메뉴 건너뛰기




Volumn 134, Issue , 2016, Pages 1-4

Towards deciphering proteomes via the proteoform, protein speciation, moonlighting and protein code concepts

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 2U GLOBULIN; ENOLASE; GLYCAN; GLYCOPROTEIN; PHOSPHOGLYCERATE KINASE; PROTEOME;

EID: 84958245699     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2016.01.012     Document Type: Editorial
Times cited : (24)

References (29)
  • 1
    • 84904417334 scopus 로고    scopus 로고
    • The proteomics quantification dilemma
    • Jungblut P.R. The proteomics quantification dilemma. J. Proteome 2014, 107:98-102.
    • (2014) J. Proteome , vol.107 , pp. 98-102
    • Jungblut, P.R.1
  • 2
    • 84868229162 scopus 로고    scopus 로고
    • A cell-based approach to the human proteome project
    • Kelleher N.L. A cell-based approach to the human proteome project. J. Am. Soc. Mass Spectrom. Oct 2012, 23:1617-1624.
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , pp. 1617-1624
    • Kelleher, N.L.1
  • 3
    • 84874055523 scopus 로고    scopus 로고
    • High resolution quantitative proteomics of HeLa cells protein species using stable isotope labeling with amino acids in cell culture (SILAC), two-dimensional gel electrophoresis (2DE) and nano-liquid chromatography coupled to an LTQ-Orbitrap Mass spectrometer
    • Thiede B., Koehler C.J., Strozynski M., Treumann A., Stein R., Zimny-Arndt U., et al. High resolution quantitative proteomics of HeLa cells protein species using stable isotope labeling with amino acids in cell culture (SILAC), two-dimensional gel electrophoresis (2DE) and nano-liquid chromatography coupled to an LTQ-Orbitrap Mass spectrometer. Mol. Cell. Proteomics 2013, 12:529-538.
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 529-538
    • Thiede, B.1    Koehler, C.J.2    Strozynski, M.3    Treumann, A.4    Stein, R.5    Zimny-Arndt, U.6
  • 7
    • 84874625369 scopus 로고    scopus 로고
    • Consortium for top-down proteomics. Proteoform: a single term describing protein complexity
    • Smith L.M., Kelleher N.L. Consortium for top-down proteomics. Proteoform: a single term describing protein complexity. Nat. Methods 2013, 10:186-187.
    • (2013) Nat. Methods , vol.10 , pp. 186-187
    • Smith, L.M.1    Kelleher, N.L.2
  • 9
    • 52449132322 scopus 로고    scopus 로고
    • Is there a code embedded in proteins that is based on post-translational modifications?
    • Sims R.J., Reinberg D. Is there a code embedded in proteins that is based on post-translational modifications?. Nat. Rev. Mol. Cell Biol. 2008, 9:815-820.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 815-820
    • Sims, R.J.1    Reinberg, D.2
  • 11
    • 84958158556 scopus 로고    scopus 로고
    • Protein Species and Moonlighting Proteins: Very Small Changes in a Protein's Covalent Structure Can Change its Biochemical Function
    • Jeffery C.J. Protein Species and Moonlighting Proteins: Very Small Changes in a Protein's Covalent Structure Can Change its Biochemical Function. J. Proteome 2016, 134:19-24.
    • (2016) J. Proteome , vol.134 , pp. 19-24
    • Jeffery, C.J.1
  • 12
    • 84957448655 scopus 로고    scopus 로고
    • Genomic Variability and Protein Species - Improving Sequence Coverage for Proteogenomics
    • Bischoff R., Permentier H., Guryev V., Horvatovich P. Genomic Variability and Protein Species - Improving Sequence Coverage for Proteogenomics. J. Proteome 2016, 134:25-36.
    • (2016) J. Proteome , vol.134 , pp. 25-36
    • Bischoff, R.1    Permentier, H.2    Guryev, V.3    Horvatovich, P.4
  • 13
    • 84958185888 scopus 로고    scopus 로고
    • Biological significance of co- and post-translational modifications of the yeast 26S proteasome
    • Hirano H., Kimura Y., Kimura A. Biological significance of co- and post-translational modifications of the yeast 26S proteasome. J. Proteome 2016, 134:37-46.
    • (2016) J. Proteome , vol.134 , pp. 37-46
    • Hirano, H.1    Kimura, Y.2    Kimura, A.3
  • 15
    • 84958158076 scopus 로고    scopus 로고
    • Proteomic Analysis of Post-Translational Modifications in Cyanobacteria
    • Xiong Q., Chen Z., Ge F. Proteomic Analysis of Post-Translational Modifications in Cyanobacteria. J. Proteome 2016, 134:57-64.
    • (2016) J. Proteome , vol.134 , pp. 57-64
    • Xiong, Q.1    Chen, Z.2    Ge, F.3
  • 16
    • 84958154360 scopus 로고    scopus 로고
    • In silico prediction and characterization of protein post-translational modifications
    • Gianazza E., Parravicini C., Primi R., Miller I., Eberini I. In silico prediction and characterization of protein post-translational modifications. J. Proteome 2016, 134:65-75.
    • (2016) J. Proteome , vol.134 , pp. 65-75
    • Gianazza, E.1    Parravicini, C.2    Primi, R.3    Miller, I.4    Eberini, I.5
  • 18
    • 84958182305 scopus 로고    scopus 로고
    • Recombinant glycoproteins: The impact of cell lines and culture conditions on the generation of protein species
    • Rosenlöcher J., Sandig G., Kannicht C., Blanchard V., Reinke S.O., Hinderlich S. Recombinant glycoproteins: The impact of cell lines and culture conditions on the generation of protein species. J. Proteome 2016, 134:85-92.
    • (2016) J. Proteome , vol.134 , pp. 85-92
    • Rosenlöcher, J.1    Sandig, G.2    Kannicht, C.3    Blanchard, V.4    Reinke, S.O.5    Hinderlich, S.6
  • 21
    • 84958269281 scopus 로고    scopus 로고
    • Hexose-derived glycation sites in processed bovine milk
    • Milkovska-Stamenova S., Hoffmann R. Hexose-derived glycation sites in processed bovine milk. J. Proteome 2016, 134:102-111.
    • (2016) J. Proteome , vol.134 , pp. 102-111
    • Milkovska-Stamenova, S.1    Hoffmann, R.2
  • 22
    • 84958180103 scopus 로고    scopus 로고
    • Identification and quantification of bovine protein lactosylation sites in different milk products
    • Milkovska-Stamenova S., Hoffmann R. Identification and quantification of bovine protein lactosylation sites in different milk products. J. Proteome 2016, 134:112-126.
    • (2016) J. Proteome , vol.134 , pp. 112-126
    • Milkovska-Stamenova, S.1    Hoffmann, R.2
  • 23
    • 84958254209 scopus 로고    scopus 로고
    • Identification of multiple transferrin species in spleen and serum from mice with collagen-induced arthritis which may reflect changes in transferrin glycosylation associated with disease activity: the role of CD38
    • Rosal-Vela A., Barroso A., Giménez E., García-Rodriguez S., Longobardo V., Postigo J., et al. Identification of multiple transferrin species in spleen and serum from mice with collagen-induced arthritis which may reflect changes in transferrin glycosylation associated with disease activity: the role of CD38. J. Proteome 2016, 134:127-137.
    • (2016) J. Proteome , vol.134 , pp. 127-137
    • Rosal-Vela, A.1    Barroso, A.2    Giménez, E.3    García-Rodriguez, S.4    Longobardo, V.5    Postigo, J.6
  • 24
    • 84958181515 scopus 로고    scopus 로고
    • Protein species-specific characterization of conformational change induced by multisite phosphorylation
    • Pan J., Zhang S., Borchers C.H. Protein species-specific characterization of conformational change induced by multisite phosphorylation. J. Proteome 2016, 134:138-143.
    • (2016) J. Proteome , vol.134 , pp. 138-143
    • Pan, J.1    Zhang, S.2    Borchers, C.H.3
  • 25
    • 84958164162 scopus 로고    scopus 로고
    • Seroprofiling at the Candida albicans protein species level unveils an accurate molecular discriminator for candidemia
    • Pitarch A., Nombela C., Gil C. Seroprofiling at the Candida albicans protein species level unveils an accurate molecular discriminator for candidemia. J. Proteome 2016, 134:144-162.
    • (2016) J. Proteome , vol.134 , pp. 144-162
    • Pitarch, A.1    Nombela, C.2    Gil, C.3
  • 26
    • 84958164156 scopus 로고    scopus 로고
    • Molecular responses of alveolar epithelial A549 cells to chronic exposure to titanium dioxide nanoparticles: a proteomic view
    • Armand L., Biola-Clier M., Bobyk L., Collin-Faure V., Diemer H., Strub J.-M., et al. Molecular responses of alveolar epithelial A549 cells to chronic exposure to titanium dioxide nanoparticles: a proteomic view. J. Proteome 2016, 134:163-173.
    • (2016) J. Proteome , vol.134 , pp. 163-173
    • Armand, L.1    Biola-Clier, M.2    Bobyk, L.3    Collin-Faure, V.4    Diemer, H.5    Strub, J.-M.6
  • 27
    • 84958181930 scopus 로고    scopus 로고
    • A combined proteomic and targeted analysis unravels new toxic mechanisms for zinc oxide nanoparticles in macrophages
    • Aude-Garcia C., Dalzon B., Ravanat J.-L., Collin-Faure V., Diemer H., Jean-Marc Strub J.-M., et al. A combined proteomic and targeted analysis unravels new toxic mechanisms for zinc oxide nanoparticles in macrophages. J. Proteome 2016, 134:174-185.
    • (2016) J. Proteome , vol.134 , pp. 174-185
    • Aude-Garcia, C.1    Dalzon, B.2    Ravanat, J.-L.3    Collin-Faure, V.4    Diemer, H.5    Jean-Marc Strub, J.-M.6
  • 28
    • 84958166375 scopus 로고    scopus 로고
    • Differentiation of protein species of alpha-2u-globulin according to database entries: a half-theoretical approach
    • Aksu S., Tanrikulu F. Differentiation of protein species of alpha-2u-globulin according to database entries: a half-theoretical approach. J. Proteome 2016, 134:186-192.
    • (2016) J. Proteome , vol.134 , pp. 186-192
    • Aksu, S.1    Tanrikulu, F.2
  • 29
    • 84958169667 scopus 로고    scopus 로고
    • Homogenization of human tissues via picosecond-infrared laser (PIRL) ablation: Giving a closer view on the in-vivo composition of protein species as compared to mechanical homogenization
    • Kwiatkowski M., Wurlitzer M., Krutilin A., Lübberstedt J., Küpker N., Kiani P., et al. Homogenization of human tissues via picosecond-infrared laser (PIRL) ablation: Giving a closer view on the in-vivo composition of protein species as compared to mechanical homogenization. J. Proteome 2016, 134:193-202.
    • (2016) J. Proteome , vol.134 , pp. 193-202
    • Kwiatkowski, M.1    Wurlitzer, M.2    Krutilin, A.3    Lübberstedt, J.4    Küpker, N.5    Kiani, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.