{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T19:24:29Z","timestamp":1761765869393,"version":"3.44.0"},"reference-count":41,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,11,1]],"date-time":"2014-11-01T00:00:00Z","timestamp":1414800000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100000923","name":"Australian Research Council","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000923","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochemical and Biophysical Research Communications"],"published-print":{"date-parts":[[2014,11]]},"DOI":"10.1016\/j.bbrc.2014.10.062","type":"journal-article","created":{"date-parts":[[2014,10,18]],"date-time":"2014-10-18T05:51:39Z","timestamp":1413611499000},"page":"295-300","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"title":["Hemin as a generic and potent protein misfolding inhibitor"],"prefix":"10.1016","volume":"454","author":[{"given":"Yanqin","family":"Liu","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"John A.","family":"Carver","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lam H.","family":"Ho","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Abigail K.","family":"Elias","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ian F.","family":"Musgrave","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tara L.","family":"Pukala","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbrc.2014.10.062_b0005","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1098\/rstb.2000.0758","article-title":"The structural basis of protein folding and its links with human disease","volume":"356","author":"Dobson","year":"2001","journal-title":"Philos. Trans. R. Soc. Lond. B"},{"key":"10.1016\/j.bbrc.2014.10.062_b0010","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1126\/science.181.4096.223","article-title":"Principles that govern the folding of protein chains","volume":"181","author":"Anfinsen","year":"1973","journal-title":"Science"},{"issue":"12","key":"10.1016\/j.bbrc.2014.10.062_b0015","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1080\/15216540310001640498","article-title":"Small heat-shock proteins and clusterin: intra- and extracellular molecular chaperones with a common mechanism of action and function?","volume":"55","author":"Carver","year":"2003","journal-title":"IUBMB Life"},{"issue":"12","key":"10.1016\/j.bbrc.2014.10.062_b0020","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1038\/sj.embor.7400586","article-title":"Quality control of protein folding in extracellular space","volume":"6","author":"Yerbury","year":"2005","journal-title":"EMBO Rep."},{"key":"10.1016\/j.bbrc.2014.10.062_b0025","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1126\/science.1068408","article-title":"Molecular chaperones in the cytosol: from nascent chain to folded protein","volume":"295","author":"Hartl","year":"2002","journal-title":"Science"},{"issue":"051907","key":"10.1016\/j.bbrc.2014.10.062_b0030","first-page":"1","article-title":"Model for amorphous aggregation process","volume":"80","author":"Stranks","year":"2009","journal-title":"Phys. Rev. E"},{"issue":"12","key":"10.1016\/j.bbrc.2014.10.062_b0035","doi-asserted-by":"crossref","first-page":"769","DOI":"10.1002\/iub.117","article-title":"Unraveling the mysteries of protein folding and misfolding","volume":"60","author":"Ecroyd","year":"2008","journal-title":"IUBMB Life"},{"issue":"10","key":"10.1016\/j.bbrc.2014.10.062_b0040","doi-asserted-by":"crossref","first-page":"3935","DOI":"10.1021\/pr070138h","article-title":"Post-translational modifications in the nuclear region of young, aged, and cataract human lenses","volume":"6","author":"Hains","year":"2007","journal-title":"J. Proteome Res."},{"issue":"12","key":"10.1016\/j.bbrc.2014.10.062_b0045","doi-asserted-by":"crossref","first-page":"1959","DOI":"10.1016\/j.bbapap.2008.07.016","article-title":"Proteomic analysis of the oxidation of cysteine residues in human age-related nuclear cataract lenses","volume":"1784","author":"Hains","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.bbrc.2014.10.062_b0050","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1006\/exer.1998.0481","article-title":"Age-related changes in human lens crystallins identified by two-dimensional electrophoresis and mass spectrometry","volume":"67","author":"Lampi","year":"1998","journal-title":"Exp. Eye Res."},{"issue":"3","key":"10.1016\/j.bbrc.2014.10.062_b0055","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1016\/S0014-4835(03)00159-3","article-title":"Human beta-crystallins modified by backbone cleavage, deamidation and oxidation are prone to associate","volume":"77","author":"Zhang","year":"2003","journal-title":"Exp. Eye Res."},{"issue":"10","key":"10.1016\/j.bbrc.2014.10.062_b0060","first-page":"1911","article-title":"Cataract as a protein condensation disease \u2013 the proctor lecture","volume":"38","author":"Benedek","year":"1997","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.bbrc.2014.10.062_b0065","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/B978-0-12-385883-2.00012-6","article-title":"Alzheimer\u2019s disease and the amyloid beta-protein","volume":"107","author":"Walsh","year":"2012","journal-title":"Prog. Mol. Biol Transl. Sci."},{"issue":"6968","key":"10.1016\/j.bbrc.2014.10.062_b0070","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1038\/nature02264","article-title":"Folding proteins in fatal ways","volume":"426","author":"Selkoe","year":"2003","journal-title":"Nature"},{"issue":"17","key":"10.1016\/j.bbrc.2014.10.062_b0075","doi-asserted-by":"crossref","first-page":"9831","DOI":"10.1073\/pnas.1734009100","article-title":"Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities","volume":"100","author":"Foguel","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"4\u20135","key":"10.1016\/j.bbrc.2014.10.062_b0080","first-page":"373","article-title":"Protein conformation and disease","volume":"27","author":"Nandi","year":"1996","journal-title":"Vet. Res."},{"issue":"25","key":"10.1016\/j.bbrc.2014.10.062_b0085","doi-asserted-by":"crossref","first-page":"12243","DOI":"10.1073\/pnas.91.25.12243","article-title":"Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red","volume":"91","author":"Lorenzo","year":"1994","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"issue":"4","key":"10.1016\/j.bbrc.2014.10.062_b0090","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1016\/S1474-4422(13)70044-9","article-title":"Amyloid beta deposition, neurodegeneration, and cognitive decline in sporadic Alzheimer\u2019s disease: a prospective cohort study","volume":"12","author":"Villemagne","year":"2013","journal-title":"Lancet Neurol."},{"issue":"5","key":"10.1016\/j.bbrc.2014.10.062_b0095","doi-asserted-by":"crossref","first-page":"375","DOI":"10.3233\/JAD-2002-4505","article-title":"Tau, where are we now?","volume":"4","author":"Johnson","year":"2002","journal-title":"J. Alzheimer\u2019s Dis."},{"key":"10.1016\/j.bbrc.2014.10.062_b0100","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1146\/annurev.biochem.74.082803.133400","article-title":"The biochemistry of Parkinson\u2019s disease","volume":"74","author":"Cookson","year":"2005","journal-title":"Annu. Rev. Biochem."},{"issue":"3","key":"10.1016\/j.bbrc.2014.10.062_b0105","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1097\/00005072-196507000-00003","article-title":"Phase and electron microscopic observations of Lewy bodies and melanin granules in the substantia nigra and locus coeruleus in Parkinson\u2019s disease","volume":"24","author":"Duffy","year":"1965","journal-title":"J. Neuropathol. Exp. Neurol."},{"issue":"6645","key":"10.1016\/j.bbrc.2014.10.062_b0110","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1038\/42166","article-title":"Alpha-synuclein in Lewy bodies","volume":"388","author":"Spillantini","year":"1997","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.bbrc.2014.10.062_b0115","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1038\/nsmb1182","article-title":"Heme is involved in microRNA processing","volume":"14","author":"Faller","year":"2007","journal-title":"Nat. Struct. Mol. Biol."},{"issue":"12","key":"10.1016\/j.bbrc.2014.10.062_b0120","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1021\/ar040020w","article-title":"Reversible binding of heme to proteins in cellular signal transduction","volume":"39","author":"Hou","year":"2006","journal-title":"Acc. Chem. Res."},{"issue":"2","key":"10.1016\/j.bbrc.2014.10.062_b0125","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/S0014-5793(97)01290-8","article-title":"Hemin and related porphyrins inhibit beta-amyloid aggregation","volume":"417","author":"Howlett","year":"1997","journal-title":"FEBS Lett."},{"issue":"3","key":"10.1016\/j.bbrc.2014.10.062_b0130","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1023\/A:1025020503769","article-title":"Environmental influences on bovine kappa-casein: reduction and conversion to fibrillar (amyloid) structures","volume":"22","author":"Farrell","year":"2003","journal-title":"J. Protein Chem."},{"issue":"18","key":"10.1016\/j.bbrc.2014.10.062_b0135","doi-asserted-by":"crossref","first-page":"3407","DOI":"10.1021\/bi00742a007","article-title":"Selective reduction of cystine 1\u20138 in alpha-lactalbumin","volume":"12","author":"Schechter","year":"1973","journal-title":"Biochemistry"},{"issue":"5","key":"10.1016\/j.bbrc.2014.10.062_b0140","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.1016\/j.jmb.2006.12.044","article-title":"Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity","volume":"366","author":"Volles","year":"2007","journal-title":"J. Mol. Biol."},{"issue":"6","key":"10.1016\/j.bbrc.2014.10.062_b0145","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1007\/s12192-010-0212-z","article-title":"Alpha B-crystallin inhibits the cell toxicity associated with amyloid fibril formation by kappa-casein and the amyloid-beta peptide","volume":"15","author":"Dehle","year":"2010","journal-title":"Cell Stress Chaperones"},{"issue":"1","key":"10.1016\/j.bbrc.2014.10.062_b0150","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1016\/j.bmc.2009.10.063","article-title":"Carboxymethylated-kappa-casein: a convenient tool for the identification of polyphenolic inhibitors of amyloid fibril formation","volume":"18","author":"Carver","year":"2010","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/j.bbrc.2014.10.062_b0155","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/j.jsb.2005.06.006","article-title":"Mechanism of thioflavin T binding to amyloid fibrils","volume":"151","author":"Khurana","year":"2005","journal-title":"J. Struct. Biol."},{"issue":"7","key":"10.1016\/j.bbrc.2014.10.062_b0160","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/j.bbapap.2010.04.001","article-title":"Molecular mechanism of thioflavin-T binding to amyloid fibrils","volume":"1804","author":"Biancalana","year":"2010","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbrc.2014.10.062_b0165","first-page":"1","article-title":"Amyloid peptides and proteins in review","volume":"159","author":"Harrison","year":"2007","journal-title":"Rev. Physiol. Biochem. Pharmacol."},{"key":"10.1016\/j.bbrc.2014.10.062_b0170","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1006\/jmbi.1997.1348","article-title":"Common core structure of amyloid fibrils by synchrotron X-ray diffraction","volume":"273","author":"Sunde","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbrc.2014.10.062_b0175","doi-asserted-by":"crossref","first-page":"185","DOI":"10.2174\/1874196700902010185","article-title":"Insights into the structure of amyloid fibrils","volume":"2","author":"Marshall","year":"2009","journal-title":"Open Biol. J."},{"issue":"9","key":"10.1016\/j.bbrc.2014.10.062_b0180","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1016\/j.bbapap.2014.04.013","article-title":"Gallic acid interacts with alpha-synuclein to prevent the structural collapse necessary for its aggregation","volume":"1844","author":"Liu","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"issue":"4","key":"10.1016\/j.bbrc.2014.10.062_b0185","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.3233\/JAD-2010-091363","article-title":"An in vitro model for neuroscience. differentiation of SH-SY5Y cells into cells with morphological and biochemical characteristics of mature neurons","volume":"20","author":"Agholme","year":"2010","journal-title":"J. Alzheimer\u2019s Dis."},{"issue":"7\u20138","key":"10.1016\/j.bbrc.2014.10.062_b0190","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1080\/1029842021000045624","article-title":"Hemin-induced apoptosis in PC12 and neuroblastoma cells: implications for local neuronal death associated with intracerebral hemorrhage","volume":"4","author":"Levy","year":"2002","journal-title":"Neurotox. Res."},{"issue":"2\u20133","key":"10.1016\/j.bbrc.2014.10.062_b0195","doi-asserted-by":"crossref","first-page":"291","DOI":"10.3233\/JAD-2006-102-313","article-title":"The nucleation growth and reversibility of amyloid-beta deposition in vivo","volume":"10","author":"Dolev","year":"2006","journal-title":"J. Alzheimer\u2019s Dis."},{"issue":"24","key":"10.1016\/j.bbrc.2014.10.062_b0200","doi-asserted-by":"crossref","first-page":"16884","DOI":"10.1074\/jbc.M114.548354","article-title":"Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: relevance to its storage and secretion","volume":"289","author":"Anoop","year":"2014","journal-title":"J. Biol. Chem."},{"issue":"9","key":"10.1016\/j.bbrc.2014.10.062_b0205","first-page":"1609","article-title":"Aggregation in aqueous solutions of bovine lens gamma-crystallins: special role of gamma(s)","volume":"39","author":"Liu","year":"1998","journal-title":"Invest. Ophthalmol. Vis. Sci."}],"container-title":["Biochemical and Biophysical Research Communications"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X14018610?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006291X14018610?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,13]],"date-time":"2025-09-13T11:10:31Z","timestamp":1757761831000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006291X14018610"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,11]]},"references-count":41,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2014,11]]}},"alternative-id":["S0006291X14018610"],"URL":"https:\/\/doi.org\/10.1016\/j.bbrc.2014.10.062","relation":{},"ISSN":["0006-291X"],"issn-type":[{"type":"print","value":"0006-291X"}],"subject":[],"published":{"date-parts":[[2014,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Hemin as a generic and potent protein misfolding inhibitor","name":"articletitle","label":"Article Title"},{"value":"Biochemical and Biophysical Research Communications","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bbrc.2014.10.062","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}