{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T12:45:23Z","timestamp":1790685923227,"version":"4.1.0"},"reference-count":45,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2015,1,1]],"date-time":"2015-01-01T00:00:00Z","timestamp":1420070400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,12,16]],"date-time":"2014-12-16T00:00:00Z","timestamp":1418688000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100001659","name":"Deutsche Forschungsgemeinschaft","doi-asserted-by":"publisher","award":["SFB 604"],"award-info":[{"award-number":["SFB 604"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Fritz Lipmann Institute"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2015,1]]},"DOI":"10.1016\/j.jmb.2014.12.005","type":"journal-article","created":{"date-parts":[[2014,12,19]],"date-time":"2014-12-19T12:53:10Z","timestamp":1418993590000},"page":"433-442","source":"Crossref","is-referenced-by-count":28,"title":["The Amyloid Precursor Protein Shows a pH-Dependent Conformational Switch in Its E1 Domain"],"prefix":"10.1016","volume":"427","author":[{"given":"Sandra","family":"Hoefgen","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sven O.","family":"Dahms","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kathrin","family":"Oertwig","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manuel E.","family":"Than","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2014.12.005_bb0005","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0140-6736(06)69113-7","article-title":"Alzheimer's disease","volume":"368","author":"Blennow","year":"2006","journal-title":"Lancet"},{"key":"10.1016\/j.jmb.2014.12.005_bb0010","doi-asserted-by":"crossref","first-page":"29615","DOI":"10.1074\/jbc.R800019200","article-title":"Amyloid precursor protein trafficking, processing, and function","volume":"283","author":"Thinakaran","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0015","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1111\/j.1471-4159.2011.07248.x","article-title":"Regulated intramembrane proteolysis\u2014lessons from amyloid precursor protein processing","volume":"117","author":"Lichtenthaler","year":"2011","journal-title":"J Neurochem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0020","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/0896-6273(92)90228-6","article-title":"The amyloid protein precursor of Alzheimer's disease is a mediator of the effects of nerve growth factor on neurite outgrowth","volume":"9","author":"Milward","year":"1992","journal-title":"Neuron"},{"key":"10.1016\/j.jmb.2014.12.005_bb0025","doi-asserted-by":"crossref","first-page":"5193","DOI":"10.1021\/cr300009x","article-title":"Bioinorganic chemistry of Alzheimer's disease","volume":"112","author":"Kepp","year":"2012","journal-title":"Chem Rev"},{"key":"10.1016\/j.jmb.2014.12.005_bb0030","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1016\/j.jmb.2011.12.057","article-title":"Metal binding dictates conformation and function of the amyloid precursor protein (APP) E2 domain","volume":"416","author":"Dahms","year":"2012","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2014.12.005_bb0035","doi-asserted-by":"crossref","first-page":"4435","DOI":"10.1242\/jcs.01323","article-title":"The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor","volume":"117","author":"von Rotz","year":"2004","journal-title":"J Cell Sci"},{"key":"10.1016\/j.jmb.2014.12.005_bb0040","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1091\/mbc.E06-04-0283","article-title":"Modulation of gene expression and cytoskeletal dynamics by the amyloid precursor protein intracellular domain (AICD)","volume":"18","author":"M\u00fcller","year":"2007","journal-title":"Mol Biol Cell"},{"key":"10.1016\/j.jmb.2014.12.005_bb0045","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1002\/jnr.490280109","article-title":"Beta amyloid precursor protein mediates neuronal cell-cell and cell-surface adhesion","volume":"28","author":"Breen","year":"1991","journal-title":"J Neurosci Res"},{"key":"10.1016\/j.jmb.2014.12.005_bb0050","doi-asserted-by":"crossref","first-page":"3624","DOI":"10.1038\/sj.emboj.7600824","article-title":"Homo- and heterodimerization of APP family members promotes intercellular adhesion","volume":"24","author":"Soba","year":"2005","journal-title":"EMBO J"},{"key":"10.1016\/j.jmb.2014.12.005_bb0055","doi-asserted-by":"crossref","first-page":"2548","DOI":"10.1073\/pnas.0308655100","article-title":"Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage","volume":"101","author":"Ho","year":"2004","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.jmb.2014.12.005_bb0060","doi-asserted-by":"crossref","first-page":"a006270","DOI":"10.1101\/cshperspect.a006270","article-title":"Trafficking and proteolytic processing of APP","volume":"2","author":"Haass","year":"2012","journal-title":"Cold Spring Harbor Perspect Med"},{"key":"10.1016\/j.jmb.2014.12.005_bb0065","first-page":"1","article-title":"pH homeostasis of cellular organelles","volume":"17","author":"Demaurex","year":"2002","journal-title":"News Physiol Sci"},{"key":"10.1016\/j.jmb.2014.12.005_bb0070","doi-asserted-by":"crossref","first-page":"16736","DOI":"10.3390\/s131216736","article-title":"Illumination of the spatial order of intracellular pH by genetically encoded pH-sensitive sensors","volume":"13","author":"Bencina","year":"2013","journal-title":"Sensors"},{"key":"10.1016\/j.jmb.2014.12.005_bb0075","doi-asserted-by":"crossref","first-page":"5637","DOI":"10.1074\/jbc.M109119200","article-title":"Apical sorting of beta-secretase limits amyloid beta-peptide production","volume":"277","author":"Capell","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0080","doi-asserted-by":"crossref","first-page":"10956","DOI":"10.1021\/ja503535m","article-title":"The N-terminal region of amyloid beta controls the aggregation rate and fibril stability at low pH through a gain of function mechanism","volume":"136","author":"Brannstrom","year":"2014","journal-title":"J Am Chem Soc"},{"key":"10.1016\/j.jmb.2014.12.005_bb0085","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.jpba.2014.04.021","article-title":"The protease activity of transthyretin reverses the effect of pH on the amyloid-beta protein\/heparan sulfate proteoglycan interaction: a biochromatographic study","volume":"97","author":"Geneste","year":"2014","journal-title":"J Pharm Biomed Anal"},{"key":"10.1016\/j.jmb.2014.12.005_bb0090","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1515\/hsz-2013-0280","article-title":"The structural biology of the amyloid precursor protein APP\u2014a complex puzzle reveals its multi-domain architecture","volume":"395","author":"Coburger","year":"2014","journal-title":"Biol Chem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0095","doi-asserted-by":"crossref","first-page":"5281","DOI":"10.1073\/pnas.0911326107","article-title":"Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein","volume":"107","author":"Dahms","year":"2010","journal-title":"Proc Natl Acad Sci"},{"key":"10.1016\/j.jmb.2014.12.005_bb0100","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1016\/j.molcel.2004.06.037","article-title":"The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain","volume":"15","author":"Wang","year":"2004","journal-title":"Mol Cell"},{"key":"10.1016\/j.jmb.2014.12.005_bb0105","doi-asserted-by":"crossref","first-page":"1614","DOI":"10.1107\/S0907444904015343","article-title":"Cloning, expression, crystallization and initial crystallographic analysis of the C-terminal domain of the amyloid precursor protein APP","volume":"60","author":"Keil","year":"2004","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0110","doi-asserted-by":"crossref","first-page":"e81926","DOI":"10.1371\/journal.pone.0081926","article-title":"The overall structure of the multi-domain amyloid precursor protein (APP)","volume":"8","author":"Coburger","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2014.12.005_bb0115","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1038\/7562","article-title":"Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein","volume":"6","author":"Rossjohn","year":"1999","journal-title":"Nat Struct Biol"},{"key":"10.1016\/j.jmb.2014.12.005_bb0120","doi-asserted-by":"crossref","first-page":"17401","DOI":"10.1074\/jbc.M300629200","article-title":"Structure of the Alzheimer's disease amyloid precursor protein copper binding domain","volume":"278","author":"Barnham","year":"2003","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0125","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.jmb.2006.12.041","article-title":"Structural studies of the Alzheimer's amyloid precursor protein copper-binding domain reveal how it binds copper ions","volume":"367","author":"Kong","year":"2007","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2014.12.005_bb0130","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0135","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1107\/S1744309107041139","article-title":"Structure of Alzheimer's disease amyloid precursor protein copper-binding domain at atomic resolution","volume":"63","author":"Kong","year":"2007","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"10.1016\/j.jmb.2014.12.005_bb0140","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1039\/C3MT00258F","article-title":"Quantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological function","volume":"6","author":"Leong","year":"2013","journal-title":"Metallomics"},{"key":"10.1016\/j.jmb.2014.12.005_bb0145","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1016\/j.jsb.2014.05.006","article-title":"Heparin induced dimerization of APP is primarily mediated by E1 and regulated by its acidic domain","volume":"187","author":"Hoefgen","year":"2014","journal-title":"J Struct Biol"},{"key":"10.1016\/j.jmb.2014.12.005_bb0150","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J Mol Biol"},{"key":"10.1016\/j.jmb.2014.12.005_bb0155","doi-asserted-by":"crossref","first-page":"7271","DOI":"10.1074\/jbc.M708046200","article-title":"Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect \u03b3-secretase cleavage of APP","volume":"283","author":"Kaden","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0160","doi-asserted-by":"crossref","first-page":"13979","DOI":"10.1021\/bi971004s","article-title":"Human thioredoxin homodimers: regulation by pH, role of aspartate 60, and crystal structure of the aspartate 60\u2192asparagine mutant","volume":"36","author":"Andersen","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2014.12.005_bb0165","doi-asserted-by":"crossref","first-page":"26840","DOI":"10.1074\/jbc.M112.355743","article-title":"The amyloid precursor protein copper binding domain histidine residues 149 and 151 mediate APP stability and metabolism","volume":"287","author":"Spoerri","year":"2012","journal-title":"J Biol Chem"},{"key":"10.1016\/j.jmb.2014.12.005_bb0170","doi-asserted-by":"crossref","first-page":"e72177","DOI":"10.1371\/journal.pone.0072177","article-title":"The amyloid precursor protein (APP) does not have a ferroxidase site in its E2 domain","volume":"8","author":"Honarmand Ebrahimi","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2014.12.005_bb0175","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1107\/S0909049512006395","article-title":"Facilities for macromolecular crystallography at the Helmholtz-Zentrum Berlin","volume":"19","author":"Mueller","year":"2012","journal-title":"J Synchrotron Radiat"},{"key":"10.1016\/j.jmb.2014.12.005_bb0180","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1107\/S0021889812011715","article-title":"XDSAPP: a graphical user interface for the convenient processing of diffraction data using XDS","volume":"45","author":"Krug","year":"2012","journal-title":"J Appl Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0185","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0190","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1107\/S0907444995014983","article-title":"xdlMAPMAN and xdlDATAMAN\u2014programs for reformatting, analysis and manipulation of biomacromolecular electron-density maps and reflection data sets","volume":"52","author":"Kleywegt","year":"1996","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0195","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J Appl Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0200","doi-asserted-by":"crossref","first-page":"1131","DOI":"10.1107\/S0907444903008126","article-title":"A graphical user interface to the CCP4 program suite","volume":"59","author":"Potterton","year":"2003","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0205","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0210","doi-asserted-by":"crossref","first-page":"2728","DOI":"10.1038\/nprot.2007.406","article-title":"Version 1.2 of the crystallography and NMR system","volume":"2","author":"Brunger","year":"2007","journal-title":"Nat Protoc"},{"key":"10.1016\/j.jmb.2014.12.005_bb0215","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr Sect D Biol Crystallogr"},{"key":"10.1016\/j.jmb.2014.12.005_bb0220","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: application to microtubules and the ribosome","volume":"98","author":"Baker","year":"2001","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1016\/j.jmb.2014.12.005_bb0225","doi-asserted-by":"crossref","first-page":"2947","DOI":"10.1093\/bioinformatics\/btm404","article-title":"Clustal W and Clustal X version 2.0","volume":"23","author":"Larkin","year":"2007","journal-title":"Bioinformatics"}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283614006214?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0022283614006214?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2018,9,26]],"date-time":"2018-09-26T22:20:38Z","timestamp":1538000438000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0022283614006214"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,1]]},"references-count":45,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2015,1]]}},"alternative-id":["S0022283614006214"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2014.12.005","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2015,1]]}}}