메뉴 건너뛰기




Volumn 280, Issue 19, 2013, Pages 4915-4927

α-Synuclein as an intrinsically disordered monomer - Fact or artefact?

Author keywords

synuclein; dimer; disordered monomer; Escherichia coli; purification

Indexed keywords

ALPHA SYNUCLEIN; MONOMER; OLIGOMER; RECOMBINANT PROTEIN; TETRAMER;

EID: 84884596392     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12471     Document Type: Article
Times cited : (61)

References (38)
  • 1
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba M, Nakajo S, Tu PH, Tomita T, Nakaya K, Lee VM, Trojanowsky JQ, &, Iwatsubo T, (1998) Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am J Pathol 152, 879-884.
    • (1998) Am J Pathol , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6    Trojanowsky, J.Q.7    Iwatsubo, T.8
  • 2
    • 0035409575 scopus 로고    scopus 로고
    • Alpha-synuclein and neurodegenerative diseases
    • Goedert M, (2001) Alpha-synuclein and neurodegenerative diseases. Nat Rev Neurosci 2, 492-501.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 492-501
    • Goedert, M.1
  • 4
    • 0032546895 scopus 로고    scopus 로고
    • Alpha-synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy
    • Wakabayashi K, Yoshimoto M, Tsuji S, &, Takahashi H, (1998) Alpha-synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy. Neuroscience 249, 180-182.
    • (1998) Neuroscience , vol.249 , pp. 180-182
    • Wakabayashi, K.1    Yoshimoto, M.2    Tsuji, S.3    Takahashi, H.4
  • 7
    • 33749841522 scopus 로고    scopus 로고
    • The aggregation and fibrillation of alpha-synuclein
    • Fink AL, (2006) The aggregation and fibrillation of alpha-synuclein. Acc Chem Res 39, 628-634.
    • (2006) Acc Chem Res , vol.39 , pp. 628-634
    • Fink, A.L.1
  • 8
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • Weinreb PH, Zhen Z, Poon AW, Conway KA, &, Lansbury PT Jr, (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35, 13709-13715.
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, Z.2    Poon, A.W.3    Conway, K.A.4    Lansbury, Jr.P.T.5
  • 9
    • 80052398365 scopus 로고    scopus 로고
    • α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • Bartels T, Choi JG, &, Selkoe DJ, (2011) α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477, 107-110.
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 11
    • 84874769548 scopus 로고    scopus 로고
    • In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells
    • Dettmer U, Newman AJ, Luth ES, Bartels T, &, Selkoe D, (2013) In vivo cross-linking reveals principally oligomeric forms of α-synuclein and β-synuclein in neurons and non-neural cells. J Biol Chem 288, 6371-6385.
    • (2013) J Biol Chem , vol.288 , pp. 6371-6385
    • Dettmer, U.1    Newman, A.J.2    Luth, E.S.3    Bartels, T.4    Selkoe, D.5
  • 12
    • 84859577559 scopus 로고    scopus 로고
    • Alpha-synuclein in the central nervous system and from erythrocytes, mammalian cells and Escherichia coli exists predominantly as a disordered monomer
    • Fauvet B, Mbefo MK, Fares MB, Desobry C, Michael S, Ardah MT, Tsika E, Coune P, Prudent M, Lion N, et al,. (2012) Alpha-synuclein in the central nervous system and from erythrocytes, mammalian cells and Escherichia coli exists predominantly as a disordered monomer. J Biol Chem 287, 15345-15364.
    • (2012) J Biol Chem , vol.287 , pp. 15345-15364
    • Fauvet, B.1    Mbefo, M.K.2    Fares, M.B.3    Desobry, C.4    Michael, S.5    Ardah, M.T.6    Tsika, E.7    Coune, P.8    Prudent, M.9    Lion, N.10
  • 13
    • 84860172516 scopus 로고    scopus 로고
    • N-Terminal acetylation is critical for forming α-helical oligomer of α-synuclein
    • Trexler AJ, &, Rhoades E, (2012) N-Terminal acetylation is critical for forming α-helical oligomer of α-synuclein. Protein Sci 21, 601-605.
    • (2012) Protein Sci , vol.21 , pp. 601-605
    • Trexler, A.J.1    Rhoades, E.2
  • 14
    • 20444412385 scopus 로고    scopus 로고
    • A new method for purification of recombinant human alpha-synuclein in Escherichia coli
    • Huang C, Ren G, Zhou H, &, Wang CC, (2005) A new method for purification of recombinant human alpha-synuclein in Escherichia coli. Protein Expr Purif 42, 173-177.
    • (2005) Protein Expr Purif , vol.42 , pp. 173-177
    • Huang, C.1    Ren, G.2    Zhou, H.3    Wang, C.C.4
  • 15
    • 34147151003 scopus 로고    scopus 로고
    • Translocation of alpha-synuclein expressed in Escherichia coli
    • Ren G, Wang X, Hao S, Hu H, &, Wang CC, (2007) Translocation of alpha-synuclein expressed in Escherichia coli. J Bacteriol 189, 2777-2786.
    • (2007) J Bacteriol , vol.189 , pp. 2777-2786
    • Ren, G.1    Wang, X.2    Hao, S.3    Hu, H.4    Wang, C.C.5
  • 16
    • 0037013194 scopus 로고    scopus 로고
    • Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein
    • Golts N, Snyder H, Frasier M, Theisler C, Choi P, &, Wolozin B, (2002) Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein. J Biol Chem 277, 16116-16123.
    • (2002) J Biol Chem , vol.277 , pp. 16116-16123
    • Golts, N.1    Snyder, H.2    Frasier, M.3    Theisler, C.4    Choi, P.5    Wolozin, B.6
  • 17
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson BI, Uryu K, Trojanowski JQ, &, Lee VM, (1999) Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J Biol Chem 274, 7619-7622.
    • (1999) J Biol Chem , vol.274 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 18
    • 0036386364 scopus 로고    scopus 로고
    • Dependence of alpha-synuclein aggregate morphology on solution conditions
    • Hoyer W, Antony T, Cherny D, Heim G, Jovin TM, &, Subramaniam V, (2002) Dependence of alpha-synuclein aggregate morphology on solution conditions. J Mol Biol 322, 383-393.
    • (2002) J Mol Biol , vol.322 , pp. 383-393
    • Hoyer, W.1    Antony, T.2    Cherny, D.3    Heim, G.4    Jovin, T.M.5    Subramaniam, V.6
  • 19
    • 79952188071 scopus 로고    scopus 로고
    • Assays for α-synuclein aggregation
    • Giehm L, Lorenzen N, &, Otzen DE, (2011) Assays for α-synuclein aggregation. Methods 53, 295-305.
    • (2011) Methods , vol.53 , pp. 295-305
    • Giehm, L.1    Lorenzen, N.2    Otzen, D.E.3
  • 21
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • Uversky NV, Li J, &, Fink AL, (2001) Evidence for a partially folded intermediate in alpha-synuclein fibril formation. J Biol Chem 276, 10737-10744.
    • (2001) J Biol Chem , vol.276 , pp. 10737-10744
    • Uversky, N.V.1    Li, J.2    Fink, A.L.3
  • 22
    • 77952571567 scopus 로고    scopus 로고
    • Detection of transient interchain interactions in the intrinsically disordered protein alpha-synuclein by NMR paramagnetic relaxation enhancement
    • Wu KP, &, Baum J, (2010) Detection of transient interchain interactions in the intrinsically disordered protein alpha-synuclein by NMR paramagnetic relaxation enhancement. J Am Chem Soc 132, 5546-5547.
    • (2010) J Am Chem Soc , vol.132 , pp. 5546-5547
    • Wu, K.P.1    Baum, J.2
  • 23
    • 77949885897 scopus 로고    scopus 로고
    • Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: Conformational heterogeneity of alpha-synuclein
    • Frimpong AK, Abzalimov RR, Uversky VN, &, Kaltashov IA, (2010) Characterization of intrinsically disordered proteins with electrospray ionization mass spectrometry: conformational heterogeneity of alpha-synuclein. Proteins Struct Funct Bioinform 78, 714-722.
    • (2010) Proteins Struct Funct Bioinform , vol.78 , pp. 714-722
    • Frimpong, A.K.1    Abzalimov, R.R.2    Uversky, V.N.3    Kaltashov, I.A.4
  • 26
    • 0027733616 scopus 로고
    • Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule
    • Uversky VN, (1993) Use of fast protein size-exclusion liquid chromatography to study the unfolding of proteins which denature through the molten globule. Biochemistry 32, 13288-13298.
    • (1993) Biochemistry , vol.32 , pp. 13288-13298
    • Uversky, V.N.1
  • 27
    • 68149132468 scopus 로고    scopus 로고
    • Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations
    • Wu KP, Weinstock DS, Narayanan C, Levy RM, &, Baum J, (2009) Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations. J Mol Biol 391, 784-796.
    • (2009) J Mol Biol , vol.391 , pp. 784-796
    • Wu, K.P.1    Weinstock, D.S.2    Narayanan, C.3    Levy, R.M.4    Baum, J.5
  • 28
    • 29544433937 scopus 로고    scopus 로고
    • Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder
    • McNulty BC, Young GB, &, Pielak GJ, (2006) Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder. J Mol Biol 355, 893-897.
    • (2006) J Mol Biol , vol.355 , pp. 893-897
    • McNulty, B.C.1    Young, G.B.2    Pielak, G.J.3
  • 30
    • 84866671599 scopus 로고    scopus 로고
    • Bacterial in-cell NMR of human alpha-synuclein: A disordered monomer by nature?
    • Binolfi A, Theillet FX, &, Selenko P, (2012) Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature? Biochem Soc Trans 40, 950-954.
    • (2012) Biochem Soc Trans , vol.40 , pp. 950-954
    • Binolfi, A.1    Theillet, F.X.2    Selenko, P.3
  • 33
    • 0027367977 scopus 로고
    • Helix capping propensities in peptides parallel those in proteins
    • Chakrabartty A, Doig AJ, &, Baldwin RL, (1993) Helix capping propensities in peptides parallel those in proteins. Proc Natl Acad Sci USA 90, 11332-11336.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11332-11336
    • Chakrabartty, A.1    Doig, A.J.2    Baldwin, R.L.3
  • 34
    • 80555131132 scopus 로고    scopus 로고
    • N-Terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex
    • Scott DC, Monda JK, Bennett EJ, Harper JW, &, Schulman BA, (2011) N-Terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex. Science 334, 674-678.
    • (2011) Science , vol.334 , pp. 674-678
    • Scott, D.C.1    Monda, J.K.2    Bennett, E.J.3    Harper, J.W.4    Schulman, B.A.5
  • 35
    • 84862893457 scopus 로고    scopus 로고
    • Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties
    • Maltsev AS, Ying J, &, Bax A, (2012) Impact of N-terminal acetylation of α-synuclein on its random coil and lipid binding properties. Biochemistry 51, 5004-5013.
    • (2012) Biochemistry , vol.51 , pp. 5004-5013
    • Maltsev, A.S.1    Ying, J.2    Bax, A.3
  • 36
    • 84865249504 scopus 로고    scopus 로고
    • Characterization of semisynthetic and naturally N-α-acetylated α-synuclein in vitro and in intact cells: Implications for aggregation and cellular properties of α-synuclein
    • Fauvet B, Fares MB, Samuel F, Dikiy I, Tandon A, Eliezer D, &, Lashuel HA, (2012) Characterization of semisynthetic and naturally N-α-acetylated α-synuclein in vitro and in intact cells: implications for aggregation and cellular properties of α-synuclein. J Biol Chem 287, 28243-28262.
    • (2012) J Biol Chem , vol.287 , pp. 28243-28262
    • Fauvet, B.1    Fares, M.B.2    Samuel, F.3    Dikiy, I.4    Tandon, A.5    Eliezer, D.6    Lashuel, H.A.7
  • 37
    • 84862555977 scopus 로고    scopus 로고
    • N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer
    • Kang L, Moriarty GM, Woods LA, Ashcroft AE, Radford SE, &, Baum J, (2012) N-terminal acetylation of α-synuclein induces increased transient helical propensity and decreased aggregation rates in the intrinsically disordered monomer. Protein Sci 21, 911-917.
    • (2012) Protein Sci , vol.21 , pp. 911-917
    • Kang, L.1    Moriarty, G.M.2    Woods, L.A.3    Ashcroft, A.E.4    Radford, S.E.5    Baum, J.6
  • 38
    • 67449097463 scopus 로고    scopus 로고
    • Effect of pseudorepeat rearrangement on alpha-synuclein misfolding, vesicle binding, and micelle binding
    • Rao JN, Kim YE, Park LS, &, Ulmer TS, (2009) Effect of pseudorepeat rearrangement on alpha-synuclein misfolding, vesicle binding, and micelle binding. J Mol Biol 390, 516-529.
    • (2009) J Mol Biol , vol.390 , pp. 516-529
    • Rao, J.N.1    Kim, Y.E.2    Park, L.S.3    Ulmer, T.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.