LEADER 05226nam 2200589 450 001 9910813330403321 005 20230803221257.0 010 $a1-118-84536-6 010 $a1-118-85503-5 035 $a(CKB)2550000001273730 035 $a(EBL)1666525 035 $a(OCoLC)867001331 035 $a(MiAaPQ)EBC1666525 035 $a(Au-PeEL)EBL1666525 035 $a(CaPaEBR)ebr10861013 035 $a(CaONFJC)MIL595761 035 $a(EXLCZ)992550000001273730 100 $a20140504h20142014 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $2rdacontent 182 $2rdamedia 183 $2rdacarrier 200 00$aProtein aggregation in bacteria $efunctional and structural properties of inclusion bodies in bacterial cells /$fedited by Silvia Maria Doglia, Marina Lotti 210 1$aHoboken, New Jersey :$cWiley,$d2014. 210 4$d©2014 215 $a1 online resource (300 p.) 225 1 $aWiley Series in Protein and Peptide Science 300 $aDescription based upon print version of record. 311 $a1-118-44852-9 311 $a1-306-64510-7 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $aProtein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells; Copyright; Contents; Contributors; Preface ; Introduction to the WileySeries in Protein and PeptideScience; 1 Fundamentals of Protein Folding ; 1.1 Folding-misfolding-nonfolding crossroads; 1.2 Protein folding; 1.2.1 Protein-Folding Code; 1.2.2 Protein-Folding Models; 1.2.3 Polymer Aspects of Protein Folding; 1.2.4 Different Conformations Seen in Protein Folding; 1.3 Nonfolding; 1.3.1 Intrinsically Disordered Proteins and Their Abundance; 1.3.2 Some Functional Advantages of IDPs 327 $a1.3.3 Function-Induced Folding of IDPs1.3.4 IDPs and Human Diseases; 1.3.5 How Does an Amino Acid Sequence Encode Intrinsic Disorder?; 1.3.6 Polymer Aspects of Nonfolding; 1.4 Misfolding; 1.4.1 Molecular Mechanisms of Protein Misfolding; 1.4.2 Fibrillogenesis of Globular Proteins: Requirement for Partial Unfolding; 1.4.3 Fibrillogenesis of IDPs: Requirement for Partial Folding; 1.4.4 Conformational Prerequisites for Amyloidogenesis; 1.4.5 Multiple Pathways of Protein Misfolding; 1.4.6 Polymer Aspects of Protein Misfolding; References 327 $a2 Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins 2.1 Introduction; 2.2 Chemical Chaperones; 2.3 PPIs and PDIs are folding enzymes; 2.4 Molecular Chaperones; 2.5 The small Hsps; 2.6 Hsp90 ; 2.7 Hsp70/Hsp40; 2.8 GroEL Chaperonins; 2.9 Conclusions; References; 3 Osmolytes as Chemical Chaperones to Use in Protein Biotechnology ; 3.1 Introduction; 3.2 Protein-destabilizing conditions and counteracting mechanisms: shared or independent routes?; 3.3 Proposed molecular mechanisms for osmolyte activities; 3.4 Osmolytes and expression of recombinant proteins 327 $a3.5 Biotechnological relevance of osmolytes for preserving purified proteins3.6 Conclusions; References; 4 Inclusion Bodies in the Study of Amyloid Aggregation ; 4.1 Introduction; 4.2 Structure of IBs ; 4.2.1 Amyloid-like Nature of IBs ; 4.2.2 Detection and Characterization of Amyloid Conformations Inside IBs ; 4.3 Formation of IBs ; 4.3.1 In Vivo Formation Kinetics; 4.3.2 Molecular Determinants of IB Aggregation; 4.3.3 Sequence Specificity in IB Formation; 4.4 IBs as the simplest model for in vivo amyloid toxicity; 4.4.1 The Fitness Cost of Amyloid Aggregation 327 $a4.4.2 Citotoxicity of Amyloid IBs 4.4.3 Infectious Properties of IBs ; 4.5 Using IBs to screen for amyloid inhibitors; 4.6 Conclusions; References; 5 Protein Aggregation in Unicellular Eukaryotes ; 5.1 Introduction; 5.2 UPR: Unfolded protein response in the ER; 5.3 Removing persistent misfolded proteins with the proteasome; 5.4 Lysosomal/vacuolar proteolysis (overload UPS); 5.4.1 Autophagy; 5.4.2 Selective Types of Autophagy; 5.5 Refolding of protein aggregates in cytosol and nucleus; 5.6 JUNQ and IPOD; 5.7 Segregation of aggregates in yeast 327 $a5.8 Proteins forming nonpathological amyloid-like fibrils in unicellular eukaryotes 330 $aThis book focuses on the aggregation of recombinant proteins in bacterial cells in the form of inclusion bodies. Recent reports revolutionized the current view of inclusion bodies from that of inert deposits of inactive proteins to reservoirs of proteins that can eventually maintain biological activity and/or be rescued by cells. Aggregation is put in the context of updated knowledge about the folding and aggregation of proteins in simple cells and new perspectives derived from the application of this knowledge are presented. The following topics are addressed: a) molecular and c 410 0$aWiley series in protein and peptide science. 606 $aBacterial proteins 615 0$aBacterial proteins. 676 $a572/.69 702 $aDoglia$b Silvia Maria 702 $aLotti$b Marina 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910813330403321 996 $aProtein aggregation in bacteria$93938897 997 $aUNINA LEADER 02614nam 2200541Ia 450 001 9911031646903321 005 20240426104009.0 010 $a2-7606-5473-7 010 $a2-7606-4649-1 024 7 $a10.1515/9782760646490 035 $a(CKB)5580000000342521 035 $a(PPN)26513594X 035 $a(DE-B1597)671148 035 $a(DE-B1597)9782760646490 035 $a(MiAaPQ)EBC30826810 035 $a(Au-PeEL)EBL30826810 035 $a(FR-PaCSA)88933672 035 $a(FRCYB88933672)88933672 035 $a(OCoLC)1443935059 035 $a(Perlego)3553747 035 $a(EXLCZ)995580000000342521 100 $a20240426h20222022 fg 101 0 $afre 135 $aur||||||||||| 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aDe l'assemblage au montage cinématographique /$fLaurent Le Forestier, André Gaudreault 205 $a1st ed. 210 1$aMontréal : $cLes Presses de l'Université de Montréal, $d[2022] 210 4$d©2022 215 $a1 online resource (376 p.) 311 08$a2-7606-4648-3 327 $tFront Matter -- $tAvant-propos -- $tPréface -- $tAssemblage contre montage -- $tRaccommoder et rapiécer -- $tAbouter et coupler -- $tTruquer et raccorder -- $tAccumuler et élaguer -- $tAlterner et inter(s)caler -- $tOrdonner et (encore) raccorder -- $tMontage contre assemblage -- $tBibliographie des ouvrages cités -- $tIndex des films -- $tIndex général -- $tGlossaire -- $tRemerciements -- $tTable des matières 330 $aMobilisant une approche resolument technique, attentive tant aux outils et aux gestes qu'aux discours qui les accompagnent, ce livre veut montrer comment une serie d'ope?rations d'assemblage, disseminees tant dans la chronologie que dans l'espace du processus de postproduction des films dits muets, et acque?rant au fil des ans des valeurs et des statuts diffe?rents, finit par constituer une phase autonome de ce processus, qui se cristallise, avant sa conceptualisation, dans la notion de montage. 606 $aMotion pictures$xEditing 606 $aMotion pictures$xEditing$xHistory 615 0$aMotion pictures$xEditing. 615 0$aMotion pictures$xEditing$xHistory. 676 $a777/.55 700 $aGaudreault$b André, $4aut$4http://id.loc.gov/vocabulary/relators/aut$0530484 702 $aLe Forestier$b Laurent, $4aut$4http://id.loc.gov/vocabulary/relators/aut 801 0$bDE-B1597 801 1$bDE-B1597 906 $aBOOK 912 $a9911031646903321 996 $aDe l'assemblage au montage cinématographique$94445087 997 $aUNINA