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@ARTICLE{RezaeiGhaleh:996736,
      author       = {Rezaei-Ghaleh, Nasrollah and Amininasab, Mehriar and
                      Giller, Karin and Becker, Stefan},
      title        = {{F}amilial {A}lzheimer’s {D}isease-{R}elated {M}utations
                      {D}ifferentially {A}lter {S}tability of {A}myloid-{B}eta
                      {A}ggregates},
      journal      = {The journal of physical chemistry letters},
      volume       = {14},
      issn         = {1948-7185},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2023-01152},
      pages        = {1427 - 1435},
      year         = {2023},
      abstract     = {Amyloid-beta (Aβ) deposition as senile plaques is a
                      pathological hallmark of Alzheimer's disease (AD). AD is
                      characterized by a large level of heterogeneity in amyloid
                      pathology, whose molecular origin is poorly understood.
                      Here, we employ NMR spectroscopy and MD simulation at
                      ambient and high pressures and investigate how AD-related
                      mutations in Aβ peptide influence the stability of Aβ
                      aggregates. The pressure-induced monomer dissociation from
                      Aβ aggregates monitored by NMR demonstrated that the Iowa
                      (D23N), Arctic (E22G), and Osaka (ΔE22) mutations altered
                      the pressure stability of Aβ40 aggregates in distinct
                      manners. While the NMR data of monomeric Aβ40 showed only
                      small localized effects of mutations, the MD simulation of
                      mutated Aβ fibrils revealed their distinct susceptibility
                      to elevated pressure. Our data propose a structural basis
                      for the distinct stability of various Aβ fibrils and
                      highlights "stability" as a molecular property potentially
                      contributing to the large heterogeneity of amyloid pathology
                      in AD.},
      cin          = {IBI-7},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36734539},
      UT           = {WOS:000928873500001},
      doi          = {10.1021/acs.jpclett.2c03729},
      url          = {https://juser.fz-juelich.de/record/996736},
}