메뉴 건너뛰기




Volumn 11, Issue 7, 2015, Pages 1134-1146

Quantitative Interaction Proteomics of Neurodegenerative Disease Proteins

(103)  Hosp, Fabian a,f   Vossfeldt, Hannes b   Heinig, Matthias a,c   Vasiljevic, Djordje a   Arumughan, Anup a   Wyler, Emanuel a   Landthaler, Markus a   Hubner, Norbert a   Wanker, Erich E a   Lannfelt, Lars d   Ingelsson, Martin d   Lalowski, Maciej e   Voigt, Aaron b   Selbach, Matthias a   Harold, Denise g   Abraham, Richard g   Hollingworth, Paul g   Sims, Rebecca g   Gerrish, Amy g   Chapman, Jade g   more..


Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; ATAXIN 1; HUNTINGTIN; MITOCHONDRIAL PROTEIN; PARKIN; PRESENILIN 1; PROTEIN LRPPRC; UNCLASSIFIED DRUG;

EID: 84929709547     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2015.04.030     Document Type: Article
Times cited : (79)

References (61)
  • 1
    • 0037437192 scopus 로고    scopus 로고
    • Mitochondrial targeting and a novel transmembrane arrest of Alzheimer’s amyloid precursor protein impairs mitochondrial function in neuronal cells
    • Anandatheerthavarada H.K., Biswas G., Robin M.A., Avadhani N.G. Mitochondrial targeting and a novel transmembrane arrest of Alzheimer’s amyloid precursor protein impairs mitochondrial function in neuronal cells. J.Cell Biol. 2003, 161:41-54.
    • (2003) J.Cell Biol. , vol.161 , pp. 41-54
    • Anandatheerthavarada, H.K.1    Biswas, G.2    Robin, M.A.3    Avadhani, N.G.4
  • 2
    • 78650373804 scopus 로고    scopus 로고
    • Network medicine: a network-based approach to human disease
    • Barabási A.L., Gulbahce N., Loscalzo J. Network medicine: a network-based approach to human disease. Nat. Rev. Genet. 2011, 12:56-68.
    • (2011) Nat. Rev. Genet. , vol.12 , pp. 56-68
    • Barabási, A.L.1    Gulbahce, N.2    Loscalzo, J.3
  • 3
    • 57649203362 scopus 로고    scopus 로고
    • Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model
    • Chatterjee S., Sang T.K., Lawless G.M., Jackson G.R. Dissociation of tau toxicity and phosphorylation: role of GSK-3beta, MARK and Cdk5 in a Drosophila model. Hum. Mol. Genet. 2009, 18:164-177.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 164-177
    • Chatterjee, S.1    Sang, T.K.2    Lawless, G.M.3    Jackson, G.R.4
  • 6
    • 0027495515 scopus 로고
    • Evidence for a mechanism predisposing to intergenerational CAG repeat instability in spinocerebellar ataxia type I
    • Chung M.Y., Ranum L.P., Duvick L.A., Servadio A., Zoghbi H.Y., Orr H.T. Evidence for a mechanism predisposing to intergenerational CAG repeat instability in spinocerebellar ataxia type I. Nat. Genet. 1993, 5:254-258.
    • (1993) Nat. Genet. , vol.5 , pp. 254-258
    • Chung, M.Y.1    Ranum, L.P.2    Duvick, L.A.3    Servadio, A.4    Zoghbi, H.Y.5    Orr, H.T.6
  • 7
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 2008, 26:1367-1372.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 8
    • 77957360461 scopus 로고    scopus 로고
    • Partial loss of ataxin-1 function contributes to transcriptional dysregulation in spinocerebellar ataxia type 1 pathogenesis
    • Crespo-Barreto J., Fryer J.D., Shaw C.A., Orr H.T., Zoghbi H.Y. Partial loss of ataxin-1 function contributes to transcriptional dysregulation in spinocerebellar ataxia type 1 pathogenesis. PLoS Genet. 2010, 6:e1001021.
    • (2010) PLoS Genet. , vol.6 , pp. e1001021
    • Crespo-Barreto, J.1    Fryer, J.D.2    Shaw, C.A.3    Orr, H.T.4    Zoghbi, H.Y.5
  • 9
    • 71949090833 scopus 로고    scopus 로고
    • Mitochondrial trafficking ofAPP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer’s and Parkinson’s diseases
    • Devi L., Anandatheerthavarada H.K. Mitochondrial trafficking ofAPP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer’s and Parkinson’s diseases. Biochim. Biophys. Acta 2010, 1802:11-19.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 11-19
    • Devi, L.1    Anandatheerthavarada, H.K.2
  • 10
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer’s disease brain is associated with mitochondrial dysfunction
    • Devi L., Prabhu B.M., Galati D.F., Avadhani N.G., Anandatheerthavarada H.K. Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer’s disease brain is associated with mitochondrial dysfunction. J.Neurosci. 2006, 26:9057-9068.
    • (2006) J.Neurosci. , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 13
    • 0029092610 scopus 로고
    • Correlation of two-hybrid affinity data with invitro measurements
    • Estojak J., Brent R., Golemis E.A. Correlation of two-hybrid affinity data with invitro measurements. Mol. Cell. Biol. 1995, 15:5820-5829.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5820-5829
    • Estojak, J.1    Brent, R.2    Golemis, E.A.3
  • 16
    • 0036121191 scopus 로고    scopus 로고
    • Aconitase: sensitive target and measure of superoxide
    • Gardner P.R. Aconitase: sensitive target and measure of superoxide. Methods Enzymol. 2002, 349:9-23.
    • (2002) Methods Enzymol. , vol.349 , pp. 9-23
    • Gardner, P.R.1
  • 17
    • 84864619937 scopus 로고    scopus 로고
    • Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactions
    • Gingras A.C., Raught B. Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactions. FEBS Lett. 2012, 586:2723-2731.
    • (2012) FEBS Lett. , vol.586 , pp. 2723-2731
    • Gingras, A.C.1    Raught, B.2
  • 24
    • 56649097558 scopus 로고    scopus 로고
    • GSEA-SNP: applying gene set enrichment analysis to SNP data from genome-wide association studies
    • Holden M., Deng S., Wojnowski L., Kulle B. GSEA-SNP: applying gene set enrichment analysis to SNP data from genome-wide association studies. Bioinformatics 2008, 24:2784-2785.
    • (2008) Bioinformatics , vol.24 , pp. 2784-2785
    • Holden, M.1    Deng, S.2    Wojnowski, L.3    Kulle, B.4
  • 25
    • 41649119247 scopus 로고    scopus 로고
    • Protein networks in disease
    • Ideker T., Sharan R. Protein networks in disease. Genome Res. 2008, 18:644-652.
    • (2008) Genome Res. , vol.18 , pp. 644-652
    • Ideker, T.1    Sharan, R.2
  • 26
    • 0347064343 scopus 로고    scopus 로고
    • A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death
    • Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R. A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death. J.Biol. Chem. 2003, 278:51901-51910.
    • (2003) J.Biol. Chem. , vol.278 , pp. 51901-51910
    • Imai, Y.1    Soda, M.2    Murakami, T.3    Shoji, M.4    Abe, K.5    Takahashi, R.6
  • 29
    • 0037144422 scopus 로고    scopus 로고
    • Complex N-linked glycosylated nicastrin associates withactive gamma-secretase and undergoes tight cellular regulation
    • Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., Selkoe D.J. Complex N-linked glycosylated nicastrin associates withactive gamma-secretase and undergoes tight cellular regulation. J.Biol. Chem. 2002, 277:35113-35117.
    • (2002) J.Biol. Chem. , vol.277 , pp. 35113-35117
    • Kimberly, W.T.1    LaVoie, M.J.2    Ostaszewski, B.L.3    Ye, W.4    Wolfe, M.S.5    Selkoe, D.J.6
  • 34
    • 33750683018 scopus 로고    scopus 로고
    • Alzheimer’s APP mangles mitochondria
    • Lin M.T., Beal M.F. Alzheimer’s APP mangles mitochondria. Nat. Med. 2006, 12:1241-1243.
    • (2006) Nat. Med. , vol.12 , pp. 1241-1243
    • Lin, M.T.1    Beal, M.F.2
  • 35
    • 84903521521 scopus 로고    scopus 로고
    • Genetics and genomics of Parkinson’s disease
    • Lin M.K., Farrer M.J. Genetics and genomics of Parkinson’s disease. Genome Med. 2014, 6:48.
    • (2014) Genome Med. , vol.6 , pp. 48
    • Lin, M.K.1    Farrer, M.J.2
  • 38
    • 0042847291 scopus 로고    scopus 로고
    • Neurotoxic mechanisms caused by the Alzheimer’s disease-linked Swedish amyloid precursor protein mutation: oxidative stress, caspases, and the JNK pathway
    • Marques C.A., Keil U., Bonert A., Steiner B., Haass C., Muller W.E., Eckert A. Neurotoxic mechanisms caused by the Alzheimer’s disease-linked Swedish amyloid precursor protein mutation: oxidative stress, caspases, and the JNK pathway. J.Biol. Chem. 2003, 278:28294-28302.
    • (2003) J.Biol. Chem. , vol.278 , pp. 28294-28302
    • Marques, C.A.1    Keil, U.2    Bonert, A.3    Steiner, B.4    Haass, C.5    Muller, W.E.6    Eckert, A.7
  • 40
    • 33845918450 scopus 로고    scopus 로고
    • Beta-amyloid precursor protein is a direct cleavage target of HtrA2 serine protease. Implications for the physiological function of HtrA2 in the mitochondria
    • Park H.J., Kim S.S., Seong Y.M., Kim K.H., Goo H.G., Yoon E.J., Min S., Kang S., Rhim H. Beta-amyloid precursor protein is a direct cleavage target of HtrA2 serine protease. Implications for the physiological function of HtrA2 in the mitochondria. J.Biol. Chem. 2006, 281:34277-34287.
    • (2006) J.Biol. Chem. , vol.281 , pp. 34277-34287
    • Park, H.J.1    Kim, S.S.2    Seong, Y.M.3    Kim, K.H.4    Goo, H.G.5    Yoon, E.J.6    Min, S.7    Kang, S.8    Rhim, H.9
  • 41
    • 79959211995 scopus 로고    scopus 로고
    • Analyzing protein-protein interactions by quantitative mass spectrometry
    • Paul F.E., Hosp F., Selbach M. Analyzing protein-protein interactions by quantitative mass spectrometry. Methods 2011, 54:387-395.
    • (2011) Methods , vol.54 , pp. 387-395
    • Paul, F.E.1    Hosp, F.2    Selbach, M.3
  • 43
    • 33947182552 scopus 로고    scopus 로고
    • An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
    • Rinner O., Mueller L.N., Hubálek M., Müller M., Gstaiger M., Aebersold R. An integrated mass spectrometric and computational framework for the analysis of protein interaction networks. Nat. Biotechnol. 2007, 25:345-352.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 345-352
    • Rinner, O.1    Mueller, L.N.2    Hubálek, M.3    Müller, M.4    Gstaiger, M.5    Aebersold, R.6
  • 44
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross C.A., Poirier M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10(Suppl):S10-S17.
    • (2004) Nat. Med. , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 45
    • 79851502150 scopus 로고    scopus 로고
    • Proteins encoded in genomic regions associated with immune-mediated disease physically interact and suggest underlying biology
    • Rossin E.J., Lage K., Raychaudhuri S., Xavier R.J., Tatar D., Benita Y., Cotsapas C., Daly M.J. Proteins encoded in genomic regions associated with immune-mediated disease physically interact and suggest underlying biology. PLoS Genet. 2011, 7:e1001273. International Inflammatory Bowel Disease Genetics Constortium.
    • (2011) PLoS Genet. , vol.7 , pp. e1001273
    • Rossin, E.J.1    Lage, K.2    Raychaudhuri, S.3    Xavier, R.J.4    Tatar, D.5    Benita, Y.6    Cotsapas, C.7    Daly, M.J.8
  • 47
    • 0029997090 scopus 로고    scopus 로고
    • Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36-39 repeats
    • Rubinsztein D.C., Leggo J., Coles R., Almqvist E., Biancalana V., Cassiman J.J., Chotai K., Connarty M., Crauford D., Curtis A., et al. Phenotypic characterization of individuals with 30-40 CAG repeats in the Huntington disease (HD) gene reveals HD cases with 36 repeats and apparently normal elderly individuals with 36-39 repeats. Am. J. Hum. Genet. 1996, 59:16-22.
    • (1996) Am. J. Hum. Genet. , vol.59 , pp. 16-22
    • Rubinsztein, D.C.1    Leggo, J.2    Coles, R.3    Almqvist, E.4    Biancalana, V.5    Cassiman, J.J.6    Chotai, K.7    Connarty, M.8    Crauford, D.9    Curtis, A.10
  • 49
    • 77950901962 scopus 로고    scopus 로고
    • LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria
    • Sasarman F., Brunel-Guitton C., Antonicka H., Wai T., Shoubridge E.A. LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria. Mol. Biol. Cell 2010, 21:1315-1323. LSFC Consortium.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1315-1323
    • Sasarman, F.1    Brunel-Guitton, C.2    Antonicka, H.3    Wai, T.4    Shoubridge, E.A.5
  • 50
    • 45949108954 scopus 로고    scopus 로고
    • Protein interactions in human genetic diseases
    • Schuster-Böckler B., Bateman A. Protein interactions in human genetic diseases. Genome Biol. 2008, 9:R9.
    • (2008) Genome Biol. , vol.9 , pp. R9
    • Schuster-Böckler, B.1    Bateman, A.2
  • 54
    • 13944276825 scopus 로고    scopus 로고
    • Twenty years of the Alzheimer’s disease amyloid hypothesis: a genetic perspective
    • Tanzi R.E., Bertram L. Twenty years of the Alzheimer’s disease amyloid hypothesis: a genetic perspective. Cell 2005, 120:545-555.
    • (2005) Cell , vol.120 , pp. 545-555
    • Tanzi, R.E.1    Bertram, L.2
  • 55
    • 49549121813 scopus 로고    scopus 로고
    • High confidence determination of specific protein-protein interactions using quantitative mass spectrometry
    • Vermeulen M., Hubner N.C., Mann M. High confidence determination of specific protein-protein interactions using quantitative mass spectrometry. Curr. Opin. Biotechnol. 2008, 19:331-337.
    • (2008) Curr. Opin. Biotechnol. , vol.19 , pp. 331-337
    • Vermeulen, M.1    Hubner, N.C.2    Mann, M.3
  • 56
    • 79952674000 scopus 로고    scopus 로고
    • Interactome networks and human disease
    • Vidal M., Cusick M.E., Barabási A.L. Interactome networks and human disease. Cell 2011, 144:986-998.
    • (2011) Cell , vol.144 , pp. 986-998
    • Vidal, M.1    Cusick, M.E.2    Barabási, A.L.3
  • 59
    • 52049093169 scopus 로고    scopus 로고
    • Polyglutamine neurodegeneration: protein misfolding revisited
    • Williams A.J., Paulson H.L. Polyglutamine neurodegeneration: protein misfolding revisited. Trends Neurosci. 2008, 31:521-528.
    • (2008) Trends Neurosci. , vol.31 , pp. 521-528
    • Williams, A.J.1    Paulson, H.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.