메뉴 건너뛰기




Volumn 378, Issue 4, 2008, Pages 790-803

TRPM7 Regulates Myosin IIA Filament Stability and Protein Localization by Heavy Chain Phosphorylation

Author keywords

actin; cytoskeleton; myosin IIA; phosphorylation; TRPM7

Indexed keywords

ALANINE; ASPARTIC ACID; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN IIA; SERINE; THREONINE; TRANSIENT RECEPTOR POTENTIAL CHANNEL M; TRANSIENT RECEPTOR POTENTIAL CHANNEL M7; UNCLASSIFIED DRUG;

EID: 41949091771     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.057     Document Type: Article
Times cited : (121)

References (54)
  • 1
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V., and Sheetz M. Local force and geometry sensing regulate cell functions. Nat. Rev. Mol. Cell Biol. 7 (2006) 265-275
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 2
    • 24644441368 scopus 로고    scopus 로고
    • The comings and goings of actin: coupling protrusion and retraction in cell motility
    • Small J.V., and Resch G.P. The comings and goings of actin: coupling protrusion and retraction in cell motility. Curr. Opin. Cell Biol. 17 (2005) 517-523
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 517-523
    • Small, J.V.1    Resch, G.P.2
  • 3
    • 21744445075 scopus 로고    scopus 로고
    • Regulation of myosin II during cytokinesis in higher eukaryotes
    • Matsumura F. Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol. 15 (2005) 371-377
    • (2005) Trends Cell Biol. , vol.15 , pp. 371-377
    • Matsumura, F.1
  • 4
    • 33644856260 scopus 로고    scopus 로고
    • New insights into myosin evolution and classification
    • Foth B.J., Goedecke M.C., and Soldati D. New insights into myosin evolution and classification. Proc. Natl Acad. Sci. USA 103 (2006) 3681-3686
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 3681-3686
    • Foth, B.J.1    Goedecke, M.C.2    Soldati, D.3
  • 6
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton S.L., and Waterman-Storer C.M. Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125 (2006) 1361-1374
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 7
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler A.J., Sen S., Sweeney H.L., and Discher D.E. Matrix elasticity directs stem cell lineage specification. Cell 126 (2006) 677-689
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 8
    • 0347477365 scopus 로고    scopus 로고
    • Mechanobiology and diseases of mechanotransduction
    • Ingber D.E. Mechanobiology and diseases of mechanotransduction. Ann. Med. 35 (2003) 564-577
    • (2003) Ann. Med. , vol.35 , pp. 564-577
    • Ingber, D.E.1
  • 9
    • 24044500344 scopus 로고    scopus 로고
    • Myosins: tails (and heads) of functional diversity
    • Krendel M., and Mooseker M.S. Myosins: tails (and heads) of functional diversity. Physiology (Bethesda) 20 (2005) 239-251
    • (2005) Physiology (Bethesda) , vol.20 , pp. 239-251
    • Krendel, M.1    Mooseker, M.S.2
  • 10
    • 14044278735 scopus 로고    scopus 로고
    • Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod
    • Hostetter D., Rice S., Dean S., Altman D., McMahon P.M., Sutton S., et al. Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod. PLoS Biol. 2 (2004) 1880-1892
    • (2004) PLoS Biol. , vol.2 , pp. 1880-1892
    • Hostetter, D.1    Rice, S.2    Dean, S.3    Altman, D.4    McMahon, P.M.5    Sutton, S.6
  • 11
    • 21244469821 scopus 로고    scopus 로고
    • Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis
    • Bao J., Jana S.S., and Adelstein R.S. Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis. J. Biol. Chem. 280 (2005) 19594-19599
    • (2005) J. Biol. Chem. , vol.280 , pp. 19594-19599
    • Bao, J.1    Jana, S.S.2    Adelstein, R.S.3
  • 12
    • 9144261091 scopus 로고    scopus 로고
    • Identification and characterization of nonmuscle myosin II-C, a new member of the myosin II family
    • Golomb E., Ma X., Jana S.S., Preston Y.A., Kawamoto S., Shoham N.G., et al. Identification and characterization of nonmuscle myosin II-C, a new member of the myosin II family. J. Biol. Chem. 279 (2004) 2800-2808
    • (2004) J. Biol. Chem. , vol.279 , pp. 2800-2808
    • Golomb, E.1    Ma, X.2    Jana, S.S.3    Preston, Y.A.4    Kawamoto, S.5    Shoham, N.G.6
  • 13
    • 0344012487 scopus 로고    scopus 로고
    • Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction
    • Kolega J. Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction. Mol. Biol. Cell 14 (2003) 4745-4757
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4745-4757
    • Kolega, J.1
  • 14
    • 33749503375 scopus 로고    scopus 로고
    • The role of myosin II motor activity in distributing myosin asymmetrically and coupling protrusive activity to cell translocation
    • Kolega J. The role of myosin II motor activity in distributing myosin asymmetrically and coupling protrusive activity to cell translocation. Mol. Biol. Cell 17 (2006) 4435-4445
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4435-4445
    • Kolega, J.1
  • 16
    • 20744438782 scopus 로고    scopus 로고
    • Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II-C
    • Kim K.Y., Kovacs M., Kawamoto S., Sellers J.R., and Adelstein R.S. Disease-associated mutations and alternative splicing alter the enzymatic and motile activity of nonmuscle myosins II-B and II-C. J. Biol. Chem. 280 (2005) 22769-22775
    • (2005) J. Biol. Chem. , vol.280 , pp. 22769-22775
    • Kim, K.Y.1    Kovacs, M.2    Kawamoto, S.3    Sellers, J.R.4    Adelstein, R.S.5
  • 17
    • 33747642291 scopus 로고    scopus 로고
    • A specific isoform of nonmuscle myosin II-C is required for cytokinesis in a tumor cell line
    • Jana S.S., Kawamoto S., and Adelstein R.S. A specific isoform of nonmuscle myosin II-C is required for cytokinesis in a tumor cell line. J. Biol. Chem. 281 (2006) 24662-24670
    • (2006) J. Biol. Chem. , vol.281 , pp. 24662-24670
    • Jana, S.S.1    Kawamoto, S.2    Adelstein, R.S.3
  • 18
    • 1642448472 scopus 로고    scopus 로고
    • Functional divergence of human cytoplasmic myosin II: kinetic characterization of the non-muscle IIA isoform
    • Kovacs M., Wang F., Hu A., Zhang Y., and Sellers J.R. Functional divergence of human cytoplasmic myosin II: kinetic characterization of the non-muscle IIA isoform. J. Biol. Chem. 278 (2003) 38132-38140
    • (2003) J. Biol. Chem. , vol.278 , pp. 38132-38140
    • Kovacs, M.1    Wang, F.2    Hu, A.3    Zhang, Y.4    Sellers, J.R.5
  • 19
    • 0042347443 scopus 로고    scopus 로고
    • Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance
    • Wang F., Kovacs M., Hu A., Limouze J., Harvey E.V., and Sellers J.R. Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance. J. Biol. Chem. 278 (2003) 27439-27448
    • (2003) J. Biol. Chem. , vol.278 , pp. 27439-27448
    • Wang, F.1    Kovacs, M.2    Hu, A.3    Limouze, J.4    Harvey, E.V.5    Sellers, J.R.6
  • 20
    • 0344198168 scopus 로고    scopus 로고
    • Mts1 regulates the assembly of nonmuscle myosin-IIA
    • Li Z.H., Spektor A., Varlamova O., and Bresnick A.R. Mts1 regulates the assembly of nonmuscle myosin-IIA. Biochemistry 42 (2003) 14258-14266
    • (2003) Biochemistry , vol.42 , pp. 14258-14266
    • Li, Z.H.1    Spektor, A.2    Varlamova, O.3    Bresnick, A.R.4
  • 22
    • 4744364577 scopus 로고    scopus 로고
    • Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice
    • Conti M.A., Even-Ram S., Liu C., Yamada K.M., and Adelstein R.S. Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice. J. Biol. Chem. 279 (2004) 41263-41266
    • (2004) J. Biol. Chem. , vol.279 , pp. 41263-41266
    • Conti, M.A.1    Even-Ram, S.2    Liu, C.3    Yamada, K.M.4    Adelstein, R.S.5
  • 23
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase. Physiol. Rev. 83 (2003) 1325-1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 25
    • 18244385740 scopus 로고    scopus 로고
    • Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation
    • Dulyaninova N.G., Malashkevich V.N., Almo S.C., and Bresnick A.R. Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation. Biochemistry 44 (2005) 6867-6876
    • (2005) Biochemistry , vol.44 , pp. 6867-6876
    • Dulyaninova, N.G.1    Malashkevich, V.N.2    Almo, S.C.3    Bresnick, A.R.4
  • 26
    • 33644865885 scopus 로고    scopus 로고
    • Protein kinase Cgamma regulates myosin IIB phosphorylation, cellular localization, and filament assembly
    • Rosenberg M., and Ravid S. Protein kinase Cgamma regulates myosin IIB phosphorylation, cellular localization, and filament assembly. Mol. Biol. Cell 17 (2006) 1364-1374
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1364-1374
    • Rosenberg, M.1    Ravid, S.2
  • 27
    • 33745625368 scopus 로고    scopus 로고
    • PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly
    • Even-Faitelson L., and Ravid S. PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly. Mol. Biol. Cell 17 (2006) 2869-2881
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2869-2881
    • Even-Faitelson, L.1    Ravid, S.2
  • 30
    • 1842536165 scopus 로고    scopus 로고
    • Alpha-kinases: analysis of the family and comparison with conventional protein kinases
    • Drennan D., and Ryazanov A.G. Alpha-kinases: analysis of the family and comparison with conventional protein kinases. Prog. Biophys. Mol. Biol. 85 (2004) 1-32
    • (2004) Prog. Biophys. Mol. Biol. , vol.85 , pp. 1-32
    • Drennan, D.1    Ryazanov, A.G.2
  • 31
    • 33748256486 scopus 로고    scopus 로고
    • The regulation of myosin II in Dictyostelium
    • Bosgraaf L., and van Haastert P.J. The regulation of myosin II in Dictyostelium. Eur. J. Cell Biol. 85 (2006) 969-979
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 969-979
    • Bosgraaf, L.1    van Haastert, P.J.2
  • 33
    • 0033787392 scopus 로고    scopus 로고
    • Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells
    • Wei Q., and Adelstein R.S. Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells. Mol. Biol. Cell 11 (2000) 3617-3627
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3617-3627
    • Wei, Q.1    Adelstein, R.S.2
  • 34
    • 41949095658 scopus 로고    scopus 로고
    • MHC-IIB filament assembly and cellular localization are governed by the rod net charge
    • Rosenberg M., Straussman R., Ben-Ya'acov A., Ronen D., and Ravid S. MHC-IIB filament assembly and cellular localization are governed by the rod net charge. PLoS ONE 3 (2008) e1496
    • (2008) PLoS ONE , vol.3
    • Rosenberg, M.1    Straussman, R.2    Ben-Ya'acov, A.3    Ronen, D.4    Ravid, S.5
  • 35
    • 0034602323 scopus 로고    scopus 로고
    • Calcium-dependent threonine phosphorylation of nonmuscle myosin in stimulated RBL-2H3 mast cells
    • Buxton D.B., and Adelstein R.S. Calcium-dependent threonine phosphorylation of nonmuscle myosin in stimulated RBL-2H3 mast cells. J. Biol. Chem. 275 (2000) 34772-34779
    • (2000) J. Biol. Chem. , vol.275 , pp. 34772-34779
    • Buxton, D.B.1    Adelstein, R.S.2
  • 36
    • 34547757869 scopus 로고    scopus 로고
    • Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells
    • Dulyaninova N.G., House R.P., Betapudi V., and Bresnick A.R. Myosin-IIA heavy-chain phosphorylation regulates the motility of MDA-MB-231 carcinoma cells. Mol. Biol. Cell 18 (2007) 3144-3155
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3144-3155
    • Dulyaninova, N.G.1    House, R.P.2    Betapudi, V.3    Bresnick, A.R.4
  • 37
    • 0035131504 scopus 로고    scopus 로고
    • TRP-PLIK, a bifunctional protein with kinase and ion channel activities
    • Runnels L.W., Yue L., and Clapham D.E. TRP-PLIK, a bifunctional protein with kinase and ion channel activities. Science 291 (2001) 1043-1047
    • (2001) Science , vol.291 , pp. 1043-1047
    • Runnels, L.W.1    Yue, L.2    Clapham, D.E.3
  • 38
    • 0035978239 scopus 로고    scopus 로고
    • LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability
    • Nadler M.J., Hermosura M.C., Inabe K., Perraud A.L., Zhu Q., Stokes A.J., et al. LTRPC7 is a Mg.ATP-regulated divalent cation channel required for cell viability. Nature 411 (2001) 590-595
    • (2001) Nature , vol.411 , pp. 590-595
    • Nadler, M.J.1    Hermosura, M.C.2    Inabe, K.3    Perraud, A.L.4    Zhu, Q.5    Stokes, A.J.6
  • 39
    • 0035146457 scopus 로고    scopus 로고
    • Separate but linked functions of conventional myosins modulate adhesion and neurite outgrowth
    • Wylie S.R., and Chantler P.D. Separate but linked functions of conventional myosins modulate adhesion and neurite outgrowth. Nat. Cell Biol. 3 (2001) 88-92
    • (2001) Nat. Cell Biol. , vol.3 , pp. 88-92
    • Wylie, S.R.1    Chantler, P.D.2
  • 40
    • 11144225866 scopus 로고    scopus 로고
    • Rod mutations associated with MYH9-related disorders disrupt nonmuscle myosin-IIA assembly
    • Franke J.D., Dong F., Rickoll W.L., Kelley M.J., and Kiehart D.P. Rod mutations associated with MYH9-related disorders disrupt nonmuscle myosin-IIA assembly. Blood 105 (2005) 161-169
    • (2005) Blood , vol.105 , pp. 161-169
    • Franke, J.D.1    Dong, F.2    Rickoll, W.L.3    Kelley, M.J.4    Kiehart, D.P.5
  • 41
    • 0033812573 scopus 로고    scopus 로고
    • Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes. The May-Hegglin/Fechtner Syndrome Consortium
    • Seri M., Cusano R., Gangarossa S., Caridi G., Bordo D., Lo Nigro C., et al. Mutations in MYH9 result in the May-Hegglin anomaly, and Fechtner and Sebastian syndromes. The May-Hegglin/Fechtner Syndrome Consortium. Nat. Genet. 26 (2000) 103-105
    • (2000) Nat. Genet. , vol.26 , pp. 103-105
    • Seri, M.1    Cusano, R.2    Gangarossa, S.3    Caridi, G.4    Bordo, D.5    Lo Nigro, C.6
  • 42
    • 0033822065 scopus 로고    scopus 로고
    • Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly
    • Kelley M.J., Jawien W., Ortel T.L., and Korczak J.F. Mutation of MYH9, encoding non-muscle myosin heavy chain A, in May-Hegglin anomaly. Nat. Genet. 26 (2000) 106-108
    • (2000) Nat. Genet. , vol.26 , pp. 106-108
    • Kelley, M.J.1    Jawien, W.2    Ortel, T.L.3    Korczak, J.F.4
  • 43
    • 21644467031 scopus 로고    scopus 로고
    • PAK1 regulates myosin II-B phosphorylation, filament assembly, localization and cell chemotaxis
    • Even-Faitelson L., Rosenberg M., and Ravid S. PAK1 regulates myosin II-B phosphorylation, filament assembly, localization and cell chemotaxis. Cell. Signalling 17 (2005) 1137-1148
    • (2005) Cell. Signalling , vol.17 , pp. 1137-1148
    • Even-Faitelson, L.1    Rosenberg, M.2    Ravid, S.3
  • 44
    • 0034687146 scopus 로고    scopus 로고
    • Two distinct mechanisms for regulation of nonmuscle myosin assembly via the heavy chain: phosphorylation for MIIB and mts1 binding for MIIA
    • Murakami N., Kotula L., and Hwang Y.W. Two distinct mechanisms for regulation of nonmuscle myosin assembly via the heavy chain: phosphorylation for MIIB and mts1 binding for MIIA. Biochemistry 39 (2000) 11441-11451
    • (2000) Biochemistry , vol.39 , pp. 11441-11451
    • Murakami, N.1    Kotula, L.2    Hwang, Y.W.3
  • 45
    • 0034845686 scopus 로고    scopus 로고
    • Myosin II heavy chain isoforms are phosphorylated in an EGF-dependent manner: involvement of protein kinase C
    • Straussman R., Even L., and Ravid S. Myosin II heavy chain isoforms are phosphorylated in an EGF-dependent manner: involvement of protein kinase C. J. Cell Sci. 114 (2001) 3047-3057
    • (2001) J. Cell Sci. , vol.114 , pp. 3047-3057
    • Straussman, R.1    Even, L.2    Ravid, S.3
  • 46
    • 33746215280 scopus 로고    scopus 로고
    • Phosphorylation of nonmuscle myosin heavy chain IIA on Ser1917 is mediated by protein kinase C beta II and coincides with the onset of stimulated degranulation of RBL-2H3 mast cells
    • Ludowyke R.I., Elgundi Z., Kranenburg T., Stehn J.R., Schmitz-Peiffer C., Hughes W.E., and Biden T.J. Phosphorylation of nonmuscle myosin heavy chain IIA on Ser1917 is mediated by protein kinase C beta II and coincides with the onset of stimulated degranulation of RBL-2H3 mast cells. J. Immunol. 177 (2006) 1492-1499
    • (2006) J. Immunol. , vol.177 , pp. 1492-1499
    • Ludowyke, R.I.1    Elgundi, Z.2    Kranenburg, T.3    Stehn, J.R.4    Schmitz-Peiffer, C.5    Hughes, W.E.6    Biden, T.J.7
  • 47
    • 0032539586 scopus 로고    scopus 로고
    • Two nonmuscle myosin II heavy chain isoforms expressed in rabbit brains: filament forming properties, the effects of phosphorylation by protein kinase C and casein kinase II, and location of the phosphorylation sites
    • Murakami N., Chauhan V.P., and Elzinga M. Two nonmuscle myosin II heavy chain isoforms expressed in rabbit brains: filament forming properties, the effects of phosphorylation by protein kinase C and casein kinase II, and location of the phosphorylation sites. Biochemistry 37 (1998) 1989-2003
    • (1998) Biochemistry , vol.37 , pp. 1989-2003
    • Murakami, N.1    Chauhan, V.P.2    Elzinga, M.3
  • 48
    • 33744961824 scopus 로고    scopus 로고
    • TRPM7 regulates cell adhesion by controlling the calcium-dependent protease calpain
    • Su L.T., Agapito M.A., Li M., Simonson W.T., Huttenlocher A., Habas R., et al. TRPM7 regulates cell adhesion by controlling the calcium-dependent protease calpain. J. Biol. Chem. 281 (2006) 11260-11270
    • (2006) J. Biol. Chem. , vol.281 , pp. 11260-11270
    • Su, L.T.1    Agapito, M.A.2    Li, M.3    Simonson, W.T.4    Huttenlocher, A.5    Habas, R.6
  • 49
    • 0036905264 scopus 로고    scopus 로고
    • Move over protein kinase C, you've got company: alternative cellular effectors of diacylglycerol and phorbol esters
    • Brose N., and Rosenmund C. Move over protein kinase C, you've got company: alternative cellular effectors of diacylglycerol and phorbol esters. J. Cell Sci. 115 (2002) 4399-4411
    • (2002) J. Cell Sci. , vol.115 , pp. 4399-4411
    • Brose, N.1    Rosenmund, C.2
  • 50
    • 1642421365 scopus 로고    scopus 로고
    • Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains
    • Burgstaller G., and Gimona M. Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains. J. Cell Sci. 117 (2004) 223-231
    • (2004) J. Cell Sci. , vol.117 , pp. 223-231
    • Burgstaller, G.1    Gimona, M.2
  • 52
    • 0012059894 scopus 로고    scopus 로고
    • Identification of protein phosphorylation sites by a combination of mass spectrometry and solid phase Edman sequencing
    • Campbell D.G., and Morrice N.A. Identification of protein phosphorylation sites by a combination of mass spectrometry and solid phase Edman sequencing. J. Biomol. Tech. 13 (2002) 119-130
    • (2002) J. Biomol. Tech. , vol.13 , pp. 119-130
    • Campbell, D.G.1    Morrice, N.A.2
  • 53
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desor7ption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber J., Ishihama Y., and Mann M. Stop and go extraction tips for matrix-assisted laser desor7ption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal. Chem. 75 (2003) 663-670
    • (2003) Anal. Chem. , vol.75 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 54
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127 (2006) 635-648
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.