{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T02:59:18Z","timestamp":1791946758854,"version":"4.3.4"},"reference-count":75,"publisher":"National Academy of Sciences","issue":"16","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2014,4,22]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>We find that the core domain of the human molecular chaperone \u03b1B-crystallin can function effectively in preventing protein aggregation and amyloid toxicity. The core domain represents only half the total sequence of the protein, but it is one of the most potent known inhibitors of the aggregation of amyloid-\u03b2, a process implicated in Alzheimer\u2019s disease. We have determined high-resolution structures of this core domain and investigated its biophysical properties in solution. We find that the excised domain efficiently prevents amyloid aggregation and thereby reduces the toxicity of the resulting aggregates to cells. The structures of these domains that we present should represent useful scaffolds for the design of novel amyloid inhibitors.<\/jats:p>","DOI":"10.1073\/pnas.1322673111","type":"journal-article","created":{"date-parts":[[2014,4,8]],"date-time":"2014-04-08T00:10:32Z","timestamp":1396915832000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":203,"title":["The structured core domain of \u03b1B-crystallin can prevent amyloid fibrillation and associated toxicity"],"prefix":"10.1073","volume":"111","author":[{"given":"Georg K. A.","family":"Hochberg","sequence":"first","affiliation":[{"name":"Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Heath","family":"Ecroyd","sequence":"additional","affiliation":[{"name":"Illawarra Health and Medical Research Institute and"},{"name":"School of Biological Sciences, University of Wollongong, Wollongong, NSW 2522, Australia;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cong","family":"Liu","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute,"},{"name":"University of California, Los Angeles\u2013Department of Energy Institute for Genomics and Proteomics, and"},{"name":"Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dezerae","family":"Cox","sequence":"additional","affiliation":[{"name":"Illawarra Health and Medical Research Institute and"},{"name":"School of Biological Sciences, University of Wollongong, Wollongong, NSW 2522, Australia;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Duilio","family":"Cascio","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute,"},{"name":"University of California, Los Angeles\u2013Department of Energy Institute for Genomics and Proteomics, and"},{"name":"Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael R.","family":"Sawaya","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute,"},{"name":"University of California, Los Angeles\u2013Department of Energy Institute for Genomics and Proteomics, and"},{"name":"Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miranda P.","family":"Collier","sequence":"additional","affiliation":[{"name":"Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Stroud","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute,"},{"name":"University of California, Los Angeles\u2013Department of Energy Institute for Genomics and Proteomics, and"},{"name":"Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"John A.","family":"Carver","sequence":"additional","affiliation":[{"name":"Research School of Chemistry, The Australian National University, Canberra, ACT 0200, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew J.","family":"Baldwin","sequence":"additional","affiliation":[{"name":"Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carol V.","family":"Robinson","sequence":"additional","affiliation":[{"name":"Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David S.","family":"Eisenberg","sequence":"additional","affiliation":[{"name":"Howard Hughes Medical Institute,"},{"name":"University of California, Los Angeles\u2013Department of Energy Institute for Genomics and Proteomics, and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Justin L. P.","family":"Benesch","sequence":"additional","affiliation":[{"name":"Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arthur","family":"Laganowsky","sequence":"additional","affiliation":[{"name":"Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, United Kingdom;"},{"name":"Howard Hughes Medical Institute,"},{"name":"University of California, Los Angeles\u2013Department of Energy Institute for Genomics and Proteomics, and"},{"name":"Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2014,4,7]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"14160","DOI":"10.1021\/ja2017703","article-title":"Metastability of native proteins and the phenomenon of amyloid formation","volume":"133","author":"Baldwin AJ","year":"2011","unstructured":"AJ Baldwin, et al., Metastability of native proteins and the phenomenon of amyloid formation. J Am Chem Soc 133, 14160\u201314163 (2011).","journal-title":"J Am Chem Soc"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.cell.2010.11.050","article-title":"Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions","volume":"144","author":"Olzscha H","year":"2011","unstructured":"H Olzscha, et al., Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144, 67\u201378 (2011).","journal-title":"Cell"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nrm3542","article-title":"Diversity in the origins of proteostasis networks\u2013a driver for protein function in evolution","volume":"14","author":"Powers ET","year":"2013","unstructured":"ET Powers, WE Balch, Diversity in the origins of proteostasis networks\u2013a driver for protein function in evolution. Nat Rev Mol Cell Biol 14, 237\u2013248 (2013).","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"916","DOI":"10.1126\/science.1141448","article-title":"Adapting proteostasis for disease intervention","volume":"319","author":"Balch WE","year":"2008","unstructured":"WE Balch, RI Morimoto, A Dillin, JW Kelly, Adapting proteostasis for disease intervention. Science 319, 916\u2013919 (2008).","journal-title":"Science"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1038\/nature10317","article-title":"Molecular chaperones in protein folding and proteostasis","volume":"475","author":"Hartl FU","year":"2011","unstructured":"FU Hartl, A Bracher, M Hayer-Hartl, Molecular chaperones in protein folding and proteostasis. Nature 475, 324\u2013332 (2011).","journal-title":"Nature"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.molcel.2010.10.006","article-title":"The heat shock response: Life on the verge of death","volume":"40","author":"Richter K","year":"2010","unstructured":"K Richter, M Haslbeck, J Buchner, The heat shock response: Life on the verge of death. Mol Cell 40, 253\u2013266 (2010).","journal-title":"Mol Cell"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.tibs.2011.11.005","article-title":"Small heat shock proteins and \u03b1-crystallins: Dynamic proteins with flexible functions","volume":"37","author":"Basha E","year":"2012","unstructured":"E Basha, H O\u2019Neill, E Vierling, Small heat shock proteins and \u03b1-crystallins: Dynamic proteins with flexible functions. Trends Biochem Sci 37, 106\u2013117 (2012).","journal-title":"Trends Biochem Sci"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1007\/128_2012_324","article-title":"Small heat-shock proteins: Paramedics of the cell","volume":"328","author":"Hilton GR","year":"2013","unstructured":"GR Hilton, H Lioe, F Stengel, AJ Baldwin, JLP Benesch, Small heat-shock proteins: Paramedics of the cell. Top Curr Chem 328, 69\u201398 (2013).","journal-title":"Top Curr Chem"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"3828","DOI":"10.1021\/bi900212j","article-title":"Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins","volume":"48","author":"McHaourab HS","year":"2009","unstructured":"HS McHaourab, JA Godar, PL Stewart, Structure and mechanism of protein stability sensors: Chaperone activity of small heat shock proteins. Biochemistry 48, 3828\u20133837 (2009).","journal-title":"Biochemistry"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"20110409","DOI":"10.1098\/rstb.2011.0409","article-title":"Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders","volume":"368","author":"Carra S","year":"2013","unstructured":"S Carra, et al., Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders. Philos Trans R Soc Lond B Biol Sci 368, 20110409 (2013).","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"1588","DOI":"10.1016\/j.biocel.2012.02.022","article-title":"The small heat shock proteins family: The long forgotten chaperones","volume":"44","author":"Garrido C","year":"2012","unstructured":"C Garrido, C Paul, R Seigneuric, HH Kampinga, The small heat shock proteins family: The long forgotten chaperones. Int J Biochem Cell Biol 44, 1588\u20131592 (2012).","journal-title":"Int J Biochem Cell Biol"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"10449","DOI":"10.1073\/pnas.89.21.10449","article-title":"Alpha-crystallin can function as a molecular chaperone","volume":"89","author":"Horwitz J","year":"1992","unstructured":"J Horwitz, Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA 89, 10449\u201310453 (1992).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"1657","DOI":"10.1016\/j.biocel.2012.03.011","article-title":"The family of mammalian small heat shock proteins (HSPBs): Implications in protein deposit diseases and motor neuropathies","volume":"44","author":"Boncoraglio A","year":"2012","unstructured":"A Boncoraglio, M Minoia, S Carra, The family of mammalian small heat shock proteins (HSPBs): Implications in protein deposit diseases and motor neuropathies. Int J Biochem Cell Biol 44, 1657\u20131669 (2012).","journal-title":"Int J Biochem Cell Biol"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1007\/s00018-008-8327-4","article-title":"Crystallin proteins and amyloid fibrils","volume":"66","author":"Ecroyd H","year":"2009","unstructured":"H Ecroyd, JA Carver, Crystallin proteins and amyloid fibrils. Cell Mol Life Sci 66, 62\u201381 (2009).","journal-title":"Cell Mol Life Sci"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"1706","DOI":"10.1016\/j.biocel.2012.06.005","article-title":"HSPBs: Small proteins with big implications in human disease","volume":"44","author":"Kampinga HH","year":"2012","unstructured":"HH Kampinga, C Garrido, HSPBs: Small proteins with big implications in human disease. Int J Biochem Cell Biol 44, 1706\u20131710 (2012).","journal-title":"Int J Biochem Cell Biol"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1146\/annurev.biochem.75.101304.123901","article-title":"Protein misfolding, functional amyloid, and human disease","volume":"75","author":"Chiti F","year":"2006","unstructured":"F Chiti, CM Dobson, Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75, 333\u2013366 (2006).","journal-title":"Annu Rev Biochem"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.02.022","article-title":"The amyloid state of proteins in human diseases","volume":"148","author":"Eisenberg D","year":"2012","unstructured":"D Eisenberg, M Jucker, The amyloid state of proteins in human diseases. Cell 148, 1188\u20131203 (2012).","journal-title":"Cell"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer\u2019s amyloid beta-peptide","volume":"8","author":"Haass C","year":"2007","unstructured":"C Haass, DJ Selkoe, Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer\u2019s amyloid beta-peptide. Nat Rev Mol Cell Biol 8, 101\u2013112 (2007).","journal-title":"Nat Rev Mol Cell Biol"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.brainres.2006.03.058","article-title":"Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity","volume":"1089","author":"Wilhelmus MM","year":"2006","unstructured":"MM Wilhelmus, et al., Small heat shock proteins inhibit amyloid-beta protein aggregation and cerebrovascular amyloid-beta protein toxicity. Brain Res 1089, 67\u201378 (2006).","journal-title":"Brain Res"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"12479","DOI":"10.1073\/pnas.1117799109","article-title":"Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers","volume":"109","author":"Mannini B","year":"2012","unstructured":"B Mannini, et al., Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc Natl Acad Sci USA 109, 12479\u201312484 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"10016","DOI":"10.1073\/pnas.0610659104","article-title":"Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass","volume":"104","author":"Knowles TP","year":"2007","unstructured":"TP Knowles, et al., Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass. Proc Natl Acad Sci USA 104, 10016\u201310021 (2007).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1042\/BJ20050339","article-title":"AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin","volume":"392","author":"Raman B","year":"2005","unstructured":"B Raman, et al., AlphaB-crystallin, a small heat-shock protein, prevents the amyloid fibril growth of an amyloid beta-peptide and beta2-microglobulin. Biochem J 392, 573\u2013581 (2005).","journal-title":"Biochem J"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"1167","DOI":"10.1016\/j.jmb.2004.05.054","article-title":"Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: Effects on amyloid fibril formation and chaperone activity","volume":"340","author":"Rekas A","year":"2004","unstructured":"A Rekas, et al., Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: Effects on amyloid fibril formation and chaperone activity. J Mol Biol 340, 1167\u20131183 (2004).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1016\/j.bpj.2011.07.056","article-title":"Binding of the molecular chaperone \u03b1B-crystallin to A\u03b2 amyloid fibrils inhibits fibril elongation","volume":"101","author":"Shammas SL","year":"2011","unstructured":"SL Shammas, et al., Binding of the molecular chaperone \u03b1B-crystallin to A\u03b2 amyloid fibrils inhibits fibril elongation. Biophys J 101, 1681\u20131689 (2011).","journal-title":"Biophys J"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1016\/j.bpj.2009.10.056","article-title":"The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation","volume":"98","author":"Waudby CA","year":"2010","unstructured":"CA Waudby, et al., The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation. Biophys J 98, 843\u2013851 (2010).","journal-title":"Biophys J"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"1214","DOI":"10.1096\/fj.12-220657","article-title":"Avoiding the oligomeric state: \u03b1B-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils","volume":"27","author":"Binger KJ","year":"2013","unstructured":"KJ Binger, et al., Avoiding the oligomeric state: \u03b1B-crystallin inhibits fragmentation and induces dissociation of apolipoprotein C-II amyloid fibrils. FASEB J 27, 1214\u20131222 (2013).","journal-title":"FASEB J"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/j.jmb.2011.07.016","article-title":"\u03b1B-crystallin polydispersity is a consequence of unbiased quaternary dynamics","volume":"413","author":"Baldwin AJ","year":"2011","unstructured":"AJ Baldwin, H Lioe, CV Robinson, LE Kay, JLP Benesch, \u03b1B-crystallin polydispersity is a consequence of unbiased quaternary dynamics. J Mol Biol 413, 297\u2013309 (2011).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"13602","DOI":"10.1074\/jbc.M112.443812","article-title":"Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins \u03b1B-crystallin and HSP27","volume":"288","author":"Aquilina JA","year":"2013","unstructured":"JA Aquilina, S Shrestha, AM Morris, H Ecroyd, Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins \u03b1B-crystallin and HSP27. J Biol Chem 288, 13602\u201313609 (2013).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/j.febslet.2013.01.021","article-title":"One size does not fit all: The oligomeric states of \u03b1B crystallin","volume":"587","author":"Delbecq SP","year":"2013","unstructured":"SP Delbecq, RE Klevit, One size does not fit all: The oligomeric states of \u03b1B crystallin. FEBS Lett 587, 1073\u20131080 (2013).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bbrc.2006.12.176","article-title":"The N-terminal domain of alphaB-crystallin is protected from proteolysis by bound substrate","volume":"353","author":"Aquilina JA","year":"2007","unstructured":"JA Aquilina, SJ Watt, The N-terminal domain of alphaB-crystallin is protected from proteolysis by bound substrate. Biochem Biophys Res Commun 353, 1115\u20131120 (2007).","journal-title":"Biochem Biophys Res Commun"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"3069","DOI":"10.1021\/bi0518141","article-title":"Mini-alphaB-crystallin: A functional element of alphaB-crystallin with chaperone-like activity","volume":"45","author":"Bhattacharyya J","year":"2006","unstructured":"J Bhattacharyya, EG Padmanabha Udupa, J Wang, KK Sharma, Mini-alphaB-crystallin: A functional element of alphaB-crystallin with chaperone-like activity. Biochemistry 45, 3069\u20133076 (2006).","journal-title":"Biochemistry"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"14854","DOI":"10.1021\/bi0503910","article-title":"Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin","volume":"44","author":"Ghosh JG","year":"2005","unstructured":"JG Ghosh, MR Estrada, JI Clark, Interactive domains for chaperone activity in the small heat shock protein, human alphaB crystallin. Biochemistry 44, 14854\u201314869 (2005).","journal-title":"Biochemistry"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"5941","DOI":"10.1016\/j.febslet.2006.09.063","article-title":"alphaB-crystallin competes with Alzheimer\u2019s disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35","volume":"580","author":"Narayanan S","year":"2006","unstructured":"S Narayanan, B Kamps, WC Boelens, B Reif, alphaB-crystallin competes with Alzheimer\u2019s disease beta-amyloid peptide for peptide-peptide interactions and induces oxidation of Abeta-Met35. FEBS Lett 580, 5941\u20135946 (2006).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_34_2","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1006\/bbrc.1997.7460","article-title":"Functional elements in molecular chaperone alpha-crystallin: Identification of binding sites in alpha B-crystallin","volume":"239","author":"Sharma KK","year":"1997","unstructured":"KK Sharma, H Kaur, K Kester, Functional elements in molecular chaperone alpha-crystallin: Identification of binding sites in alpha B-crystallin. Biochem Biophys Res Commun 239, 217\u2013222 (1997).","journal-title":"Biochem Biophys Res Commun"},{"key":"e_1_3_4_35_2","doi-asserted-by":"crossref","first-page":"29511","DOI":"10.1074\/jbc.272.47.29511","article-title":"Subunit exchange of alphaA-crystallin","volume":"272","author":"Bova MP","year":"1997","unstructured":"MP Bova, LL Ding, J Horwitz, BKK Fung, Subunit exchange of alphaA-crystallin. J Biol Chem 272, 29511\u201329517 (1997).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_36_2","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/j.exer.2004.08.010","article-title":"Dissociation is not required for alpha-crystallin\u2019s chaperone function","volume":"79","author":"Augusteyn RC","year":"2004","unstructured":"RC Augusteyn, Dissociation is not required for alpha-crystallin\u2019s chaperone function. Exp Eye Res 79, 781\u2013784 (2004).","journal-title":"Exp Eye Res"},{"key":"e_1_3_4_37_2","doi-asserted-by":"crossref","first-page":"14485","DOI":"10.1074\/jbc.M500135200","article-title":"Subunit exchange of polydisperse proteins: Mass spectrometry reveals consequences of alphaA-crystallin truncation","volume":"280","author":"Aquilina JA","year":"2005","unstructured":"JA Aquilina, et al., Subunit exchange of polydisperse proteins: Mass spectrometry reveals consequences of alphaA-crystallin truncation. J Biol Chem 280, 14485\u201314491 (2005).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_38_2","doi-asserted-by":"crossref","first-page":"1242","DOI":"10.1016\/j.jmb.2009.07.069","article-title":"Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20","volume":"392","author":"Bagn\u00e9ris C","year":"2009","unstructured":"C Bagn\u00e9ris, et al., Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. J Mol Biol 392, 1242\u20131252 (2009).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_39_2","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.jmb.2011.02.020","article-title":"Crystal structure of R120G disease mutant of human \u03b1B-crystallin domain dimer shows closure of a groove","volume":"408","author":"Clark AR","year":"2011","unstructured":"AR Clark, CE Naylor, C Bagn\u00e9ris, NH Keep, C Slingsby, Crystal structure of R120G disease mutant of human \u03b1B-crystallin domain dimer shows closure of a groove. J Mol Biol 408, 118\u2013134 (2011).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_40_2","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1038\/nsmb.1891","article-title":"Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers","volume":"17","author":"Jehle S","year":"2010","unstructured":"S Jehle, et al., Solid-state NMR and SAXS studies provide a structural basis for the activation of alphaB-crystallin oligomers. Nat Struct Mol Biol 17, 1037\u20131042 (2010).","journal-title":"Nat Struct Mol Biol"},{"key":"e_1_3_4_41_2","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1002\/pro.380","article-title":"Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function","volume":"19","author":"Laganowsky A","year":"2010","unstructured":"A Laganowsky, et al., Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function. Protein Sci 19, 1031\u20131043 (2010).","journal-title":"Protein Sci"},{"key":"e_1_3_4_42_2","doi-asserted-by":"crossref","first-page":"1978","DOI":"10.1002\/pro.471","article-title":"Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin","volume":"19","author":"Laganowsky A","year":"2010","unstructured":"A Laganowsky, D Eisenberg, Non-3D domain swapped crystal structure of truncated zebrafish alphaA crystallin. Protein Sci 19, 1978\u20131984 (2010).","journal-title":"Protein Sci"},{"key":"e_1_3_4_43_2","doi-asserted-by":"crossref","first-page":"4587","DOI":"10.1038\/emboj.2012.318","article-title":"Binding determinants of the small heat shock protein, \u03b1B-crystallin: Recognition of the \u2018IxI\u2019 motif","volume":"31","author":"Delbecq SP","year":"2012","unstructured":"SP Delbecq, S Jehle, R Klevit, Binding determinants of the small heat shock protein, \u03b1B-crystallin: Recognition of the \u2018IxI\u2019 motif. EMBO J 31, 4587\u20134594 (2012).","journal-title":"EMBO J"},{"key":"e_1_3_4_44_2","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1007\/s12192-009-0151-8","article-title":"The pivotal role of the beta 7 strand in the intersubunit contacts of different human small heat shock proteins","volume":"15","author":"Mymrikov EV","year":"2010","unstructured":"EV Mymrikov, OV Bukach, AS Seit-Nebi, NB Gusev, The pivotal role of the beta 7 strand in the intersubunit contacts of different human small heat shock proteins. Cell Stress Chaperones 15, 365\u2013377 (2010).","journal-title":"Cell Stress Chaperones"},{"key":"e_1_3_4_45_2","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.jmb.2011.05.024","article-title":"Three-dimensional structure of \u03b1-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6","volume":"411","author":"Baranova EV","year":"2011","unstructured":"EV Baranova, et al., Three-dimensional structure of \u03b1-crystallin domain dimers of human small heat shock proteins HSPB1 and HSPB6. J Mol Biol 411, 110\u2013122 (2011).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_46_2","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1080\/152165401317291156","article-title":"Hsp27: Novel regulator of intracellular redox state","volume":"52","author":"Arrigo AP","year":"2001","unstructured":"AP Arrigo, Hsp27: Novel regulator of intracellular redox state. IUBMB Life 52, 303\u2013307 (2001).","journal-title":"IUBMB Life"},{"key":"e_1_3_4_47_2","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1002\/prot.22878","article-title":"Conformational analysis and design of cross-strand disulfides in antiparallel \u03b2-sheets","volume":"79","author":"Indu S","year":"2011","unstructured":"S Indu, V Kochat, S Thakurela, C Ramakrishnan, R Varadarajan, Conformational analysis and design of cross-strand disulfides in antiparallel \u03b2-sheets. Proteins 79, 244\u2013260 (2011).","journal-title":"Proteins"},{"key":"e_1_3_4_48_2","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1016\/j.jmb.2008.10.097","article-title":"alphaB-crystallin: A hybrid solid-state\/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer","volume":"385","author":"Jehle S","year":"2009","unstructured":"S Jehle, et al., alphaB-crystallin: A hybrid solid-state\/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer. J Mol Biol 385, 1481\u20131497 (2009).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_49_2","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1038\/nprot.2008.78","article-title":"Ion mobility-mass spectrometry analysis of large protein complexes","volume":"3","author":"Ruotolo BT","year":"2008","unstructured":"BT Ruotolo, JLP Benesch, AM Sandercock, SJ Hyung, CV Robinson, Ion mobility-mass spectrometry analysis of large protein complexes. Nat Protoc 3, 1139\u20131152 (2008).","journal-title":"Nat Protoc"},{"key":"e_1_3_4_50_2","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/j.sbi.2011.08.002","article-title":"Mass spectrometry: Come of age for structural and dynamical biology","volume":"21","author":"Benesch JLP","year":"2011","unstructured":"JLP Benesch, BT Ruotolo, Mass spectrometry: Come of age for structural and dynamical biology. Curr Opin Struct Biol 21, 641\u2013649 (2011).","journal-title":"Curr Opin Struct Biol"},{"key":"e_1_3_4_51_2","doi-asserted-by":"crossref","first-page":"20110405","DOI":"10.1098\/rstb.2011.0405","article-title":"C-terminal interactions mediate the quaternary dynamics of \u03b1B-crystallin","volume":"368","author":"Hilton GR","year":"2013","unstructured":"GR Hilton, et al., C-terminal interactions mediate the quaternary dynamics of \u03b1B-crystallin. Philos Trans R Soc Lond B Biol Sci 368, 20110405 (2013).","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"e_1_3_4_52_2","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1016\/S0022-2836(02)00144-4","article-title":"The interaction of the molecular chaperone \u03b1-crystallin with unfolding \u03b1-lactalbumin: A structural and kinetic spectroscopic study","volume":"318","author":"Carver JA","year":"2002","unstructured":"JA Carver, et al., The interaction of the molecular chaperone \u03b1-crystallin with unfolding \u03b1-lactalbumin: A structural and kinetic spectroscopic study. J Mol Biol 318, 815\u2013827 (2002).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_53_2","doi-asserted-by":"crossref","first-page":"12024","DOI":"10.1074\/jbc.M010856200","article-title":"A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity","volume":"276","author":"Feil IK","year":"2001","unstructured":"IK Feil, M Malfois, J Hendle, H van Der Zandt, DI Svergun, A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity. J Biol Chem 276, 12024\u201312029 (2001).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_54_2","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.jmb.2011.12.062","article-title":"Inhibition of amyloid formation","volume":"421","author":"H\u00e4rd T","year":"2012","unstructured":"T H\u00e4rd, C Lendel, Inhibition of amyloid formation. J Mol Biol 421, 441\u2013465 (2012).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_55_2","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1038\/sj.emboj.7601970","article-title":"Chaperones in control of protein disaggregation","volume":"27","author":"Liberek K","year":"2008","unstructured":"K Liberek, A Lewandowska, S Zietkiewicz, Chaperones in control of protein disaggregation. EMBO J 27, 328\u2013335 (2008).","journal-title":"EMBO J"},{"key":"e_1_3_4_56_2","doi-asserted-by":"crossref","first-page":"1078","DOI":"10.1126\/science.252.5009.1078","article-title":"The recruitment of crystallins: New functions precede gene duplication","volume":"252","author":"Piatigorsky J","year":"1991","unstructured":"J Piatigorsky, G Wistow, The recruitment of crystallins: New functions precede gene duplication. Science 252, 1078\u20131079 (1991).","journal-title":"Science"},{"key":"e_1_3_4_57_2","doi-asserted-by":"crossref","first-page":"20407","DOI":"10.1073\/pnas.1209565109","article-title":"Alternative bacterial two-component small heat shock protein systems","volume":"109","author":"Bepperling A","year":"2012","unstructured":"A Bepperling, et al., Alternative bacterial two-component small heat shock protein systems. Proc Natl Acad Sci USA 109, 20407\u201320412 (2012).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_58_2","doi-asserted-by":"crossref","first-page":"1683","DOI":"10.1016\/j.jmb.2013.02.011","article-title":"An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones","volume":"425","author":"Basha E","year":"2013","unstructured":"E Basha, et al., An unusual dimeric small heat shock protein provides insight into the mechanism of this class of chaperones. J Mol Biol 425, 1683\u20131696 (2013).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_59_2","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1046\/j.1432-1033.2003.03928.x","article-title":"Some properties of human small heat shock protein Hsp20 (HspB6)","volume":"271","author":"Bukach OV","year":"2004","unstructured":"OV Bukach, AS Seit-Nebi, SB Marston, NB Gusev, Some properties of human small heat shock protein Hsp20 (HspB6). Eur J Biochem 271, 291\u2013302 (2004).","journal-title":"Eur J Biochem"},{"key":"e_1_3_4_60_2","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1042\/BJ20121187","article-title":"The small heat-shock protein \u03b1B-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of \u03b1-lactalbumin","volume":"448","author":"Kulig M","year":"2012","unstructured":"M Kulig, H Ecroyd, The small heat-shock protein \u03b1B-crystallin uses different mechanisms of chaperone action to prevent the amorphous versus fibrillar aggregation of \u03b1-lactalbumin. Biochem J 448, 343\u2013352 (2012).","journal-title":"Biochem J"},{"key":"e_1_3_4_61_2","doi-asserted-by":"crossref","first-page":"9012","DOI":"10.1074\/jbc.M709928200","article-title":"Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein","volume":"283","author":"Ecroyd H","year":"2008","unstructured":"H Ecroyd, et al., Dissociation from the oligomeric state is the rate-limiting step in fibril formation by kappa-casein. J Biol Chem 283, 9012\u20139022 (2008).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_62_2","doi-asserted-by":"crossref","first-page":"1228","DOI":"10.1126\/science.1213151","article-title":"Atomic view of a toxic amyloid small oligomer","volume":"335","author":"Laganowsky A","year":"2012","unstructured":"A Laganowsky, et al., Atomic view of a toxic amyloid small oligomer. Science 335, 1228\u20131231 (2012).","journal-title":"Science"},{"key":"e_1_3_4_63_2","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1107\/S0021889893005588","article-title":"Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants","volume":"26","author":"Kabsch W","year":"1993","unstructured":"W Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Cryst 26, 795\u2013800 (1993).","journal-title":"J Appl Cryst"},{"key":"e_1_3_4_64_2","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy AJ","year":"2007","unstructured":"AJ McCoy, et al., Phaser crystallographic software. J Appl Cryst 40, 658\u2013674 (2007).","journal-title":"J Appl Cryst"},{"key":"e_1_3_4_65_2","doi-asserted-by":"crossref","first-page":"1948","DOI":"10.1107\/S0907444902016657","article-title":"PHENIX: Building new software for automated crystallographic structure determination","volume":"58","author":"Adams PD","year":"2002","unstructured":"PD Adams, et al., PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D Biol Crystallogr 58, 1948\u20131954 (2002).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_66_2","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley P","year":"2010","unstructured":"P Emsley, B Lohkamp, WG Scott, K Cowtan, Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_67_2","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1107\/S0907444996012255","article-title":"Refinement of macromolecular structures by the maximum-likelihood method","volume":"53","author":"Murshudov GN","year":"1997","unstructured":"GN Murshudov, AA Vagin, EJ Dodson, Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53, 240\u2013255 (1997).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_68_2","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1107\/S0907444911056058","article-title":"Exploiting structure similarity in refinement: Automated NCS and target-structure restraints in BUSTER","volume":"68","author":"Smart OS","year":"2012","unstructured":"OS Smart, et al., Exploiting structure similarity in refinement: Automated NCS and target-structure restraints in BUSTER. Acta Crystallogr D Biol Crystallogr 68, 368\u2013380 (2012).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_69_2","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 E","year":"2007","unstructured":"E Krissinel, K Henrick, Inference of macromolecular assemblies from crystalline state. J Mol Biol 372, 774\u2013797 (2007).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_70_2","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 MA","year":"2007","unstructured":"MA Larkin, et al., Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947\u20132948 (2007).","journal-title":"Bioinformatics"},{"key":"e_1_3_4_71_2","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen EF","year":"2004","unstructured":"EF Pettersen, et al., UCSF Chimera\u2014a visualization system for exploratory research and analysis. J Comput Chem 25, 1605\u20131612 (2004).","journal-title":"J Comput Chem"},{"key":"e_1_3_4_72_2","doi-asserted-by":"crossref","first-page":"9557","DOI":"10.1021\/ac1022953","article-title":"Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology","volume":"82","author":"Bush MF","year":"2010","unstructured":"MF Bush, et al., Collision cross sections of proteins and their complexes: A calibration framework and database for gas-phase structural biology. Anal Chem 82, 9557\u20139565 (2010).","journal-title":"Anal Chem"},{"key":"e_1_3_4_73_2","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio F","year":"1995","unstructured":"F Delaglio, et al., NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6, 277\u2013293 (1995).","journal-title":"J Biomol NMR"},{"key":"e_1_3_4_74_2","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1111\/j.1742-4658.2008.06257.x","article-title":"The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation","volume":"275","author":"Ecroyd H","year":"2008","unstructured":"H Ecroyd, JA Carver, The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation. FEBS J 275, 935\u2013947 (2008).","journal-title":"FEBS J"},{"key":"e_1_3_4_75_2","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1093\/toxsci\/66.2.298","article-title":"Dose-response modeling of continuous endpoints","volume":"66","author":"Slob W","year":"2002","unstructured":"W Slob, Dose-response modeling of continuous endpoints. Toxicol Sci 66, 298\u2013312 (2002).","journal-title":"Toxicol Sci"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1322673111","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T06:49:00Z","timestamp":1654584540000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1322673111"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,4,7]]},"references-count":75,"journal-issue":{"issue":"16","published-print":{"date-parts":[[2014,4,22]]}},"alternative-id":["10.1073\/pnas.1322673111"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1322673111","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,4,7]]},"assertion":[{"value":"2014-04-07","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}