{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T09:59:15Z","timestamp":1792835955563,"version":"4.5.0"},"reference-count":99,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2018,3,1]],"date-time":"2018-03-01T00:00:00Z","timestamp":1519862400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,3]],"date-time":"2020-09-03T00:00:00Z","timestamp":1599091200000},"content-version":"vor","delay-in-days":917,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000065","name":"HHS NIH National Institute of Neurological Disorders and Stroke (NINDS)","doi-asserted-by":"publisher","award":["R01NS089932"],"award-info":[{"award-number":["R01NS089932"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000065","name":"HHS NIH National Institute of Neurological Disorders and Stroke (NINDS)","doi-asserted-by":"publisher","award":["R01NS056114"],"award-info":[{"award-number":["R01NS056114"]}],"id":[{"id":"10.13039\/100000065","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2018,3]]},"DOI":"10.1074\/jbc.ra117.000357","type":"journal-article","created":{"date-parts":[[2018,1,22]],"date-time":"2018-01-22T15:45:16Z","timestamp":1516635916000},"page":"3734-3746","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":138,"title":["Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers"],"prefix":"10.1016","volume":"293","author":[{"given":"Ammon E.","family":"Posey","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kiersten M.","family":"Ruff","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tyler S.","family":"Harmon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Scott L.","family":"Crick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Aimin","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc I.","family":"Diamond","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rohit V.","family":"Pappu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.RA117.000357_bib1","doi-asserted-by":"crossref","first-page":"S10","DOI":"10.1038\/nm1066","article-title":"Protein aggregation and neurodegenerative disease","volume":"10","author":"Ross","year":"2004","journal-title":"Nat. Med"},{"key":"10.1074\/jbc.RA117.000357_bib2","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1038\/nrd3050","article-title":"Protein aggregation diseases: pathogenicity and therapeutic perspectives","volume":"9","author":"Aguzzi","year":"2010","journal-title":"Nat. Rev. Drug Discov"},{"key":"10.1074\/jbc.RA117.000357_bib3","doi-asserted-by":"crossref","first-page":"132","DOI":"10.1016\/j.abb.2007.08.033","article-title":"A polymer physics perspective on driving forces and mechanisms for protein aggregation","volume":"469","author":"Pappu","year":"2008","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.RA117.000357_bib4","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1146\/annurev.physchem.53.082301.111949","article-title":"Reversible polymerizations and aggregations","volume":"53","author":"Greer","year":"2002","journal-title":"Annu. Rev. Phys. Chem"},{"key":"10.1074\/jbc.RA117.000357_bib5","first-page":"2898","article-title":"Phase transitions in a \u201cmany-letter\u201d random heteropolymer","volume":"50","author":"Sfatos","year":"1994","journal-title":"Phys. Rev. E Stat. Phys. Plasmas Fluids Relat. Interdiscip. Topics"},{"key":"10.1074\/jbc.RA117.000357_bib6","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1002\/bip.360281003","article-title":"Theory of cooperative transitions in protein molecules. I. Why denaturation of globular protein is a first-order phase transition","volume":"28","author":"Shakhnovich","year":"1989","journal-title":"Biopolymers"},{"key":"10.1074\/jbc.RA117.000357_bib7","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1038\/nature10879","article-title":"Phase transitions in the assembly of multivalent signalling proteins","volume":"483","author":"Li","year":"2012","journal-title":"Nature"},{"key":"10.1074\/jbc.RA117.000357_bib8","doi-asserted-by":"crossref","first-page":"1729","DOI":"10.1126\/science.1172046","article-title":"Germline P granules are liquid droplets that localize by controlled dissolution\/condensation","volume":"324","author":"Brangwynne","year":"2009","journal-title":"Science"},{"key":"10.1074\/jbc.RA117.000357_bib9","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.molcel.2015.09.017","article-title":"RNA controls PolyQ protein phase transitions","volume":"60","author":"Zhang","year":"2015","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA117.000357_bib10","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2015.09.015","article-title":"Phase separation by low complexity domains promotes stress granule assembly and drives pathological fibrillization","volume":"163","author":"Molliex","year":"2015","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib11","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1126\/science.aad9964","article-title":"Phase separation of signaling molecules promotes T cell receptor signal transduction","volume":"352","author":"Su","year":"2016","journal-title":"Science"},{"key":"10.1074\/jbc.RA117.000357_bib12","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/nrm.2017.7","article-title":"Biomolecular condensates: organizers of cellular biochemistry","volume":"18","author":"Banani","year":"2017","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.RA117.000357_bib13","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1146\/annurev-cellbio-100913-013325","article-title":"Liquid-liquid phase separation in biology","volume":"30","author":"Hyman","year":"2014","journal-title":"Annu. Rev. Cell Dev. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib14","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1038\/nphys3532","article-title":"Polymer physics of intracellular phase transitions","volume":"11","author":"Brangwynne","year":"2015","journal-title":"Nat. Phys"},{"key":"10.1074\/jbc.RA117.000357_bib15","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.30294","article-title":"Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins","volume":"6","author":"Harmon","year":"2017","journal-title":"Elife"},{"key":"10.1074\/jbc.RA117.000357_bib16","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1016\/j.cell.2016.04.047","article-title":"Coexisting liquid phases underlie nucleolar subcompartments","volume":"165","author":"Feric","year":"2016","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib17","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/j.bpj.2016.10.043","article-title":"Phase transitions in biological systems with many components","volume":"112","author":"Jacobs","year":"2017","journal-title":"Biophys. J"},{"key":"10.1074\/jbc.RA117.000357_bib18","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1016\/j.cell.2015.12.038","article-title":"ATPase-modulated stress granules contain a diverse proteome and substructure","volume":"164","author":"Jain","year":"2016","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib19","doi-asserted-by":"crossref","first-page":"20075","DOI":"10.1073\/pnas.1320626110","article-title":"Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation","volume":"110","author":"Crick","year":"2013","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib20","doi-asserted-by":"crossref","first-page":"1028","DOI":"10.1016\/j.cell.2017.02.027","article-title":"Stress-triggered phase separation is an adaptive, Evolutionarily tuned response","volume":"168","author":"Riback","year":"2017","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib21","doi-asserted-by":"crossref","first-page":"678","DOI":"10.1016\/j.neuron.2015.10.030","article-title":"ALS\/FTD mutation-induced phase transition of FUS liquid droplets and reversible hydrogels into irreversible hydrogels impairs RNP granule function","volume":"88","author":"Murakami","year":"2015","journal-title":"Neuron"},{"key":"10.1074\/jbc.RA117.000357_bib22","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.devcel.2016.09.002","article-title":"Adaptation to stressors by systemic protein amyloidogenesis","volume":"39","author":"Audas","year":"2016","journal-title":"Dev. Cell"},{"key":"10.1074\/jbc.RA117.000357_bib23","doi-asserted-by":"crossref","first-page":"1188","DOI":"10.1016\/j.cell.2012.05.022","article-title":"Getting RNA and protein in phase","volume":"149","author":"Weber","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib24","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.cell.2015.07.047","article-title":"A liquid-to-solid phase transition of the ALS protein FUS accelerated by disease mutation","volume":"162","author":"Patel","year":"2015","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib25","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1016\/j.cell.2012.04.017","article-title":"Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels","volume":"149","author":"Kato","year":"2012","journal-title":"Cell"},{"key":"10.1074\/jbc.RA117.000357_bib26","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.tips.2014.12.004","article-title":"Supersaturation is a major driving force for protein aggregation in neurodegenerative diseases","volume":"36","author":"Ciryam","year":"2015","journal-title":"Trends Pharmacol. Sci"},{"key":"10.1074\/jbc.RA117.000357_bib27","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1016\/j.celrep.2013.09.043","article-title":"Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins","volume":"5","author":"Ciryam","year":"2013","journal-title":"Cell Rep"},{"key":"10.1074\/jbc.RA117.000357_bib28","doi-asserted-by":"crossref","first-page":"E3935","DOI":"10.1073\/pnas.1613854114","article-title":"Spinal motor neuron protein supersaturation patterns are associated with inclusion body formation in ALS","volume":"114","author":"Ciryam","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib29","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.sbi.2015.11.009","article-title":"Revisiting supersaturation as a factor determining amyloid fibrillation","volume":"36","author":"So","year":"2016","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib30","doi-asserted-by":"crossref","first-page":"5239","DOI":"10.1073\/pnas.77.9.5239","article-title":"Ligand-linked phase changes in a biological system: applications to sickle cell hemoglobin","volume":"77","author":"Wyman","year":"1980","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib31","series-title":"Binding and Linkage: Functional Chemistry of Biological Macromolecules","author":"Wyman","year":"1990"},{"key":"10.1074\/jbc.RA117.000357_bib32","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1016\/S0140-6736(07)60111-1","article-title":"Huntington's disease","volume":"369","author":"Walker","year":"2007","journal-title":"Lancet"},{"key":"10.1074\/jbc.RA117.000357_bib33","doi-asserted-by":"crossref","first-page":"7487","DOI":"10.1073\/pnas.1204542109","article-title":"Dysregulation of dopamine receptor D2 as a sensitive measure for Huntington disease pathology in model mice","volume":"109","author":"Crook","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib34","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1038\/nature02998","article-title":"Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death","volume":"431","author":"Arrasate","year":"2004","journal-title":"Nature"},{"key":"10.1074\/jbc.RA117.000357_bib35","doi-asserted-by":"crossref","first-page":"1642","DOI":"10.1016\/S0140-6736(03)13304-1","article-title":"Huntingtin aggregation and toxicity in Huntington's disease","volume":"361","author":"Bates","year":"2003","journal-title":"Lancet"},{"key":"10.1074\/jbc.RA117.000357_bib36","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.expneurol.2011.12.013","article-title":"Protein aggregates in Huntington's disease","volume":"238","author":"Arrasate","year":"2012","journal-title":"Exp. Neurol"},{"key":"10.1074\/jbc.RA117.000357_bib37","doi-asserted-by":"crossref","first-page":"16017","DOI":"10.1074\/jbc.M111.252577","article-title":"Identification of novel potentially toxic oligomers formed in vitro from mammalian-derived expanded huntingtin exon-1 protein","volume":"287","author":"Nucifora","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000357_bib38","doi-asserted-by":"crossref","first-page":"1029","DOI":"10.1098\/rstb.1999.0455","article-title":"Evidence for a recruitment and sequestration mechanism in Huntington's disease","volume":"354","author":"Preisinger","year":"1999","journal-title":"Philos. Trans. R. Soc. Lond. B Biol. Sci"},{"key":"10.1074\/jbc.RA117.000357_bib39","doi-asserted-by":"crossref","first-page":"8892","DOI":"10.1073\/pnas.1530212100","article-title":"Ubiquitin-mediated sequestration of normal cellular proteins into polyglutamine aggregates","volume":"100","author":"Donaldson","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib40","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.mcn.2005.04.005","article-title":"Evidence for sequestration of polyglutamine inclusions by Drosophila myeloid leukemia factor","volume":"29","author":"Kim","year":"2005","journal-title":"Mol. Cell. Neurosci"},{"key":"10.1074\/jbc.RA117.000357_bib41","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.febslet.2013.11.023","article-title":"Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies","volume":"588","author":"Schipper-Krom","year":"2014","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.RA117.000357_bib42","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.nbd.2015.06.017","article-title":"Differential recruitment of UBQLN2 to nuclear inclusions in the polyglutamine diseases HD and SCA3","volume":"82","author":"Zeng","year":"2015","journal-title":"Neurobiol. Dis"},{"key":"10.1074\/jbc.RA117.000357_bib43","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1073\/pnas.022662599","article-title":"Conformational Abs recognizing a generic amyloid fibril epitope","volume":"99","author":"O'Nuallain","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib44","doi-asserted-by":"crossref","first-page":"2905","DOI":"10.1093\/hmg\/11.23.2905","article-title":"Aggregated polyglutamine peptides delivered to nuclei are toxic to mammalian cells","volume":"11","author":"Yang","year":"2002","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA117.000357_bib45","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1016\/j.celrep.2017.04.029","article-title":"Huntingtin inclusions trigger cellular quiescence, deactivate apoptosis, and lead to delayed necrosis","volume":"19","author":"Ramdzan","year":"2017","journal-title":"Cell Rep"},{"key":"10.1074\/jbc.RA117.000357_bib46","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1007\/112_2007_704","article-title":"The profile of profilins","volume":"159","author":"Jockusch","year":"2007","journal-title":"Rev. Physiol. Biochem. Pharmacol"},{"key":"10.1074\/jbc.RA117.000357_bib47","doi-asserted-by":"crossref","first-page":"1575","DOI":"10.1126\/science.2157283","article-title":"The actin-binding protein profilin binds to PIP2 and inhibits its hydrolysis by phospholipase C","volume":"247","author":"Goldschmidt-Clermont","year":"1990","journal-title":"Science"},{"key":"10.1074\/jbc.RA117.000357_bib48","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1083\/jcb.113.5.1081","article-title":"Mechanism of the interaction of human platelet profilin with actin","volume":"113","author":"Goldschmidt-Clermont","year":"1991","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.RA117.000357_bib49","doi-asserted-by":"crossref","first-page":"16535","DOI":"10.1021\/bi961498d","article-title":"Structural requirements and thermodynamics of the interaction of proline peptides with profilin","volume":"35","author":"Petrella","year":"1996","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA117.000357_bib50","doi-asserted-by":"crossref","first-page":"3832","DOI":"10.1073\/pnas.051515498","article-title":"Profilin I is essential for cell survival and cell division in early mouse development","volume":"98","author":"Witke","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib51","doi-asserted-by":"crossref","first-page":"5196","DOI":"10.1128\/MCB.00079-08","article-title":"Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation","volume":"28","author":"Shao","year":"2008","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib52","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.nbd.2009.06.011","article-title":"Y-27632 improves rotarod performance and reduces huntingtin levels in R6\/2 mice","volume":"36","author":"Li","year":"2009","journal-title":"Neurobiol. Dis"},{"key":"10.1074\/jbc.RA117.000357_bib53","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1093\/hmg\/ddr500","article-title":"An aggregation sensing reporter identifies leflunomide and teriflunomide as polyglutamine aggregate inhibitors","volume":"21","author":"Fuentealba","year":"2012","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA117.000357_bib54","doi-asserted-by":"crossref","first-page":"26304","DOI":"10.1074\/jbc.M110.125039","article-title":"Interaction with polyglutamine aggregates reveals a Q\/N-rich domain in TDP-43","volume":"285","author":"Fuentealba","year":"2010","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000357_bib55","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1016\/S0896-6273(03)00697-4","article-title":"A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor","volume":"40","author":"Pollitt","year":"2003","journal-title":"Neuron"},{"key":"10.1074\/jbc.RA117.000357_bib56","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1186\/s13024-015-0063-2","article-title":"The N17 domain mitigates nuclear toxicity in a novel zebrafish Huntington's disease model","volume":"10","author":"Veldman","year":"2015","journal-title":"Mol. Neurodegener"},{"key":"10.1074\/jbc.RA117.000357_bib57","doi-asserted-by":"crossref","first-page":"726","DOI":"10.1016\/j.neuron.2015.01.008","article-title":"N17 Modifies mutant Huntingtin nuclear pathogenesis and severity of disease in HD BAC transgenic mice","volume":"85","author":"Gu","year":"2015","journal-title":"Neuron"},{"key":"10.1074\/jbc.RA117.000357_bib58","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1038\/ng0893-398","article-title":"The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease","volume":"4","author":"Andrew","year":"1993","journal-title":"Nat. Genet"},{"key":"10.1074\/jbc.RA117.000357_bib59","doi-asserted-by":"crossref","DOI":"10.1063\/1.2822322","article-title":"Quasihomogeneous nucleation of amyloid \u03b2 yields numerical bounds for the critical radius, the surface tension, and the free energy barrier for nucleus formation","volume":"128","author":"Garai","year":"2008","journal-title":"J. Chem. Phys"},{"key":"10.1074\/jbc.RA117.000357_bib60","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1063\/1.462468","article-title":"Concentration and molecular weight regime diagram of salt-free polyelectrolyte solutions as studied by light scattering","volume":"96","author":"Sedl\u00e1k","year":"1992","journal-title":"J. Chem. Phys"},{"key":"10.1074\/jbc.RA117.000357_bib61","doi-asserted-by":"crossref","first-page":"31739","DOI":"10.1074\/jbc.M112.353839","article-title":"Structural features and domain organization of huntingtin fibrils","volume":"287","author":"Bugg","year":"2012","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000357_bib62","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/S0076-6879(08)04205-5","article-title":"Isothermal titration calorimetry: general formalism using binding polynomials","volume":"455","author":"Freire","year":"2009","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.RA117.000357_bib63","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1038\/nsb1197-953","article-title":"Structure of the profilin-poly-l-proline complex involved in morphogenesis and cytoskeletal regulation","volume":"4","author":"Mahoney","year":"1997","journal-title":"Nat. Struct. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib64","doi-asserted-by":"crossref","first-page":"666","DOI":"10.1038\/10722","article-title":"Profilin binds proline-rich ligands in two distinct amide backbone orientations","volume":"6","author":"Mahoney","year":"1999","journal-title":"Nat. Struct. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib65","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1006\/jmbi.1996.0070","article-title":"Characterization of actin and poly-l-proline binding sites of Acanthamoeba profilin with monoclonal antibodies and by mutagenesis","volume":"256","author":"Kaiser","year":"1996","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib66","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1021\/acs.biochem.6b01263","article-title":"Self-assembly of human profilin-1 detected by Carr-Purcell-Meiboom-Gill nuclear magnetic resonance (CPMG NMR) spectroscopy","volume":"56","author":"Rennella","year":"2017","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA117.000357_bib67","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1006\/jcph.1995.1039","article-title":"Fast parallel algorithms for short-range molecular dynamics","volume":"117","author":"Plimpton","year":"1995","journal-title":"J. Comput. Phys"},{"key":"10.1074\/jbc.RA117.000357_bib68","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.18065","article-title":"Control of the structural landscape and neuronal proteotoxicity of mutant Huntingtin by domains flanking the polyQ tract","volume":"5","author":"Shen","year":"2016","journal-title":"Elife"},{"key":"10.1074\/jbc.RA117.000357_bib69","doi-asserted-by":"crossref","first-page":"3897","DOI":"10.1021\/bi500300c","article-title":"Aggregation behavior of chemically synthesized, full-length huntingtin exon1","volume":"53","author":"Sahoo","year":"2014","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.RA117.000357_bib70","series-title":"Fragment-based Approaches in Drug Discovery","first-page":"11","article-title":"Multivalency in ligand design","author":"Krishnamurthy","year":"2006"},{"key":"10.1074\/jbc.RA117.000357_bib71","doi-asserted-by":"crossref","first-page":"2754","DOI":"10.1002\/(SICI)1521-3773(19981102)37:20<2754::AID-ANIE2754>3.0.CO;2-3","article-title":"Polyvalent interactions in biological systems: implications for design and use of multivalent ligands and inhibitors","volume":"37","author":"Mammen","year":"1998","journal-title":"Angew. Chem. Int. Ed. Engl"},{"key":"10.1074\/jbc.RA117.000357_bib72","doi-asserted-by":"crossref","first-page":"4046","DOI":"10.1073\/pnas.78.7.4046","article-title":"On the attribution and additivity of binding energies","volume":"78","author":"Jencks","year":"1981","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib73","doi-asserted-by":"crossref","first-page":"12085","DOI":"10.1073\/pnas.1412504111","article-title":"Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1","volume":"111","author":"Kayatekin","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib74","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0136362","article-title":"Proteins with intrinsically disordered domains are preferentially recruited to polyglutamine aggregates","volume":"10","author":"Wear","year":"2015","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA117.000357_bib75","doi-asserted-by":"crossref","first-page":"18219","DOI":"10.1073\/pnas.1421313111","article-title":"Overexpression of Q-rich prion-like proteins suppresses polyQ cytotoxicity and alters the polyQ interactome","volume":"111","author":"Ripaud","year":"2014","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib76","doi-asserted-by":"crossref","first-page":"14456","DOI":"10.1021\/jacs.7b06659","article-title":"Monomeric huntingtin exon 1 has similar overall structural features for wild type and pathological polyglutamine lengths","volume":"139","author":"Warner","year":"2017","journal-title":"J. Am. Chem. Soc"},{"key":"10.1074\/jbc.RA117.000357_bib77","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/j.ijbiomac.2009.06.001","article-title":"Profilin oligomerization and its effect on poly (l-proline) binding and phosphorylation","volume":"45","author":"Korupolu","year":"2009","journal-title":"Int. J. Biol. Macromol"},{"key":"10.1074\/jbc.RA117.000357_bib78","doi-asserted-by":"crossref","first-page":"9974","DOI":"10.1021\/acsnano.6b04160","article-title":"Nonspecific colloidal-type interaction explains size-dependent specific binding of membrane-targeted nanoparticles","volume":"10","author":"Lundgren","year":"2016","journal-title":"ACS Nano"},{"key":"10.1074\/jbc.RA117.000357_bib79","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1007\/s10989-010-9230-z","article-title":"Multivalent antimicrobial peptides as therapeutics: design principles and structural diversities","volume":"16","author":"Liu","year":"2010","journal-title":"Int. J. Pept. Res. Ther"},{"key":"10.1074\/jbc.RA117.000357_bib80","doi-asserted-by":"crossref","first-page":"637","DOI":"10.2174\/138161209787315648","article-title":"Multivalent and multifunctional ligands to \u03b2-amyloid","volume":"15","author":"Kim","year":"2009","journal-title":"Curr. Pharm. Des"},{"key":"10.1074\/jbc.RA117.000357_bib81","doi-asserted-by":"crossref","first-page":"1600","DOI":"10.1093\/hmg\/ddw036","article-title":"Interactome network analysis identifies multiple caspase-6 interactors involved in the pathogenesis of HD","volume":"25","author":"Riechers","year":"2016","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA117.000357_bib82","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.molcel.2016.07.022","article-title":"Soluble oligomers of polyQ-expanded huntingtin target a multiplicity of key cellular factors","volume":"63","author":"Kim","year":"2016","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA117.000357_bib83","doi-asserted-by":"crossref","first-page":"19287","DOI":"10.1074\/jbc.M114.623561","article-title":"Integration-independent transgenic Huntington disease fragment mouse models reveal distinct phenotypes and life span in vivo","volume":"290","author":"O'Brien","year":"2015","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.RA117.000357_bib84","doi-asserted-by":"crossref","first-page":"103","DOI":"10.12688\/f1000research.6358.1","article-title":"The unfolded protein response and its potential role in Huntington's disease elucidated by a systems biology approach","volume":"4","author":"Kalathur","year":"2015","journal-title":"F1000Research"},{"key":"10.1074\/jbc.RA117.000357_bib85","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1016\/j.celrep.2015.04.030","article-title":"Quantitative interaction proteomics of neurodegenerative disease proteins","volume":"11","author":"Hosp","year":"2015","journal-title":"Cell Rep"},{"key":"10.1074\/jbc.RA117.000357_bib86","doi-asserted-by":"crossref","first-page":"1135","DOI":"10.1016\/j.celrep.2014.09.042","article-title":"A chaperome subnetwork safeguards proteostasis in aging and neurodegenerative disease","volume":"9","author":"Brehme","year":"2014","journal-title":"Cell Rep"},{"key":"10.1074\/jbc.RA117.000357_bib87","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.neuron.2012.05.024","article-title":"Network organization of the huntingtin proteomic interactome in mammalian brain","volume":"75","author":"Shirasaki","year":"2012","journal-title":"Neuron"},{"key":"10.1074\/jbc.RA117.000357_bib88","doi-asserted-by":"crossref","first-page":"2006","DOI":"10.4161\/cc.20423","article-title":"Huntingtin protein interactions altered by polyglutamine expansion as determined by quantitative proteomic analysis","volume":"11","author":"Ratovitski","year":"2012","journal-title":"Cell Cycle"},{"key":"10.1074\/jbc.RA117.000357_bib89","doi-asserted-by":"crossref","first-page":"E681","DOI":"10.1073\/pnas.1104384108","article-title":"Huntingtin-interacting protein 14 is a type 1 diabetes candidate protein regulating insulin secretion and \u03b2-cell apoptosis","volume":"108","author":"Berchtold","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.RA117.000357_bib90","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1038\/nn.4256","article-title":"Integrated genomics and proteomics define huntingtin CAG length-dependent networks in mice","volume":"19","author":"Langfelder","year":"2016","journal-title":"Nat. Neurosci"},{"key":"10.1074\/jbc.RA117.000357_bib91","article-title":"Intravitreal administration of HA-1077, a ROCK inhibitor, improves retinal function in a mouse model of Huntington disease","volume":"8","author":"Li","year":"2013","journal-title":"PLoS One"},{"key":"10.1074\/jbc.RA117.000357_bib92","doi-asserted-by":"crossref","first-page":"2795","DOI":"10.1093\/hmg\/ddr178","article-title":"Huntingtin affinity for partners is not changed by polyglutamine length: aggregation itself triggers aberrant interactions","volume":"20","author":"Davranche","year":"2011","journal-title":"Hum. Mol. Genet"},{"key":"10.1074\/jbc.RA117.000357_bib93","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/S1097-2765(00)80142-2","article-title":"SH3GL3 associates with the Huntingtin exon 1 protein and promotes the formation of polygln-containing protein aggregates","volume":"2","author":"Sittler","year":"1998","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.RA117.000357_bib94","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1038\/msb.2011.82","article-title":"The quantitative proteome of a human cell line","volume":"7","author":"Beck","year":"2011","journal-title":"Mol. Syst. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib95","doi-asserted-by":"crossref","first-page":"RE8","DOI":"10.1126\/stke.2003.179.re8","article-title":"The structure and function of proline recognition domains","volume":"2003","author":"Zarrinpar","year":"2003","journal-title":"Sci. STKE"},{"key":"10.1074\/jbc.RA117.000357_bib96","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.sbi.2016.11.002","article-title":"Engineering cell signaling modulators from native protein-protein interactions","volume":"45","author":"Zhang","year":"2017","journal-title":"Curr. Opin. Struct. Biol"},{"key":"10.1074\/jbc.RA117.000357_bib97","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0003-2697(85)90442-7","article-title":"Measurement of protein using bicinchoninic acid","volume":"150","author":"Smith","year":"1985","journal-title":"Anal. Biochem"},{"key":"10.1074\/jbc.RA117.000357_bib98","doi-asserted-by":"crossref","first-page":"6862","DOI":"10.1021\/jp212637r","article-title":"Improved atomistic Monte Carlo simulations demonstrate that poly-l-proline adopts heterogeneous ensembles of conformations of semi-rigid segments interrupted by kinks","volume":"116","author":"Radhakrishnan","year":"2012","journal-title":"J. Phys. Chem. B"},{"key":"10.1074\/jbc.RA117.000357_bib99","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1002\/jcc.21005","article-title":"ABSINTH: a new continuum solvation model for simulations of polypeptides in aqueous solutions","volume":"30","author":"Vitalis","year":"2009","journal-title":"J. Comput. Chem"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820404120?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820404120?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.RA117.000357","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,8,12]],"date-time":"2022-08-12T20:35:22Z","timestamp":1660336522000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820404120"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,3]]},"references-count":99,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2018,3]]}},"alternative-id":["S0021925820404120"],"URL":"https:\/\/doi.org\/10.1074\/jbc.ra117.000357","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2018,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.RA117.000357","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 by The American Society for Biochemistry and Molecular Biology, Inc.","name":"copyright","label":"Copyright"}]}}