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Volumn 38, Issue 7, 2012, Pages 525-533

Temporary secondary structures in tau, an intrinsically disordered protein

Author keywords

intrinsically disordered proteins; molecular dynamics; secondary structures; tau protein

Indexed keywords

ALZHEIMER DISEASE; DISORDERED PROTEINS; EXPERIMENTAL DATA; LOCAL TRANSITIONS; MICROTUBULES; MOLECULAR DYNAMICS SIMULATIONS; N-TERMINALS; NATIVE STATE; PAIRED HELICAL FILAMENTS; PHYSIOLOGICAL STATE; RANDOM COIL; SECONDARY STRUCTURES; SMALL ANGLE X-RAY SCATTERING; STABLE STRUCTURES; TAU PROTEINS;

EID: 84862072035     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927022.2011.633347     Document Type: Article
Times cited : (27)

References (31)
  • 1
    • 84856303283 scopus 로고    scopus 로고
    • Intrinsically disordered proteins
    • J. Sussman, and I. Silman, eds., World Scientific, Singapore
    • P. Tompa, Intrinsically disordered proteins, in Structural Proteomics and its Impact on the Life Sciences, J. Sussman, and I. Silman, eds., World Scientific, Singapore, 2008, pp. 153-158.
    • (2008) Structural Proteomics and its Impact on the Life Sciences , pp. 153-158
    • Tompa, P.1
  • 4
    • 0028170411 scopus 로고
    • Structural studies of tau protein and alzheimer paired helical filaments show no evidence for p-structure
    • O. Schweers, E. Schoenbrunn-Hanebeck, A. Marx, and E. Mandelkow, Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for p-structure, J. Biol. Chem. 269 (1994), pp. 24290-24297.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24290-24297
    • Schweers, O.1    Schoenbrunn-Hanebeck, E.2    Marx, A.3    Mandelkow, E.4
  • 5
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • J. Avila, J.J. Lucas, M. Pérez, and F. Hernández, Role of tau protein in both physiological and pathological conditions, Physiol. Rev. 84 (2004), pp. 361-384.
    • (2004) Physiol. Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Pérez, M.3    Hernández, F.4
  • 8
    • 0034625060 scopus 로고    scopus 로고
    • Assembly of tau protein into alzheimer paired helical filaments depends on a local sequence motif ((306)vqivyk(311)) forming beta structure
    • M. von Bergen, P. Friedhoff, J. Biernat, J. Heberle, E.-M. Mandelkow, and E. Mandelkow, 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 97 (2000), pp. 5129-5134.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5129-5134
    • Von Bergen, M.1    Friedhoff, P.2    Biernat, J.3    Heberle, J.4    Mandelkow, E.-M.5    Mandelkow, E.6
  • 11
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • P. Tompa, Intrinsically unstructured proteins, Trends Biochem. Sci. 27 (2002), pp. 527-533.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 13
    • 52949123661 scopus 로고    scopus 로고
    • Domain conformation of tau protein studied by solution small-angle x-ray scattering
    • E. Mylonas, A. Hascher, P. Bernad, M. Blackledge, E. Mandelkow, and D.I. Svergun, Domain conformation of tau protein studied by solution small-angle X-ray scattering, Biochemistry 47 (2008), pp. 10345-10353.
    • (2008) Biochemistry , vol.47 , pp. 10345-10353
    • Mylonas, E.1    Hascher, A.2    Bernad, P.3    Blackledge, M.4    Mandelkow, E.5    Svergun, D.I.6
  • 16
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • P. Tompa, The interplay between structure and function in intrinsically unstructured proteins, FEBS Lett. 579 (2005), pp. 3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 18
    • 84856279313 scopus 로고    scopus 로고
    • Molecular dynamics simulation of intrinsically disordered proteins
    • (to appear), DOI: 10.1080/08927022.2011.608671
    • A. Battisti and A. Tenenbaum, Molecular dynamics simulation of intrinsically disordered proteins, Mol. Simulat. (to appear), DOI: 10.1080/08927022.2011.608671.
    • Mol. Simulat
    • Battisti, A.1    Tenenbaum, A.2
  • 20
    • 0037465354 scopus 로고    scopus 로고
    • Tau polymerization: Role of the amino terminus
    • T.C. Gamblin, R.W. Berry, and L.I. Binder, Tau polymerization: Role of the amino terminus, Biochemistry 42 (2003), pp. 2252-2257.
    • (2003) Biochemistry , vol.42 , pp. 2252-2257
    • Gamblin, T.C.1    Berry, R.W.2    Binder, L.I.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage t4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of Bacteriophage T4, Nature 227 (1970), pp. 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0029185933 scopus 로고
    • Crysol a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • D.I. Svergun, C. Barberato, and M.H.J. Koch, CRYSOL a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates, J. Appl. Crystallogr. 28 (1995), pp. 768-773.
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.J.3
  • 24
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle x-ray scattering
    • P. Bernadó, E. Mylonas, M.V. Petoukhov, M. Blackledge, and D.I. Svergun, Structural characterization of flexible proteins using small-angle X-ray scattering, J. Am. Chem. Soc. 129 (2007), pp. 5656-5664.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5656-5664
    • Bernadó, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 25
    • 79952727620 scopus 로고    scopus 로고
    • Towards the structural characterization of intrinsically disordered proteins by saxs and md simulation
    • T. Oroguchi, M. Ikoguchi, and M. Sato, Towards the structural characterization of intrinsically disordered proteins by SAXS and MD simulation, J. Phys. Conf. Ser. 272 (2011), p. 012005.
    • (2011) J. Phys. Conf. Ser. , vol.272 , pp. 012005
    • Oroguchi, T.1    Ikoguchi, M.2    Sato, M.3
  • 26
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch and C. Sander, Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers 22 (1983), pp. 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 28
    • 28044458515 scopus 로고    scopus 로고
    • A structural model for unfolded proteins from residual dipolar couplings and small-angle x-ray scattering
    • P. Bernadó , L. Blanchard, P. Timmins, D. Marion, R.W.H. Ruigrok, and M. Blackledge, A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering, Proc. Natl. Acad. Sci. USA 102 (2005), pp. 17002-17007.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 17002-17007
    • Bernadó, P.1    Blanchard, L.2    Timmins, P.3    Marion, D.4    Ruigrok, R.W.H.5    Blackledge, M.6
  • 29
    • 0000577041 scopus 로고
    • Large-amplitude nonlinear motions in proteins
    • A.E. Garcia, Large-amplitude nonlinear motions in proteins, Phys. Rev. Lett. 68 (1992), pp. 2696-2699.
    • (1992) Phys. Rev. Lett. , vol.68 , pp. 2696-2699
    • Garcia, A.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.