메뉴 건너뛰기




Volumn 247, Issue 9-10, 2014, Pages 941-947

APols-Aided Protein Precipitation: A Rapid Method for Concentrating Proteins for Proteomic Analysis

Author keywords

Amphipols; Concentrating protein; Mass spectrometry; Protein precipitation; Proteomics

Indexed keywords

AMPHIPOL; POLYMER; UNCLASSIFIED DRUG; PROTEIN; PROTEOME; SOLUTION AND SOLUBILITY; SURFACTANT;

EID: 84911004169     PISSN: 00222631     EISSN: 14321424     Source Type: Journal    
DOI: 10.1007/s00232-014-9668-6     Document Type: Article
Times cited : (17)

References (20)
  • 1
    • 84863914144 scopus 로고    scopus 로고
    • MALDI-TOF mass spectrometry analysis of amphipol-trapped membrane proteins
    • PID: 22703540, COI: 1:CAS:528:DC%2BC38XosFeksrs%3D
    • Bechara C, Bolbach G, Bazzaco P, Sharma KS, Durand G, Popot JL, Zito F, Sagan S (2012) MALDI-TOF mass spectrometry analysis of amphipol-trapped membrane proteins. Anal Chem 84(14):6128–6135. doi:10.1021/ac301035r
    • (2012) Anal Chem , vol.84 , Issue.14 , pp. 6128-6135
    • Bechara, C.1    Bolbach, G.2    Bazzaco, P.3    Sharma, K.S.4    Durand, G.5    Popot, J.L.6    Zito, F.7    Sagan, S.8
  • 2
    • 84871860708 scopus 로고    scopus 로고
    • Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples
    • PID: 23090970
    • Boersema PJ, Geiger T, Wisniewski JR, Mann M (2013) Quantification of the N-glycosylated secretome by super-SILAC during breast cancer progression and in human blood samples. Mol Cell Proteomics 12(1):158–171. doi:10.1074/mcp.M112.023614
    • (2013) Mol Cell Proteomics , vol.12 , Issue.1 , pp. 158-171
    • Boersema, P.J.1    Geiger, T.2    Wisniewski, J.R.3    Mann, M.4
  • 4
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • PID: 19029910, COI: 1:CAS:528:DC%2BD1cXhsVWjtLzJ
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26(12):1367–1372. doi:10.1038/nbt.1511
    • (2008) Nat Biotechnol , vol.26 , Issue.12 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 6
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • PID: 7108955, COI: 1:CAS:528:DyaL38Xks1yjtro%3D
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157(1):105–132
    • (1982) J Mol Biol , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 7
    • 84876541392 scopus 로고    scopus 로고
    • Direct proteomic quantification of the secretome of activated immune cells
    • PID: 23620052, COI: 1:CAS:528:DC%2BC3sXmt1yrsLw%3D
    • Meissner F, Scheltema RA, Mollenkopf HJ, Mann M (2013) Direct proteomic quantification of the secretome of activated immune cells. Science 340(6131):475–478. doi:10.1126/science.1232578
    • (2013) Science , vol.340 , Issue.6131 , pp. 475-478
    • Meissner, F.1    Scheltema, R.A.2    Mollenkopf, H.J.3    Mann, M.4
  • 8
    • 84874617914 scopus 로고    scopus 로고
    • From cells to peptides: “one-stop” integrated proteomic processing using amphipols
    • PID: 23394071, COI: 1:CAS:528:DC%2BC3sXit1Sqt74%3D
    • Ning Z, Seebun D, Hawley B, Chiang CK, Figeys D (2013) From cells to peptides: “one-stop” integrated proteomic processing using amphipols. J Proteome Res 12(3):1512–1519. doi:10.1021/pr301064z
    • (2013) J Proteome Res , vol.12 , Issue.3 , pp. 1512-1519
    • Ning, Z.1    Seebun, D.2    Hawley, B.3    Chiang, C.K.4    Figeys, D.5
  • 9
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • PID: 16249172, COI: 1:CAS:528:DC%2BD2MXhtlWqsb%2FK
    • Olsen JV, de Godoy LM, Li G, Macek B, Mortensen P, Pesch R, Makarov A, Lange O, Horning S, Mann M (2005) Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol Cell Proteomics 4(12):2010–2021. doi:10.1074/mcp.T500030-MCP200
    • (2005) Mol Cell Proteomics , vol.4 , Issue.12 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4    Mortensen, P.5    Pesch, R.6    Makarov, A.7    Lange, O.8    Horning, S.9    Mann, M.10
  • 10
    • 77954745768 scopus 로고    scopus 로고
    • Differences in the secretome of cartilage explants and cultured chondrocytes unveiled by SILAC technology
    • PID: 20108312, COI: 1:CAS:528:DC%2BC3cXhtVWmtb3L
    • Polacek M, Bruun JA, Johansen O, Martinez I (2010) Differences in the secretome of cartilage explants and cultured chondrocytes unveiled by SILAC technology. J Orthop Res 28(8):1040–1049. doi:10.1002/jor.21067
    • (2010) J Orthop Res , vol.28 , Issue.8 , pp. 1040-1049
    • Polacek, M.1    Bruun, J.A.2    Johansen, O.3    Martinez, I.4
  • 11
    • 0037420211 scopus 로고    scopus 로고
    • Optimization of protein precipitation based upon effectiveness of protein removal and ionization effect in liquid chromatography-tandem mass spectrometry
    • COI: 1:CAS:528:DC%2BD3sXmtVaksbc%3D
    • Polson C, Sarkar P, Incledon B, Raguvaran V, Grant R (2003) Optimization of protein precipitation based upon effectiveness of protein removal and ionization effect in liquid chromatography-tandem mass spectrometry. J Chromatogr B Anal Technol Biomed Life Sci 785(2):263–275
    • (2003) J Chromatogr B Anal Technol Biomed Life Sci , vol.785 , Issue.2 , pp. 263-275
    • Polson, C.1    Sarkar, P.2    Incledon, B.3    Raguvaran, V.4    Grant, R.5
  • 13
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • PID: 17703201, COI: 1:CAS:528:DC%2BD2sXhtFagtr3O
    • Rappsilber J, Mann M, Ishihama Y (2007) Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2(8):1896–1906. doi:10.1038/nprot.2007.261
    • (2007) Nat Protoc , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 14
    • 0017406459 scopus 로고
    • Acid precipitation of protein in the presence of Triton X-100 and deoxycholate
    • PID: 869188, COI: 1:CAS:528:DyaE2sXhs1Ontro%3D
    • Retz KC, Steele WJ (1977) Acid precipitation of protein in the presence of Triton X-100 and deoxycholate. Anal Biochem 79(1–2):457–461. doi:10.1016/0003-2697(77)90421-3
    • (1977) Anal Biochem , vol.79 , Issue.1-2 , pp. 457-461
    • Retz, K.C.1    Steele, W.J.2
  • 15
    • 0019975308 scopus 로고
    • Factors influencing protein structure during acid precipitation: a study of soya proteins
    • COI: 1:CAS:528:DyaL38Xkt1Ciur8%3D
    • Salt DJ, Leslie RB, Lillford PJ, Dunnill P (1982) Factors influencing protein structure during acid precipitation: a study of soya proteins. Eur J Appl Microbiol Biotechnol 14(3):144–148. doi:10.1007/BF00497890
    • (1982) Eur J Appl Microbiol Biotechnol , vol.14 , Issue.3 , pp. 144-148
    • Salt, D.J.1    Leslie, R.B.2    Lillford, P.J.3    Dunnill, P.4
  • 16
    • 84863239359 scopus 로고    scopus 로고
    • BuildSummary: using a group-based approach to improve the sensitivity of peptide/protein identification in shotgun proteomics
    • PID: 22217156, COI: 1:CAS:528:DC%2BC38XhvVCitA%3D%3D
    • Sheng Q, Dai J, Wu Y, Tang H, Zeng R (2012) BuildSummary: using a group-based approach to improve the sensitivity of peptide/protein identification in shotgun proteomics. J Proteome Res 11(3):1494–1502. doi:10.1021/pr200194p
    • (2012) J Proteome Res , vol.11 , Issue.3 , pp. 1494-1502
    • Sheng, Q.1    Dai, J.2    Wu, Y.3    Tang, H.4    Zeng, R.5
  • 17
    • 84911006806 scopus 로고    scopus 로고
    • Tehei M, Giusti, F, Zaccai, G, Popot J-L () Thermal fluctuations in amphipol A8-35 measured by neutron scattering. J Membr Biol (under review)
    • Tehei M, Giusti, F, Zaccai, G, Popot J-L (2014) Thermal fluctuations in amphipol A8-35 measured by neutron scattering. J Membr Biol (under review)
    • (2014)
  • 18
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: polymers that keep membrane proteins soluble in aqueous solutions
    • PID: 8986761, COI: 1:CAS:528:DyaK2sXmslyq
    • Tribet C, Audebert R, Popot JL (1996) Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc Natl Acad Sci USA 93(26):15047–15050
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.26 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.L.3
  • 19
    • 84864817904 scopus 로고    scopus 로고
    • PaxDb, a database of protein abundance averages across all three domains of life
    • PID: 22535208, COI: 1:STN:280:DC%2BC38rotFygtA%3D%3D
    • Wang M, Weiss M, Simonovic M, Haertinger G, Schrimpf SP, Hengartner MO, von Mering C (2012) PaxDb, a database of protein abundance averages across all three domains of life. Mol Cell Proteomics 11(8):492–500. doi:10.1074/mcp.O111.014704
    • (2012) Mol Cell Proteomics , vol.11 , Issue.8 , pp. 492-500
    • Wang, M.1    Weiss, M.2    Simonovic, M.3    Haertinger, G.4    Schrimpf, S.P.5    Hengartner, M.O.6    von Mering, C.7
  • 20
    • 21144446624 scopus 로고    scopus 로고
    • NMR study of a membrane protein in detergent-free aqueous solution
    • PID: 15956183, COI: 1:CAS:528:DC%2BD2MXlvF2qurg%3D
    • Zoonens M, Catoire LJ, Giusti F, Popot JL (2005) NMR study of a membrane protein in detergent-free aqueous solution. Proc Natl Acad Sci USA 102(25):8893–8898. doi:10.1073/pnas.0503750102
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.25 , pp. 8893-8898
    • Zoonens, M.1    Catoire, L.J.2    Giusti, F.3    Popot, J.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.