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Volumn 13, Issue 5, 2013, Pages 797-801

Novel approaches for studying amyloidogenic peptides/proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; AMYLOID PROTEIN; EPIGALLOCATECHIN GALLATE; IMMUNOGLOBULIN LIGHT CHAIN;

EID: 84892992289     PISSN: 14714892     EISSN: 14714973     Source Type: Journal    
DOI: 10.1016/j.coph.2013.05.010     Document Type: Review
Times cited : (15)

References (45)
  • 1
    • 79955842001 scopus 로고    scopus 로고
    • Amyloidosis: Pathogenesis and new therapeutic options
    • Merlini G, Seldin DC, Gertz MA: Amyloidosis: pathogenesis and new therapeutic options. J Clin Oncol 2011, 29: 1924-1933.
    • (2011) J Clin Oncol , vol.29 , pp. 1924-1933
    • Merlini, G.1    Seldin, D.C.2    Gertz, M.A.3
  • 2
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM: Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006, 75: 333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: Experimental approaches, mechanism of formation, and structure-toxicity relationships
    • Bemporad F, Chiti F: Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem Biol 2012, 19: 315-327.
    • (2012) Chem Biol , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 4
    • 84857642949 scopus 로고    scopus 로고
    • The toxic Ab oligomer and Alzheimer's disease: An emperor in need of clothes
    • Benilova I, Karran E, De Strooper B: The toxic Ab oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 2012, 15: 349-357.
    • (2012) Nat Neurosci , vol.15 , pp. 349-357
    • Benilova, I.1    Karran, E.2    De Strooper, B.3
  • 5
    • 84877346858 scopus 로고    scopus 로고
    • Analysis of protein aggregation in neurodegenerative disease
    • Epub ahead of print
    • Pedersen JT, Heegaard NH: Analysis of protein aggregation in neurodegenerative disease. Anal Chem 2013 http://dx.doi.org/10.1021/ac400023c. Epub ahead of print.
    • (2013) Anal Chem
    • Pedersen, J.T.1    Heegaard, N.H.2
  • 7
    • 33845902552 scopus 로고    scopus 로고
    • Higher-throughput, label-free, real-time molecular interaction analysis
    • DOI 10.1016/j.ab.2006.10.040, PII S0003269706008037
    • Rich RL, Myszka DG: Higher-throughput, label-free, real-time molecular interaction analysis. Anal Biochem 2007, 361: 1-6. (Pubitemid 46026999)
    • (2007) Analytical Biochemistry , vol.361 , Issue.1 , pp. 1-6
    • Rich, R.L.1    Myszka, D.G.2
  • 8
    • 77950937554 scopus 로고    scopus 로고
    • Development of a proteolytically stable retro-inverso peptide inhibitor of b-amyloid oligomerization as a potential novel treatment for Alzheimer's disease
    • Taylor M, Moore S, Mayes J, Parkin E, Beeg M, Canovi M, Gobbi M, Mann DM, Allsop D: Development of a proteolytically stable retro-inverso peptide inhibitor of b-amyloid oligomerization as a potential novel treatment for Alzheimer's disease. Biochemistry 2010, 49: 3261-3272.
    • (2010) Biochemistry , vol.49 , pp. 3261-3272
    • Taylor, M.1    Moore, S.2    Mayes, J.3    Parkin, E.4    Beeg, M.5    Canovi, M.6    Gobbi, M.7    Mann, D.M.8    Allsop, D.9
  • 10
    • 78650626543 scopus 로고    scopus 로고
    • Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Ab(1-42) peptide, synthesized by depsi-peptide technique
    • Stravalaci M, Beeg M, Salmona M, Gobbi M: Use of surface plasmon resonance to study the elongation kinetics and the binding properties of the highly amyloidogenic Ab(1-42) peptide, synthesized by depsi-peptide technique. Biosens Bioelectron 2011, 26: 2772-2775.
    • (2011) Biosens Bioelectron , vol.26 , pp. 2772-2775
    • Stravalaci, M.1    Beeg, M.2    Salmona, M.3    Gobbi, M.4
  • 16
    • 78649754766 scopus 로고    scopus 로고
    • Amyloid-b oligomer specificity mediated by the IgM isotype - Implications for a specific protective mechanism exerted by endogenous auto-antibodies
    • Lindhagen-Persson M, Brännström K, Vestling M, Steinitz M, Olofsson A: Amyloid-b oligomer specificity mediated by the IgM isotype - implications for a specific protective mechanism exerted by endogenous auto-antibodies. PLoS ONE 2010, 5:e13928.
    • (2010) PLoS ONE , vol.5
    • Lindhagen-Persson, M.1    Brännström, K.2    Vestling, M.3    Steinitz, M.4    Olofsson, A.5
  • 17
    • 84865040298 scopus 로고    scopus 로고
    • Specific recognition of biologically active amyloid-beta oligomers by a new surface plasmon resonance-based immunoassay and an in vivo assay in Caenorhabditis elegans
    • Stravalaci M, Bastone A, Beeg M, Cagnotto A, Colombo L, Di Fede G, Tagliavini F, Cantu L, Del Favero E, Mazzanti M et al.: Specific recognition of biologically active amyloid-beta oligomers by a new surface plasmon resonance-based immunoassay and an in vivo assay in Caenorhabditis elegans. J Biol Chem 2012, 287: 27796-27805.
    • (2012) J Biol Chem , vol.287 , pp. 27796-27805
    • Stravalaci, M.1    Bastone, A.2    Beeg, M.3    Cagnotto, A.4    Colombo, L.5    Di Fede, G.6    Tagliavini, F.7    Cantu, L.8    Del Favero, E.9    Mazzanti, M.10
  • 18
    • 1842686289 scopus 로고    scopus 로고
    • Kinetic analysis of beta-amyloid fibril elongation
    • DOI 10.1016/j.ab.2004.01.014, PII S0003269704000922
    • Cannon MJ, Williams AD, Wetzel R, Myszka DG: Kinetic analysis of b-amyloid fibril elongation. Anal Biochem 2004, 328: 67-75. (Pubitemid 38479619)
    • (2004) Analytical Biochemistry , vol.328 , Issue.1 , pp. 67-75
    • Cannon, M.J.1    Williams, A.D.2    Wetzel, R.3    Myszka, D.G.4
  • 19
    • 41849116004 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of Alzheimer's β-amyloid aggregation on a solid surface: From monomers to fully-grown fibrils
    • DOI 10.1021/ac7019514
    • Ryu J, Joung HA, Kim MG, Park CB: Surface plasmon resonance analysis of Alzheimer's b-amyloid aggregation on a solid surface: from monomers to fully-grown fibrils. Anal Chem 2008, 80: 2400-2407. (Pubitemid 351499821)
    • (2008) Analytical Chemistry , vol.80 , Issue.7 , pp. 2400-2407
    • Ryu, J.1    Joung, H.-A.2    Kim, M.-G.3    Chan, B.P.4
  • 21
    • 79952453932 scopus 로고    scopus 로고
    • A modified protocol to prepare seed-free starting solutions of amyloid-b Ab(1-40) and Ab (1-42) from the corresponding depsipeptides
    • Beeg M, Stravalaci M, Bastone A, Salmona M, Gobbi M: A modified protocol to prepare seed-free starting solutions of amyloid-b Ab(1-40) and Ab (1-42) from the corresponding depsipeptides. Anal Biochem 2011, 411: 297-299.
    • (2011) Anal Biochem , vol.411 , pp. 297-299
    • Beeg, M.1    Stravalaci, M.2    Bastone, A.3    Salmona, M.4    Gobbi, M.5
  • 23
    • 84864634085 scopus 로고    scopus 로고
    • Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances
    • Buell AK, Dobson CM, Welland ME: Measuring the kinetics of amyloid fibril elongation using quartz crystal microbalances. Methods Mol Biol 2012, 849: 101-119.
    • (2012) Methods Mol Biol , vol.849 , pp. 101-119
    • Buell, A.K.1    Dobson, C.M.2    Welland, M.E.3
  • 27
    • 57649148788 scopus 로고    scopus 로고
    • Structural classification of toxic amyloid oligomers
    • Glabe CG: Structural classification of toxic amyloid oligomers. J Biol Chem 2008, 283: 29639-29643.
    • (2008) J Biol Chem , vol.283 , pp. 29639-29643
    • Glabe, C.G.1
  • 30
    • 77951554481 scopus 로고    scopus 로고
    • Caenorhabditis elegans as a model system to study intercompartmental proteostasis: Interrelation of mitochondrial function, longevity, and neurodegenerative diseases
    • Kirstein-Miles J, Morimoto RI: Caenorhabditis elegans as a model system to study intercompartmental proteostasis: interrelation of mitochondrial function, longevity, and neurodegenerative diseases. Dev Dyn 2010, 239: 1529-1538.
    • (2010) Dev Dyn , vol.239 , pp. 1529-1538
    • Kirstein-Miles, J.1    Morimoto, R.I.2
  • 31
    • 17644382712 scopus 로고    scopus 로고
    • Invertebrate models of Alzheimer's disease
    • DOI 10.1111/j.1601-183X.2004.00105.x
    • Link CD: Invertebrate models of Alzheimer's disease. Genes Brain Behav 2005, 4: 147-156. (Pubitemid 40559141)
    • (2005) Genes, Brain and Behavior , vol.4 , Issue.3 , pp. 147-156
    • Link, C.D.1
  • 32
    • 33751397131 scopus 로고    scopus 로고
    • C. Elegans models of age-associated neurodegenerative diseases: Lessons from transgenic worm models of Alzheimer's disease
    • DOI 10.1016/j.exger.2006.06.059, PII S0531556506002385
    • Link CD: C. elegans models of age-associated neurodegenerative diseases: lessons from transgenic worm models of Alzheimer's disease. Exp Gerontol 2006, 41: 1007-1013. (Pubitemid 44821699)
    • (2006) Experimental Gerontology , vol.41 , Issue.10 , pp. 1007-1013
    • Link, C.D.1
  • 33
    • 77951975674 scopus 로고    scopus 로고
    • Heat shock treatment reduces b-amyloid toxicity in vivo by diminishing oligomers
    • Wu Y, Cao Z, Klein WL, Luo Y: Heat shock treatment reduces b-amyloid toxicity in vivo by diminishing oligomers. Neurobiol Aging 2010, 31: 1055-1058.
    • (2010) Neurobiol Aging , vol.31 , pp. 1055-1058
    • Wu, Y.1    Cao, Z.2    Klein, W.L.3    Luo, Y.4
  • 35
    • 84881396342 scopus 로고    scopus 로고
    • A new face for old antibiotics: Tetracyclines in treatment of amyloidoses
    • Epub ahead of print
    • Stoilova T, Colombo L, Forloni G, Tagliavini F, Salmona M: A new face for old antibiotics: tetracyclines in treatment of amyloidoses. J Med Chem 2013 http://dx.doi.org/10.1021/jm400161p. Epub ahead of print.
    • (2013) J Med Chem
    • Stoilova, T.1    Colombo, L.2    Forloni, G.3    Tagliavini, F.4    Salmona, M.5
  • 37
    • 77952580505 scopus 로고    scopus 로고
    • Mouse model to study human Ab2M amyloidosis: Generation of a transgenic mouse with excessive expression of human b2-microglobulin
    • Zhang P, Fu X, Sawashita J, Yao J, Zhang B, Qian J, Tomozawa H, Mori M, Ando Y, Naiki H et al.: Mouse model to study human Ab2M amyloidosis: generation of a transgenic mouse with excessive expression of human b2-microglobulin. Amyloid 2010, 17: 50-62.
    • (2010) Amyloid , vol.17 , pp. 50-62
    • Zhang, P.1    Fu, X.2    Sawashita, J.3    Yao, J.4    Zhang, B.5    Qian, J.6    Tomozawa, H.7    Mori, M.8    Ando, Y.9    Naiki, H.10
  • 38
    • 84868358491 scopus 로고    scopus 로고
    • Overexpression of human amyloidogenic light chains causes heart failure in embryonic zebrafish: A preliminary report
    • Shin JT, Ward JE, Collins PA, Dai M, Semigran HL, Semigran MJ, Seldin DC: Overexpression of human amyloidogenic light chains causes heart failure in embryonic zebrafish: a preliminary report. Amyloid 2012, 19: 191-196.
    • (2012) Amyloid , vol.19 , pp. 191-196
    • Shin, J.T.1    Ward, J.E.2    Collins, P.A.3    Dai, M.4    Semigran, H.L.5    Semigran, M.J.6    Seldin, D.C.7
  • 41
    • 0033168208 scopus 로고    scopus 로고
    • Feeding is inhibited by sublethal concentrations of toxicants and by heat stress in the nematode Caenorhabditis elegans: Relationship to the cellular stress response
    • DOI 10.1002/(SICI)1097-010X(19990701)284:2<147::AID-JEZ4>3.0.CO;2-Z
    • Jones D, Candido EP: Feeding is inhibited by sublethal concentrations of toxicants and by heat stress in the nematode Caenorhabditis elegans: relationship to the cellular stress response. J Exp Zool 1999, 284: 147-157. (Pubitemid 29311513)
    • (1999) Journal of Experimental Zoology , vol.284 , Issue.2 , pp. 147-157
    • Jones, D.1    Candido, E.P.M.2
  • 42
    • 33646597285 scopus 로고    scopus 로고
    • Circulating amyloidogenic free light chains and serum N-terminal natriuretic peptide type B decrease simultaneously in association with improvement of survival in AL
    • DOI 10.1182/blood-2005-11-4385
    • Palladini G, Lavatelli F, Russo P, Perlini S, Perfetti V, Bosoni T, Obici L, Bradwell AR, D'Eril GM, Fogari R et al.: Circulating amyloidogenic free light chains and serum N-terminal natriuretic peptide type B decrease simultaneously in association with improvement of survival in AL. Blood 2006, 107: 3854-3858. (Pubitemid 43726787)
    • (2006) Blood , vol.107 , Issue.10 , pp. 3854-3858
    • Palladini, G.1    Lavatelli, F.2    Russo, P.3    Perlini, S.4    Perfetti, V.5    Bosoni, T.6    Obici, L.7    Bradwell, A.R.8    D'Eril, G.M.9    Fogari, R.10    Moratti, R.11    Merlini, G.12
  • 43
    • 0035797855 scopus 로고    scopus 로고
    • Infusion of light chains from patients with cardiac amyloidosis causes diastolic dysfunction in isolated mouse hearts
    • Liao R, Jain M, Teller P, Connors LH, Ngoy S, Skinner M, Falk RH, Apstein CS: Infusion of light chains from patients with cardiac amyloidosis causes diastolic dysfunction in isolated mouse hearts. Circulation 2001, 104: 1594-1597. (Pubitemid 32947519)
    • (2001) Circulation , vol.104 , Issue.14 , pp. 1594-1597
    • Liao, R.1    Jain, M.2    Teller, P.3    Connors, L.H.4    Ngoy, S.5    Skinner, M.6    Falk, R.H.7    Apstein, C.S.8
  • 44
    • 2342525940 scopus 로고    scopus 로고
    • Human Amyloidogenic Light Chains Directly Impair Cardiomyocyte Function Through an Increase in Cellular Oxidant Stress
    • DOI 10.1161/01.RES.0000126569.75419.74
    • Brenner DA, Jain M, Pimentel DR, Wang B, Connors LH, Skinner M, Apstein CS, Liao R: Human amyloidogenic light chains directly impair cardiomyocyte function through an increase in cellular oxidant stress. Circ Res 2004, 94: 1008-1010. (Pubitemid 38579694)
    • (2004) Circulation Research , vol.94 , Issue.8 , pp. 1008-1010
    • Brenner, D.A.1    Jain, M.2    Pimentel, D.R.3    Wang, B.4    Connors, L.H.5    Skinner, M.6    Apstein, C.S.7    Liao, R.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.