{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,6]],"date-time":"2026-04-06T19:37:34Z","timestamp":1775504254802,"version":"3.50.1"},"reference-count":37,"publisher":"Public Library of Science (PLoS)","issue":"3","license":[{"start":{"date-parts":[[2012,3,5]],"date-time":"2012-03-05T00:00:00Z","timestamp":1330905600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0031924","type":"journal-article","created":{"date-parts":[[2012,3,6]],"date-time":"2012-03-06T03:38:52Z","timestamp":1331005132000},"page":"e31924","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":13,"title":["Molecular Interpretation of ACTH-\u03b2-Endorphin Coaggregation: Relevance to Secretory Granule Biogenesis"],"prefix":"10.1371","volume":"7","author":[{"given":"Srivastav","family":"Ranganathan","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Pradeep K.","family":"Singh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Uday","family":"Singh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Praful S.","family":"Singru","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ranjith","family":"Padinhateeri","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Samir K.","family":"Maji","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"340","published-online":{"date-parts":[[2012,3,5]]},"reference":[{"key":"ref1","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":"F Chiti","year":"2006","journal-title":"Annu Rev Biochem"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1016\/j.febslet.2009.07.003","article-title":"Structure-activity relationship of amyloid fibrils.","volume":"583","author":"SK Maji","year":"2009","journal-title":"FEBS Lett"},{"key":"ref3","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":"CM Dobson","year":"2001","journal-title":"Philos Trans R Soc Lond B Biol Sci"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/j.tibs.2007.03.003","article-title":"Functional amyloid\u2013from bacteria to humans.","volume":"32","author":"DM Fowler","year":"2007","journal-title":"Trends Biochem Sci"},{"key":"ref5","first-page":"79","article-title":"Native Functions of Amyloid.","author":"R Jacob","year":"2010"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1126\/science.1067484","article-title":"Role of Escherichia coli curli operons in directing amyloid fiber formation.","volume":"295","author":"MR Chapman","year":"2002","journal-title":"Science"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1038\/nrmicro1127","article-title":"Amyloids\u2013a functional coat for microorganisms.","volume":"3","author":"MF Gebbink","year":"2005","journal-title":"Nat Rev Microbiol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"R696","DOI":"10.1016\/j.cub.2003.08.040","article-title":"Aerial morphogenesis: enter the chaplins.","volume":"13","author":"NJ Talbot","year":"2003","journal-title":"Curr Biol"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/35035005","article-title":"A yeast prion provides a mechanism for genetic variation and phenotypic diversity.","volume":"407","author":"HL True","year":"2000","journal-title":"Nature"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/S1534-5807(02)00118-1","article-title":"The utility of prions.","volume":"2","author":"LZ Osherovich","year":"2002","journal-title":"Developmental Cell"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"7402","DOI":"10.1073\/pnas.072199199","article-title":"Amyloid aggregates of the HET-s prion protein are infectious.","volume":"99","author":"ML Maddelein","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"e6","DOI":"10.1371\/journal.pbio.0040006","article-title":"Functional amyloid formation within mammalian tissue.","volume":"4","author":"DM Fowler","year":"2006","journal-title":"PLoS Biol"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1126\/science.1173155","article-title":"Functional amyloids as natural storage of peptide hormones in pituitary secretory granules.","volume":"325","author":"SK Maji","year":"2009","journal-title":"Science"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1126\/science.2994224","article-title":"Pathways of protein secretion in eukaryotes.","volume":"230","author":"RB Kelly","year":"1985","journal-title":"Science"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1038\/326014a0","article-title":"Protein transport. From organelle to organelle.","volume":"326","author":"RB Kelly","year":"1987","journal-title":"Nature"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"315","DOI":"10.2165\/00063030-200317050-00002","article-title":"Manipulating the reversible aggregation of protein hormones in secretory granules: potential impact on biopharmaceutical development.","volume":"17","author":"P Dannies","year":"2003","journal-title":"BioDrugs"},{"key":"ref17","first-page":"3","article-title":"Protein hormone storage in secretory granules: mechanisms for concentration and sorting.","volume":"20","author":"PS Dannies","year":"1999","journal-title":"Endocr Rev"},{"issue":"Pt 3","key":"ref18","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1042\/bj3320593","article-title":"Sorting and storage during secretory granule biogenesis: looking backward and looking forward.","volume":"332","author":"P Arvan","year":"1998","journal-title":"Biochem J"},{"key":"ref19","first-page":"135","article-title":"Formation of secretory granules involves the amyloid structure.","author":"SK Maji","year":"2010"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1016\/S0969-2126(03)00031-5","article-title":"Dissecting the assembly of A beta(16\u201322) amyloid peptides into antiparallel beta sheets.","volume":"11","author":"DK Klimov","year":"2003","journal-title":"Structure"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"18258","DOI":"10.1073\/pnas.0509276102","article-title":"Solvent and mutation effects on the nucleation of amyloid beta-protein folding.","volume":"102","author":"L Cruz","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"17345","DOI":"10.1073\/pnas.0408153101","article-title":"In silico study of amyloid beta-protein folding and oligomerization.","volume":"101","author":"B Urbanc","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.cbpa.2006.08.018","article-title":"Simulations as analytical tools to understand protein aggregation and predict amyloid conformation.","volume":"10","author":"B Ma","year":"2006","journal-title":"Curr Opin Chem Biol"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1006\/jmbi.2000.3518","article-title":"Molecular dynamics simulations of a beta-hairpin fragment of protein G: balance between side-chain and backbone forces.","volume":"296","author":"B Ma","year":"2000","journal-title":"J Mol Biol"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1002\/jcc.20289","article-title":"Scalable molecular dynamics with NAMD.","volume":"26","author":"JC Phillips","year":"2005","journal-title":"J Comput Chem"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: visual molecular dynamics.","volume":"14","author":"W Humphrey","year":"1996","journal-title":"J Mol Graph"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1023\/B:JCAM.0000035186.90683.f2","article-title":"VEGA\u2013an open platform to develop chemo-bio-informatics applications, using plug-in architecture and script programming.","volume":"18","author":"A Pedretti","year":"2004","journal-title":"J Comput Aided Mol Des"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1017\/S003358359800345X","article-title":"Trifluoroethanol and colleagues: cosolvents come of age. Recent studies with peptides and proteins.","volume":"31","author":"M Buck","year":"1998","journal-title":"Q Rev Biophys"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1016\/0196-9781(82)90098-5","article-title":"The opiomelanotropinergic neuronal and endocrine systems.","volume":"3","author":"TL O'Donohue","year":"1982","journal-title":"Peptides"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"1302","DOI":"10.1038\/nbt1012","article-title":"Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins.","volume":"22","author":"AM Fernandez-Escamilla","year":"2004","journal-title":"Nat Biotechnol"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1006\/bbrc.1995.2436","article-title":"Aggregation and concentration-dependent sorting of exocrine regulated secretory proteins.","volume":"215","author":"SU Gorr","year":"1995","journal-title":"Biochem Biophys Res Commun"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"C365","DOI":"10.1152\/ajpcell.00338.2003","article-title":"Differential aggregation properties of secretory proteins that are stored in exocrine secretory granules of the pancreas and parotid glands.","volume":"286","author":"SG Venkatesh","year":"2004","journal-title":"Am J Physiol Cell Physiol"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1210\/edrv-1-1-1","article-title":"Structure and biosynthesis of pro-adrenocorticotropin\/endorphin and related peptides.","volume":"1","author":"BA Eipper","year":"1980","journal-title":"Endocr Rev"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/0006-8993(78)90047-1","article-title":"Concomitant storage of ACTH- and endorphin-like immunoreactivity in the secretory granules of anterior pituitary corticotrophs.","volume":"157","author":"E Weber","year":"1978","journal-title":"Brain Res"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0022-2836(82)90515-0","article-title":"A simple method for displaying the hydropathic character of a protein.","volume":"157","author":"J Kyte","year":"1982","journal-title":"J Mol Biol"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"636","DOI":"10.1126\/science.1082324","article-title":"Initiation and synergistic fibrillization of tau and \u03b1-synuclein.","volume":"300","author":"BI Giasson","year":"2003","journal-title":"Science"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/1074-5521(95)90071-3","article-title":"The core Alzheimer&apos;s peptide Nac forms amyloid fibrils which seed and are seeded by \u03b2-Amyloid - is Nac a common trigger or target in neurodegenerative disease?","volume":"2","author":"HY Han","year":"1995","journal-title":"Chem Biol"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0031924","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,24]],"date-time":"2018-10-24T06:31:27Z","timestamp":1540362687000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0031924"}},"subtitle":[],"editor":[{"given":"Vladimir N.","family":"Uversky","sequence":"first","affiliation":[],"role":[{"role":"editor","vocabulary":"crossref"}]}],"short-title":[],"issued":{"date-parts":[[2012,3,5]]},"references-count":37,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2012,3,5]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0031924","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,3,5]]}}}