메뉴 건너뛰기




Volumn 111, Issue 2, 2016, Pages 349-362

Acetylation within the First 17 Residues of Huntingtin Exon 1 Alters Aggregation and Lipid Binding

Author keywords

[No Author keywords available]

Indexed keywords

HUNTINGTIN; LIPID BILAYER; PEPTIDE; POLYGLUTAMINE; PROTEIN AGGREGATE;

EID: 84979587970     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2016.06.018     Document Type: Article
Times cited : (53)

References (115)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • 1 The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72 (1993), 971–983.
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
    • 0027261537 scopus 로고
    • Relationship between trinucleotide repeat expansion and phenotypic variation in Huntington's disease
    • 2 Snell, R.G., MacMillan, J.C., et al., Shaw, D.J., Relationship between trinucleotide repeat expansion and phenotypic variation in Huntington's disease. Nat. Genet. 4 (1993), 393–397.
    • (1993) Nat. Genet. , vol.4 , pp. 393-397
    • Snell, R.G.1    MacMillan, J.C.2    Shaw, D.J.3
  • 3
    • 0034571171 scopus 로고    scopus 로고
    • Huntington's disease: the challenge for cell biologists
    • 3 Tobin, A.J., Signer, E.R., Huntington's disease: the challenge for cell biologists. Trends Cell Biol. 10 (2000), 531–536.
    • (2000) Trends Cell Biol. , vol.10 , pp. 531-536
    • Tobin, A.J.1    Signer, E.R.2
  • 4
    • 77951988103 scopus 로고    scopus 로고
    • Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo
    • 4 Legleiter, J., Mitchell, E., et al., Muchowski, P.J., Mutant huntingtin fragments form oligomers in a polyglutamine length-dependent manner in vitro and in vivo. J. Biol. Chem. 285 (2010), 14777–14790.
    • (2010) J. Biol. Chem. , vol.285 , pp. 14777-14790
    • Legleiter, J.1    Mitchell, E.2    Muchowski, P.J.3
  • 6
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • 6 Poirier, M.A., Li, H., et al., Ross, C.A., Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. 277 (2002), 41032–41037.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Ross, C.A.3
  • 7
    • 0035940412 scopus 로고    scopus 로고
    • Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis
    • 7 Kim, Y.J., Yi, Y., et al., DiFiglia, M., Caspase 3-cleaved N-terminal fragments of wild-type and mutant huntingtin are present in normal and Huntington's disease brains, associate with membranes, and undergo calpain-dependent proteolysis. Proc. Natl. Acad. Sci. USA 98 (2001), 12784–12789.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12784-12789
    • Kim, Y.J.1    Yi, Y.2    DiFiglia, M.3
  • 8
    • 7144253143 scopus 로고    scopus 로고
    • Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
    • 8 Cooper, J.K., Schilling, G., et al., Ross, C.A., Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum. Mol. Genet. 7 (1998), 783–790.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 783-790
    • Cooper, J.K.1    Schilling, G.2    Ross, C.A.3
  • 9
    • 25644434918 scopus 로고    scopus 로고
    • Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers
    • 9 Hoffner, G., Island, M.-L., Djian, P., Purification of neuronal inclusions of patients with Huntington's disease reveals a broad range of N-terminal fragments of expanded huntingtin and insoluble polymers. J. Neurochem. 95 (2005), 125–136.
    • (2005) J. Neurochem. , vol.95 , pp. 125-136
    • Hoffner, G.1    Island, M.-L.2    Djian, P.3
  • 10
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation
    • 10 Davies, S.W., Turmaine, M., et al., Bates, G.P., Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation. Cell 90 (1997), 537–548.
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Bates, G.P.3
  • 11
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • 11 Landles, C., Sathasivam, K., et al., Bates, G.P., Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J. Biol. Chem. 285 (2010), 8808–8823.
    • (2010) J. Biol. Chem. , vol.285 , pp. 8808-8823
    • Landles, C.1    Sathasivam, K.2    Bates, G.P.3
  • 12
    • 84873463075 scopus 로고    scopus 로고
    • Aberrant splicing of HTT generates the pathogenic exon 1 protein in Huntington disease
    • 12 Sathasivam, K., Neueder, A., et al., Bates, G.P., Aberrant splicing of HTT generates the pathogenic exon 1 protein in Huntington disease. Proc. Natl. Acad. Sci. USA 110 (2013), 2366–2370.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 2366-2370
    • Sathasivam, K.1    Neueder, A.2    Bates, G.P.3
  • 13
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • 13 DiFiglia, M., Sapp, E., et al., Aronin, N., Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277 (1997), 1990–1993.
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Aronin, N.3
  • 14
    • 0029152808 scopus 로고
    • Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies
    • 14 Gutekunst, C.A., Levey, A.I., et al., Hersch, S.M., Identification and localization of huntingtin in brain and human lymphoblastoid cell lines with anti-fusion protein antibodies. Proc. Natl. Acad. Sci. USA 92 (1995), 8710–8714.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8710-8714
    • Gutekunst, C.A.1    Levey, A.I.2    Hersch, S.M.3
  • 15
    • 0033119123 scopus 로고    scopus 로고
    • Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology
    • 15 Gutekunst, C.A., Li, S.H., et al., Li, X.J., Nuclear and neuropil aggregates in Huntington's disease: relationship to neuropathology. J. Neurosci. 19 (1999), 2522–2534.
    • (1999) J. Neurosci. , vol.19 , pp. 2522-2534
    • Gutekunst, C.A.1    Li, S.H.2    Li, X.J.3
  • 16
    • 77955273305 scopus 로고    scopus 로고
    • Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated
    • 16 Kodali, R., Williams, A.D., et al., Wetzel, R., Abeta(1-40) forms five distinct amyloid structures whose beta-sheet contents and fibril stabilities are correlated. J. Mol. Biol. 401 (2010), 503–517.
    • (2010) J. Mol. Biol. , vol.401 , pp. 503-517
    • Kodali, R.1    Williams, A.D.2    Wetzel, R.3
  • 17
    • 0034307476 scopus 로고    scopus 로고
    • Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy
    • 17 Kegel, K.B., Kim, M., et al., DiFiglia, M., Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy. J. Neurosci. 20 (2000), 7268–7278.
    • (2000) J. Neurosci. , vol.20 , pp. 7268-7278
    • Kegel, K.B.1    Kim, M.2    DiFiglia, M.3
  • 18
    • 0842322740 scopus 로고    scopus 로고
    • Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction
    • 18 Qin, Z.H., Wang, Y., et al., DiFiglia, M., Huntingtin bodies sequester vesicle-associated proteins by a polyproline-dependent interaction. J. Neurosci. 24 (2004), 269–281.
    • (2004) J. Neurosci. , vol.24 , pp. 269-281
    • Qin, Z.H.1    Wang, Y.2    DiFiglia, M.3
  • 19
    • 33645104605 scopus 로고    scopus 로고
    • Interaction of huntingtin fragments with brain membranes–clues to early dysfunction in Huntington's disease
    • 19 Suopanki, J., Götz, C., et al., Wanker, E.E., Interaction of huntingtin fragments with brain membranes–clues to early dysfunction in Huntington's disease. J. Neurochem. 96 (2006), 870–884.
    • (2006) J. Neurochem. , vol.96 , pp. 870-884
    • Suopanki, J.1    Götz, C.2    Wanker, E.E.3
  • 20
    • 73949155373 scopus 로고    scopus 로고
    • Mutant huntingtin and glycogen synthase kinase 3-beta accumulate in neuronal lipid rafts of a presymptomatic knock-in mouse model of Huntington's disease
    • 20 Valencia, A., Reeves, P.B., et al., DiFiglia, M., Mutant huntingtin and glycogen synthase kinase 3-beta accumulate in neuronal lipid rafts of a presymptomatic knock-in mouse model of Huntington's disease. J. Neurosci. Res. 88 (2010), 179–190.
    • (2010) J. Neurosci. Res. , vol.88 , pp. 179-190
    • Valencia, A.1    Reeves, P.B.2    DiFiglia, M.3
  • 21
    • 35448994487 scopus 로고    scopus 로고
    • Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity
    • 21 Atwal, R.S., Xia, J., et al., Truant, R., Huntingtin has a membrane association signal that can modulate huntingtin aggregation, nuclear entry and toxicity. Hum. Mol. Genet. 16 (2007), 2600–2615.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2600-2615
    • Atwal, R.S.1    Xia, J.2    Truant, R.3
  • 22
    • 33846540080 scopus 로고    scopus 로고
    • The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis
    • 22 Rockabrand, E., Slepko, N., et al., Thompson, L.M., The first 17 amino acids of Huntingtin modulate its sub-cellular localization, aggregation and effects on calcium homeostasis. Hum. Mol. Genet. 16 (2007), 61–77.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 61-77
    • Rockabrand, E.1    Slepko, N.2    Thompson, L.M.3
  • 23
    • 84878217830 scopus 로고    scopus 로고
    • The interaction of polyglutamine peptides with lipid membranes is regulated by flanking sequences associated with huntingtin
    • 23 Burke, K.A., Kauffman, K.J., et al., Legleiter, J., The interaction of polyglutamine peptides with lipid membranes is regulated by flanking sequences associated with huntingtin. J. Biol. Chem. 288 (2013), 14993–15005.
    • (2013) J. Biol. Chem. , vol.288 , pp. 14993-15005
    • Burke, K.A.1    Kauffman, K.J.2    Legleiter, J.3
  • 24
    • 84856226648 scopus 로고    scopus 로고
    • Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments
    • 24 Jayaraman, M., Kodali, R., et al., Wetzel, R., Slow amyloid nucleation via α-helix-rich oligomeric intermediates in short polyglutamine-containing huntingtin fragments. J. Mol. Biol. 415 (2012), 881–899.
    • (2012) J. Mol. Biol. , vol.415 , pp. 881-899
    • Jayaraman, M.1    Kodali, R.2    Wetzel, R.3
  • 25
    • 64049119303 scopus 로고    scopus 로고
    • Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism
    • 25 Thakur, A.K., Jayaraman, M., et al., Wetzel, R., Polyglutamine disruption of the huntingtin exon 1 N terminus triggers a complex aggregation mechanism. Nat. Struct. Mol. Biol. 16 (2009), 380–389.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 380-389
    • Thakur, A.K.1    Jayaraman, M.2    Wetzel, R.3
  • 26
    • 84856212436 scopus 로고    scopus 로고
    • Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates
    • 26 Mishra, R., Jayaraman, M., et al., Wetzel, R., Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates. J. Mol. Biol. 415 (2012), 900–917.
    • (2012) J. Mol. Biol. , vol.415 , pp. 900-917
    • Mishra, R.1    Jayaraman, M.2    Wetzel, R.3
  • 27
    • 84873381579 scopus 로고    scopus 로고
    • Membrane interactions of the amphipathic amino terminus of huntingtin
    • 27 Michalek, M., Salnikov, E.S., et al., Bechinger, B., Membrane interactions of the amphipathic amino terminus of huntingtin. Biochemistry 52 (2013), 847–858.
    • (2013) Biochemistry , vol.52 , pp. 847-858
    • Michalek, M.1    Salnikov, E.S.2    Bechinger, B.3
  • 28
    • 77649271684 scopus 로고    scopus 로고
    • Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin
    • 28 Williamson, T.E., Vitalis, A., et al., Pappu, R.V., Modulation of polyglutamine conformations and dimer formation by the N-terminus of huntingtin. J. Mol. Biol. 396 (2010), 1295–1309.
    • (2010) J. Mol. Biol. , vol.396 , pp. 1295-1309
    • Williamson, T.E.1    Vitalis, A.2    Pappu, R.V.3
  • 29
    • 80053923210 scopus 로고    scopus 로고
    • Secondary structures of native and pathogenic huntingtin N-terminal fragments
    • 29 Długosz, M., Trylska, J., Secondary structures of native and pathogenic huntingtin N-terminal fragments. J. Phys. Chem. B 115 (2011), 11597–11608.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11597-11608
    • Długosz, M.1    Trylska, J.2
  • 30
    • 67349278762 scopus 로고    scopus 로고
    • The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation
    • 30 Kelley, N.W., Huang, X., et al., Pande, V.S., The predicted structure of the headpiece of the Huntingtin protein and its implications on Huntingtin aggregation. J. Mol. Biol. 388 (2009), 919–927.
    • (2009) J. Mol. Biol. , vol.388 , pp. 919-927
    • Kelley, N.W.1    Huang, X.2    Pande, V.S.3
  • 31
    • 84868142101 scopus 로고    scopus 로고
    • All-atom stability and oligomerization simulations of polyglutamine nanotubes with and without the 17-amino-acid N-terminal fragment of the Huntingtin protein
    • 31 Côté, S., Wei, G., Mousseau, N., All-atom stability and oligomerization simulations of polyglutamine nanotubes with and without the 17-amino-acid N-terminal fragment of the Huntingtin protein. J. Phys. Chem. B 116 (2012), 12168–12179.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 12168-12179
    • Côté, S.1    Wei, G.2    Mousseau, N.3
  • 32
    • 84902164061 scopus 로고    scopus 로고
    • Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations
    • 32 Côté, S., Wei, G., Mousseau, N., Atomistic mechanisms of huntingtin N-terminal fragment insertion on a phospholipid bilayer revealed by molecular dynamics simulations. Proteins 82 (2014), 1409–1427.
    • (2014) Proteins , vol.82 , pp. 1409-1427
    • Côté, S.1    Wei, G.2    Mousseau, N.3
  • 33
    • 77954616668 scopus 로고    scopus 로고
    • Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences
    • 33 Lakhani, V.V., Ding, F., Dokholyan, N.V., Polyglutamine induced misfolding of huntingtin exon1 is modulated by the flanking sequences. PLOS Comput. Biol., 6, 2010, e1000772.
    • (2010) PLOS Comput. Biol. , vol.6 , pp. e1000772
    • Lakhani, V.V.1    Ding, F.2    Dokholyan, N.V.3
  • 34
    • 84902970753 scopus 로고    scopus 로고
    • The effects of flanking sequences in the interaction of polyglutamine peptides with a membrane bilayer
    • 34 Nagarajan, A., Jawahery, S., Matysiak, S., The effects of flanking sequences in the interaction of polyglutamine peptides with a membrane bilayer. J. Phys. Chem. B 118 (2014), 6368–6379.
    • (2014) J. Phys. Chem. B , vol.118 , pp. 6368-6379
    • Nagarajan, A.1    Jawahery, S.2    Matysiak, S.3
  • 35
    • 84903214409 scopus 로고    scopus 로고
    • Aggregation behavior of chemically synthesized, full-length huntingtin exon1
    • 35 Sahoo, B., Singer, D., et al., Wetzel, R., Aggregation behavior of chemically synthesized, full-length huntingtin exon1. Biochemistry 53 (2014), 3897–3907.
    • (2014) Biochemistry , vol.53 , pp. 3897-3907
    • Sahoo, B.1    Singer, D.2    Wetzel, R.3
  • 36
    • 79953067377 scopus 로고    scopus 로고
    • The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils
    • 36 Sivanandam, V.N., Jayaraman, M., et al., van der Wel, P.C.A., The aggregation-enhancing huntingtin N-terminus is helical in amyloid fibrils. J. Am. Chem. Soc. 133 (2011), 4558–4566.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 4558-4566
    • Sivanandam, V.N.1    Jayaraman, M.2    van der Wel, P.C.A.3
  • 37
    • 84881409549 scopus 로고    scopus 로고
    • Structure and topology of the huntingtin 1-17 membrane anchor by a combined solution and solid-state NMR approach
    • 37 Michalek, M., Salnikov, E.S., Bechinger, B., Structure and topology of the huntingtin 1-17 membrane anchor by a combined solution and solid-state NMR approach. Biophys. J. 105 (2013), 699–710.
    • (2013) Biophys. J. , vol.105 , pp. 699-710
    • Michalek, M.1    Salnikov, E.S.2    Bechinger, B.3
  • 38
    • 84937576786 scopus 로고    scopus 로고
    • Huntingtin N-terminal monomeric and multimeric structures destabilized by covalent modification of heteroatomic residues
    • 38 Arndt, J.R., Kondalaji, S.G., et al., Valentine, S.J., Huntingtin N-terminal monomeric and multimeric structures destabilized by covalent modification of heteroatomic residues. Biochemistry 54 (2015), 4285–4296.
    • (2015) Biochemistry , vol.54 , pp. 4285-4296
    • Arndt, J.R.1    Kondalaji, S.G.2    Valentine, S.J.3
  • 39
    • 80053573543 scopus 로고    scopus 로고
    • Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease
    • 39 Ehrnhoefer, D.E., Sutton, L., Hayden, M.R., Small changes, big impact: posttranslational modifications and function of huntingtin in Huntington disease. Neuroscientist 17 (2011), 475–492.
    • (2011) Neuroscientist , vol.17 , pp. 475-492
    • Ehrnhoefer, D.E.1    Sutton, L.2    Hayden, M.R.3
  • 40
    • 79952338055 scopus 로고    scopus 로고
    • Potential application of grape derived polyphenols in Huntington's Disease
    • 40 Wang, J., Pfleger, C.M., et al., Pasinetti, G.M., Potential application of grape derived polyphenols in Huntington's Disease. Transl. Neurosci. 1 (2010), 95–100.
    • (2010) Transl. Neurosci. , vol.1 , pp. 95-100
    • Wang, J.1    Pfleger, C.M.2    Pasinetti, G.M.3
  • 41
    • 84860698596 scopus 로고    scopus 로고
    • Putting proteins in their place: palmitoylation in Huntington disease and other neuropsychiatric diseases
    • 41 Young, F.B., Butland, S.L., et al., Hayden, M.R., Putting proteins in their place: palmitoylation in Huntington disease and other neuropsychiatric diseases. Prog. Neurobiol. 97 (2012), 220–238.
    • (2012) Prog. Neurobiol. , vol.97 , pp. 220-238
    • Young, F.B.1    Butland, S.L.2    Hayden, M.R.3
  • 42
    • 63149139630 scopus 로고    scopus 로고
    • Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity
    • 42 Pennuto, M., Palazzolo, I., Poletti, A., Post-translational modifications of expanded polyglutamine proteins: impact on neurotoxicity. Hum. Mol. Genet. 18:R1 (2009), R40–R47.
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.R1 , pp. R40-R47
    • Pennuto, M.1    Palazzolo, I.2    Poletti, A.3
  • 43
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of Huntingtin and Huntington's disease pathology
    • 43 Steffan, J.S., Agrawal, N., et al., Marsh, J.L., SUMO modification of Huntingtin and Huntington's disease pathology. Science 304 (2004), 100–104.
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Marsh, J.L.3
  • 44
    • 80054036817 scopus 로고    scopus 로고
    • Mass spectrometric identification of novel lysine acetylation sites in huntingtin
    • M111.009829
    • 44 Cong, X., Held, J.M., et al., Ellerby, L.M., Mass spectrometric identification of novel lysine acetylation sites in huntingtin. Mol. Cell. Proteomics., 10, 2011 M111.009829.
    • (2011) Mol. Cell. Proteomics. , vol.10
    • Cong, X.1    Held, J.M.2    Ellerby, L.M.3
  • 45
    • 84898837728 scopus 로고    scopus 로고
    • Huntingtin interactions with membrane phospholipids: strategic targets for therapeutic intervention?
    • 45 Kegel-Gleason, K.B., Huntingtin interactions with membrane phospholipids: strategic targets for therapeutic intervention?. J. Huntingtons Dis. 2 (2013), 239–250.
    • (2013) J. Huntingtons Dis. , vol.2 , pp. 239-250
    • Kegel-Gleason, K.B.1
  • 46
    • 84930046200 scopus 로고    scopus 로고
    • The impairment of cholesterol metabolism in Huntington disease
    • 46 Leoni, V., Caccia, C., The impairment of cholesterol metabolism in Huntington disease. Biochim. Biophys. Acta. 1851 (2015), 1095–1105.
    • (2015) Biochim. Biophys. Acta. , vol.1851 , pp. 1095-1105
    • Leoni, V.1    Caccia, C.2
  • 47
    • 27744510791 scopus 로고    scopus 로고
    • Huntingtin associates with acidic phospholipids at the plasma membrane
    • 47 Kegel, K.B., Sapp, E., et al., DiFiglia, M., Huntingtin associates with acidic phospholipids at the plasma membrane. J. Biol. Chem. 280 (2005), 36464–36473.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36464-36473
    • Kegel, K.B.1    Sapp, E.2    DiFiglia, M.3
  • 48
    • 63449090757 scopus 로고    scopus 로고
    • Huntingtin as an essential integrator of intracellular vesicular trafficking
    • 48 Caviston, J.P., Holzbaur, E.L.F., Huntingtin as an essential integrator of intracellular vesicular trafficking. Trends Cell Biol. 19 (2009), 147–155.
    • (2009) Trends Cell Biol. , vol.19 , pp. 147-155
    • Caviston, J.P.1    Holzbaur, E.L.F.2
  • 49
    • 84878868282 scopus 로고    scopus 로고
    • Huntingtin disrupts lipid bilayers in a polyQ-length dependent manner
    • 49 Burke, K.A., Hensal, K.M., et al., Legleiter, J., Huntingtin disrupts lipid bilayers in a polyQ-length dependent manner. Biochim. Biophys. Acta 1828 (2013), 1953–1961.
    • (2013) Biochim. Biophys. Acta , vol.1828 , pp. 1953-1961
    • Burke, K.A.1    Hensal, K.M.2    Legleiter, J.3
  • 50
    • 84936094359 scopus 로고    scopus 로고
    • Disruption of the nuclear membrane by perinuclear inclusions of mutant huntingtin causes cell-cycle re-entry and striatal cell death in mouse and cell models of Huntington's disease
    • 50 Liu, K.-Y., Shyu, Y.-C., et al., Marsh, J.L., Disruption of the nuclear membrane by perinuclear inclusions of mutant huntingtin causes cell-cycle re-entry and striatal cell death in mouse and cell models of Huntington's disease. Hum. Mol. Genet. 24 (2015), 1602–1616.
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 1602-1616
    • Liu, K.-Y.1    Shyu, Y.-C.2    Marsh, J.L.3
  • 51
    • 84964588021 scopus 로고    scopus 로고
    • Expanded polyglutamine embedded in the endoplasmic reticulum causes membrane distortion and coincides with Bax insertion
    • 51 Ueda, M., Li, S., et al., Nakagawa, T., Expanded polyglutamine embedded in the endoplasmic reticulum causes membrane distortion and coincides with Bax insertion. Biochem. Biophys. Res. Commun. 474 (2016), 259–263.
    • (2016) Biochem. Biophys. Res. Commun. , vol.474 , pp. 259-263
    • Ueda, M.1    Li, S.2    Nakagawa, T.3
  • 52
    • 84924957525 scopus 로고    scopus 로고
    • Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulations
    • 52 Côté, S., Binette, V., et al., Mousseau, N., Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulations. Biophys. J. 108 (2015), 1187–1198.
    • (2015) Biophys. J. , vol.108 , pp. 1187-1198
    • Côté, S.1    Binette, V.2    Mousseau, N.3
  • 53
    • 84925608540 scopus 로고    scopus 로고
    • The emerging role of the first 17 amino acids of huntingtin in Huntington's disease
    • 53 Arndt, J.R., Chaibva, M., Legleiter, J., The emerging role of the first 17 amino acids of huntingtin in Huntington's disease. Biomol. Concepts 6 (2015), 33–46.
    • (2015) Biomol. Concepts , vol.6 , pp. 33-46
    • Arndt, J.R.1    Chaibva, M.2    Legleiter, J.3
  • 54
    • 34249733176 scopus 로고    scopus 로고
    • SUMO on the road to neurodegeneration
    • 54 Dorval, V., Fraser, P.E., SUMO on the road to neurodegeneration. Biochim. Biophys. Acta. 1773 (2007), 694–706.
    • (2007) Biochim. Biophys. Acta. , vol.1773 , pp. 694-706
    • Dorval, V.1    Fraser, P.E.2
  • 55
    • 33746932115 scopus 로고    scopus 로고
    • Inhibition of 26S proteasome activity by huntingtin filaments but not inclusion bodies isolated from mouse and human brain
    • 55 Díaz-Hernández, M., Valera, A.G., et al., Lucas, J.J., Inhibition of 26S proteasome activity by huntingtin filaments but not inclusion bodies isolated from mouse and human brain. J. Neurochem. 98 (2006), 1585–1596.
    • (2006) J. Neurochem. , vol.98 , pp. 1585-1596
    • Díaz-Hernández, M.1    Valera, A.G.2    Lucas, J.J.3
  • 56
    • 33751282353 scopus 로고    scopus 로고
    • Huntington's disease: from huntingtin function and dysfunction to therapeutic strategies
    • 56 Borrell-Pagès, M., Zala, D., et al., Saudou, F., Huntington's disease: from huntingtin function and dysfunction to therapeutic strategies. Cell. Mol. Life Sci. 63 (2006), 2642–2660.
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2642-2660
    • Borrell-Pagès, M.1    Zala, D.2    Saudou, F.3
  • 57
    • 84880769535 scopus 로고    scopus 로고
    • SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation
    • 57 O'Rourke, J.G., Gareau, J.R., et al., Thompson, L.M., SUMO-2 and PIAS1 modulate insoluble mutant huntingtin protein accumulation. Cell Reports 4 (2013), 362–375.
    • (2013) Cell Reports , vol.4 , pp. 362-375
    • O'Rourke, J.G.1    Gareau, J.R.2    Thompson, L.M.3
  • 58
    • 78649753221 scopus 로고    scopus 로고
    • Post-translational modification by SUMO
    • 58 Hannoun, Z., Greenhough, S., et al., Hay, D.C., Post-translational modification by SUMO. Toxicology 278 (2010), 288–293.
    • (2010) Toxicology , vol.278 , pp. 288-293
    • Hannoun, Z.1    Greenhough, S.2    Hay, D.C.3
  • 59
    • 70350380989 scopus 로고    scopus 로고
    • Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity
    • 59 Aiken, C.T., Steffan, J.S., et al., Marsh, J.L., Phosphorylation of threonine 3: implications for Huntingtin aggregation and neurotoxicity. J. Biol. Chem. 284 (2009), 29427–29436.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29427-29436
    • Aiken, C.T.1    Steffan, J.S.2    Marsh, J.L.3
  • 60
    • 0035084096 scopus 로고    scopus 로고
    • Solubilization and disaggregation of polyglutamine peptides
    • 60 Chen, S., Wetzel, R., Solubilization and disaggregation of polyglutamine peptides. Protein Sci. 10 (2001), 887–891.
    • (2001) Protein Sci. , vol.10 , pp. 887-891
    • Chen, S.1    Wetzel, R.2
  • 61
    • 0034608868 scopus 로고    scopus 로고
    • Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils
    • 61 Muchowski, P.J., Schaffar, G., et al., Hartl, F.U., Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrils. Proc. Natl. Acad. Sci. USA 97 (2000), 7841–7846.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7841-7846
    • Muchowski, P.J.1    Schaffar, G.2    Hartl, F.U.3
  • 62
    • 79961041262 scopus 로고    scopus 로고
    • Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometry
    • 62 Mendoza, V.L., Barón-Rodríguez, M.A., et al., Vachet, R.W., Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometry. Biochemistry 50 (2011), 6711–6722.
    • (2011) Biochemistry , vol.50 , pp. 6711-6722
    • Mendoza, V.L.1    Barón-Rodríguez, M.A.2    Vachet, R.W.3
  • 63
    • 84873369029 scopus 로고    scopus 로고
    • Amyloid-forming proteins alter the local mechanical properties of lipid membranes
    • 63 Burke, K.A., Yates, E.A., Legleiter, J., Amyloid-forming proteins alter the local mechanical properties of lipid membranes. Biochemistry 52 (2013), 808–817.
    • (2013) Biochemistry , vol.52 , pp. 808-817
    • Burke, K.A.1    Yates, E.A.2    Legleiter, J.3
  • 64
    • 77957912370 scopus 로고    scopus 로고
    • Amyloid-membrane interactions: experimental approaches and techniques
    • 64 Jelinek, R., Sheynis, T., Amyloid-membrane interactions: experimental approaches and techniques. Curr. Protein Pept. Sci. 11 (2010), 372–384.
    • (2010) Curr. Protein Pept. Sci. , vol.11 , pp. 372-384
    • Jelinek, R.1    Sheynis, T.2
  • 65
    • 0033973792 scopus 로고    scopus 로고
    • A colorimetric assay for rapid screening of antimicrobial peptides
    • 65 Kolusheva, S., Boyer, L., Jelinek, R., A colorimetric assay for rapid screening of antimicrobial peptides. Nat. Biotechnol. 18 (2000), 225–227.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 225-227
    • Kolusheva, S.1    Boyer, L.2    Jelinek, R.3
  • 66
    • 0141653970 scopus 로고    scopus 로고
    • The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies
    • 66 Porat, Y., Kolusheva, S., et al., Gazit, E., The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. Biochemistry 42 (2003), 10971–10977.
    • (2003) Biochemistry , vol.42 , pp. 10971-10977
    • Porat, Y.1    Kolusheva, S.2    Gazit, E.3
  • 67
    • 52049088512 scopus 로고    scopus 로고
    • Membrane interactions and lipid binding of casein oligomers and early aggregates
    • 67 Sokolovski, M., Sheynis, T., Kolusheva, S., Jelinek, R., Membrane interactions and lipid binding of casein oligomers and early aggregates. Biochim. Biophys. Acta. 1778 (2008), 2341–2349.
    • (2008) Biochim. Biophys. Acta. , vol.1778 , pp. 2341-2349
    • Sokolovski, M.1    Sheynis, T.2    Kolusheva, S.3    Jelinek, R.4
  • 68
    • 0025991836 scopus 로고
    • Morphological characterization of immortalized hypothalamic neurons synthesizing luteinizing hormone-releasing hormone
    • 68 Liposits, Z., Merchenthaler, I., et al., Negro-Vilar, A., Morphological characterization of immortalized hypothalamic neurons synthesizing luteinizing hormone-releasing hormone. Endocrinology 129 (1991), 1575–1583.
    • (1991) Endocrinology , vol.129 , pp. 1575-1583
    • Liposits, Z.1    Merchenthaler, I.2    Negro-Vilar, A.3
  • 69
    • 0025279155 scopus 로고
    • Immortalization of hypothalamic GnRH neurons by genetically targeted tumorigenesis
    • 69 Mellon, P.L., Windle, J.J., et al., Weiner, R.I., Immortalization of hypothalamic GnRH neurons by genetically targeted tumorigenesis. Neuron 5 (1990), 1–10.
    • (1990) Neuron , vol.5 , pp. 1-10
    • Mellon, P.L.1    Windle, J.J.2    Weiner, R.I.3
  • 70
    • 0026058687 scopus 로고
    • Metabolism of pro-luteinizing hormone-releasing hormone in immortalized hypothalamic neurons
    • 70 Wetsel, W.C., Mellon, P.L., et al., Negro-Vilar, A., Metabolism of pro-luteinizing hormone-releasing hormone in immortalized hypothalamic neurons. Endocrinology 129 (1991), 1584–1595.
    • (1991) Endocrinology , vol.129 , pp. 1584-1595
    • Wetsel, W.C.1    Mellon, P.L.2    Negro-Vilar, A.3
  • 71
    • 0026518980 scopus 로고
    • Intrinsic pulsatile secretory activity of immortalized luteinizing hormone-releasing hormone-secreting neurons
    • 71 Wetsel, W.C., Valença, M.M., et al., Negro-Vilar, A., Intrinsic pulsatile secretory activity of immortalized luteinizing hormone-releasing hormone-secreting neurons. Proc. Natl. Acad. Sci. USA 89 (1992), 4149–4153.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4149-4153
    • Wetsel, W.C.1    Valença, M.M.2    Negro-Vilar, A.3
  • 72
    • 0028898975 scopus 로고
    • A neuron-specific enhancer targets expression of the gonadotropin-releasing hormone gene to hypothalamic neurosecretory neurons
    • 72 Whyte, D.B., Lawson, M.A., et al., Mellon, P.L., A neuron-specific enhancer targets expression of the gonadotropin-releasing hormone gene to hypothalamic neurosecretory neurons. Mol. Endocrinol. 9 (1995), 467–477.
    • (1995) Mol. Endocrinol. , vol.9 , pp. 467-477
    • Whyte, D.B.1    Lawson, M.A.2    Mellon, P.L.3
  • 73
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera—a visualization system for exploratory research and analysis
    • 73 Pettersen, E.F., Goddard, T.D., et al., Ferrin, T.E., UCSF Chimera—a visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004), 1605–1612.
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1    Goddard, T.D.2    Ferrin, T.E.3
  • 74
    • 29244438431 scopus 로고    scopus 로고
    • PyMOL User's Guide
    • DeLano Scientific LLC San Carlos, CA
    • 74 DeLano, W., Bromberg, S., PyMOL User's Guide. 2004, DeLano Scientific LLC, San Carlos, CA.
    • (2004)
    • DeLano, W.1    Bromberg, S.2
  • 76
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • 76 Cornell, W.D., Cieplak, P., et al., Kollman, P.A., A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117 (1995), 5179–5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Kollman, P.A.3
  • 77
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • 77 Hornak, V., Abel, R., et al., Simmerling, C., Comparison of multiple Amber force fields and development of improved protein backbone parameters. Proteins 65 (2006), 712–725.
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Simmerling, C.3
  • 78
    • 20544435097 scopus 로고    scopus 로고
    • Exploring the helix-coil transition via all-atom equilibrium ensemble simulations
    • 78 Sorin, E.J., Pande, V.S., Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys. J. 88 (2005), 2472–2493.
    • (2005) Biophys. J. , vol.88 , pp. 2472-2493
    • Sorin, E.J.1    Pande, V.S.2
  • 79
    • 84859882285 scopus 로고    scopus 로고
    • Structural role of RKS motifs in chromatin interactions: a molecular dynamics study of HP1 bound to a variably modified histone tail
    • 79 Papamokos, G.V., Tziatzos, G., et al., Kaxiras, E., Structural role of RKS motifs in chromatin interactions: a molecular dynamics study of HP1 bound to a variably modified histone tail. Biophys. J. 102 (2012), 1926–1933.
    • (2012) Biophys. J. , vol.102 , pp. 1926-1933
    • Papamokos, G.V.1    Tziatzos, G.2    Kaxiras, E.3
  • 80
    • 84858321169 scopus 로고    scopus 로고
    • Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids
    • 80 Jämbeck, J.P.M., Lyubartsev, A.P., Derivation and systematic validation of a refined all-atom force field for phosphatidylcholine lipids. J. Phys. Chem. B 116 (2012), 3164–3179.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 3164-3179
    • Jämbeck, J.P.M.1    Lyubartsev, A.P.2
  • 81
    • 84865101970 scopus 로고    scopus 로고
    • An extension and further validation of an all-atomistic force field for biological membranes
    • 81 Jämbeck, J.P.M., Lyubartsev, A.P., An extension and further validation of an all-atomistic force field for biological membranes. J. Chem. Theory Comput. 8 (2012), 2938–2948.
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 2938-2948
    • Jämbeck, J.P.M.1    Lyubartsev, A.P.2
  • 82
    • 84872131879 scopus 로고    scopus 로고
    • Another piece of the membrane puzzle: extending slipids further
    • 82 Jämbeck, J.P.M., Lyubartsev, A.P., Another piece of the membrane puzzle: extending slipids further. J. Chem. Theory Comput. 9 (2013), 774–784.
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 774-784
    • Jämbeck, J.P.M.1    Lyubartsev, A.P.2
  • 83
    • 84895763429 scopus 로고    scopus 로고
    • Sulfo-NHS-SS-biotin derivatization: a versatile tool for MALDI mass analysis of PTMs in lysine-rich proteins
    • 83 Markoutsa, S., Bahr, U., et al., Sorg, B.L., Sulfo-NHS-SS-biotin derivatization: a versatile tool for MALDI mass analysis of PTMs in lysine-rich proteins. Proteomics 14 (2014), 659–667.
    • (2014) Proteomics , vol.14 , pp. 659-667
    • Markoutsa, S.1    Bahr, U.2    Sorg, B.L.3
  • 84
    • 0033551063 scopus 로고    scopus 로고
    • Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology
    • 84 Scherzinger, E., Sittler, A., et al., Wanker, E.E., Self-assembly of polyglutamine-containing huntingtin fragments into amyloid-like fibrils: implications for Huntington's disease pathology. Proc. Natl. Acad. Sci. USA 96 (1999), 4604–4609.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4604-4609
    • Scherzinger, E.1    Sittler, A.2    Wanker, E.E.3
  • 85
    • 79952193876 scopus 로고    scopus 로고
    • Assessing mutant huntingtin fragment and polyglutamine aggregation by atomic force microscopy
    • 85 Burke, K.A., Godbey, J., Legleiter, J., Assessing mutant huntingtin fragment and polyglutamine aggregation by atomic force microscopy. Methods 53 (2011), 275–284.
    • (2011) Methods , vol.53 , pp. 275-284
    • Burke, K.A.1    Godbey, J.2    Legleiter, J.3
  • 86
    • 84877715036 scopus 로고    scopus 로고
    • Specific domains of Aβ facilitate aggregation on and association with lipid bilayers
    • 86 Yates, E.A., Owens, S.L., et al., Legleiter, J., Specific domains of Aβ facilitate aggregation on and association with lipid bilayers. J. Mol. Biol. 425 (2013), 1915–1933.
    • (2013) J. Mol. Biol. , vol.425 , pp. 1915-1933
    • Yates, E.A.1    Owens, S.L.2    Legleiter, J.3
  • 87
    • 81155134630 scopus 로고    scopus 로고
    • A quantitative method for the measurement of membrane affinity by polydiacetylene-based colorimetric assay
    • 87 Zheng, F., Wu, Z., Chen, Y., A quantitative method for the measurement of membrane affinity by polydiacetylene-based colorimetric assay. Anal. Biochem. 420 (2012), 171–176.
    • (2012) Anal. Biochem. , vol.420 , pp. 171-176
    • Zheng, F.1    Wu, Z.2    Chen, Y.3
  • 88
    • 0031056234 scopus 로고    scopus 로고
    • Micropatterning fluid lipid bilayers on solid supports
    • 88 Groves, J.T., Ulman, N., Boxer, S.G., Micropatterning fluid lipid bilayers on solid supports. Science 275 (1997), 651–653.
    • (1997) Science , vol.275 , pp. 651-653
    • Groves, J.T.1    Ulman, N.2    Boxer, S.G.3
  • 89
    • 0033639204 scopus 로고    scopus 로고
    • From liposomes to supported, planar bilayer structures on hydrophilic and hydrophobic surfaces: an atomic force microscopy study
    • 89 Jass, J., Tjärnhage, T., Puu, G., From liposomes to supported, planar bilayer structures on hydrophilic and hydrophobic surfaces: an atomic force microscopy study. Biophys. J. 79 (2000), 3153–3163.
    • (2000) Biophys. J. , vol.79 , pp. 3153-3163
    • Jass, J.1    Tjärnhage, T.2    Puu, G.3
  • 90
    • 84862701723 scopus 로고    scopus 로고
    • Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells
    • 90 Pieri, L., Madiona, K., et al., Melki, R., Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys. J. 102 (2012), 2894–2905.
    • (2012) Biophys. J. , vol.102 , pp. 2894-2905
    • Pieri, L.1    Madiona, K.2    Melki, R.3
  • 91
    • 0035118736 scopus 로고    scopus 로고
    • Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption
    • 91 Yip, C.M., McLaurin, J., Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption. Biophys. J. 80 (2001), 1359–1371.
    • (2001) Biophys. J. , vol.80 , pp. 1359-1371
    • Yip, C.M.1    McLaurin, J.2
  • 92
    • 84906046797 scopus 로고    scopus 로고
    • Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement
    • 92 Michalek, M., Aisenbrey, C., Bechinger, B., Investigation of membrane penetration depth and interactions of the amino-terminal domain of huntingtin: refined analysis by tryptophan fluorescence measurement. Eur. Biophys. J. 43 (2014), 347–360.
    • (2014) Eur. Biophys. J. , vol.43 , pp. 347-360
    • Michalek, M.1    Aisenbrey, C.2    Bechinger, B.3
  • 93
    • 79959376288 scopus 로고    scopus 로고
    • Kinase inhibitors modulate huntingtin cell localization and toxicity
    • 93 Atwal, R.S., Desmond, C.R., et al., Truant, R., Kinase inhibitors modulate huntingtin cell localization and toxicity. Nat. Chem. Biol. 7 (2011), 453–460.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 453-460
    • Atwal, R.S.1    Desmond, C.R.2    Truant, R.3
  • 94
    • 72149107077 scopus 로고    scopus 로고
    • Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice
    • 94 Gu, X., Greiner, E.R., et al., Yang, X.W., Serines 13 and 16 are critical determinants of full-length human mutant huntingtin induced disease pathogenesis in HD mice. Neuron 64 (2009), 828–840.
    • (2009) Neuron , vol.64 , pp. 828-840
    • Gu, X.1    Greiner, E.R.2    Yang, X.W.3
  • 95
    • 72149124383 scopus 로고    scopus 로고
    • IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
    • 95 Thompson, L.M., Aiken, C.T., et al., Steffan, J.S., IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome. J. Cell Biol. 187 (2009), 1083–1099.
    • (2009) J. Cell Biol. , vol.187 , pp. 1083-1099
    • Thompson, L.M.1    Aiken, C.T.2    Steffan, J.S.3
  • 96
    • 84874787234 scopus 로고    scopus 로고
    • An N-terminal nuclear export signal regulates trafficking and aggregation of Huntingtin (Htt) protein exon 1
    • 96 Zheng, Z., Li, A., et al., Diamond, M.I., An N-terminal nuclear export signal regulates trafficking and aggregation of Huntingtin (Htt) protein exon 1. J. Biol. Chem. 288 (2013), 6063–6071.
    • (2013) J. Biol. Chem. , vol.288 , pp. 6063-6071
    • Zheng, Z.1    Li, A.2    Diamond, M.I.3
  • 97
    • 84890288534 scopus 로고    scopus 로고
    • Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation
    • 97 Crick, S.L., Ruff, K.M., et al., Pappu, R.V., Unmasking the roles of N- and C-terminal flanking sequences from exon 1 of huntingtin as modulators of polyglutamine aggregation. Proc. Natl. Acad. Sci. USA 110 (2013), 20075–20080.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 20075-20080
    • Crick, S.L.1    Ruff, K.M.2    Pappu, R.V.3
  • 98
    • 80052304480 scopus 로고    scopus 로고
    • Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides
    • 98 Vitalis, A., Pappu, R.V., Assessing the contribution of heterogeneous distributions of oligomers to aggregation mechanisms of polyglutamine peptides. Biophys. Chem. 159 (2011), 14–23.
    • (2011) Biophys. Chem. , vol.159 , pp. 14-23
    • Vitalis, A.1    Pappu, R.V.2
  • 99
    • 84866419575 scopus 로고    scopus 로고
    • Structural features and domain organization of huntingtin fibrils
    • 99 Bugg, C.W., Isas, J.M., et al., Langen, R., Structural features and domain organization of huntingtin fibrils. J. Biol. Chem. 287 (2012), 31739–31746.
    • (2012) J. Biol. Chem. , vol.287 , pp. 31739-31746
    • Bugg, C.W.1    Isas, J.M.2    Langen, R.3
  • 100
    • 77954379810 scopus 로고    scopus 로고
    • Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool
    • 100 Olshina, M.A., Angley, L.M., et al., Hatters, D.M., Tracking mutant huntingtin aggregation kinetics in cells reveals three major populations that include an invariant oligomer pool. J. Biol. Chem. 285 (2010), 21807–21816.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21807-21816
    • Olshina, M.A.1    Angley, L.M.2    Hatters, D.M.3
  • 101
    • 33847302564 scopus 로고    scopus 로고
    • Wild-type huntingtin participates in protein trafficking between the Golgi and the extracellular space
    • 101 Strehlow, A.N.T., Li, J.Z., Myers, R.M., Wild-type huntingtin participates in protein trafficking between the Golgi and the extracellular space. Hum. Mol. Genet. 16 (2007), 391–409.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 391-409
    • Strehlow, A.N.T.1    Li, J.Z.2    Myers, R.M.3
  • 102
    • 79955571230 scopus 로고    scopus 로고
    • Deficiency of huntingtin has pleiotropic effects in the social amoeba Dictyostelium discoideum
    • 102 Myre, M.A., Lumsden, A.L., et al., Gusella, J.F., Deficiency of huntingtin has pleiotropic effects in the social amoeba Dictyostelium discoideum. PLoS Genet., 7, 2011, e1002052.
    • (2011) PLoS Genet. , vol.7 , pp. e1002052
    • Myre, M.A.1    Lumsden, A.L.2    Gusella, J.F.3
  • 103
    • 84860221941 scopus 로고    scopus 로고
    • Multiple phenotypes in Huntington disease mouse neural stem cells
    • 103 Ritch, J.J., Valencia, A., et al., Kegel, K.B., Multiple phenotypes in Huntington disease mouse neural stem cells. Mol. Cell. Neurosci. 50 (2012), 70–81.
    • (2012) Mol. Cell. Neurosci. , vol.50 , pp. 70-81
    • Ritch, J.J.1    Valencia, A.2    Kegel, K.B.3
  • 104
    • 79959796625 scopus 로고    scopus 로고
    • HD CAG-correlated gene expression changes support a simple dominant gain of function
    • 104 Jacobsen, J.C., Gregory, G.C., et al., Lee, J.-M., HD CAG-correlated gene expression changes support a simple dominant gain of function. Hum. Mol. Genet. 20 (2011), 2846–2860.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2846-2860
    • Jacobsen, J.C.1    Gregory, G.C.2    Lee, J.-M.3
  • 105
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • 105 Saudou, F., Finkbeiner, S., et al., Greenberg, M.E., Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95 (1998), 55–66.
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Greenberg, M.E.3
  • 106
    • 4344636957 scopus 로고    scopus 로고
    • Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice
    • 106 Schilling, G., Savonenko, A.V., et al., Borchelt, D.R., Nuclear-targeting of mutant huntingtin fragments produces Huntington's disease-like phenotypes in transgenic mice. Hum. Mol. Genet. 13 (2004), 1599–1610.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1599-1610
    • Schilling, G.1    Savonenko, A.V.2    Borchelt, D.R.3
  • 107
    • 77951896130 scopus 로고    scopus 로고
    • Amphipathic helices and membrane curvature
    • 107 Drin, G., Antonny, B., Amphipathic helices and membrane curvature. FEBS Lett. 584 (2010), 1840–1847.
    • (2010) FEBS Lett. , vol.584 , pp. 1840-1847
    • Drin, G.1    Antonny, B.2
  • 108
    • 0037040923 scopus 로고    scopus 로고
    • An amino-terminal amphipathic α-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A
    • 108 Brass, V., Bieck, E., et al., Moradpour, D., An amino-terminal amphipathic α-helix mediates membrane association of the hepatitis C virus nonstructural protein 5A. J. Biol. Chem. 277 (2002), 8130–8139.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8130-8139
    • Brass, V.1    Bieck, E.2    Moradpour, D.3
  • 109
    • 84909606592 scopus 로고    scopus 로고
    • Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats
    • 109 Georgieva, E.R., Xiao, S., et al., Eliezer, D., Tau binds to lipid membrane surfaces via short amphipathic helices located in its microtubule-binding repeats. Biophys. J. 107 (2014), 1441–1452.
    • (2014) Biophys. J. , vol.107 , pp. 1441-1452
    • Georgieva, E.R.1    Xiao, S.2    Eliezer, D.3
  • 110
    • 79953862815 scopus 로고    scopus 로고
    • Mechanism of membrane curvature sensing by amphipathic helix containing proteins
    • 110 Cui, H., Lyman, E., Voth, G.A., Mechanism of membrane curvature sensing by amphipathic helix containing proteins. Biophys. J. 100 (2011), 1271–1279.
    • (2011) Biophys. J. , vol.100 , pp. 1271-1279
    • Cui, H.1    Lyman, E.2    Voth, G.A.3
  • 111
    • 84873340106 scopus 로고    scopus 로고
    • The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal
    • 111 Maiuri, T., Woloshansky, T., et al., Truant, R., The huntingtin N17 domain is a multifunctional CRM1 and Ran-dependent nuclear and cilial export signal. Hum. Mol. Genet. 22 (2013), 1383–1394.
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 1383-1394
    • Maiuri, T.1    Woloshansky, T.2    Truant, R.3
  • 112
    • 84898881372 scopus 로고    scopus 로고
    • Curvature enhances binding and aggregation of huntingtin at lipid membranes
    • 112 Chaibva, M., Burke, K.A., Legleiter, J., Curvature enhances binding and aggregation of huntingtin at lipid membranes. Biochemistry 53 (2014), 2355–2365.
    • (2014) Biochemistry , vol.53 , pp. 2355-2365
    • Chaibva, M.1    Burke, K.A.2    Legleiter, J.3
  • 113
    • 84863003858 scopus 로고    scopus 로고
    • An acetylation switch regulates SUMO-dependent protein interaction networks
    • 113 Ullmann, R., Chien, C.D., et al., Muller, S., An acetylation switch regulates SUMO-dependent protein interaction networks. Mol. Cell 46 (2012), 759–770.
    • (2012) Mol. Cell , vol.46 , pp. 759-770
    • Ullmann, R.1    Chien, C.D.2    Muller, S.3
  • 114
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • 114 Jeong, H., Then, F., et al., Krainc, D., Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 137 (2009), 60–72.
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1    Then, F.2    Krainc, D.3
  • 115
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • 115 Kabsch, W., Sander, C., Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22 (1983), 2577–2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.