메뉴 건너뛰기




Volumn 586, Issue 21, 2012, Pages 3914-3919

Altered tubulin assembly dynamics with N-homocysteinylated human 4R/1N tau in vitro

Author keywords

Homocysteine thiolactone; Microtubule protein; N Homocysteinylation; Tau protein (4R 1N)

Indexed keywords

HOMOCYSTEINE; LYSINE; MICROTUBULE PROTEIN; TAU PROTEIN; TUBULIN;

EID: 84868099610     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.09.024     Document Type: Article
Times cited : (21)

References (33)
  • 1
    • 0031597388 scopus 로고    scopus 로고
    • Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease
    • R. Clarke, A.D. Smith, K.A. Jobst, H. Refsum, L. Sutton, and P.M. Ueland Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease Arch. Neurol. 55 1998 1449 1455
    • (1998) Arch. Neurol. , vol.55 , pp. 1449-1455
    • Clarke, R.1    Smith, A.D.2    Jobst, K.A.3    Refsum, H.4    Sutton, L.5    Ueland, P.M.6
  • 3
    • 1542373560 scopus 로고    scopus 로고
    • Molecular basis of homocysteine toxicity in humans
    • H. Jakubowski Molecular basis of homocysteine toxicity in humans Cell. Mol. Life Sci. 61 2004 470 487
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 470-487
    • Jakubowski, H.1
  • 4
    • 0027534543 scopus 로고
    • Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells
    • H. Jakubowski, and E. Goldman Synthesis of homocysteine thiolactone by methionyl-tRNA synthetase in cultured mammalian cells FEBS Lett. 317 1993 237 240
    • (1993) FEBS Lett. , vol.317 , pp. 237-240
    • Jakubowski, H.1    Goldman, E.2
  • 5
    • 0032778517 scopus 로고    scopus 로고
    • Protein homocysteinylation: Possible mechanism underlying pathological consequences of elevated homocysteine levels
    • H. Jakubowski Protein homocysteinylation: possible mechanism underlying pathological consequences of elevated homocysteine levels FASEB J. 13 1999 2277 2283
    • (1999) FASEB J. , vol.13 , pp. 2277-2283
    • Jakubowski, H.1
  • 7
    • 0023674299 scopus 로고
    • Microtubule-associated proteins: Their potential role in determining neuronal morphology
    • A. Matus Microtubule-associated proteins: their potential role in determining neuronal morphology Annu. Rev. Neurosci. 11 1988 29 44
    • (1988) Annu. Rev. Neurosci. , vol.11 , pp. 29-44
    • Matus, A.1
  • 9
    • 0024745894 scopus 로고
    • Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease
    • M. Goedert, M.G. Spillantini, R. Jakes, D. Rutherford, and R.A. Crowther Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease Neuron 3 1989 519 526
    • (1989) Neuron , vol.3 , pp. 519-526
    • Goedert, M.1    Spillantini, M.G.2    Jakes, R.3    Rutherford, D.4    Crowther, R.A.5
  • 10
    • 0028175215 scopus 로고
    • Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau
    • B.L. Goode, and S.C. Feinstein Identification of a novel microtubule binding and assembly domain in the developmentally regulated inter-repeat region of tau J. Cell Biol. 124 1994 769 782
    • (1994) J. Cell Biol. , vol.124 , pp. 769-782
    • Goode, B.L.1    Feinstein, S.C.2
  • 11
    • 0029098802 scopus 로고
    • Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau
    • D. Panda, B.L. Goode, S.C. Feinstein, and L. Wilson Kinetic stabilization of microtubule dynamics at steady state by tau and microtubule-binding domains of tau Biochemistry 34 1995 11117 11127
    • (1995) Biochemistry , vol.34 , pp. 11117-11127
    • Panda, D.1    Goode, B.L.2    Feinstein, S.C.3    Wilson, L.4
  • 12
    • 0042924434 scopus 로고    scopus 로고
    • Differential regulation of microtubule dynamics by three- and four-repeat tau: Implications for the onset of neurodegenerative disease
    • D. Panda, J.C. Samuel, M. Massie, S.C. Feinstein, and L. Wilson Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease Proc. Natl. Acad. Sci. U.S.A. 100 2003 9548 9553
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9548-9553
    • Panda, D.1    Samuel, J.C.2    Massie, M.3    Feinstein, S.C.4    Wilson, L.5
  • 14
    • 0036323020 scopus 로고    scopus 로고
    • The role of tau in Alzheimer's disease
    • J.Q. Trojanowski, and V.M. Lee The role of tau in Alzheimer's disease Med. Clin. North Am. 86 2002 615 627
    • (2002) Med. Clin. North Am. , vol.86 , pp. 615-627
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 15
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • J. Avila, J.J. Lucas, M. Perez, and F. Hernandez Role of tau protein in both physiological and pathological conditions Physiol. Rev. 84 2004 361 384
    • (2004) Physiol. Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3    Hernandez, F.4
  • 18
    • 0037070224 scopus 로고    scopus 로고
    • Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease
    • F. Liu, T. Zaidi, K. Iqbal, I. Grundke-Iqbal, R.K. Merkle, and C.X. Gong Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease FEBS Lett. 512 2002 101 106
    • (2002) FEBS Lett. , vol.512 , pp. 101-106
    • Liu, F.1    Zaidi, T.2    Iqbal, K.3    Grundke-Iqbal, I.4    Merkle, R.K.5    Gong, C.X.6
  • 19
    • 0023140474 scopus 로고
    • Ubiquitin is a component of paired helical filaments in Alzheimer's disease
    • H. Mori, J. Kondo, and Y. Ihara Ubiquitin is a component of paired helical filaments in Alzheimer's disease Science 235 1987 1641 1644
    • (1987) Science , vol.235 , pp. 1641-1644
    • Mori, H.1    Kondo, J.2    Ihara, Y.3
  • 20
    • 0029114196 scopus 로고
    • Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments
    • O. Schweers, E.M. Mandelkow, J. Biernat, and E. Mandelkow Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments Proc. Natl. Acad. Sci. U.S.A. 92 1995 8463 8467
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8463-8467
    • Schweers, O.1    Mandelkow, E.M.2    Biernat, J.3    Mandelkow, E.4
  • 21
    • 0020959274 scopus 로고
    • Nonenzymatic glucosylation and glucose-dependent cross-linking of protein
    • A.S. Eble, S.R. Thorpe, and J.W. Baynes Nonenzymatic glucosylation and glucose-dependent cross-linking of protein J. Biol. Chem. 258 1983 9406 9412
    • (1983) J. Biol. Chem. , vol.258 , pp. 9406-9412
    • Eble, A.S.1    Thorpe, S.R.2    Baynes, J.W.3
  • 22
    • 79960983524 scopus 로고    scopus 로고
    • Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties
    • Y. Furukawa, K. Kaneko, and N. Nukina Tau protein assembles into isoform- and disulfide-dependent polymorphic fibrils with distinct structural properties J. Biol. Chem. 286 2011 27236 27246
    • (2011) J. Biol. Chem. , vol.286 , pp. 27236-27246
    • Furukawa, Y.1    Kaneko, K.2    Nukina, N.3
  • 23
    • 2442641844 scopus 로고    scopus 로고
    • Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation
    • R. Glowacki, and H. Jakubowski Cross-talk between Cys34 and lysine residues in human serum albumin revealed by N-homocysteinylation J. Biol. Chem. 279 2004 10864 10871
    • (2004) J. Biol. Chem. , vol.279 , pp. 10864-10871
    • Glowacki, R.1    Jakubowski, H.2
  • 24
    • 0014428865 scopus 로고
    • Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
    • J. Sedlak, and R.H. Lindsay Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent Anal. Biochem. 25 1968 192 205
    • (1968) Anal. Biochem. , vol.25 , pp. 192-205
    • Sedlak, J.1    Lindsay, R.H.2
  • 25
    • 0033594925 scopus 로고    scopus 로고
    • Phosphate release during microtubule assembly: What stabilizes growing microtubules?
    • A. Vandecandelaere, M. Brune, M.R. Webb, S.R. Martin, and P.M. Bayley Phosphate release during microtubule assembly: what stabilizes growing microtubules? Biochemistry 38 1999 8179 8188
    • (1999) Biochemistry , vol.38 , pp. 8179-8188
    • Vandecandelaere, A.1    Brune, M.2    Webb, M.R.3    Martin, S.R.4    Bayley, P.M.5
  • 26
    • 0028118917 scopus 로고
    • Microtubule organization and dynamics dependent on microtubule-associated proteins
    • N. Hirokawa Microtubule organization and dynamics dependent on microtubule-associated proteins Curr. Opin. Cell Biol. 6 1994 74 81
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 74-81
    • Hirokawa, N.1
  • 27
    • 0032484089 scopus 로고    scopus 로고
    • Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17
    • M. Hong Mutation-specific functional impairments in distinct tau isoforms of hereditary FTDP-17 Science 282 1998 1914 1917
    • (1998) Science , vol.282 , pp. 1914-1917
    • Hong, M.1
  • 28
    • 0027406644 scopus 로고
    • Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro
    • R. Brandt, and G. Lee Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation in vitro J. Biol. Chem. 268 1993 3414 3419
    • (1993) J. Biol. Chem. , vol.268 , pp. 3414-3419
    • Brandt, R.1    Lee, G.2
  • 29
    • 0025219653 scopus 로고
    • Microtubule oscillations. Role of nucleation and microtubule number concentration
    • H. Obermann, E.M. Mandelkow, G. Lange, and E. Mandelkow Microtubule oscillations. Role of nucleation and microtubule number concentration J. Biol. Chem. 265 1990 4382 4388
    • (1990) J. Biol. Chem. , vol.265 , pp. 4382-4388
    • Obermann, H.1    Mandelkow, E.M.2    Lange, G.3    Mandelkow, E.4
  • 30
  • 31
    • 0017758306 scopus 로고
    • Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly
    • D.W. Cleveland, S.Y. Hwo, and M.W. Kirschner Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly J. Mol. Biol. 116 1977 227 247
    • (1977) J. Mol. Biol. , vol.116 , pp. 227-247
    • Cleveland, D.W.1    Hwo, S.Y.2    Kirschner, M.W.3
  • 32
    • 0017718447 scopus 로고
    • Role of tubulin-associated proteins in microtubule nucleation and elongation
    • D.B. Murphy, K.A. Johnson, and G.G. Borisy Role of tubulin-associated proteins in microtubule nucleation and elongation J. Mol. Biol. 117 1977 33 52
    • (1977) J. Mol. Biol. , vol.117 , pp. 33-52
    • Murphy, D.B.1    Johnson, K.A.2    Borisy, G.G.3
  • 33
    • 0020010265 scopus 로고
    • Physical properties of purified calf brain tubulin
    • G.C. Na, and S.N. Timasheff Physical properties of purified calf brain tubulin Methods Enzymol. 85 Pt B 1982 393 408
    • (1982) Methods Enzymol. , vol.85 , Issue.PART B , pp. 393-408
    • Na, G.C.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.