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@ARTICLE{Dharan:472135,
      author       = {Dharan, Raviv and Shemesh, Asaf and Millgram, Abigail and
                      Zalk, Ran and Frank, Gabriel A. and Levi-Kalisman, Yael and
                      Ringel, Israel and Raviv, Uri},
      title        = {{H}ierarchical {A}ssembly {P}athways of
                      {S}permine-{I}nduced {T}ubulin {C}onical-{S}piral
                      {A}rchitectures},
      journal      = {ACS nano},
      volume       = {15},
      number       = {5},
      issn         = {1936-0851},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PUBDB-2021-04858},
      pages        = {8836 - 8847},
      year         = {2021},
      abstract     = {Tubulin, an essential cytoskeletal protein, assembles into
                      various morphologies by interacting with an array of
                      cellular factors. One of these factors is the endogenous
                      polyamine spermine, which may promote and stabilize tubulin
                      assemblies. Nevertheless, the assembled structures and their
                      formation pathways are poorly known. Here we show that
                      spermine induced the in vitro assembly of tubulin into
                      several hierarchical architectures based on a tubulin
                      conical-spiral subunit. Using solution X-ray scattering and
                      cryo-TEM, we found that with progressive increase of
                      spermine concentration tubulin dimers assembled into
                      conical-frustum-spirals of increasing length, containing up
                      to three helical turns. The subunits with three helical
                      turns were then assembled into tubules through base-to-top
                      packing and formed antiparallel bundles of tubulin
                      conical-spiral tubules in a distorted hexagonal symmetry.
                      Further increase of the spermine concentration led to
                      inverted tubulin tubules assembled in hexagonal bundles.
                      Time-resolved experiments revealed that tubulin assemblies
                      formed at higher spermine concentrations assembled from
                      intermediates, similar to those formed at low spermine
                      concentrations. These results are distinct from the
                      classical transition between twisted ribbons, helical, and
                      tubular assemblies, and provide insight into the versatile
                      morphologies that tubulin can form. Furthermore, they may
                      contribute to our understanding of the interactions that
                      control the composition and construction of protein-based
                      biomaterials.},
      cin          = {EMBL-User},
      ddc          = {540},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33900736},
      UT           = {WOS:000656994100081},
      doi          = {10.1021/acsnano.1c01374},
      url          = {https://bib-pubdb1.desy.de/record/472135},
}