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Article

Transient tertiary structures in tau, an intrinsically disordered protein

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Pages 1084-1092 | Received 21 Jan 2013, Accepted 04 Apr 2013, Published online: 11 Jun 2013

REFERENCES

  • TompaP. Intrinsically disordered proteins. In: SussmanJ, SilmanI, editors. Structural proteomics and its impact on the life sciences. World Scientific, Singapore; 2008. p. 153–180.
  • DunkerAK, BrownCJ, LawsonJD, IakouchevaLM, ObradovicZ. Intrinsic disorder and protein function. Biochemistry. 2002;41:6573–6582.
  • MukraschMD, BibowS, KorukottuJ, JeganathanS, BiernatJ, GriesingerC, MandelkowE, ZweckstetterM. Structural polymorphism of 441-residue tau at single residue resolution. PLoS Biol. 2009;7:0399–0414.
  • SickmeierM, HamiltonJA, LeGallT, VacicV, CorteseMS, TantosA, SzaboB, TompaP, ChenJ, UverskyVN, ObradovicZ, DunkerAK. DisProt: the database of disordered proteins. Nucl Acids Res. 2007;35:D786–D793.
  • AvilaJ, LucasJJ, PérezM, HernándezF. Role of tau protein in both physiological and pathological conditions. Physiol Rev. 2004;84:361–384.
  • LiuL, DrouetV, WuJW, WitterMP, SmallSA, ClellandC, DuffK. Trans-synaptic spread of tau pathology in vivo. PLoS ONE. 2012;7 e31302 (9 pp).
  • CarmelG, MagerEM, BinderLI, KuretJ. The structural basis of monoclonal antibody Alz50s selectivity for Alzheimers disease pathology. J Biol Chem. 1996;271:32789–32795.
  • GamblinTC, BerryRW, BinderLI. Tau polymerization: role of the amino terminus. Biochemistry. 2003;42:2252–2257.
  • JeganathanS, von BergenM, BrutlachH, SteinhoffHJ, MandelkowE. Global hairpin folding of tau in solution. Biochemistry. 2006;45:2283–2293.
  • MylonasE, HascherA, BernadòP, BlackledgeM, MandelkowE, SvergunDI. Domain conformation of tau protein studied by solution small-angle X-ray scattering. Biochemistry. 2008;47:10345–10353.
  • BibowS, MukraschMD, ChinnathambiS, BiernatJ, GriesingerC, MandelkowE, ZweckstetterM. The dynamic structure of filamentous tau. Angew Chem Int Ed. 2011;50:11520–11524.
  • BattistiA, TenenbaumA. Molecular dynamics simulation of intrinsically disordered proteins. Mol Simul. 2012;38:139–143.
  • BattistiA, CiascaG, GrottesiA, BianconiA, TenenbaumA. Temporary secondary structures in tau, an intrinsically disordered protein. Mol Simul. 2012;38:525–533.
  • HumphreyW, DalkaA, SchultenK. Visual molecular dynamics. J Mol Graph. 1996;14:33–38.
  • StillWC, TempczykA, HawleyRC, HendricksonT. Semianalytical treatment of solvation for molecular mechanics and dynamics. J Am Chem Soc. 1990;112:6127–6129.
  • LaioA, GervasioFL. Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science. Rep Prog Phys. 2008;71: 126601 (22 pp).
  • CiascaG, CampiG, BattistiA, ReaG, RodioM, PapiM, PernotP, TenenbaumA, BianconiA. Continuous thermal collapse of the intrinsically disordered protein tau is driven by its entropic flexible domain. Langmuir. 2012;28:13405–13410.
  • LaemmliUK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227:680–685.
  • PernotP, TheveneauP, GiraudT, NogueiraRF, NurizzoD, SurrJ, McSweeneyS, RoundA, FelisazF, FoedingerL, GobboA, HuetJ, VillardC, CiprianiF. New beamline dedicated to solution scattering from biological macromolecules at the ESRF. J Phys Conf Ser. 2010;247:012009.
  • BernadòP, MylonasE, PetoukhovMV, BlackledgeM, SvergunDI. Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc. 2007;129:5656–5664.
  • EOM manual online: http://www.embl-hamburg.de/biosaxs/eom.html.
  • SvergunDI, BarberatoC, KochMHJ. CRYSOL – a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr. 1995;28:768–773.
  • OroguchiT, IkoguchiM, SatoM. Towards the structural characterization of intrinsically disordered proteins by SAXS and MD simulation. J Phys Conf Ser. 2011;272:012005.
  • KohnJE, MillettIS, JacobsJ, ZagrovicB, DillonTM, CingelN, DothagerRS, SeifertS, ThiyagarajanP, SosnickTS, HasanMZ, PandeVS, RuczinskiI, DoniachS, PlaxcoKW. Random-coil behavior and the dimensions of chemically unfolded proteins. Proc Natl Acad Sci USA. 2004;101:12491–12496.
  • MukraschMD, MarkwickP, BiernatJ, von BergenM, BernadòP, GriesingerC, MandelkowE, ZweckstetterM, BlackledgeM. Highly populated turn conformations in natively unfolded tau protein identified from residual dipolar couplings and molecular simulation. J Am Chem Soc. 2007;129:5235–5243.
  • MendietaJ, FuertesMA, KunjishapathamR, Santa-MaríaI, MorenoFJ, AlonsoC, GagoF, MuñozV, AvilaJ, HernándezF. Phosphorylation modulates the alpha-helical structure and polymerization of a peptide from the third tau microtubule-binding repeat. Biochim Biophys Acta. 2005;1721:16–26.
  • von BergenM, FriedhoffP, BiernatJ, HeberleJ, MandelkowE-M, MandelkowE. Assembly of tau protein into Alzheimer paired helical filaments depends on a local sequence motif ((306)VQIVYK(311)) forming beta structure. Proc Natl Acad Sci USA. 2000;97:5129–5134.
  • von BergenM, BarghornS, BiernatJ, MandelkowE-M, MandelkowE. Tau aggregation is driven by a transition from random coil to beta sheet structure. Biochim Biophys Acta. 2005;1739:158–166.

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