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Volumn 11, Issue 3, 2012, Pages

Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN DEPOLYMERIZING FACTOR; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; ALANINE TRANSFER RNA LIGASE; AMINO ACID; ANTIVIRUS AGENT; ARGININOSUCCINATE SYNTHASE 1; BILIVERDIN; CALCYCLIN; CALPAIN 1; CELLULAR RETINOIC ACID BINDING PROTEIN 2; CHAPERONIN CONTAINING TCP1; CHROMATIN MODIFYING PROTEIN 6; COATOMER PROTEIN; COFILIN 1; CONCANAMYCIN A; COPINE III; CYSTATIN B; ENOLASE; EUKARYOTIC TRANSLATION ELONGATION 2; EUKARYOTIC TRANSLATION ELONGATION FACTOR 1GAMMA; FATTY ACID SYNTHASE; FK 506 BINDING PROTEIN; FRUCTOSE 1,6 BISPHOSPHATASE 1; GAMMA GLUTAMYLCYCLOTRANSFERASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GREEN FLUORESCENT PROTEIN; IMMUNOSUPPRESSIVE AGENT; LIPOCORTIN 4; LIPOCORTIN 5; MACROLIDE; MONOCLONAL ANTIBODY; PHARMACOLOGY; PHOSPHORIBOSYLAMINOIMIDAZOLECARBOXAMIDE FORMYLTRANSFERASE; PROTEASOME; PROTEIN; RAPAMYCIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84857954964     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M111.014035     Document Type: Article
Times cited : (116)

References (59)
  • 1
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • DOI 10.1038/nrc1738
    • Kroemer, G., and Jäättelä, M. (2005) Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 5, 886-897 (Pubitemid 41746033)
    • (2005) Nature Reviews Cancer , vol.5 , Issue.11 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 2
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • Mizushima, N., Levine, B., Cuervo, A. M., and Klionsky, D. J. (2008) Autophagy fights disease through cellular self-digestion. Nature 451, 1069-1075 (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 3
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: Lessons from yeast
    • Nakatogawa, H., Suzuki, K., Kamada, Y., and Ohsumi, Y. (2009) Dynamics and diversity in autophagy mechanisms: Lessons from yeast. Nat. Rev. Mol. Cell Biol. 10, 458-467
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 4
    • 84857959247 scopus 로고    scopus 로고
    • The degradative inventory of the cell: Proteomic insights
    • doi: 10.1089/ars.2011.4393
    • Engelke, R., Becker, A. C., and Dengjel, J. (2012) The degradative inventory of the cell: Proteomic insights. Antioxid. Redox Signal., doi: 10.1089/ars.2011.4393
    • (2012) Antioxid. Redox Signal.
    • Engelke, R.1    Becker, A.C.2    Dengjel, J.3
  • 5
    • 46849115787 scopus 로고    scopus 로고
    • Autophagy is essential for preimplantation development of mouse embryos
    • DOI 10.1126/science.1154822
    • Tsukamoto, S., Kuma, A., Murakami, M., Kishi, C., Yamamoto, A., and Mizushima, N. (2008) Autophagy is essential for preimplantation development of mouse embryos. Science 321, 117-120 (Pubitemid 351956245)
    • (2008) Science , vol.321 , Issue.5885 , pp. 117-120
    • Tsukamoto, S.1    Kuma, A.2    Murakami, M.3    Kishi, C.4    Yamamoto, A.5    Mizushima, N.6
  • 7
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D. C. (2006) The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 443, 780-786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 8
    • 36448943299 scopus 로고    scopus 로고
    • Role of autophagy in cancer
    • DOI 10.1038/nrc2254, PII NRC2254
    • Mathew, R., Karantza-Wadsworth, V., and White, E. (2007) Role of autophagy in cancer. Nat. Rev. Cancer 7, 961-967 (Pubitemid 350165856)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.12 , pp. 961-967
    • Mathew, R.1    Karantza-Wadsworth, V.2    White, E.3
  • 9
    • 0024299286 scopus 로고
    • Prelysosomal convergence of autophagic and endocytic pathways
    • Gordon, P. B., and Seglen, P. O. (1988) Prelysosomal convergence of autophagic and endocytic pathways. Biochem. Biophys. Res. Commun. 151, 40-47
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 40-47
    • Gordon, P.B.1    Seglen, P.O.2
  • 10
    • 33745365931 scopus 로고    scopus 로고
    • Proteolytic and lipolytic responses to starvation
    • DOI 10.1016/j.nut.2006.04.008, PII S0899900706001766
    • Finn, P. F., and Dice, J. F. (2006) Proteolytic and lipolytic responses to starvation. Nutrition 22, 830-844 (Pubitemid 43947502)
    • (2006) Nutrition , vol.22 , Issue.7-8 , pp. 830-844
    • Finn, P.F.1    Dice, J.F.2
  • 12
    • 0035286734 scopus 로고    scopus 로고
    • Molecular dissection of autophagy: Two ubiquitin-like systems
    • Ohsumi, Y. (2001) Molecular dissection of autophagy: Two ubiquitin-like systems. Nat. Rev. Mol. Cell Biol. 2, 211-216
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 211-216
    • Ohsumi, Y.1
  • 13
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang, Z., and Klionsky, D. J. (2010) Mammalian autophagy: Core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 22, 124-131
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 14
    • 34249934085 scopus 로고    scopus 로고
    • Selective degradation of mitochondria by mitophagy
    • DOI 10.1016/j.abb.2007.03.034, PII S0003986107001622, Highlight Issue: Pro- and antiapoptotic Signalling
    • Kim, I., Rodriguez-Enriquez, S., and Lemasters, J. J. (2007) Selective degradation of mitochondria by mitophagy. Arch. Biochem. Biophys. 462, 245-253 (Pubitemid 46876640)
    • (2007) Archives of Biochemistry and Biophysics , vol.462 , Issue.2 , pp. 245-253
    • Kim, I.1    Rodriguez-Enriquez, S.2    Lemasters, J.J.3
  • 15
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counter-balances endoplasmic reticulum expansion during the unfolded protein response
    • Bernales, S., McDonald, K. L., and Walter, P. (2006) Autophagy counter-balances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 4, e423
    • (2006) PLoS Biol. , vol.4
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 17
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • DOI 10.1038/ncb1723, PII NCB1723
    • Kraft, C., Deplazes, A., Sohrmann, M., and Peter, M. (2008) Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease. Nat. Cell Biol. 10, 602-610 (Pubitemid 351627380)
    • (2008) Nature Cell Biology , vol.10 , Issue.5 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 18
    • 58149344946 scopus 로고    scopus 로고
    • Midbody ring disposal by autophagy is a post-abscission event of cytokinesis
    • Pohl, C., and Jentsch, S. (2009) Midbody ring disposal by autophagy is a post-abscission event of cytokinesis. Nat. Cell Biol. 11, 65-70
    • (2009) Nat. Cell Biol. , vol.11 , pp. 65-70
    • Pohl, C.1    Jentsch, S.2
  • 20
    • 11244309014 scopus 로고    scopus 로고
    • Proteolysis: From the lysosome to ubiquitin and the proteasome
    • Ciechanover, A. (2005) Proteolysis: From the lysosome to ubiquitin and the proteasome. Nat. Rev. Mol. Cell Biol. 6, 79-87
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 79-87
    • Ciechanover, A.1
  • 22
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk, V. I., Mansilla, A., Menzies, F. M., and Rubinsztein, D. C. (2009) Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol. Cell 33, 517-527
    • (2009) Mol. Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 23
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: Ubiquitin-mediated recognition and beyond
    • Kraft, C., Peter, M., and Hofmann, K. (2010) Selective autophagy: Ubiquitin-mediated recognition and beyond. Nat. Cell Biol. 12, 836-841
    • (2010) Nat. Cell Biol. , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 24
    • 77951248828 scopus 로고    scopus 로고
    • Autophagy: Links with the proteasome
    • Lamark, T., and Johansen, T. (2010) Autophagy: Links with the proteasome. Curr. Opin. Cell Biol. 22, 192-198
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 192-198
    • Lamark, T.1    Johansen, T.2
  • 25
    • 78649301860 scopus 로고    scopus 로고
    • Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy
    • Zimmermann, A. C., Zarei, M., Eiselein, S., and Dengjel, J. (2010) Quantitative proteomics for the analysis of spatio-temporal protein dynamics during autophagy. Autophagy 6, 1009-1016
    • (2010) Autophagy , vol.6 , pp. 1009-1016
    • Zimmermann, A.C.1    Zarei, M.2    Eiselein, S.3    Dengjel, J.4
  • 26
    • 0346874342 scopus 로고    scopus 로고
    • Proteomic characterization of the human centrosome by protein correlation profiling
    • DOI 10.1038/nature02166
    • Andersen, J. S., Wilkinson, C. J., Mayor, T., Mortensen, P., Nigg, E. A., and Mann, M. (2003) Proteomic characterization of the human centrosome by protein correlation profiling. Nature 426, 570-574 (Pubitemid 37522644)
    • (2003) Nature , vol.426 , Issue.6966 , pp. 570-574
    • Andersen, J.S.1    Wilkinson, C.J.2    Mayor, T.3    Mortensen, P.4    Nigg, E.A.5    Mann, M.6
  • 27
    • 70349321247 scopus 로고    scopus 로고
    • Receptor tyrosine kinase signaling: A view from quantitative proteomics
    • Dengjel, J., Kratchmarova, I., and Blagoev, B. (2009) Receptor tyrosine kinase signaling: A view from quantitative proteomics. Mol. Biosyst. 5, 1112-1121
    • (2009) Mol. Biosyst. , vol.5 , pp. 1112-1121
    • Dengjel, J.1    Kratchmarova, I.2    Blagoev, B.3
  • 28
    • 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, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. 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
  • 29
    • 36549040957 scopus 로고    scopus 로고
    • Monitoring autophagy in yeast: The Pho8Delta60 assay
    • Klionsky, D. J. (2007) Monitoring autophagy in yeast: The Pho8Delta60 assay. Methods Mol. Biol. 390, 363-371
    • (2007) Methods Mol. Biol. , vol.390 , pp. 363-371
    • Klionsky, D.J.1
  • 30
    • 70349634805 scopus 로고    scopus 로고
    • Identification of novel autophagy regulators by a luciferase-based assay for the kinetics of autophagic flux
    • Farkas, T., Hoyer-Hansen, M., and Jaattela, M. (2009) Identification of novel autophagy regulators by a luciferase-based assay for the kinetics of autophagic flux. Autophagy 5, 1018-1025
    • (2009) Autophagy , vol.5 , pp. 1018-1025
    • Farkas, T.1    Hoyer-Hansen, M.2    Jaattela, M.3
  • 32
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • Behrends, C., Sowa, M. E., Gygi, S. P., and Harper, J. W. (2010) Network organization of the human autophagy system. Nature 466, 68-76
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 33
    • 74049106190 scopus 로고    scopus 로고
    • Biochemical isolation and characterization of the tubulovesicular LC3-positive autophagosomal compartment
    • Gao, W., Kang, J. H., Liao, Y., Ding, W. X., Gambotto, A. A., Watkins, S. C., Liu, Y. J., Stolz, D. B., and Yin, X. M. (2010) Biochemical isolation and characterization of the tubulovesicular LC3-positive autophagosomal compartment. J. Biol. Chem. 285, 1371-1383
    • (2010) J. Biol. Chem. , vol.285 , pp. 1371-1383
    • Gao, W.1    Kang, J.H.2    Liao, Y.3    Ding, W.X.4    Gambotto, A.A.5    Watkins, S.C.6    Liu, Y.J.7    Stolz, D.B.8    Yin, X.M.9
  • 34
    • 34250828455 scopus 로고    scopus 로고
    • Proteomic analysis of membrane-associated proteins from rat liver autophagosomes
    • Øverbye, A., Fengsrud, M., and Seglen, P. O. (2007) Proteomic analysis of membrane-associated proteins from rat liver autophagosomes. Autophagy 3, 300-322 (Pubitemid 46986335)
    • (2007) Autophagy , vol.3 , Issue.4 , pp. 300-322
    • Overbye, A.1    Fengsrud, M.2    Seglen, P.O.3
  • 35
    • 33749523582 scopus 로고    scopus 로고
    • Organellar proteomics: Turning inventories into insights
    • DOI 10.1038/sj.embor.7400780, PII 7400780
    • Andersen, J. S., and Mann, M. (2006) Organellar proteomics: Turning inventories into insights. EMBO Rep. 7, 874-879 (Pubitemid 44523965)
    • (2006) EMBO Reports , vol.7 , Issue.9 , pp. 874-879
    • Andersen, J.S.1    Mann, M.2
  • 37
    • 33750336592 scopus 로고    scopus 로고
    • Quantitative proteomics to study mitogen-activated protein kinases
    • DOI 10.1016/j.ymeth.2006.08.001, PII S1046202306001691
    • Blagoev, B., and Mann, M. (2006) Quantitative proteomics to study mitogen-activated protein kinases. Methods 40, 243-250 (Pubitemid 44635297)
    • (2006) Methods , vol.40 , Issue.3 , pp. 243-250
    • Blagoev, B.1    Mann, M.2
  • 38
    • 22544432531 scopus 로고    scopus 로고
    • Noise-robust soft clustering of gene expression time-course data
    • DOI 10.1142/S0219720005001375, PII S0219720005001375
    • Futschik, M. E., and Carlisle, B. (2005) Noise-robust soft clustering of gene expression time-course data. J. Bioinform. Comput. Biol. 3, 965-988 (Pubitemid 41015297)
    • (2005) Journal of Bioinformatics and Computational Biology , vol.3 , Issue.4 , pp. 965-988
    • Futschik, M.E.1    Carlisle, B.2
  • 41
    • 27944504351 scopus 로고    scopus 로고
    • p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • DOI 10.1083/jcb.200507002
    • Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Overvatn, A., Stenmark, H., and Johansen, T. (2005) p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin- induced cell death. J. Cell Biol. 171, 603-614 (Pubitemid 41668720)
    • (2005) Journal of Cell Biology , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6    Stenmark, H.7    Johansen, T.8
  • 42
    • 53849101821 scopus 로고    scopus 로고
    • The structure and function of the retromer protein complex
    • Collins, B. M. (2008) The structure and function of the retromer protein complex. Traffic 9, 1811-1822
    • (2008) Traffic , vol.9 , pp. 1811-1822
    • Collins, B.M.1
  • 43
    • 34848886914 scopus 로고    scopus 로고
    • Autophagosome formation: Core machinery and adaptations
    • DOI 10.1038/ncb1007-1102, PII NCB1007-1102
    • Xie, Z., and Klionsky, D. J. (2007) Autophagosome formation: Core machinery and adaptations. Nat. Cell Biol. 9, 1102-1109 (Pubitemid 47500484)
    • (2007) Nature Cell Biology , vol.9 , Issue.10 , pp. 1102-1109
    • Xie, Z.1    Klionsky, D.J.2
  • 44
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 Coordinately Activates Protein Degradation by the Autophagic/Lysosomal and Proteasomal Pathways in Atrophying Muscle Cells
    • DOI 10.1016/j.cmet.2007.11.004, PII S1550413107003397
    • Zhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., and Goldberg, A. L. (2007) FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 6, 472-483 (Pubitemid 350163056)
    • (2007) Cell Metabolism , vol.6 , Issue.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8
  • 45
    • 0028797005 scopus 로고
    • Degradation of proteasomes by lysosomes in rat liver
    • Cuervo, A. M., Palmer, A., Rivett, A. J., and Knecht, E. (1995) Degradation of proteasomes by lysosomes in rat liver. Eur. J. Biochem. 227, 792-800
    • (1995) Eur. J. Biochem. , vol.227 , pp. 792-800
    • Cuervo, A.M.1    Palmer, A.2    Rivett, A.J.3    Knecht, E.4
  • 46
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • DOI 10.1016/0014-5793(93)80398-E
    • Tsukada, M., and Ohsumi, Y. (1993) Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett. 333, 169-174 (Pubitemid 23306962)
    • (1993) FEBS Letters , vol.333 , Issue.1-2 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 47
    • 57349162369 scopus 로고    scopus 로고
    • Ordered bulk degradation via autophagy
    • Dengjel, J., Kristensen, A. R., and Andersen, J. S. (2008) Ordered bulk degradation via autophagy. Autophagy 4, 1057-1059
    • (2008) Autophagy , vol.4 , pp. 1057-1059
    • Dengjel, J.1    Kristensen, A.R.2    Andersen, J.S.3
  • 48
    • 0034646618 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Rheb G-protein is involved in regulating canavanine resistance and arginine uptake
    • DOI 10.1074/jbc.275.15.11198
    • Urano, J., Tabancay, A. P., Yang, W., and Tamanoi, F. (2000) The Saccharomyces cerevisiae Rheb G-protein is involved in regulating canavanine resistance and arginine uptake. J. Biol. Chem. 275, 11198-11206 (Pubitemid 30212764)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.15 , pp. 11198-11206
    • Urano, J.1    Tabancay, A.P.2    Yang, W.3    Tamanoi, F.4
  • 50
    • 4644273585 scopus 로고    scopus 로고
    • Uth1p is involved in the autophagic degradation of mitochondria
    • DOI 10.1074/jbc.M406960200
    • Kissová, I., Deffieu, M., Manon, S., and Camougrand, N. (2004) Uth1p is involved in the autophagic degradation of mitochondria. J. Biol. Chem. 279, 39068-39074 (Pubitemid 39296069)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.37 , pp. 39068-39074
    • Kissova, I.1    Deffieu, M.2    Manon, S.3    Camougrand, N.4
  • 51
    • 0032532323 scopus 로고    scopus 로고
    • Purification and characterization of autophagosomes from rat hepatocytes
    • Strømhaug, P. E., Berg, T. O., Fengsrud, M., and Seglen, P. O. (1998) Purification and characterization of autophagosomes from rat hepatocytes. Biochem. J. 335, 217-224 (Pubitemid 28491054)
    • (1998) Biochemical Journal , vol.335 , Issue.2 , pp. 217-224
    • Stromhaug, P.E.1    Berg, T.O.2    Fengsrud, M.3    Seglen, P.O.4
  • 52
    • 79952114917 scopus 로고    scopus 로고
    • Organelle proteomics by label-free and SILAC-based protein correlation profiling
    • Dengjel, J., Jakobsen, L., and Andersen, J. S. (2010) Organelle proteomics by label-free and SILAC-based protein correlation profiling. Methods Mol. Biol. 658, 255-265
    • (2010) Methods Mol. Biol. , vol.658 , pp. 255-265
    • Dengjel, J.1    Jakobsen, L.2    Andersen, J.S.3
  • 53
    • 79961217471 scopus 로고    scopus 로고
    • Comparison of ERLIC-TiO2, HILIC-TiO2, and SCX-TiO2 for global phosphoproteomics approaches
    • Zarei, M., Sprenger, A., Metzger, F., Gretzmeier, C., and Dengjel, J. (2011) Comparison of ERLIC-TiO2, HILIC-TiO2, and SCX-TiO2 for global phosphoproteomics approaches. J. Proteome Res. 10, 3474-3483
    • (2011) J. Proteome Res. , vol.10 , pp. 3474-3483
    • Zarei, M.1    Sprenger, A.2    Metzger, F.3    Gretzmeier, C.4    Dengjel, J.5
  • 54
    • 34249807325 scopus 로고    scopus 로고
    • A mass spectrometry-friendly database for cSNP identification [1]
    • DOI 10.1038/nmeth0607-465, PII NMETH0607-465
    • Schandorff, S., Olsen, J. V., Bunkenborg, J., Blagoev, B., Zhang, Y., Andersen, J. S., and Mann, M. (2007) A mass spectrometry-friendly database for cSNP identification. Nat. Methods 4, 465-466 (Pubitemid 46852063)
    • (2007) Nature Methods , vol.4 , Issue.6 , pp. 465-466
    • Schandorff, S.1    Olsen, J.V.2    Bunkenborg, J.3    Blagoev, B.4    Zhang, Y.5    Andersen, J.S.6    Mann, M.7
  • 56
    • 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., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 57
    • 80051631238 scopus 로고    scopus 로고
    • GProX, a user-friendly platform for bioinformatics analysis and visualization of quantitative proteomics data
    • 10.1074/ mcp.O110.007450
    • Rigbolt, K. T., Vanselow, J. T., and Blagoev, B. (2011) GProX, a user-friendly platform for bioinformatics analysis and visualization of quantitative proteomics data. Mol. Cell. Proteomics 10.1074/ mcp.O110.007450
    • (2011) Mol. Cell. Proteomics
    • Rigbolt, K.T.1    Vanselow, J.T.2    Blagoev, B.3
  • 58
    • 3242888703 scopus 로고    scopus 로고
    • LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation
    • DOI 10.1242/jcs.01131
    • Kabeya, Y., Mizushima, N., Yamamoto, A., Oshitani-Okamoto, S., Ohsumi, Y., and Yoshimori, T. (2004) LC3, GABARAP and GATE16 localize to autophagosomal membrane depending on form-II formation. J. Cell Sci. 117, 2805-2812 (Pubitemid 38997262)
    • (2004) Journal of Cell Science , vol.117 , Issue.13 , pp. 2805-2812
    • Kabeya, Y.1    Mizushima, N.2    Yamamoto, A.3    Oshitani-Okamoto, S.4    Ohsumi, Y.5    Yoshimori, T.6
  • 59
    • 4344563878 scopus 로고    scopus 로고
    • Role and regulation of starvation-induced autophagy in the Drosophila fat body
    • DOI 10.1016/j.devcel.2004.07.009, PII S153458070400245X
    • Scott, R. C., Schuldiner, O., and Neufeld, T. P. (2004) Role and regulation of starvation-induced autophagy in the Drosophila fat body. Dev. Cell 7, 167-178 (Pubitemid 39145023)
    • (2004) Developmental Cell , vol.7 , Issue.2 , pp. 167-178
    • Scott, R.C.1    Schuldiner, O.2    Neufeld, T.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.