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<OAI-PMH schemaLocation=http://www.openarchives.org/OAI/2.0/ http://www.openarchives.org/OAI/2.0/OAI-PMH.xsd> <responseDate>2018-01-15T18:25:17Z</responseDate> <request identifier=oai:HAL:hal-01263103v1 verb=GetRecord metadataPrefix=oai_dc>http://api.archives-ouvertes.fr/oai/hal/</request> <GetRecord> <record> <header> <identifier>oai:HAL:hal-01263103v1</identifier> <datestamp>2017-12-21</datestamp> <setSpec>type:ART</setSpec> <setSpec>subject:sdv</setSpec> <setSpec>collection:UNIV-RENNES1</setSpec> <setSpec>collection:UNIV-AG</setSpec> <setSpec>collection:IRSET-TREC</setSpec> <setSpec>collection:IRSET</setSpec> <setSpec>collection:IFR140</setSpec> <setSpec>collection:BIOSIT</setSpec> <setSpec>collection:INSERM</setSpec> <setSpec>collection:UR1-UFR-SVE</setSpec> <setSpec>collection:STATS-UR1</setSpec> <setSpec>collection:UR1-HAL</setSpec> <setSpec>collection:EHESP</setSpec> <setSpec>collection:USPC</setSpec> <setSpec>collection:UR1-SDV</setSpec> <setSpec>collection:IRSET-6</setSpec> <setSpec>collection:UNIV-ANGERS</setSpec> </header> <metadata><dc> <publisher>HAL CCSD</publisher> <title lang=en>Modeling generic aspects of ideal fibril formation</title> <creator>Michel, Denis</creator> <contributor>Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )</contributor> <description>International audience</description> <source>Journal of Chemical Physics</source> <identifier>hal-01263103</identifier> <identifier>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01263103</identifier> <source>https://hal-univ-rennes1.archives-ouvertes.fr/hal-01263103</source> <source>Journal of Chemical Physics, 2016, 144 (3), pp.035101. 〈10.1063/1.4940149〉</source> <identifier>DOI : 10.1063/1.4940149</identifier> <relation>info:eu-repo/semantics/altIdentifier/doi/10.1063/1.4940149</relation> <identifier>PUBMED : 26801045</identifier> <relation>info:eu-repo/semantics/altIdentifier/pmid/26801045</relation> <language>en</language> <subject>[SDV] Life Sciences [q-bio]</subject> <type>info:eu-repo/semantics/article</type> <type>Journal articles</type> <description lang=en>Many different proteins self-aggregate into insoluble fibrils growing apically by reversible addition of elementary building blocks. But beyond this common principle, the modalities of fibril formation are very disparate, with various intermediate forms which can be reshuffled by minor modifications of physico-chemical conditions or amino-acid sequences. To bypass this complexity, the multifaceted phenomenon of fibril formation is reduced here to its most elementary principles defined for a linear prototype of fibril. Selected generic features, including nucleation, elongation, and conformational recruitment, are modeled using minimalist hypotheses and tools, by separating equilibrium from kinetic aspects and in vitro from in vivo conditions. These reductionist approaches allow to bring out known and new rudiments, including the kinetic and equilibrium effects of nucleation, the dual influence of elongation on nucleation, the kinetic limitations on nucleation and fibril numbers, and the accumulation of complexes in vivo by rescue from degradation. Overlooked aspects of these processes are also pointed: the exponential distribution of fibril lengths can be recovered using various models because it is attributable to randomness only. It is also suggested that the same term "critical concentration" is used for different things, involved in either nucleation or elongation</description> <date>2016-01</date> </dc> </metadata> </record> </GetRecord> </OAI-PMH>