genomics Hum. Genet. 7, 103\u2013124 (2006).","journal-title":"Annu. Rev. Genomics Hum. Genet."},{"key":"e_1_3_2_10_2","doi-asserted-by":"crossref","first-page":"151","DOI":"10.3233\/JAD-2006-9S317","article-title":"Alzheimer\u2019s disease: The amyloid cascade hypothesis: An update and reappraisal","volume":"9","author":"Hardy J.","year":"2006","unstructured":"J. Hardy, Alzheimer\u2019s disease: The amyloid cascade hypothesis: An update and reappraisal. J. Alzheimers Dis. 9, 151\u2013153 (2006).","journal-title":"J. Alzheimers Dis."},{"key":"e_1_3_2_11_2","first-page":"369808","article-title":"Alzheimer\u2019s disease and the amyloid cascade hypothesis: A critical review","volume":"2012","author":"Reitz C.","year":"2012","unstructured":"C. Reitz, Alzheimer\u2019s disease and the amyloid cascade hypothesis: A critical review. Int. J. Alzheimers Dis. 2012, 369808 (2012).","journal-title":"Int. J. Alzheimers Dis."},{"key":"e_1_3_2_12_2","doi-asserted-by":"crossref","first-page":"iii","DOI":"10.1111\/j.1471-4159.2011.07603.x","article-title":"Journal of Neurochemistry special issue on Alzheimer\u2019s disease: \u2019Amyloid cascade hypothesis\u201420 years on\u2019","volume":"120","author":"Checler F.","year":"2012","unstructured":"F. Checler, A. J. Turner, Journal of Neurochemistry special issue on Alzheimer\u2019s disease: \u2019Amyloid cascade hypothesis\u201420 years on\u2019. J. Neurochem. 120 Suppl 1, iii\u2013iv (2012).","journal-title":"J. Neurochem."},{"key":"e_1_3_2_13_2","doi-asserted-by":"crossref","first-page":"1075","DOI":"10.1517\/14712598.2013.789856","article-title":"Bapineuzumab and solanezumab for Alzheimer\u2019s disease: Is the \u2019amyloid cascade hypothesis\u2019 still alive?","volume":"13","author":"Tayeb H. O.","year":"2013","unstructured":"H. O. Tayeb, E. D. Murray, B. H. Price, F. I. Tarazi, Bapineuzumab and solanezumab for Alzheimer\u2019s disease: Is the \u2019amyloid cascade hypothesis\u2019 still alive? Expert. Opin. Biol. Ther. 13, 1075\u20131084 (2013).","journal-title":"Expert. Opin. Biol. Ther."},{"key":"e_1_3_2_14_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1072994"},{"key":"e_1_3_2_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrd3505"},{"key":"e_1_3_2_16_2","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/S1474-4422(11)70123-5","article-title":"Clinical amyloid imaging in Alzheimer\u2019s disease","volume":"10","author":"Herholz K.","year":"2011","unstructured":"K. Herholz, K. Ebmeier, Clinical amyloid imaging in Alzheimer\u2019s disease. Lancet Neurol. 10, 667\u2013670 (2011).","journal-title":"Lancet Neurol."},{"key":"e_1_3_2_17_2","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/s00259-011-2045-0","article-title":"A\u03b2 imaging: Feasible, pertinent, and vital to progress in Alzheimer\u2019s disease","volume":"39","author":"Villemagne V. L.","year":"2012","unstructured":"V. L. Villemagne, W. E. Klunk, C. A. Mathis, C. C. Rowe, D. J. Brooks, B. T. Hyman, M. D. Ikonomovic, K. Ishii, C. R. Jack, W. J. Jagust, K. A. Johnson, R. A. Koeppe, V. J. Lowe, C. L. Masters, T. J. Montine, J. C. Morris, A. Nordberg, R. C. Petersen, E. M. Reiman, D. J. Selkoe, R. A. Sperling, K. Van Laere, M. W. Weiner, A. Drzezga, A\u03b2 imaging: Feasible, pertinent, and vital to progress in Alzheimer\u2019s disease. Eur. J. Nucl. Med. Mol. Imaging 39, 209\u2013219 (2012).","journal-title":"Eur. J. Nucl. Med. Mol. Imaging"},{"key":"e_1_3_2_18_2","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.brainresrev.2006.08.001","article-title":"Congo red and protein aggregation in neurodegenerative diseases","volume":"53","author":"Frid P.","year":"2007","unstructured":"P. Frid, S. V. Anisimov, N. Popovic, Congo red and protein aggregation in neurodegenerative diseases. Brain Res. Rev. 53, 135\u2013160 (2007).","journal-title":"Brain Res. Rev."},{"key":"e_1_3_2_19_2","doi-asserted-by":"crossref","first-page":"15294","DOI":"10.1073\/pnas.2534647100","article-title":"Imaging linear birefringence and dichroism in cerebral amyloid pathologies","volume":"100","author":"Jin L.-W.","year":"2003","unstructured":"L.-W. Jin, K. A. Claborn, M. Kurimoto, M. A. Geday, I. Maezawa, F. Sohraby, M. Estrada, W. Kaminksy, B. Kahr, Imaging linear birefringence and dichroism in cerebral amyloid pathologies. Proc. Natl. Acad. Sci. U.S.A. 100, 15294\u201315298 (2003).","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"e_1_3_2_20_2","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1007\/BF03401708","article-title":"Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid \u03b2 peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer\u2019s disease and cerebral amyloid angiopathy cases","volume":"3","author":"Barelli H.","year":"1997","unstructured":"H. Barelli, A. Lebeau, J. Vizzavona, P. Delaere, N. Chevallier, C. Drouot, P. Marambaud, K. Ancolio, J. D. Buxbaum, O. Khorkova, J. Heroux, S. Sahasrabudhe, J. Martinez, J. M. Warter, M. Mohr, F. Checler, Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid \u03b2 peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer\u2019s disease and cerebral amyloid angiopathy cases. Mol. Med. 3, 695\u2013707 (1997).","journal-title":"Mol. Med."},{"key":"e_1_3_2_21_2","doi-asserted-by":"crossref","first-page":"26","DOI":"10.3389\/fpsyt.2012.00026","article-title":"A peephole into the brain: Neuropathological features of Alzheimer\u2019s disease revealed by in vivo two-photon imaging","volume":"3","author":"Liebscher S.","year":"2012","unstructured":"S. Liebscher, M. Meyer-Luehmann, A peephole into the brain: Neuropathological features of Alzheimer\u2019s disease revealed by in vivo two-photon imaging. Front. Psychiatry 3, 26 (2012).","journal-title":"Front. Psychiatry"},{"key":"e_1_3_2_22_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature06616"},{"key":"e_1_3_2_23_2","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.ymeth.2010.12.009","article-title":"Monitoring protein aggregation and toxicity in Alzheimer\u2019s disease mouse models using in vivo imaging","volume":"53","author":"Spires-Jones T. L.","year":"2011","unstructured":"T. L. Spires-Jones, A. de Calignon, M. Meyer-Luehmann, B. J. Bacskai, B. T. Hyman, Monitoring protein aggregation and toxicity in Alzheimer\u2019s disease mouse models using in vivo imaging. Methods 53, 201\u2013207 (2011).","journal-title":"Methods"},{"key":"e_1_3_2_24_2","doi-asserted-by":"publisher","DOI":"10.1017\/S0033583502003815"},{"key":"e_1_3_2_25_2","doi-asserted-by":"publisher","DOI":"10.1110\/ps.9.10.1960"},{"key":"e_1_3_2_26_2","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1016\/S0022-2836(83)80285-X","article-title":"Estimation of protein secondary structure from the laser Raman amide I spectrum","volume":"166","author":"Williams R. W.","year":"1983","unstructured":"R. W. Williams, Estimation of protein secondary structure from the laser Raman amide I spectrum. J. Mol. Biol. 166, 581\u2013603 (1983).","journal-title":"J. Mol. Biol."},{"key":"e_1_3_2_27_2","doi-asserted-by":"crossref","first-page":"137","DOI":"10.3389\/fnmol.2017.00137","article-title":"Structural changes of amyloid beta in hippocampus of rats exposed to ozone: A Raman spectroscopy study","volume":"10","author":"Rivas-Arancibia S.","year":"2017","unstructured":"S. Rivas-Arancibia, E. Rodr\u00edguez-Mart\u00ednez, I. Badillo-Ram\u00edrez, U. L\u00f3pez-Gonz\u00e1lez, J. M. Saniger, Structural changes of amyloid beta in hippocampus of rats exposed to ozone: A Raman spectroscopy study. Front. Mol. Neurosci. 10, 137 (2017).","journal-title":"Front. Mol. Neurosci."},{"key":"e_1_3_2_28_2","doi-asserted-by":"publisher","DOI":"10.1021\/bi0272151"},{"key":"e_1_3_2_29_2","doi-asserted-by":"crossref","first-page":"4743","DOI":"10.1364\/AO.48.004743","article-title":"Raman signature from brain hippocampus could aid Alzheimer\u2019s disease diagnosis","volume":"48","author":"Chen P.","year":"2009","unstructured":"P. Chen, A. Shen, W. Zhao, S.-J. Baek, H. Yuan, J. Hu, Raman signature from brain hippocampus could aid Alzheimer\u2019s disease diagnosis. Appl. Opt. 48, 4743\u20134748 (2009).","journal-title":"Appl. Opt."},{"key":"e_1_3_2_30_2","doi-asserted-by":"crossref","first-page":"150","DOI":"10.1016\/j.bpc.2007.03.012","article-title":"Analysis of insulin amyloid fibrils by Raman spectroscopy","volume":"128","author":"Ortiz C.","year":"2007","unstructured":"C. Ortiz, D. Zhang, A. E. Ribbe, Y. Xie, D. Ben-Amotz, Analysis of insulin amyloid fibrils by Raman spectroscopy. Biophys. Chem. 128, 150\u2013155 (2007).","journal-title":"Biophys. Chem."},{"key":"e_1_3_2_31_2","doi-asserted-by":"crossref","first-page":"2399","DOI":"10.1021\/ja0356176","article-title":"Raman spectroscopic characterization of secondary structure in natively unfolded proteins: \u03b1-Synuclein","volume":"126","author":"Maiti N. C.","year":"2004","unstructured":"N. C. Maiti, M. M. Apetri, M. G. Zagorski, P. R. Carey, V. E. Anderson, Raman spectroscopic characterization of secondary structure in natively unfolded proteins: \u03b1-Synuclein. J. Am. Chem. Soc. 126, 2399\u20132408 (2004).","journal-title":"J. Am. Chem. Soc."},{"key":"e_1_3_2_32_2","doi-asserted-by":"crossref","first-page":"15603","DOI":"10.1038\/s41598-017-16002-3","article-title":"Hyperspectral Raman imaging of neuritic plaques and neurofibrillary tangles in brain tissue from Alzheimer\u2019s disease patients","volume":"7","author":"Michael R.","year":"2017","unstructured":"R. Michael, A. Lenferink, G. F. J. M. Vrensen, E. Gelpi, R. I. Barraquer, C. Otto, Hyperspectral Raman imaging of neuritic plaques and neurofibrillary tangles in brain tissue from Alzheimer\u2019s disease patients. Sci. Rep. 7, 15603 (2017).","journal-title":"Sci. Rep."},{"key":"e_1_3_2_33_2","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s11060-014-1536-9","article-title":"Raman molecular imaging of brain frozen tissue sections","volume":"120","author":"Kast R. E.","year":"2014","unstructured":"R. E. Kast, G. W. Auner, M. L. Rosenblum, T. Mikkelsen, S. M. Yurgelevic, A. Raghunathan, L. M. Poisson, S. N. Kalkanis, Raman molecular imaging of brain frozen tissue sections. J. Neurooncol. 120, 55\u201362 (2014).","journal-title":"J. Neurooncol."},{"key":"e_1_3_2_34_2","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s11468-007-9027-x","article-title":"Application of surface-enhanced Raman spectroscopy for detection of beta amyloid using nanoshells","volume":"2","author":"Beier H. T.","year":"2007","unstructured":"H. T. Beier, C. B. Cowan, I.-H. Chou, J. Pallikal, J. E. Henry, M. E. Benford, J. B. Jackson, T. A. Good, G. L. Cot\u00e9, Application of surface-enhanced Raman spectroscopy for detection of beta amyloid using nanoshells. Plasmonics 2, 55\u201364 (2007).","journal-title":"Plasmonics"},{"key":"e_1_3_2_35_2","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1002\/jbio.201100142","article-title":"Tracking of nanoscale structural variations on a single amyloid fibril with tip-enhanced Raman scattering","volume":"5","author":"Deckert-Gaudig T.","year":"2012","unstructured":"T. Deckert-Gaudig, E. K\u00e4mmer, V. Deckert, Tracking of nanoscale structural variations on a single amyloid fibril with tip-enhanced Raman scattering. J. Biophotonics 5, 215\u2013219 (2012).","journal-title":"J. Biophotonics"},{"key":"e_1_3_2_36_2","doi-asserted-by":"crossref","first-page":"11002","DOI":"10.1021\/ja073798w","article-title":"Probing the cross-\u03b2 core structure of amyloid fibrils by hydrogen\u2013deuterium exchange deep ultraviolet resonance Raman spectroscopy","volume":"129","author":"Xu M.","year":"2007","unstructured":"M. Xu, V. Shashilov, I. K. Lednev, Probing the cross-\u03b2 core structure of amyloid fibrils by hydrogen\u2013deuterium exchange deep ultraviolet resonance Raman spectroscopy. J. Am. Chem. Soc. 129, 11002\u201311003 (2007).","journal-title":"J. Am. Chem. Soc."},{"key":"e_1_3_2_37_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1165758"},{"key":"e_1_3_2_38_2","doi-asserted-by":"crossref","first-page":"4142","DOI":"10.1103\/PhysRevLett.82.4142","article-title":"Three-dimensional vibrational imaging by coherent anti-Stokes Raman scattering","volume":"82","author":"Zumbusch A.","year":"1999","unstructured":"A. Zumbusch, G. R. Holtom, X. S. Xie, Three-dimensional vibrational imaging by coherent anti-Stokes Raman scattering. Phys. Rev. Lett. 82, 4142\u20134145 (1999).","journal-title":"Phys. Rev. Lett."},{"key":"e_1_3_2_39_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1197236"},{"key":"e_1_3_2_40_2","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.3005954"},{"key":"e_1_3_2_41_2","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1364\/OPTICA.4.000044","article-title":"Dual-phase stimulated Raman scattering microscopy for real-time two-color imaging","volume":"4","author":"He R.","year":"2017","unstructured":"R. He, Y. Xu, L. Zhang, S. Ma, X. Wang, D. Ye, M. Ji, Dual-phase stimulated Raman scattering microscopy for real-time two-color imaging. Optica 4, 44\u201347 (2017).","journal-title":"Optica"},{"key":"e_1_3_2_42_2","doi-asserted-by":"publisher","DOI":"10.1021\/ja210081h"},{"key":"e_1_3_2_43_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1515121112"},{"key":"e_1_3_2_44_2","doi-asserted-by":"publisher","DOI":"10.1126\/scitranslmed.aab0195"},{"key":"e_1_3_2_45_2","doi-asserted-by":"publisher","DOI":"10.1038\/nmeth.2878"},{"key":"e_1_3_2_46_2","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1002\/cphc.201100890","article-title":"Label-free live-cell imaging of nucleic acids using stimulated Raman scattering microscopy","volume":"13","author":"Zhang X.","year":"2012","unstructured":"X. Zhang, M. B. Roeffaers, S. Basu, J. R. Daniele, D. Fu, C. W. Freudiger, G. R. Holtom, X. S. Xie, Label-free live-cell imaging of nucleic acids using stimulated Raman scattering microscopy. ChemPhysChem 13, 1054\u20131059 (2012).","journal-title":"ChemPhysChem"},{"key":"e_1_3_2_47_2","doi-asserted-by":"crossref","first-page":"1927","DOI":"10.1080\/00268976.2012.695028","article-title":"Multicolor stimulated Raman scattering (SRS) microscopy","volume":"110","author":"Lu F.-K.","year":"2012","unstructured":"F.-K. Lu, M. Ji, D. Fu, X. Ni, C. W. Freudiger, G. Holtom, X. S. Xie, Multicolor stimulated Raman scattering (SRS) microscopy. Mol. Phys. 110, 1927\u20131932 (2012).","journal-title":"Mol. Phys."},{"key":"e_1_3_2_48_2","unstructured":"G. J. Siegel B. W. Agranoff R. W. Albers Basic Neurochemistry: Molecular Cellular and Medical Aspects (Lippincott-Raven 1999)."},{"key":"e_1_3_2_49_2","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1364\/OL.42.000659","article-title":"Stimulated Raman scattering microscopy and spectroscopy with a rapid scanning optical delay line","volume":"42","author":"He R.","year":"2017","unstructured":"R. He, Z. Liu, Y. Xu, W. Huang, H. Ma, M. Ji, Stimulated Raman scattering microscopy and spectroscopy with a rapid scanning optical delay line. Opt. Lett. 42, 659\u2013662 (2017).","journal-title":"Opt. Lett."},{"key":"e_1_3_2_50_2","doi-asserted-by":"publisher","DOI":"10.1038\/lsa.2015.38"},{"key":"e_1_3_2_51_2","doi-asserted-by":"publisher","DOI":"10.1038\/nphoton.2012.263"},{"key":"e_1_3_2_52_2","doi-asserted-by":"crossref","first-page":"6550","DOI":"10.1021\/bi500528x","article-title":"Resonance Raman spectroscopic measurements delineate the structural changes that occur during tau fibril formation","volume":"53","author":"Ramachandran G.","year":"2014","unstructured":"G. Ramachandran, E. A. Mil\u00e1n-Garc\u00e9s, J. B. Udgaonkar, M. Puranik, Resonance Raman spectroscopic measurements delineate the structural changes that occur during tau fibril formation. Biochemistry 53, 6550\u20136565 (2014).","journal-title":"Biochemistry"},{"key":"e_1_3_2_53_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.nbd.2006.08.017"},{"key":"e_1_3_2_54_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1389-0344(01)00067-3"}],"container-title":["Science Advances"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.science.org\/doi\/pdf\/10.1126\/sciadv.aat7715","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,1,9]],"date-time":"2024-01-09T14:04:56Z","timestamp":1704809096000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.science.org\/doi\/10.1126\/sciadv.aat7715"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,11,2]]},"references-count":53,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2018,11,2]]}},"alternative-id":["10.1126\/sciadv.aat7715"],"URL":"https:\/\/doi.org\/10.1126\/sciadv.aat7715","relation":{},"ISSN":["2375-2548"],"issn-type":[{"value":"2375-2548","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,11,2]]},"article-number":"eaat7715"}}