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Volumn 9, Issue 6, 2010, Pages 3280-3289

Brain phosphoproteome obtained by a fasp-based method reveals plasma membrane protein topology

Author keywords

Brain; FASP; Ion channel; Phosphoproteomics; Proteomics

Indexed keywords

ANTIBODY; BRAIN PROTEIN; CALCIUM CHANNEL; CELL MEMBRANE PROTEIN; GLUTAMATE RECEPTOR; ION CHANNEL; PEPTIDE; PHOSPHOPEPTIDE; PHOSPHOPROTEOME; PHOSPHOTYROSINE; PROTEOME; RESIN; TITANIUM DIOXIDE; UNCLASSIFIED DRUG;

EID: 77954565509     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr1002214     Document Type: Article
Times cited : (237)

References (54)
  • 2
    • 0345185172 scopus 로고    scopus 로고
    • Beta subunits of voltage-gated calcium channels
    • Dolphin, A. C. Beta subunits of voltage-gated calcium channels. J. Bioenerg. Biomembr. 2003, 35 (6), 599-620.
    • (2003) J. Bioenerg. Biomembr. , vol.35 , Issue.6 , pp. 599-620
    • Dolphin, A.C.1
  • 3
    • 73149096944 scopus 로고    scopus 로고
    • Rapid and reversible inhibition of aquaporin-4 by zinc
    • Yukutake, Y.; Hirano, Y.; Suematsu, M.; Yasui, M. Rapid and reversible inhibition of aquaporin-4 by zinc. Biochemistry 2009, 48 (51), 12059-12061
    • (2009) Biochemistry , vol.48 , Issue.51 , pp. 12059-12061
    • Yukutake, Y.1    Hirano, Y.2    Suematsu, M.3    Yasui, M.4
  • 7
    • 47849089500 scopus 로고    scopus 로고
    • Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder
    • Collins, M. O.; Yu, L.; Campuzano, I.; Grant, S. G.; Choudhary, J. S. Phosphoproteomic analysis of the mouse brain cytosol reveals a predominance of protein phosphorylation in regions of intrinsic sequence disorder. Mol. Cell. Proteomics 2008, 7 (7), 1331-1348
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.7 , pp. 1331-1348
    • Collins, M.O.1    Yu, L.2    Campuzano, I.3    Grant, S.G.4    Choudhary, J.S.5
  • 8
    • 38649139336 scopus 로고    scopus 로고
    • Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain
    • Ballif, B. A.; Carey, G. R.; Sunyaev, S. R.; Gygi, S. P. Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain. J. Proteome Res. 2008, 7 (1), 311-318
    • (2008) J. Proteome Res. , vol.7 , Issue.1 , pp. 311-318
    • Ballif, B.A.1    Carey, G.R.2    Sunyaev, S.R.3    Gygi, S.P.4
  • 9
    • 70449426592 scopus 로고    scopus 로고
    • Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain
    • Tweedie-Cullen, R. Y.; Reck, J. M.; Mansuy, I. M. Comprehensive mapping of post-translational modifications on synaptic, nuclear, and histone proteins in the adult mouse brain. J. Proteome Res. 2009, 8 (11), 4966-4982
    • (2009) J. Proteome Res. , vol.8 , Issue.11 , pp. 4966-4982
    • Tweedie-Cullen, R.Y.1    Reck, J.M.2    Mansuy, I.M.3
  • 10
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R.; Zougman, A.; Nagaraj, N.; Mann, M. Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6 (5), 359-362
    • (2009) Nat. Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 11
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski, J. R.; Zougman, A.; Mann, M. Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J. Proteome Res. 2009, 8 (12), 5674-5678
    • (2009) J. Proteome Res. , vol.8 , Issue.12 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 12
    • 68549122961 scopus 로고    scopus 로고
    • Caenorhabditis elegans has a phosphoproteome atypical for metazoans that is enriched in developmental and sex determination proteins
    • Zielinska, D. F.; Gnad, F.; Jedrusik-Bode, M.; Wisniewski, J. R.; Mann, M. Caenorhabditis elegans has a phosphoproteome atypical for metazoans that is enriched in developmental and sex determination proteins. J. Proteome Res. 2009, 8 (8), 4039-4049
    • (2009) J. Proteome Res. , vol.8 , Issue.8 , pp. 4039-4049
    • Zielinska, D.F.1    Gnad, F.2    Jedrusik-Bode, M.3    Wisniewski, J.R.4    Mann, M.5
  • 13
    • 70349972517 scopus 로고    scopus 로고
    • Global analysis of the yeast osmotic stress response by quantitative proteomics
    • Soufi, B.; Kelstrup, C. D.; Stoehr, G.; Frohlich, F.; Walther, T. C.; Olsen, J. V. Global analysis of the yeast osmotic stress response by quantitative proteomics. Mol. BioSyst. 2009, 5 (11), 1337-1346
    • (2009) Mol. BioSyst. , vol.5 , Issue.11 , pp. 1337-1346
    • Soufi, B.1    Kelstrup, C.D.2    Stoehr, G.3    Frohlich, F.4    Walther, T.C.5    Olsen, J.V.6
  • 14
    • 77953240454 scopus 로고    scopus 로고
    • Precision mapping of an in vivo N-linked glycoproteome reveals rigid topological and sequence constraints
    • May 28
    • Zielinska, D. F.; Gnad, F.; Wisniewski, J. R.; Mann, M. Precision mapping of an in vivo N-linked glycoproteome reveals rigid topological and sequence constraints. Cell 2010, 141 (May 28), in press.
    • Cell , vol.2010 , pp. 141
    • Zielinska, D.F.1    Gnad, F.2    Wisniewski, J.R.3    Mann, M.4
  • 15
    • 70350728339 scopus 로고    scopus 로고
    • Spin filter-based sample preparation for shotgun proteomics (Reply)
    • Wisniewski, J. R.; Mann, M. Spin filter-based sample preparation for shotgun proteomics (Reply). Nat. Methods 2009, 6 (11), 785-786
    • (2009) Nat. Methods , vol.6 , Issue.11 , pp. 785-786
    • Wisniewski, J.R.1    Mann, M.2
  • 17
    • 0040597130 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the acidic tails of the high mobility group 1 proteins by casein kinase II alters their conformation, stability, and DNA binding specificity
    • Wisniewski, J. R.; Szewczuk, Z.; Petry, I.; Schwanbeck, R.; Renner, U. Constitutive phosphorylation of the acidic tails of the high mobility group 1 proteins by casein kinase II alters their conformation, stability, and DNA binding specificity. J. Biol. Chem. 1999, 274 (29), 20116-20122
    • (1999) J. Biol. Chem. , vol.274 , Issue.29 , pp. 20116-20122
    • Wisniewski, J.R.1    Szewczuk, Z.2    Petry, I.3    Schwanbeck, R.4    Renner, U.5
  • 18
    • 62349122241 scopus 로고    scopus 로고
    • High accuracy mass spectrometry in largescale analysis of protein phosphorylation
    • Olsen, J. V.; Macek, B. High accuracy mass spectrometry in largescale analysis of protein phosphorylation. Methods Mol. Biol. 2009, 492, 131-142
    • (2009) Methods Mol. Biol. , vol.492 , pp. 131-142
    • Olsen, J.V.1    MacEk, B.2
  • 20
    • 11444263845 scopus 로고    scopus 로고
    • Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry
    • Nuhse, T. S.; Stensballe, A.; Jensen, O. N.; Peck, S. C. Large-scale analysis of in vivo phosphorylated membrane proteins by immobilized metal ion affinity chromatography and mass spectrometry. Mol. Cell. Proteomics 2003, 2 (11), 1234-1243
    • (2003) Mol. Cell. Proteomics , vol.2 , Issue.11 , pp. 1234-1243
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 21
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W.; Uitto, P. M.; Hilhorst, M. J.; Ooms, B.; Heck, A. J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns. Anal. Chem. 2004, 76 (14), 3935-3943
    • (2004) Anal. Chem. , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 22
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen, M. R.; Thingholm, T. E.; Jensen, O. N.; Roepstorff, P.; Jorgensen, T. J. Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol. Cell. Proteomics 2005, 4 (7), 873-886
    • (2005) Mol. Cell. Proteomics , vol.4 , Issue.7 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 24
    • 33750456519 scopus 로고    scopus 로고
    • In vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V.; Blagoev, B.; Gnad, F.; Macek, B.; Kumar, C.; Mortensen, P.; Mann, M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127 (3), 635-648
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Global, M.M.7
  • 26
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification
    • Cox, J.; Mann, M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification. Nat. Biotechnol. 2008, 26 (12), 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , Issue.12 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 27
    • 0033434080 scopus 로고    scopus 로고
    • Probabilitybased protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probabilitybased protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20 (18), 3551-3567
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 30
    • 0012252011 scopus 로고    scopus 로고
    • Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: Cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus
    • Whitelegge, J. P.; Zhang, H.; Aguilera, R.; Taylor, R. M.; Cramer, W. A. Full subunit coverage liquid chromatography electrospray ionization mass spectrometry (LCMS+) of an oligomeric membrane protein: cytochrome b(6)f complex from spinach and the cyanobacterium Mastigocladus laminosus. Mol. Cell. Proteomics 2002, 1 (10), 816-827
    • (2002) Mol. Cell. Proteomics , vol.1 , Issue.10 , pp. 816-827
    • Whitelegge, J.P.1    Zhang, H.2    Aguilera, R.3    Taylor, R.M.4    Cramer, W.A.5
  • 32
    • 70449392251 scopus 로고    scopus 로고
    • Effect of peptideto-TiO2 beads ratio on phosphopeptide enrichment selectivity
    • Li, Q. R.; Ning, Z. B.; Tang, J. S.; Nie, S.; Zeng, R. Effect of peptideto-TiO2 beads ratio on phosphopeptide enrichment selectivity. J. Proteome Res. 2009, 8 (11), 5375-5381
    • (2009) J. Proteome Res. , vol.8 , Issue.11 , pp. 5375-5381
    • Li, Q.R.1    Ning, Z.B.2    Tang, J.S.3    Nie, S.4    Zeng, R.5
  • 33
    • 75149160944 scopus 로고    scopus 로고
    • Concurrent quantification of proteome and phosphoproteome to reveal system-wide association of protein phosphorylation and gene expression
    • Wu, Y. B.; Dai, J.; Yang, X. L.; Li, S. J.; Zhao, S. L.; Sheng, Q. H.; Tang, J. S.; Zheng, G. Y.; Li, Y. X.; Wu, J. R.; Zeng, R. Concurrent quantification of proteome and phosphoproteome to reveal system-wide association of protein phosphorylation and gene expression. Mol. Cell. Proteomics 2009, 8 (12), 2809-2826
    • (2009) Mol. Cell. Proteomics , vol.8 , Issue.12 , pp. 2809-2826
    • Wu, Y.B.1    Dai, J.2    Yang, X.L.3    Li, S.J.4    Zhao, S.L.5    Sheng, Q.H.6    Tang, J.S.7    Zheng, G.Y.8    Li, Y.X.9    Wu, J.R.10    Zeng, R.11
  • 35
    • 24044440971 scopus 로고    scopus 로고
    • A Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks
    • Maere, S.; Heymans, K.; Kuiper, M. BiNGO: a Cytoscape plugin to assess overrepresentation of gene ontology categories in biological networks. Bioinformatics 2005, 21 (16), 3448-3449
    • (2005) Bioinformatics , vol.21 , Issue.16 , pp. 3448-3449
    • Maere, S.1    Heymans, K.2    Bingo, K.M.3
  • 36
    • 44149105911 scopus 로고    scopus 로고
    • PHOSIDA (phosphorylation site database): Management, structural and evolutionary investigation, and prediction of phosphosites
    • Gnad, F.; Ren, S.; Cox, J.; Olsen, J. V.; Macek, B.; Oroshi, M.; Mann, M. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites. Genome Biol. 2007, 8 (11), R250.
    • (2007) Genome Biol. , vol.8 , Issue.11
    • Gnad, F.1    Ren, S.2    Cox, J.3    Olsen, J.V.4    MacEk, B.5    Oroshi, M.6    Mann, M.7
  • 37
    • 68549085023 scopus 로고    scopus 로고
    • High-accuracy identification and bioinformatic analysis of in vivo protein phosphorylation sites in yeast
    • Gnad, F.; de Godoy, L. M.; Cox, J.; Neuhauser, N.; Ren, S.; Olsen, J. V.; Mann, M. High-accuracy identification and bioinformatic analysis of in vivo protein phosphorylation sites in yeast. Proteomics 2009, 9 (20), 4642-4652
    • (2009) Proteomics , vol.9 , Issue.20 , pp. 4642-4652
    • Gnad, F.1    De Godoy, L.M.2    Cox, J.3    Neuhauser, N.4    Ren, S.5    Olsen, J.V.6    Mann, M.7
  • 38
    • 17844381893 scopus 로고    scopus 로고
    • Linear regression models for solvent accessibility prediction in proteins
    • Wagner, M.; Adamczak, R.; Porollo, A.; Meller, J. Linear regression models for solvent accessibility prediction in proteins. J. Comput. Biol. 2005, 12 (3), 355-369
    • (2005) J. Comput. Biol. , vol.12 , Issue.3 , pp. 355-369
    • Wagner, M.1    Adamczak, R.2    Porollo, A.3    Meller, J.4
  • 40
    • 0029916911 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence data bank and its new supplement TREMBL
    • Bairoch, A.; Apweiler, R. The SWISS-PROT protein sequence data bank and its new supplement TREMBL. Nucleic Acids Res. 1996, 24 (1), 21-25
    • (1996) Nucleic Acids Res. , vol.24 , Issue.1 , pp. 21-25
    • Bairoch, A.1    Apweiler, R.2
  • 41
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A.; Larsson, B.; von Heijne, G.; Sonnhammer, E. L. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 2001, 305 (3), 567-580
    • (2001) J. Mol. Biol. , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 42
    • 4544291080 scopus 로고    scopus 로고
    • Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database
    • Nuhse, T. S.; Stensballe, A.; Jensen, O. N.; Peck, S. C. Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database. Plant Cell 2004, 16 (9), 2394-2405
    • (2004) Plant Cell , vol.16 , Issue.9 , pp. 2394-2405
    • Nuhse, T.S.1    Stensballe, A.2    Jensen, O.N.3    Peck, S.C.4
  • 43
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu, C. C.; MacCoss, M. J.; Howell, K. E.; Yates, J. R., III. A method for the comprehensive proteomic analysis of membrane proteins. Nat. Biotechnol. 2003, 21 (5), 532-538
    • (2003) Nat. Biotechnol. , vol.21 , Issue.5 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates Iii., J.R.4
  • 44
    • 68649099001 scopus 로고    scopus 로고
    • Calcium channel diversity: Multiple roles of calcium channel subunits
    • Dolphin, A. C. Calcium channel diversity: multiple roles of calcium channel subunits. Curr. Opin. Neurobiol. 2009, 19 (3), 237-244
    • (2009) Curr. Opin. Neurobiol. , vol.19 , Issue.3 , pp. 237-244
    • Dolphin, A.C.1
  • 45
    • 76549117726 scopus 로고    scopus 로고
    • The {alpha} 2{delta} subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function
    • Davies, A.; Kadurin, I.; Alvarez-Laviada, A.; Douglas, L.; Nieto-Rostro, M.; Bauer, C. S.; Pratt, W. S.; Dolphin, A. C. The {alpha}2{delta} subunits of voltage-gated calcium channels form GPI-anchored proteins, a posttranslational modification essential for function. Proc. Natl. Acad. Sci. USA 2010, 107 (4), 1654-1659
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , Issue.4 , pp. 1654-1659
    • Davies, A.1    Kadurin, I.2    Alvarez-Laviada, A.3    Douglas, L.4    Nieto-Rostro, M.5    Bauer, C.S.6    Pratt, W.S.7    Dolphin, A.C.8
  • 46
    • 1642535342 scopus 로고    scopus 로고
    • Calcium channel alpha2delta subunits: Differential expression, function, and drug binding
    • Klugbauer, N.; Marais, E.; Hofmann, F. Calcium channel alpha2delta subunits: differential expression, function, and drug binding. J. Bioenerg. Biomembr. 2003, 35 (6), 639-647
    • (2003) J. Bioenerg. Biomembr. , vol.35 , Issue.6 , pp. 639-647
    • Klugbauer, N.1    Marais, E.2    Hofmann, F.3
  • 47
    • 0033543140 scopus 로고    scopus 로고
    • Identification of the sites phosphorylated by cyclic AMP-dependent protein kinase on the beta 2 subunit of L-type voltagedependent calcium channels
    • Gerhardstein, B. L.; Puri, T. S.; Chien, A. J.; Hosey, M. M. Identification of the sites phosphorylated by cyclic AMP-dependent protein kinase on the beta 2 subunit of L-type voltagedependent calcium channels. Biochemistry 1999, 38 (32), 10361-10370
    • (1999) Biochemistry , vol.38 , Issue.32 , pp. 10361-10370
    • Gerhardstein, B.L.1    Puri, T.S.2    Chien, A.J.3    Hosey, M.M.4
  • 48
    • 71649115832 scopus 로고    scopus 로고
    • CaMKII associates with CaV1.2 L-type calcium channels via selected beta subunits to enhance regulatory phosphorylation
    • Abiria, S. A.; Colbran, R. J. CaMKII associates with CaV1.2 L-type calcium channels via selected beta subunits to enhance regulatory phosphorylation. J. Neurochem. 2010, 112 (1), 150-161
    • (2010) J. Neurochem. , vol.112 , Issue.1 , pp. 150-161
    • Abiria, S.A.1    Colbran, R.J.2
  • 49
    • 33846615765 scopus 로고    scopus 로고
    • The trick of the tail: Protein-protein interactions of metabotropic glutamate receptors
    • Enz, R. The trick of the tail: protein-protein interactions of metabotropic glutamate receptors. BioEssays 2007, 29 (1), 60-73.
    • (2007) BioEssays , vol.29 , Issue.1 , pp. 60-73
    • Enz, R.1
  • 50
    • 49949110905 scopus 로고    scopus 로고
    • Phosphorylation of group i metabotropic glutamate receptors (mGluR1/5) in vitro and in vivo
    • Mao, L. M.; Liu, X. Y.; Zhang, G. C.; Chu, X. P.; Fibuch, E. E.; Wang, L. S.; Liu, Z.; Wang, J. Q. Phosphorylation of group I metabotropic glutamate receptors (mGluR1/5) in vitro and in vivo. Neuropharmacology 2008, 55 (4), 403-408
    • (2008) Neuropharmacology , vol.55 , Issue.4 , pp. 403-408
    • Mao, L.M.1    Liu, X.Y.2    Zhang, G.C.3    Chu, X.P.4    Fibuch, E.E.5    Wang, L.S.6    Liu, Z.7    Wang, J.Q.8
  • 51
    • 66749090994 scopus 로고    scopus 로고
    • Comparative proteomic profiling of membrane proteins in rat cerebellum, spinal cord, and sciatic nerve
    • Lu, A.; Wisniewski, J. R.; Mann, M. Comparative proteomic profiling of membrane proteins in rat cerebellum, spinal cord, and sciatic nerve. J. Proteome Res. 2009, 8 (5), 2418-2425
    • (2009) J. Proteome Res. , vol.8 , Issue.5 , pp. 2418-2425
    • Lu, A.1    Wisniewski, J.R.2    Mann, M.3
  • 52
    • 58149383887 scopus 로고    scopus 로고
    • Detergent-based but gel-free method allows identification of several hundred membrane proteins in single LC-MS runs
    • Nagaraj, N.; Lu, A.; Mann, M.; Wisniewski, J. R. Detergent-based but gel-free method allows identification of several hundred membrane proteins in single LC-MS runs. J. Proteome Res. 2008, 7 (11), 5028-5032
    • (2008) J. Proteome Res. , vol.7 , Issue.11 , pp. 5028-5032
    • Nagaraj, N.1    Lu, A.2    Mann, M.3    Wisniewski, J.R.4
  • 53
    • 77950684226 scopus 로고    scopus 로고
    • Mass spectrometry-based GPCR proteomics: Comprehensive characterization of the human cannabinoid 1 receptor
    • Zvonok, N.; Xu, W.; Williams, J.; Janero, D.; Krishnan, S.; Makriyannis, A. Mass spectrometry-based GPCR proteomics: comprehensive characterization of the human cannabinoid 1 receptor. J. Proteome Res. 2010, 9 (4), 1746-1753
    • (2010) J. Proteome Res. , vol.9 , Issue.4 , pp. 1746-1753
    • Zvonok, N.1    Xu, W.2    Williams, J.3    Janero, D.4    Krishnan, S.5    Makriyannis, A.6
  • 54
    • 52049111074 scopus 로고    scopus 로고
    • Profiling the phospho-status of the BKCa channel alpha subunit in rat brain reveals unexpected patterns and complexity
    • Yan, J.; Olsen, J. V.; Park, K. S.; Li, W.; Bildl, W.; Schulte, U.; Aldrich, R. W.; Fakler, B.; Trimmer, J. S. Profiling the phospho-status of the BKCa channel alpha subunit in rat brain reveals unexpected patterns and complexity. Mol. Cell. Proteomics 2008, 7 (11), 2188-2198
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.11 , pp. 2188-2198
    • Yan, J.1    Olsen, J.V.2    Park, K.S.3    Li, W.4    Bildl, W.5    Schulte, U.6    Aldrich, R.W.7    Fakler, B.8    Trimmer, J.S.9


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