{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T01:47:54Z","timestamp":1789177674149,"version":"build-2803163510"},"reference-count":56,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2007,11,1]],"date-time":"2007-11-01T00:00:00Z","timestamp":1193875200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"published-print":{"date-parts":[[2007,11]]},"DOI":"10.1016\/j.bbapap.2007.08.014","type":"journal-article","created":{"date-parts":[[2007,8,27]],"date-time":"2007-08-27T10:57:19Z","timestamp":1188212239000},"page":"1414-1421","source":"Crossref","is-referenced-by-count":102,"title":["Impacts of Cd(II) on the conformation and self-aggregation of Alzheimer's tau fragment corresponding to the third repeat of microtubule-binding domain"],"prefix":"10.1016","volume":"1774","author":[{"given":"Ling-Feng","family":"Jiang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tian-Ming","family":"Yao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zhi-Liang","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chong","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liang-Nian","family":"Ji","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbapap.2007.08.014_bib1","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1111\/j.1532-5415.1990.tb01421.x","article-title":"Metals and the liver in Alzheimer's disease. An investigation of hepatic zinc, copper, cadmium, and metallothionein","volume":"38","author":"Lui","year":"1990","journal-title":"J. Am. Geriatr. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib2","first-page":"231","article-title":"Metals and trace elements in plasma and cerebrospinal fluid in normal aging and Alzheimer's disease","volume":"3","author":"Basun","year":"1991","journal-title":"J. Neural Transm., Parkinson's Dis. Dement. Sect."},{"key":"10.1016\/j.bbapap.2007.08.014_bib3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0022-510X(01)00672-4","article-title":"Determination of cadmium and zinc in Alzheimer's brain tissue using inductively coupled plasma mass spectrometry","volume":"195","author":"Panayi","year":"2002","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.bbapap.2007.08.014_bib4","doi-asserted-by":"crossref","first-page":"145","DOI":"10.3233\/JAD-2006-102-303","article-title":"Metals and Alzheimer's disease","volume":"10","author":"Adlard","year":"2006","journal-title":"J. Alzheimer's Dis."},{"key":"10.1016\/j.bbapap.2007.08.014_bib5","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1196\/annals.1379.023","article-title":"Fibrillar and oligomeric beta-amyloid as distinct local biomarkers for Alzheimer's disease","volume":"1097","author":"Montalto","year":"2007","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.bbapap.2007.08.014_bib6","doi-asserted-by":"crossref","first-page":"10223","DOI":"10.1021\/bi980537d","article-title":"Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by fluorescence in solution","volume":"37","author":"Friedhoff","year":"1998","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib7","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/308734a0","article-title":"Release of endogenous Zn2+ from brain tissue during activity","volume":"308","author":"Assaf","year":"1984","journal-title":"Nature"},{"key":"10.1016\/j.bbapap.2007.08.014_bib8","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.ab.2005.08.024","article-title":"Imaging and spatial distribution of beta-amyloid peptide and metal ions in Alzheimer's plaques by laser ablation-inductively coupled plasma-mass spectrometry","volume":"346","author":"Hutchinson","year":"2005","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib9","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1126\/science.8073293","article-title":"Rapid induction of Alzheimer A beta amyloid formation by zinc","volume":"265","author":"Bush","year":"1994","journal-title":"Science"},{"key":"10.1016\/j.bbapap.2007.08.014_bib10","doi-asserted-by":"crossref","first-page":"11193","DOI":"10.1073\/pnas.2135061100","article-title":"Copper, beta-amyloid, and Alzheimer's disease: tapping a sensitive connection","volume":"100","author":"Bush","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.08.014_bib11","doi-asserted-by":"crossref","first-page":"13534","DOI":"10.1021\/ja0488028","article-title":"Amyloid-\u03b2 binds Cu2+ in a mononuclear metal ion binding site","volume":"126","author":"Karr","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib12","doi-asserted-by":"crossref","first-page":"7024","DOI":"10.1021\/bi0002479","article-title":"Metal binding modes of Alzheimer's amyloid \u03b2-peptide in insoluble aggregates and soluble complexes","volume":"39","author":"Miura","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib13","doi-asserted-by":"crossref","first-page":"2768","DOI":"10.1021\/bi0272151","article-title":"Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence","volume":"42","author":"Dong","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib14","doi-asserted-by":"crossref","first-page":"173","DOI":"10.3233\/JAD-2006-102-305","article-title":"Aluminium and iron, but neither copper nor zinc, are key to the precipitation of beta-sheets of Abeta-42 in senile plaque cores in Alzheimer's disease","volume":"10","author":"Exley","year":"2006","journal-title":"J. Alzheimer's Dis."},{"key":"10.1016\/j.bbapap.2007.08.014_bib15","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/j.peptides.2005.09.002","article-title":"Copper binding properties of a tau peptide associated with Alzheimer's disease studied by CD, NMR, and MALDI-TOF MS","volume":"27","author":"Ma","year":"2006","journal-title":"Peptides"},{"key":"10.1016\/j.bbapap.2007.08.014_bib16","doi-asserted-by":"crossref","first-page":"11976","DOI":"10.1016\/S0021-9258(19)50296-4","article-title":"Aluminum-induced nonenzymatic phospho-incorporation into human tau and other proteins","volume":"268","author":"Abdel-Ghany","year":"1993","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib17","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1046\/j.1471-4159.2002.t01-1-01061.x","article-title":"Iron (III) induces aggregation of hyperphosphorylated tau and its reduction to iron (II) reverses the aggregation: implications in the formation of neurofibrillary tangles of Alzheimer's disease","volume":"82","author":"Yamamoto","year":"2002","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib18","doi-asserted-by":"crossref","first-page":"1694","DOI":"10.1021\/bi0357006","article-title":"Tau paired helical filaments from Alzheimer's disease brain and assembled in vitro are based on \u03b2-structure in the core domain","volume":"43","author":"Barghorn","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib19","doi-asserted-by":"crossref","first-page":"9034","DOI":"10.1073\/pnas.1530287100","article-title":"Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-\u03b2 structure","volume":"100","author":"Berriman","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.08.014_bib20","doi-asserted-by":"crossref","first-page":"48165","DOI":"10.1074\/jbc.M105196200","article-title":"Mutations of tau protein in frontotemporal dementia promote aggregation of paired helical filaments by enhancing local beta-structure","volume":"276","author":"von Bergen","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib21","doi-asserted-by":"crossref","first-page":"5129","DOI":"10.1073\/pnas.97.10.5129","article-title":"Assembly of \u03c4 protein into Alzheimer paired helical filaments depends on a local sequence motif (306VQIVYK311) forming \u03b2 structure","volume":"97","author":"Von Bergen","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.08.014_bib22","doi-asserted-by":"crossref","first-page":"14885","DOI":"10.1021\/bi026469j","article-title":"Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments","volume":"41","author":"Barghorn","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib23","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.bbadis.2004.09.010","article-title":"Tau aggregation is driven by a transition from random coil to beta sheet structure","volume":"1739","author":"von Bergen","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2007.08.014_bib24","doi-asserted-by":"crossref","first-page":"24978","DOI":"10.1074\/jbc.M501565200","article-title":"Sites of tau important for aggregation populate {beta}-structure and bind to microtubules and polyanions","volume":"280","author":"Mukrasch","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib25","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1021\/bi048564t","article-title":"Role for the \u03b1-helix in aberrant protein aggregation","volume":"44","author":"Kunjithapatham","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib26","doi-asserted-by":"crossref","first-page":"7150","DOI":"10.1021\/bi025777e","article-title":"\u03b1-Helix structure in Alzheimer's disease aggregates of tau-protein","volume":"41","author":"Sadqi","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib27","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.bbagen.2004.09.009","article-title":"Phosphorylation modulates the alpha-helical structure and polymerization of a peptide from the third tau microtubule-binding repeat","volume":"1721","author":"Mendieta","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2007.08.014_bib28","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1046\/j.1432-1033.2003.03956.x","article-title":"Different associational and conformational behaviors between the second and third repeat fragments in the tau microtubule-binding domain","volume":"271","author":"Minoura","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib29","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1093\/jb\/mvi142","article-title":"Possible role of each repeat structure of the microtubule-binding domain of the tau protein in in vitro aggregation","volume":"138","author":"Tomoo","year":"2005","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib30","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1016\/j.bbrc.2004.01.107","article-title":"Conformational transition state is responsible for assembly of microtubule-binding domain of tau protein","volume":"315","author":"Hiraoka","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2007.08.014_bib31","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1093\/jb\/mvg116","article-title":"Aggregation analysis of the microtubule binding domain in tau protein by spectroscopic methods","volume":"134","author":"Yao","year":"2003","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib32","doi-asserted-by":"crossref","first-page":"9403","DOI":"10.1021\/ja00181a058","article-title":"Metal ion enhanced helicity in synthetic peptides containing unnatural, metal-ligating residues","volume":"112","author":"Ruan","year":"1990","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib33","doi-asserted-by":"crossref","first-page":"1630","DOI":"10.1021\/ja00160a054","article-title":"Secondary structure nucleation in peptides. Transition metal ion stabilized \u03b1-helix","volume":"112","author":"Ghadiril","year":"1990","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib34","doi-asserted-by":"crossref","first-page":"9633","DOI":"10.1021\/ja00182a030","article-title":"Peptide architecture. Design of stable a-helical metallopeptides via a novel exchange-inert RuIII complex","volume":"112","author":"Ghadiri","year":"1990","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib35","doi-asserted-by":"crossref","first-page":"5437","DOI":"10.1021\/bi0358418","article-title":"Metal ion affinities of the zinc finger domains of the metal responsive element-binding transcription factor-1 (MTF1)","volume":"43","author":"Guerrerio","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib36","doi-asserted-by":"crossref","first-page":"44284","DOI":"10.1074\/jbc.M105343200","article-title":"Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular link between Parkinson's disease and heavy metal exposure","volume":"276","author":"Uversky","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib37","doi-asserted-by":"crossref","first-page":"9893","DOI":"10.1021\/ja0618649","article-title":"Interaction of alpha-synuclein with divalent metal ions reveals key differences: a link between structure, binding specificity and fibrillation enhancement","volume":"128","author":"Binolfi","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib38","doi-asserted-by":"crossref","first-page":"9662","DOI":"10.1021\/ja043247v","article-title":"Phosphorylation of an alpha-synuclein peptide fragment enhances metal binding","volume":"127","author":"Liu","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib39","doi-asserted-by":"crossref","first-page":"15712","DOI":"10.1073\/pnas.95.26.15712","article-title":"A nucleated assembly mechanism of Alzheimer paired helical filaments","volume":"95","author":"Friedhoff","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.08.014_bib40","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/S0006-291X(02)00457-6","article-title":"Amphipathic helical behavior of the third repeat fragment in the tau microtubule-binding domain, studied by 1H NMR spectroscopy","volume":"294","author":"Minoura","year":"2002","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbapap.2007.08.014_bib41","doi-asserted-by":"crossref","first-page":"3055","DOI":"10.1021\/bi061920i","article-title":"NMR investigation of the interaction between the neuronal protein tau and the microtubules","volume":"46","author":"Sillen","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib42","doi-asserted-by":"crossref","first-page":"3575","DOI":"10.1021\/ja054656+","article-title":"NMR analysis of a tau phosphorylation pattern","volume":"128","author":"Landrieu","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib43","doi-asserted-by":"crossref","first-page":"5527","DOI":"10.1021\/bi052662c","article-title":"Hyperphosphorylation of tau induces local polyproline II helix","volume":"45","author":"Bielska","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib44","doi-asserted-by":"crossref","first-page":"12560","DOI":"10.1021\/bi060964o","article-title":"Structural impact of heparin binding to full-length tau as studied by NMR spectroscopy","volume":"45","author":"Sibille","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbapap.2007.08.014_bib45","series-title":"Biochemical Applications of Raman and Resonance Raman Spectroscopies, A Subsidiary of Harcourt Brace Jovanovich","first-page":"71","author":"Carey","year":"1982"},{"key":"10.1016\/j.bbapap.2007.08.014_bib46","series-title":"Raman Spectroscopy in Biology: Principles and Applications","first-page":"65","author":"Tu","year":"1982"},{"key":"10.1016\/j.bbapap.2007.08.014_bib47","series-title":"Biological Science in infrared and Raman Spectroscopy (Part C)","first-page":"717","author":"Thomas","year":"1977"},{"key":"10.1016\/j.bbapap.2007.08.014_bib48","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/0022-2836(70)90208-1","article-title":"Laser-excited Raman spectroscopy of biomolecules I, native lysozyme and constituent amine acides","volume":"50","author":"Lord","year":"1970","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbapap.2007.08.014_bib49","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1016\/j.bbadis.2004.08.013","article-title":"Potential structure\/function relationships of predicted secondary structural elements of tau","volume":"1739","author":"Gamblin","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2007.08.014_bib50","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S0167-4838(98)00015-6","article-title":"Role of metal\u2013ligand coordination in the folding pathway of zinc finger peptides","volume":"1384","author":"Miura","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbapap.2007.08.014_bib51","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1002\/(SICI)1097-4555(199801)29:1<41::AID-JRS212>3.0.CO;2-R","article-title":"Raman marker bands of metal coordination sites of histidine side chains in peptides and proteins","volume":"29","author":"Miura","year":"1998","journal-title":"J. Raman Spectrosc."},{"key":"10.1016\/j.bbapap.2007.08.014_bib52","first-page":"1","article-title":"Raman and resonance Raman studies of biological systems","volume":"vol. 7","author":"Carey","year":"1980"},{"key":"10.1016\/j.bbapap.2007.08.014_bib53","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/BF02050527","article-title":"Neutron activation analysis techniques for identifying elemental status in Alzheimer's disease","volume":"113","author":"Ward","year":"1987","journal-title":"J. Radioanal. Nucl. Chem."},{"key":"10.1016\/j.bbapap.2007.08.014_bib54","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/0896-6273(91)90272-2","article-title":"The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein","volume":"7","author":"Uchida","year":"1991","journal-title":"Neuron"},{"key":"10.1016\/j.bbapap.2007.08.014_bib55","doi-asserted-by":"crossref","first-page":"6333","DOI":"10.1073\/pnas.89.14.6333","article-title":"MT-III, a brain-specific member of the metallothionein gene family","volume":"89","author":"Palmiter","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbapap.2007.08.014_bib56","doi-asserted-by":"crossref","first-page":"10540","DOI":"10.1073\/pnas.88.23.10540","article-title":"Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease","volume":"88","author":"Smith","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963907002026?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1570963907002026?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,8,22]],"date-time":"2021-08-22T07:32:12Z","timestamp":1629617532000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1570963907002026"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2007,11]]},"references-count":56,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2007,11]]}},"alternative-id":["S1570963907002026"],"URL":"https:\/\/doi.org\/10.1016\/j.bbapap.2007.08.014","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.719611760.793515201","asserted-by":"object"}]},"ISSN":["1570-9639"],"issn-type":[{"value":"1570-9639","type":"print"}],"subject":[],"published":{"date-parts":[[2007,11]]}}}