메뉴 건너뛰기




Volumn 432, Issue , 2008, Pages 175-183

Protocol to enrich and analyze plasma membrane proteins from frozen tissues

Author keywords

Frozen tissue; Membrane proteins; Mouse brain; Plasma membrane

Indexed keywords


EID: 84934436616     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-28-7_12     Document Type: Article
Times cited : (6)

References (12)
  • 1
    • 0038025565 scopus 로고    scopus 로고
    • Proteomics in brain research: Potentials and limitations
    • Lubec, G., Krapfenbauer, K., and Fountoulakis, M. (2003) Proteomics in brain research: potentials and limitations. Prog. Neurobiol. 69, 193-211.
    • (2003) Prog. Neurobiol , vol.69 , pp. 193-211
    • Lubec, G.1    Krapfenbauer, K.2    Fountoulakis, M.3
  • 3
    • 2142721825 scopus 로고    scopus 로고
    • HysTag-a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain
    • Olsen, J. V., Andersen, J. R., Nielsen, P. Aa., Nielsen, M. L., Figeys, D., Mann, M., et al. (2004) HysTag-a novel proteomic quantification tool applied to differential display analysis of membrane proteins from distinct areas of mouse brain. Mol. Cell. Proteomics 3, 82-92.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 82-92
    • Olsen, J.V.1    Andersen, J.R.2    Nielsen, P.A.3    Nielsen, M.L.4    Figeys, D.5    Mann, M.6
  • 5
    • 33750106380 scopus 로고    scopus 로고
    • Differential analysis of membrane proteins in mouse fore- and hindbrain using a label-free approach
    • Le Bihan, T., Goh, T., Stewart, I. I., Salter, A.-M., Bukhman, Y., Dharsee, M., et al. (2006) Differential analysis of membrane proteins in mouse fore- and hindbrain using a label-free approach. J. Proteome Res. 5, 2701-2710.
    • (2006) J. Proteome Res , vol.5 , pp. 2701-2710
    • Le Bihan, T.1    Goh, T.2    Stewart, I.I.3    Salter, A.-M.4    Bukhman, Y.5    Dharsee, M.6
  • 6
    • 33846376260 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of membrane proteins from the mouse brain cortex, hippocampus, and cerebellum using the HysTag reagent: Mapping of neurotransmitter receptors and ion channels
    • Olsen, J. V., Nielsen, P. Aa., Andersen, J. R., Mann, M., and Wísniewski, J. R (2007) Quantitative proteomic profiling of membrane proteins from the mouse brain cortex, hippocampus, and cerebellum using the HysTag reagent: Mapping of neurotransmitter receptors and ion channels. Brain Res., 1134, 95-106.
    • (2007) Brain Res , vol.1134 , pp. 95-106
    • Olsen, J.V.1    Nielsen, P.A.2    Andersen, J.R.3    Mann, M.4    Wísniewski, J.R.5
  • 8
    • 0020039866 scopus 로고
    • Isolation of intracellular membranes by means of sodium carbonate treatment: Application to endoplasmic reticulum
    • Fujiki, Y., Hubbard, A. L., Fowler, S., and Lazarow, P. B. (1982) Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum. J. Cell Biol. 93, 97-102.
    • (1982) J. Cell Biol , vol.93 , pp. 97-102
    • Fujiki, Y.1    Hubbard, A.L.2    Fowler, S.3    Lazarow, P.B.4
  • 9
    • 0031030055 scopus 로고    scopus 로고
    • Structural and functional consequences of mutations within the hydrophobic cores of the HMG1- box domain of the Chironomus high-mobility-group protein 1a
    • Wísniewski, J. R., Heßler, K., Claus, P., and Zechel, K. (1997) Structural and functional consequences of mutations within the hydrophobic cores of the HMG1- box domain of the Chironomus high-mobility-group protein 1a. Eur. J. Biochem. 243, 151-159.
    • (1997) Eur. J. Biochem , vol.243 , pp. 151-159
    • Wísniewski, J.R.1    Heßler, K.2    Claus, P.3    Zechel, K.4
  • 10
    • 0003409056 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton, T. E, ed, pp, IRL Press, Oxford, New York, and Tokyo
    • Pace, C. N., Shirley, B. A., and Thompson, J. A. (1989) Measuring the conformational stability of a protein. In Protein Structure - Practical Approach (Creighton, T. E., ed.), pp. 311-330, IRL Press, Oxford, New York, and Tokyo.
    • (1989) Protein Structure - Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thompson, J.A.3
  • 11
    • 0016370945 scopus 로고
    • Analytical study of microsomes and isolated subcellular membranes from rat liver. II. Preparation and composition of the microsomal fraction
    • Amar-Costesec, A., Beaufay, H., Wibo, M., Thines-Sempoux, D., Feytmans, E., Robbi, M., et al. (1974) Analytical study of microsomes and isolated subcellular membranes from rat liver. II. Preparation and composition of the microsomal fraction. J. Cell Biol. 61, 201-212.
    • (1974) J. Cell Biol , vol.61 , pp. 201-212
    • Amar-Costesec, A.1    Beaufay, H.2    Wibo, M.3    Thines-Sempoux, D.4    Feytmans, E.5    Robbi, M.6
  • 12
    • 20144365752 scopus 로고    scopus 로고
    • Experimental peptide identification repository (EPIR): An integrated peptide-centric platform for validation and mining of tandem mass spectrometry data
    • Kristensen, D. B, Børnd, J. C., Nielsen, P. Aa, Andersen, J. R., Sørensen, O. T., Jørgensen, V., et al. (2004) Experimental peptide identification repository (EPIR): an integrated peptide-centric platform for validation and mining of tandem mass spectrometry data. Mol. Cell. Proteomics 3, 1023-1038.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1023-1038
    • Kristensen, D.B.1    Børnd, J.C.2    Nielsen, P.A.3    Andersen, J.R.4    Sørensen, O.T.5    Jørgensen, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.