메뉴 건너뛰기




Volumn 34, Issue 4, 2013, Pages 501-504

Gel-based separation of phosphoproteins in samples stored in urea/thiourea after precipitation by lanthanum chloride

Author keywords

Gel based phosphoproteomics; Lanthanum; Posttranslational modification; Precipitation; Refolding buffer

Indexed keywords

CHLORINE COMPOUNDS; LANTHANUM COMPOUNDS; METABOLISM; MOLECULAR BIOLOGY; PRECIPITATION (CHEMICAL); PROTEINS;

EID: 84873970906     PISSN: 01730835     EISSN: 15222683     Source Type: Journal    
DOI: 10.1002/elps.201200278     Document Type: Article
Times cited : (5)

References (14)
  • 2
    • 79551503762 scopus 로고    scopus 로고
    • Catch me if you can: Mass spectrometry-based phosphoproteomics and quantification strategies
    • Eyrich, B., Sickmann, A., Zahedi, R. P., Catch me if you can: Mass spectrometry-based phosphoproteomics and quantification strategies. Proteomics 2011, 11, 554-570.
    • (2011) Proteomics , vol.11 , pp. 554-570
    • Eyrich, B.1    Sickmann, A.2    Zahedi, R.P.3
  • 3
    • 0642371059 scopus 로고    scopus 로고
    • Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets
    • Marcus, K., Moebius, J., Meyer, H. E., Differential analysis of phosphorylated proteins in resting and thrombin-stimulated human platelets. Anal. Bioanal. Chem. 2003, 376, 973-993.
    • (2003) Anal. Bioanal. Chem. , vol.376 , pp. 973-993
    • Marcus, K.1    Moebius, J.2    Meyer, H.E.3
  • 4
    • 27744563093 scopus 로고    scopus 로고
    • State-of-the-art in phosphoproteomics
    • Reinders, J., Sickmann, A., State-of-the-art in phosphoproteomics. Proteomics 2005, 5, 4052-4061.
    • (2005) Proteomics , vol.5 , pp. 4052-4061
    • Reinders, J.1    Sickmann, A.2
  • 5
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R., Thingholm, T. E., Jensen, O. N., Roepstorff, P., Jørgensen, T. J. D., Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell Proteomics 2005, 4, 873-886.
    • (2005) Mol. Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jørgensen, T.J.D.5
  • 7
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm, T. E., Jensen, O. N., Larsen, M. R., Analytical strategies for phosphoproteomics. Proteomics 2009, 9, 1451-1468.
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 8
    • 0038370011 scopus 로고    scopus 로고
    • The molecular basis for the chemical denaturation of proteins by urea
    • Bennion, B. J., Daggett, V., The molecular basis for the chemical denaturation of proteins by urea. Proc. Natl. Acad. Sci. USA 2003, 100, 5142-5147.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5142-5147
    • Bennion, B.J.1    Daggett, V.2
  • 9
    • 0026700861 scopus 로고
    • Protein folding and protein refolding
    • Seckler, R., Jaenicke, R., Protein folding and protein refolding. FASEB J. 1992, 6, 2545-2552.
    • (1992) FASEB J. , vol.6 , pp. 2545-2552
    • Seckler, R.1    Jaenicke, R.2
  • 10
    • 40049098125 scopus 로고    scopus 로고
    • Conservation of mechanism, variation of rate: Folding kinetics of three homologous four-helix bundle proteins
    • Dalal, S., Canet, D., Kaiser, S. E., Dobson, C. M., Regan, L., Conservation of mechanism, variation of rate: Folding kinetics of three homologous four-helix bundle proteins. Protein Eng. Des. Sel. 2008, 21, 197-206.
    • (2008) Protein Eng. Des. Sel. , vol.21 , pp. 197-206
    • Dalal, S.1    Canet, D.2    Kaiser, S.E.3    Dobson, C.M.4    Regan, L.5
  • 11
    • 15444374846 scopus 로고    scopus 로고
    • Role of Arginine in the Stabilization of Proteins against Aggregation
    • Baynes, B. M., Wang, D. I. C., Trout, B. L., Role of Arginine in the Stabilization of Proteins against Aggregation. Biochemistry 2005, 44, 4919-4925.
    • (2005) Biochemistry , vol.44 , pp. 4919-4925
    • Baynes, B.M.1    Wang, D.I.C.2    Trout, B.L.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 77149178707 scopus 로고    scopus 로고
    • CBB staining protocol with higher sensitivity and mass spectrometric compatibility
    • Pink, M., Verma, N., Rettenmeier, A. W., Schmitz-Spanke, S., CBB staining protocol with higher sensitivity and mass spectrometric compatibility. Electrophoresis 2010, 31, 593-598.
    • (2010) Electrophoresis , vol.31 , pp. 593-598
    • Pink, M.1    Verma, N.2    Rettenmeier, A.W.3    Schmitz-Spanke, S.4
  • 14
    • 0017578946 scopus 로고
    • Staining acidic phosphoproteins (phosvitin) in electrophoretic gels
    • Hegenauer, J., Ripley, L., Nace, G., Staining acidic phosphoproteins (phosvitin) in electrophoretic gels. Anal. Biochem. 1977, 78, 308-311.
    • (1977) Anal. Biochem. , vol.78 , pp. 308-311
    • Hegenauer, J.1    Ripley, L.2    Nace, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.