메뉴 건너뛰기




Volumn 74, Issue 2, 2011, Pages 167-185

Identification of human, rat and chicken ribosomal proteins by a combination of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry

Author keywords

Chicken; Human; Mass spectrometry; Rat; Ribosomal proteins; Two dimensional polyacrylamide gel electrophoresis

Indexed keywords

RIBOSOME PROTEIN; TRYPSIN;

EID: 78650304557     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2010.10.007     Document Type: Article
Times cited : (3)

References (23)
  • 1
    • 0002443434 scopus 로고
    • A small particulate component of the cytoplasm
    • Palade G.E. A small particulate component of the cytoplasm. J Biophys Biochem Cytol Jan. 1955, 1(1):59-68.
    • (1955) J Biophys Biochem Cytol , vol.1 , Issue.1 , pp. 59-68
    • Palade, G.E.1
  • 3
    • 66849109240 scopus 로고    scopus 로고
    • The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
    • Kramer G., Boehringer D., Ban N., Bukau B. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins. Nat Struct Mol Biol Jun. 2009, 16(6):589-597.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.6 , pp. 589-597
    • Kramer, G.1    Boehringer, D.2    Ban, N.3    Bukau, B.4
  • 4
    • 0029402642 scopus 로고
    • Structure and evolution of mammalian ribosomal proteins
    • Wool I.G., Chan Y.L., Glück A. Structure and evolution of mammalian ribosomal proteins. Biochem Cell Biol Nov-Dec 1995, 73(11-12):933-947.
    • (1995) Biochem Cell Biol , vol.73 , Issue.11 , pp. 933-947
    • Wool, I.G.1    Chan, Y.L.2    Glück, A.3
  • 5
    • 71149121905 scopus 로고    scopus 로고
    • Resolving the elegant architecture of the ribosome
    • Puglisi J.D. Resolving the elegant architecture of the ribosome. Mol Cell Dec 11 2009, 36(5):720-723.
    • (2009) Mol Cell , vol.36 , Issue.5 , pp. 720-723
    • Puglisi, J.D.1
  • 6
    • 0014549361 scopus 로고
    • Ribosomal proteins: VI. Preparative polyacrylamide gel electrophoresis as applied to the isolation of ribosomal proteins
    • Kaltschmidt E., Wittmann Ribosomal proteins: VI. Preparative polyacrylamide gel electrophoresis as applied to the isolation of ribosomal proteins. Anal Biochem Jul. 1969, 30(1):132-141.
    • (1969) Anal Biochem , vol.30 , Issue.1 , pp. 132-141
    • Kaltschmidt, E.1    Wittmann2
  • 7
    • 0015523286 scopus 로고
    • Determination of the number of proteins in liver ribosomes and ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis
    • Sherton C.C., Wool I.G. Determination of the number of proteins in liver ribosomes and ribosomal subunits by two-dimensional polyacrylamide gel electrophoresis. J Biol Chem Jul. 25 1972, 247(14):4460-4467.
    • (1972) J Biol Chem , vol.247 , Issue.14 , pp. 4460-4467
    • Sherton, C.C.1    Wool, I.G.2
  • 9
    • 0018961141 scopus 로고
    • Construction and identification of cDNA clones for mouse ribosomal proteins: application for the study of r-protein gene expression
    • Meyuhas O., Perry R.P. Construction and identification of cDNA clones for mouse ribosomal proteins: application for the study of r-protein gene expression. Gene Jul. 1980, 10(2):113-129.
    • (1980) Gene , vol.10 , Issue.2 , pp. 113-129
    • Meyuhas, O.1    Perry, R.P.2
  • 10
    • 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 Aug 15 1970, 227(5259):680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 69449084241 scopus 로고    scopus 로고
    • Autophagy activation by NFkappaB is essential for cell survival after heat shock
    • Nivon M., Richet E., Codogno P., Arrigo A.P., Kretz-Remy C. Autophagy activation by NFkappaB is essential for cell survival after heat shock. Autophagy Aug. 2009, 5(6):766-783.
    • (2009) Autophagy , vol.5 , Issue.6 , pp. 766-783
    • Nivon, M.1    Richet, E.2    Codogno, P.3    Arrigo, A.P.4    Kretz-Remy, C.5
  • 13
    • 0033577694 scopus 로고    scopus 로고
    • TGF-beta cooperates with TGF-alpha to induce the self-renewal of normal erythrocytic progenitors: evidence for an autocrine mechanism
    • Gandrillon O., Schmidt U., Beug H., Samarut J. TGF-beta cooperates with TGF-alpha to induce the self-renewal of normal erythrocytic progenitors: evidence for an autocrine mechanism. EMBO J May 17 1999, 18(10):2764-2781.
    • (1999) EMBO J , vol.18 , Issue.10 , pp. 2764-2781
    • Gandrillon, O.1    Schmidt, U.2    Beug, H.3    Samarut, J.4
  • 14
    • 0023645054 scopus 로고
    • Expression of the v-erbA oncogene in chicken embryo fibroblasts stimulates their proliferation in vitro and enhances tumor growth in vivo
    • Gandrillon O., Jurdic P., Benchaibi M., Xiao J.H., Ghysdael J., Samarut J. Expression of the v-erbA oncogene in chicken embryo fibroblasts stimulates their proliferation in vitro and enhances tumor growth in vivo. Cell Jun 5 1987, 49(5):687-697.
    • (1987) Cell , vol.49 , Issue.5 , pp. 687-697
    • Gandrillon, O.1    Jurdic, P.2    Benchaibi, M.3    Xiao, J.H.4    Ghysdael, J.5    Samarut, J.6
  • 15
    • 0018790592 scopus 로고
    • A method for visualizing and quantifying the total complement of free and membrane-bound ribosomes in rat liver
    • Ramsey J.C., Steele W.J. A method for visualizing and quantifying the total complement of free and membrane-bound ribosomes in rat liver. Anal Biochem Jan 15 1979, 92(2):305-313.
    • (1979) Anal Biochem , vol.92 , Issue.2 , pp. 305-313
    • Ramsey, J.C.1    Steele, W.J.2
  • 16
    • 0018292212 scopus 로고
    • Spot position of rat liver ribosomal proteins by four different two-dimensional electrophorese in polycarylamide gel
    • Madjar J.J., Arpin M., Buisson M., Reboud J.P. Spot position of rat liver ribosomal proteins by four different two-dimensional electrophorese in polycarylamide gel. Mol Gen Genet Mar 20 1979, 171(2):121-134.
    • (1979) Mol Gen Genet , vol.171 , Issue.2 , pp. 121-134
    • Madjar, J.J.1    Arpin, M.2    Buisson, M.3    Reboud, J.P.4
  • 17
    • 0002347051 scopus 로고
    • Studies on the composition of the protein from Escherichia coli ribosomes
    • Waller J.P., Harris J.I. Studies on the composition of the protein from Escherichia coli ribosomes. Proc Natl Acad Sci USA Jan 15 1961, 47:18-23.
    • (1961) Proc Natl Acad Sci USA , vol.47 , pp. 18-23
    • Waller, J.P.1    Harris, J.I.2
  • 19
    • 0032618278 scopus 로고    scopus 로고
    • Silver staining of 2-D electrophoresis gels
    • Rabilloud T. Silver staining of 2-D electrophoresis gels. Methods Mol Biol 1999, 112:297-305.
    • (1999) Methods Mol Biol , vol.112 , pp. 297-305
    • Rabilloud, T.1
  • 20
    • 48949099046 scopus 로고    scopus 로고
    • Increasing information from shotgun proteomic data by accounting for misassigned precursor ion masses
    • Scherl A., Tsai Y.S., Shaffer S.A., Goodlett D.R. Increasing information from shotgun proteomic data by accounting for misassigned precursor ion masses. Proteomics Jul. 2008, 8(14):2791-2797.
    • (2008) Proteomics , vol.8 , Issue.14 , pp. 2791-2797
    • Scherl, A.1    Tsai, Y.S.2    Shaffer, S.A.3    Goodlett, D.R.4
  • 21
    • 74849138649 scopus 로고    scopus 로고
    • Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags
    • Dayon L., Pasquarello C., Hoogland C., Sanchez J.C., Scherl A. Combining low- and high-energy tandem mass spectra for optimized peptide quantification with isobaric tags. J Proteomics Feb. 10 2010, 73(4):769-777.
    • (2010) J Proteomics , vol.73 , Issue.4 , pp. 769-777
    • Dayon, L.1    Pasquarello, C.2    Hoogland, C.3    Sanchez, J.C.4    Scherl, A.5
  • 22
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J.E., Gygi S.P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods Mar. 2007, 4(3):207-214.
    • (2007) Nat Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 23
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science Aug. 14 2009, 325(5942):834-840.
    • (2009) Science , vol.325 , Issue.5942 , pp. 834-840
    • Choudhary, C.1    Kumar, C.2    Gnad, F.3    Nielsen, M.L.4    Rehman, M.5    Walther, T.C.6    Olsen, J.V.7    Mann, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.