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Volumn 5, Issue JUN2016, 2016, Pages

Global, quantitative and dynamic mapping of protein subcellular localization

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR; PROTEIN TRANSLOCASE; PROTEIN;

EID: 84979673478     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.16950     Document Type: Article
Times cited : (442)

References (41)
  • 1
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • Andersen JS, Wilkinson CJ, Mayor T, Mortensen P, Nigg EA, Mann M. 2003. Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426: 570-574. doi: 10.1038/nature02166
    • (2003) Nature , vol.426 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 2
    • 0014694099 scopus 로고
    • Membrane-bound ribosomes in HeLa cells. I. Their proportion to total cell ribosomes and their association with messenger RNA
    • Attardi B, Cravioto B, Attardi G. 1969. Membrane-bound ribosomes in HeLa cells. I. Their proportion to total cell ribosomes and their association with messenger RNA. Journal of Molecular Biology 44: 47-70. doi: 10.1016/0022-2836(69)90404-5
    • (1969) Journal of Molecular Biology , vol.44 , pp. 47-70
    • Attardi, B.1    Cravioto, B.2    Attardi, G.3
  • 4
    • 84908147624 scopus 로고    scopus 로고
    • Fractionation profiling: A fast and versatile approach for mapping vesicle proteomes and protein-protein interactions
    • Borner GH, Hein MY, Hirst J, Edgar JR, Mann M, Robinson MS. 2014. Fractionation profiling: a fast and versatile approach for mapping vesicle proteomes and protein-protein interactions. Molecular Biology of the Cell 25: 3178-3194. doi: 10.1091/mbc.E14-07-1198
    • (2014) Molecular Biology of the Cell , vol.25 , pp. 3178-3194
    • Borner, G.H.1    Hein, M.Y.2    Hirst, J.3    Edgar, J.R.4    Mann, M.5    Robinson, M.S.6
  • 5
    • 84876305060 scopus 로고    scopus 로고
    • A novel single-cell screening platform reveals proteome plasticity during yeast stress responses
    • Breker M, Gymrek M, Schuldiner M. 2013. A novel single-cell screening platform reveals proteome plasticity during yeast stress responses. Journal of Cell Biology 200: 839-850. doi: 10.1083/jcb.201301120
    • (2013) Journal of Cell Biology , vol.200 , pp. 839-850
    • Breker, M.1    Gymrek, M.2    Schuldiner, M.3
  • 6
    • 84979518589 scopus 로고    scopus 로고
    • MitoCarta2.0: An updated inventory of mammalian mitochondrial proteins
    • Calvo SE, Clauser KR, Mootha VK. 2016. MitoCarta2.0: an updated inventory of mammalian mitochondrial proteins. Nucleic Acids Research 44: D1251-1257. doi: 10.1093/nar/gkv1003
    • (2016) Nucleic Acids Research , vol.44 , pp. D1251-D1257
    • Calvo, S.E.1    Clauser, K.R.2    Mootha, V.K.3
  • 8
    • 84907197082 scopus 로고    scopus 로고
    • Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ
    • Cox J, Hein MY, Luber CA, Paron I, Nagaraj N, Mann M. 2014. Accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction, termed MaxLFQ. Molecular & Cellular Proteomics 13: 2513-2526. doi: 10.1074/mcp.M113.031591
    • (2014) Molecular & Cellular Proteomics , vol.13 , pp. 2513-2526
    • Cox, J.1    Hein, M.Y.2    Luber, C.A.3    Paron, I.4    Nagaraj, N.5    Mann, M.6
  • 9
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M. 2008. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nature Biotechnology 26: 1367-1372. doi: 10.1038/nbt.1511
    • (2008) Nature Biotechnology , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 11
    • 84946063277 scopus 로고    scopus 로고
    • Machine Learning-based Classification of Diffuse Large B-cell Lymphoma Patients by Their Protein Expression Profiles
    • Deeb SJ, Tyanova S, Hummel M, Schmidt-Supprian M, Cox J, Mann M. 2015. Machine Learning-based Classification of Diffuse Large B-cell Lymphoma Patients by Their Protein Expression Profiles. Molecular & Cellular Proteomics 14: 2947-2960. doi: 10.1074/mcp.M115.050245
    • (2015) Molecular & Cellular Proteomics , vol.14 , pp. 2947-2960
    • Deeb, S.J.1    Tyanova, S.2    Hummel, M.3    Schmidt-Supprian, M.4    Cox, J.5    Mann, M.6
  • 13
    • 67650915105 scopus 로고    scopus 로고
    • Outliers detection with the minimum covariance determinant estimator in practice
    • Fauconnier C, Haesbroeck G. 2009. Outliers detection with the minimum covariance determinant estimator in practice. Statistical Methodology 6: 363-379. doi: 10.1016/j.stamet.2008.12.005
    • (2009) Statistical Methodology , vol.6 , pp. 363-379
    • Fauconnier, C.1    Haesbroeck, G.2
  • 14
    • 0014116306 scopus 로고
    • Electron microscope studies of the microvilli of HeLa cells
    • Fisher HW, Cooper TW. 1967. Electron microscope studies of the microvilli of HeLa cells. Journal of Cell Biology 34: 569-576. doi: 10.1083/jcb.34.2.569
    • (1967) Journal of Cell Biology , vol.34 , pp. 569-576
    • Fisher, H.W.1    Cooper, T.W.2
  • 15
  • 17
    • 77952226764 scopus 로고    scopus 로고
    • Super-SILAC mix for quantitative proteomics of human tumor tissue
    • Geiger T, Cox J, Ostasiewicz P, Wisniewski JR, Mann M. 2010. Super-SILAC mix for quantitative proteomics of human tumor tissue. Nature Methods 7: 383-385. doi: 10.1038/nmeth.1446
    • (2010) Nature Methods , vol.7 , pp. 383-385
    • Geiger, T.1    Cox, J.2    Ostasiewicz, P.3    Wisniewski, J.R.4    Mann, M.5
  • 19
    • 4744342856 scopus 로고    scopus 로고
    • Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation
    • Grøvdal LM, Stang E, Sorkin A, Madshus IH. 2004. Direct interaction of Cbl with pTyr 1045 of the EGF receptor (EGFR) is required to sort the EGFR to lysosomes for degradation. Experimental Cell Research 300: 388-395. doi: 10.1016/j.yexcr.2004.07.003
    • (2004) Experimental Cell Research , vol.300 , pp. 388-395
    • Grøvdal, L.M.1    Stang, E.2    Sorkin, A.3    Madshus, I.H.4
  • 21
    • 84941076117 scopus 로고    scopus 로고
    • High-throughput phosphoproteomics reveals in vivo insulin signaling dynamics
    • Humphrey SJ, Azimifar SB, Mann M. 2015. High-throughput phosphoproteomics reveals in vivo insulin signaling dynamics. Nature Biotechnology 33: 990-995. doi: 10.1038/nbt.3327
    • (2015) Nature Biotechnology , vol.33 , pp. 990-995
    • Humphrey, S.J.1    Azimifar, S.B.2    Mann, M.3
  • 22
    • 84898609552 scopus 로고    scopus 로고
    • Interdependent epidermal growth factor receptor signalling and trafficking
    • Jones S, Rappoport JZ. 2014. Interdependent epidermal growth factor receptor signalling and trafficking. International Journal of Biochemistry & Cell Biology 51: 23-28. doi: 10.1016/j.biocel.2014.03.014
    • (2014) International Journal of Biochemistry & Cell Biology , vol.51 , pp. 23-28
    • Jones, S.1    Rappoport, J.Z.2
  • 23
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • Kulak NA, Pichler G, Paron I, Nagaraj N, Mann M. 2014. Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nature Methods 11: 319-324. doi: 10.1038/nmeth.2834
    • (2014) Nature Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 26
    • 79955479177 scopus 로고    scopus 로고
    • ADAM17 (TACE) regulates TGFb signaling through the cleavage of vasorin
    • Malapeira J, Esselens C, Bech-Serra JJ, Canals F, Arribas J. 2011. ADAM17 (TACE) regulates TGFb signaling through the cleavage of vasorin. Oncogene 30: 1912-1922. doi: 10.1038/onc.2010.565
    • (2011) Oncogene , vol.30 , pp. 1912-1922
    • Malapeira, J.1    Esselens, C.2    Bech-Serra, J.J.3    Canals, F.4    Arribas, J.5
  • 27
    • 84940550197 scopus 로고    scopus 로고
    • Mapping proteins with spatial proteomics
    • Marx V. 2015. Mapping proteins with spatial proteomics. Nature Methods 12: 815-819. doi: 10.1038/nmeth.3555
    • (2015) Nature Methods , vol.12 , pp. 815-819
    • Marx, V.1
  • 29
    • 33746889808 scopus 로고    scopus 로고
    • A comprehensive pathway map of epidermal growth factor receptor signaling
    • 2005.0010
    • Oda K, Matsuoka Y, Funahashi A, Kitano H. 2005. A comprehensive pathway map of epidermal growth factor receptor signaling. Molecular Systems Biology 1: 2005.0010. doi: 10.1038/msb4100014
    • (2005) Molecular Systems Biology , vol.1
    • Oda, K.1    Matsuoka, Y.2    Funahashi, A.3    Kitano, H.4
  • 30
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, Mann M. 2002. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Molecular & Cellular Proteomics 1: 376-386. doi: 10.1074/mcp.M200025-MCP200
    • (2002) Molecular & Cellular Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 31
    • 79960907910 scopus 로고    scopus 로고
    • The MAPK cascades: Signaling components, nuclear roles and mechanisms of nuclear translocation
    • Plotnikov A, Zehorai E, Procaccia S, Seger R. 2011. The MAPK cascades: signaling components, nuclear roles and mechanisms of nuclear translocation. Biochimica Et Biophysica Acta 1813: 1619-1633. doi: 10.1016/j.bbamcr.2010.12.012
    • (2011) Biochimica Et Biophysica Acta , vol.1813 , pp. 1619-1633
    • Plotnikov, A.1    Zehorai, E.2    Procaccia, S.3    Seger, R.4
  • 32
    • 0021268019 scopus 로고
    • Density of newly synthesized plasma membrane proteins in intracellular membranes II. Biochemical studies
    • Quinn P, Griffiths G, Warren G. 1984. Density of newly synthesized plasma membrane proteins in intracellular membranes II. Biochemical studies. Journal of Cell Biology 98: 2142-2147. doi: 10.1083/jcb.98.6.2142
    • (1984) Journal of Cell Biology , vol.98 , pp. 2142-2147
    • Quinn, P.1    Griffiths, G.2    Warren, G.3
  • 33
    • 34548683924 scopus 로고    scopus 로고
    • Suppressor of T-cell receptor signalling 1 and 2 differentially regulate endocytosis and signalling of receptor tyrosine kinases
    • Raguz J, Wagner S, Dikic I, Hoeller D. 2007. Suppressor of T-cell receptor signalling 1 and 2 differentially regulate endocytosis and signalling of receptor tyrosine kinases. FEBS Letters 581: 4767-4772. doi: 10.1016/j.febslet.2007.08.077
    • (2007) FEBS Letters , vol.581 , pp. 4767-4772
    • Raguz, J.1    Wagner, S.2    Dikic, I.3    Hoeller, D.4
  • 36
    • 0023441053 scopus 로고
    • Functional equivalents of interferon-mediated signals needed for induction of an mRNA can be generated by double-stranded RNA and growth factors
    • Tiwari RK, Kusari J, Sen GC. 1987. Functional equivalents of interferon-mediated signals needed for induction of an mRNA can be generated by double-stranded RNA and growth factors. EMBO Journal 6: 3373-3378.
    • (1987) EMBO Journal , vol.6 , pp. 3373-3378
    • Tiwari, R.K.1    Kusari, J.2    Sen, G.C.3
  • 39
    • 84910081742 scopus 로고    scopus 로고
    • A ‘proteomic ruler’ for protein copy number and concentration estimation without spike-in standards
    • Wiśniewski JR, Hein MY, Cox J, Mann M. 2014. A ‘proteomic ruler’ for protein copy number and concentration estimation without spike-in standards. Molecular & Cellular Proteomics 13: 3497-3506. doi: 10.1074/mcp.M113.037309
    • (2014) Molecular & Cellular Proteomics , vol.13 , pp. 3497-3506
    • Wiśniewski, J.R.1    Hein, M.Y.2    Cox, J.3    Mann, M.4
  • 40
    • 80054723147 scopus 로고    scopus 로고
    • In vivo quantitative proteomics: The SILAC mouse
    • Zanivan S, Krueger M, Mann M. 2012. In vivo quantitative proteomics: the SILAC mouse. Methods in Molecular Biology 757: 435-450. doi: 10.1007/978-1-61779-166-6_25
    • (2012) Methods in Molecular Biology , vol.757 , pp. 435-450
    • Zanivan, S.1    Krueger, M.2    Mann, M.3
  • 41
    • 80855154135 scopus 로고    scopus 로고
    • A Protein Epitope Signature Tag (PrEST) library allows SILAC-based absolute quantification and multiplexed determination of protein copy numbers in cell lines
    • O111.009613
    • Zeiler M, Straube WL, Lundberg E, Uhlen M, Mann M. 2012. A Protein Epitope Signature Tag (PrEST) library allows SILAC-based absolute quantification and multiplexed determination of protein copy numbers in cell lines. Molecular & Cellular Proteomics 11: O111.009613. doi: 10.1074/mcp.O111.009613
    • (2012) Molecular & Cellular Proteomics , vol.11
    • Zeiler, M.1    Straube, W.L.2    Lundberg, E.3    Uhlen, M.4    Mann, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.