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@ARTICLE{Trner:909069,
      author       = {Törner, Ricarda and Kupreichyk, Tatsiana and Gremer,
                      Lothar and Debled, Elisa Colas and Fenel, Daphna and
                      Schemmert, Sarah and Gans, Pierre and Willbold, Dieter and
                      Schoehn, Guy and Hoyer, Wolfgang and Boisbouvier, Jerome},
      title        = {{S}tructural basis for the inhibition of {IAPP} fibril
                      formation by the co-chaperonin prefoldin.},
      journal      = {Nature Communications},
      volume       = {13},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2022-02987},
      pages        = {2363},
      year         = {2022},
      abstract     = {Chaperones, as modulators of protein conformational states,
                      are key cellular actors to prevent the accumulation of
                      fibrillar aggregates. Here, we integrated kinetic
                      investigations with structural studies to elucidate how the
                      ubiquitous co-chaperonin prefoldin inhibits diabetes
                      associated islet amyloid polypeptide (IAPP) fibril
                      formation. We demonstrated that both human and archaeal
                      prefoldin interfere similarly with the IAPP fibril
                      elongation and secondary nucleation pathways. Using archaeal
                      prefoldin model, we combined nuclear magnetic resonance
                      spectroscopy with electron microscopy to establish that the
                      inhibition of fibril formation is mediated by the binding of
                      prefoldin's coiled-coil helices to the flexible IAPP
                      N-terminal segment accessible on the fibril surface and
                      fibril ends. Atomic force microscopy demonstrates that
                      binding of prefoldin to IAPP leads to the formation of lower
                      amounts of aggregates, composed of shorter fibrils,
                      clustered together. Linking structural models with observed
                      fibrillation inhibition processes opens perspectives for
                      understanding the interference between natural chaperones
                      and formation of disease-associated amyloids.},
      keywords     = {Amyloid: metabolism / Chaperonins / Humans / Islet Amyloid
                      Polypeptide / Molecular Chaperones: metabolism / Amyloid
                      (NLM Chemicals) / Islet Amyloid Polypeptide (NLM Chemicals)
                      / Molecular Chaperones (NLM Chemicals) / prefoldin (NLM
                      Chemicals) / Chaperonins (NLM Chemicals)},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524) / BETACONTROL - Control of amyloid formation via
                      beta-hairpin molecular recognition features (726368)},
      pid          = {G:(DE-HGF)POF4-5244 / G:(EU-Grant)726368},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35501361},
      pmc          = {pmc:PMC9061850},
      UT           = {WOS:000789924700014},
      doi          = {10.1038/s41467-022-30042-y},
      url          = {https://juser.fz-juelich.de/record/909069},
}