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@ARTICLE{Gremer:837796,
      author       = {Gremer, Lothar and Schölzel, Daniel and Schenk, Carla and
                      Reinartz, Elke and Labahn, Jörg and Ravelli, Raimond B. G.
                      and Tusche, Markus and Lopez-Iglesias, Carmen and Hoyer,
                      Wolfgang and Heise, Henrike and Willbold, Dieter and
                      Schröder, Gunnar},
      title        = {{F}ibril structure of amyloid-ß(1-42) by cryoelectron
                      microscopy},
      journal      = {Science},
      volume       = {358},
      issn         = {0036-8075},
      address      = {Washington, DC [u.a.]},
      publisher    = {American Association for the Advancement of Science},
      reportid     = {FZJ-2017-06585},
      pages        = {116-119},
      year         = {2017},
      note         = {Journal title: Science},
      abstract     = {Amyloids are implicated in neurodegenerative diseases.
                      Fibrillar aggregates of the amyloid-β protein (Aβ) are the
                      main component of the senile plaques found in brains of
                      Alzheimer’s disease patients. We present the structure of
                      an Aβ(1-42) fibril composed of two intertwined
                      protofilaments determined by cryoelectron microscopy
                      (cryo-EM) to 4.0 Å resolution, complemented by solid-state
                      nuclear magnetic resonance (NMR) experiments. The backbone
                      of all 42 residues and nearly all sidechains are well
                      resolved in the EM density map, including the entire N
                      terminus, which is part of the cross-β structure resulting
                      in an overall “LS”-shaped topology of individual
                      subunits. The dimer interface protects the hydrophobic C
                      termini from the solvent. The unique staggering of the
                      nonplanar subunits results in markedly different fibril
                      ends, termed “groove” and “ridge,” leading to
                      different binding pathways on both fibril ends, which has
                      implications for fibril growth.},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28882996},
      UT           = {WOS:000412359600065},
      doi          = {10.1126/science.aao2825},
      url          = {https://juser.fz-juelich.de/record/837796},
}