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Volumn 8, Issue 9, 2014, Pages 9503-9510

Molecular tethering effect of c-terminus of amyloid peptide aβ42

Author keywords

amyloid peptide; membrane disruption; modulation; molecular tethering effect; peptide aggregation

Indexed keywords

AMINO ACIDS; GLYCOPROTEINS; MODULATION; MOLECULES; PROTEINS; SCANNING TUNNELING MICROSCOPY; SELF ASSEMBLY;

EID: 84925603237     PISSN: 19360851     EISSN: 1936086X     Source Type: Journal    
DOI: 10.1021/nn503737r     Document Type: Article
Times cited : (34)

References (39)
  • 1
    • 0021994836 scopus 로고
    • Isolation and Structure of a Novel C-Terminally Amidated Opioid Peptide, Amidorphin, from Bovine Adrenal Medulla
    • Seizinger, B. R.; Liebisch, D. C.; Gramsch, C.; Herz, A.; Weber, E.; Evans, C. J.; Esch, F. S.; Bohlen, P. Isolation and Structure of a Novel C-Terminally Amidated Opioid Peptide, Amidorphin, from Bovine Adrenal Medulla Nature 1985, 313, 57-59
    • (1985) Nature , vol.313 , pp. 57-59
    • Seizinger, B.R.1    Liebisch, D.C.2    Gramsch, C.3    Herz, A.4    Weber, E.5    Evans, C.J.6    Esch, F.S.7    Bohlen, P.8
  • 2
    • 84925595086 scopus 로고    scopus 로고
    • C-Terminus Truncation and Phosphorylation of the Human Tau Protein Enhances Tau Polymerization: An in Vitro Study Using Laser Light Scattering and Electron Microscopy
    • Abraha, A.; Kuret, J.; Binder, L. I. C-Terminus Truncation and Phosphorylation of the Human Tau Protein Enhances Tau Polymerization: An In Vitro Study Using Laser Light Scattering and Electron Microscopy J. Neurochem. 2000, 74, S15-S15
    • (2000) J. Neurochem. , vol.74 , pp. 15-S15
    • Abraha, A.1    Kuret, J.2    Binder, L.I.3
  • 3
    • 0025173617 scopus 로고
    • Phosphorylation of the C Terminus of Fos Protein Is Required for Transcriptional Transrepression of the C-Fos Promoter
    • Rivka. Ofir; Dwarki, V. J.; Rashid, D.; Verma, I. M. Phosphorylation of the C Terminus of Fos Protein Is Required for Transcriptional Transrepression of the C-Fos Promoter Nature 1990, 348, 80-82
    • (1990) Nature , vol.348 , pp. 80-82
    • Ofir, R.1    Dwarki, V.J.2    Rashid, D.3    Verma, I.M.4
  • 4
    • 0028085937 scopus 로고
    • Improvement of Outer Membrane-Permeabilizing and Lipopolysaccharide-Binding Activities of an Antimicrobial Cationic Peptide by C-Terminal Modification
    • Piers, K. L.; Brown, M. H.; Hancock, R. E. Improvement of Outer Membrane-Permeabilizing and Lipopolysaccharide-Binding Activities of an Antimicrobial Cationic Peptide by C-Terminal Modification Antimicrob. Agents Chemother. 1994, 38, 2311-2316
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2311-2316
    • Piers, K.L.1    Brown, M.H.2    Hancock, R.E.3
  • 5
    • 77954070546 scopus 로고    scopus 로고
    • Control of Membrane Protein Topology by a Single C-Terminal Residue
    • Seppala, S.; Slusky, J. S.; Lloris-Garcera, P.; Rapp, M.; von Heijne, G. Control of Membrane Protein Topology by a Single C-Terminal Residue Science 2010, 328, 1698-1700
    • (2010) Science , vol.328 , pp. 1698-1700
    • Seppala, S.1    Slusky, J.S.2    Lloris-Garcera, P.3    Rapp, M.4    Von Heijne, G.5
  • 6
    • 0037130174 scopus 로고    scopus 로고
    • Neurodegenerative Disease-Amyloid Pores from Pathogenic Mutations
    • Lashuel, H. A.; Hartley, D.; Petre, B. M.; Walz, T.; Lansbury, P. T. Neurodegenerative Disease-Amyloid Pores from Pathogenic Mutations Nature 2002, 418, 291-291
    • (2002) Nature , vol.418 , pp. 291-291
    • Lashuel, H.A.1    Hartley, D.2    Petre, B.M.3    Walz, T.4    Lansbury, P.T.5
  • 8
    • 77955312210 scopus 로고    scopus 로고
    • Amyloidogenic Protein Membrane Interactions: Mechanistic Insight from Model Systems
    • Butterfield, S. M.; Lashuel, H. A. Amyloidogenic Protein Membrane Interactions: Mechanistic Insight from Model Systems Angew. Chem., Int. Ed. 2010, 49, 5628-5654
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 5628-5654
    • Butterfield, S.M.1    Lashuel, H.A.2
  • 10
    • 33750731675 scopus 로고    scopus 로고
    • 100 Years and Counting: Prospects for Defeating Alzheimers Disease
    • Roberson, E. D.; Mucke, L. 100 Years and Counting: Prospects for Defeating Alzheimers Disease Science 2006, 314, 781-784
    • (2006) Science , vol.314 , pp. 781-784
    • Roberson, E.D.1    Mucke, L.2
  • 11
    • 33750705653 scopus 로고    scopus 로고
    • A Century of Alzheimers Disease
    • Goedert, M.; Spillantini, M. G. A Century of Alzheimers Disease Science 2006, 314, 777-781
    • (2006) Science , vol.314 , pp. 777-781
    • Goedert, M.1    Spillantini, M.G.2
  • 13
    • 0037135111 scopus 로고    scopus 로고
    • Medicine - The Amyloid Hypothesis of Alzheimers Disease: Progress and Problems on the Road to Therapeutics
    • Hardy, J.; Selkoe, D. J. Medicine-the Amyloid Hypothesis of Alzheimers Disease: Progress and Problems on the Road to Therapeutics Science 2002, 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 14
    • 0027258525 scopus 로고
    • The Carboxy Terminus of the Amyloid Protein Is Critical for the Seeding of Amyloid Formation: Implications for the Pathogenesis of Alzheimers Disease
    • Joseph, T.; Jarrett, E. P.; Berger, P. T.; Lansbury, J. The Carboxy Terminus of the Amyloid Protein Is Critical for the Seeding of Amyloid Formation: Implications for the Pathogenesis of Alzheimers Disease Biochemistry 1993, 32, 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Joseph, T.1    Jarrett, E.P.2    Berger, P.T.3    Lansbury, J.4
  • 17
    • 84861206757 scopus 로고    scopus 로고
    • Toxic Fibrillar Oligomers of Amyloid-Beta Have Cross-Beta Structure
    • Stroud, J. C.; Liu, C.; Teng, P. K.; Eisenberg, D. Toxic Fibrillar Oligomers of Amyloid-Beta Have Cross-Beta Structure Proc. Natl. Acad. Sci. U.S.A. 2012, 109, 7717-7722
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 7717-7722
    • Stroud, J.C.1    Liu, C.2    Teng, P.K.3    Eisenberg, D.4
  • 19
    • 33845192482 scopus 로고    scopus 로고
    • Congo Red and Protein Aggregation in Neurodegenerative Diseases
    • Frid, P.; Anisimov, S. V.; Popovic, N. Congo Red and Protein Aggregation in Neurodegenerative Diseases Brain Res. Rev. 2007, 53, 135-160
    • (2007) Brain Res. Rev. , vol.53 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 20
    • 0028076051 scopus 로고
    • Development of Small-Molecule Probes for the Beta-Amyloid Protein of Alzheimers Disease
    • Klunk, W. E.; Debnath, M. L.; Pettegrew, J. W. Development of Small-Molecule Probes for the Beta-Amyloid Protein of Alzheimers Disease Neurobio. Aging. 1994, 15, 691-698
    • (1994) Neurobio. Aging. , vol.15 , pp. 691-698
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 22
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic Compounds Prevent Alzheimers Pathology through Different Effects on the Amyloid-Beta Aggregation Pathway
    • Hamaguchi, T.; Ono, K.; Murase, A.; Yamada, M. Phenolic Compounds Prevent Alzheimers Pathology through Different Effects on the Amyloid-Beta Aggregation Pathway Am. J. Pathol. 2009, 175, 2557-2565
    • (2009) Am. J. Pathol. , vol.175 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3    Yamada, M.4
  • 23
    • 7444221875 scopus 로고    scopus 로고
    • Harnessing Chaperones to Generate Small-Molecule Inhibitors of Amyloid Beta Aggregation
    • Gestwicki, J. E.; Crabtree, G. R.; Graef, I. A. Harnessing Chaperones to Generate Small-Molecule Inhibitors of Amyloid Beta Aggregation Science 2004, 306, 865-869
    • (2004) Science , vol.306 , pp. 865-869
    • Gestwicki, J.E.1    Crabtree, G.R.2    Graef, I.A.3
  • 24
    • 57649130599 scopus 로고    scopus 로고
    • Sequestration of Copper from Beta-Amyloid Promotes Selective Lysis by Cyclen-Hybrid Cleavage Agents
    • Wu, W. H.; Lei, P.; Liu, Q.; Hu, J.; Gunn, A. P.; Chen, M. S.; Rui, Y. F.; Su, X. Y.; Xie, Z. P.; Zhao, Y. F. et al. Sequestration of Copper from Beta-Amyloid Promotes Selective Lysis by Cyclen-Hybrid Cleavage Agents J. Biol. Chem. 2008, 283, 31657-31664
    • (2008) J. Biol. Chem. , vol.283 , pp. 31657-31664
    • Wu, W.H.1    Lei, P.2    Liu, Q.3    Hu, J.4    Gunn, A.P.5    Chen, M.S.6    Rui, Y.F.7    Su, X.Y.8    Xie, Z.P.9    Zhao, Y.F.10
  • 25
    • 34547533771 scopus 로고    scopus 로고
    • Embedding the Amyloid Beta-Peptide Sequence in Green Fluorescent Protein Inhibits Abeta Oligomerization
    • Takahashi, T.; Ohta, K.; Mihara, H. Embedding the Amyloid Beta-Peptide Sequence in Green Fluorescent Protein Inhibits Abeta Oligomerization ChemBioChem 2007, 8, 985-988
    • (2007) ChemBioChem , vol.8 , pp. 985-988
    • Takahashi, T.1    Ohta, K.2    Mihara, H.3
  • 26
    • 58149326746 scopus 로고    scopus 로고
    • Molecular Mechanism of Thioflavin-T Binding to the Surface of Beta-Rich Peptide Self-Assemblies
    • Biancalana, M.; Makabe, K.; Koide, A.; Koide, S. Molecular Mechanism of Thioflavin-T Binding to the Surface of Beta-Rich Peptide Self-Assemblies J. Mol. Biol. 2009, 385, 1052-1063
    • (2009) J. Mol. Biol. , vol.385 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 27
  • 28
    • 67651221827 scopus 로고    scopus 로고
    • Templating Molecular Arrays in Amyloids Cross-Beta Grooves
    • Childers, W. S.; Mehta, A. K.; Lu, K.; Lynn, D. G. Templating Molecular Arrays in Amyloids Cross-Beta Grooves J. Am. Chem. Soc. 2009, 131, 10165-10172
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 10165-10172
    • Childers, W.S.1    Mehta, A.K.2    Lu, K.3    Lynn, D.G.4
  • 29
    • 84890470509 scopus 로고    scopus 로고
    • Differentiating Amino Acid Residues and Side Chain Orientations in Peptides Using Scanning Tunneling Microscopy
    • Claridge, S. A.; Thomas, J. C.; Silverman, M. A.; Schwartz, J. J.; Yang, Y. L.; Wang, C.; Weiss, P. S. Differentiating Amino Acid Residues and Side Chain Orientations in Peptides Using Scanning Tunneling Microscopy J. Am. Chem. Soc. 2013, 135, 18528-18535
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 18528-18535
    • Claridge, S.A.1    Thomas, J.C.2    Silverman, M.A.3    Schwartz, J.J.4    Yang, Y.L.5    Wang, C.6    Weiss, P.S.7
  • 30
    • 67349128044 scopus 로고    scopus 로고
    • Amyloid Beta (1-42) Folding Multiplicity and Single-Molecule Binding Behavior Studied with STM
    • Ma, X. J.; Liu, L.; Mao, X. B.; Niu, L.; Deng, K.; Wu, W. H.; Li, Y. M.; Yang, Y. L.; Wang, C. Amyloid Beta (1-42) Folding Multiplicity and Single-Molecule Binding Behavior Studied with STM J. Mol. Biol. 2009, 388, 894-901
    • (2009) J. Mol. Biol. , vol.388 , pp. 894-901
    • Ma, X.J.1    Liu, L.2    Mao, X.B.3    Niu, L.4    Deng, K.5    Wu, W.H.6    Li, Y.M.7    Yang, Y.L.8    Wang, C.9
  • 31
    • 79961063205 scopus 로고    scopus 로고
    • Observation of Reduced Cytotoxicity of Aggregated Amyloidogenic Peptides with Chaperone-Like Molecules
    • Liu, L.; Zhang, L.; Niu, L.; Xu, M.; Mao, X. B.; Yang, Y. L.; Wang, C. Observation of Reduced Cytotoxicity of Aggregated Amyloidogenic Peptides with Chaperone-Like Molecules ACS Nano 2011, 5, 6001-6007
    • (2011) ACS Nano , vol.5 , pp. 6001-6007
    • Liu, L.1    Zhang, L.2    Niu, L.3    Xu, M.4    Mao, X.B.5    Yang, Y.L.6    Wang, C.7
  • 32
    • 71949110860 scopus 로고    scopus 로고
    • Chaperon-Mediated Single Molecular Approach toward Modulating a Beta Peptide Aggregation
    • Liu, L.; Zhang, L.; Mao, X. B.; Niu, L.; Yang, Y. L.; Wang, C. Chaperon-Mediated Single Molecular Approach toward Modulating a Beta Peptide Aggregation Nano Lett. 2009, 9, 4066-4072
    • (2009) Nano Lett. , vol.9 , pp. 4066-4072
    • Liu, L.1    Zhang, L.2    Mao, X.B.3    Niu, L.4    Yang, Y.L.5    Wang, C.6
  • 36
    • 0001402095 scopus 로고
    • Two Rippled-Sheet Configurations of Polypeptide Chains, and a Note about the Pleated Sheets
    • Pauling, L.; Corey, R. B. Two Rippled-Sheet Configurations of Polypeptide Chains, and a Note about the Pleated Sheets Proc. Natl. Acad. Sci. U.S.A. 1953, 39, 253-256
    • (1953) Proc. Natl. Acad. Sci. U.S.A. , vol.39 , pp. 253-256
    • Pauling, L.1    Corey, R.B.2
  • 37
    • 24044483249 scopus 로고    scopus 로고
    • Trehalose Differentially Inhibits Aggregation and Neurotoxicity of Beta-Amyloid 40 and 42
    • Liu, R.; Barkhordarian, H.; Emadi, S.; Park, C. B.; Sierks, M. R. Trehalose Differentially Inhibits Aggregation and Neurotoxicity of Beta-Amyloid 40 and 42 Neurobiol. Dis. 2005, 20, 74-81
    • (2005) Neurobiol. Dis. , vol.20 , pp. 74-81
    • Liu, R.1    Barkhordarian, H.2    Emadi, S.3    Park, C.B.4    Sierks, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.