% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Sudarev:943312,
      author       = {Sudarev, Vsevolod V. and Dolotova, Sofya M. and
                      Bukhalovich, Siarhei M. and Bazhenov, Sergey V. and
                      Ryzhykau, Yury L. and Uversky, Vladimir N. and Bondarev,
                      Nikolay A. and Osipov, Stepan D. and Mikhailov, Anatolii E.
                      and Kuklina, Daria D. and Murugova, Tatiana N. and Manukhov,
                      Ilya V. and Rogachev, Andrey V. and Gordeliy, Valentin I.
                      and Gushchin, Ivan Yu. and Kuklin, Alexander I. and Vlasov,
                      Alexey V.},
      title        = {{F}erritin self-assembly, structure, function, and
                      biotechnological applications},
      journal      = {International journal of biological macromolecules},
      volume       = {224},
      issn         = {0141-8130},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2023-00918},
      pages        = {319 - 343},
      year         = {2023},
      abstract     = {Ferritin is a vital protein complex responsible for storing
                      iron in almost all living organisms. It plays a crucial role
                      in various metabolic pathways, inflammation processes,
                      stress response, and pathogenesis of cancer and
                      neurodegenerative diseases. In this review we discuss the
                      role of ferritin in diseases, cellular iron regulation, its
                      structural features, and its role in biotechnology. We also
                      show that molecular mechanisms of ferritin self-assembly are
                      key for a number of biotechnological and pharmaceutical
                      applications. The assembly pathways strongly depend on the
                      interface context of ferritin monomers and the stability of
                      its different intermediate oligomers. To date, several
                      schemes of self-assembly kinetics have been proposed. Here,
                      we compare different self-assembly mechanisms and discuss
                      the possibility of self-assembly control by switching
                      between deadlock intermediate states.},
      cin          = {IBI-7},
      ddc          = {570},
      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       = {36280176},
      UT           = {WOS:000907015900001},
      doi          = {10.1016/j.ijbiomac.2022.10.126},
      url          = {https://juser.fz-juelich.de/record/943312},
}