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Volumn 33, Issue , 2015, Pages 78-85

Protein networks and activation of lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; PROTEIN KINASE ZAP 70; PROTEOME; T LYMPHOCYTE RECEPTOR; PHOSPHOTRANSFERASE; PROTEIN BINDING;

EID: 84922683472     PISSN: 09527915     EISSN: 18790372     Source Type: Journal    
DOI: 10.1016/j.coi.2015.01.019     Document Type: Review
Times cited : (4)

References (82)
  • 1
    • 84887200580 scopus 로고    scopus 로고
    • Quantitation of endogenous peptides using mass spectrometry based methods
    • Romanova E.V., Dowd S.E., Sweedler J.V. Quantitation of endogenous peptides using mass spectrometry based methods. Curr Opin Chem Biol 2013, 17:801-808.
    • (2013) Curr Opin Chem Biol , vol.17 , pp. 801-808
    • Romanova, E.V.1    Dowd, S.E.2    Sweedler, J.V.3
  • 2
    • 77952538049 scopus 로고    scopus 로고
    • Quantitation in mass-spectrometry-based proteomics
    • Schulze W.X., Usadel B. Quantitation in mass-spectrometry-based proteomics. Annu Rev Plant Biol 2010, 61:491-516.
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 491-516
    • Schulze, W.X.1    Usadel, B.2
  • 3
    • 84920382645 scopus 로고    scopus 로고
    • SLP-76 N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal TCR signaling
    • Ji Q., Ding Y., Salomon A.R. SLP-76 N-terminal tyrosine residues regulate a dynamic signaling equilibrium involving feedback of proximal TCR signaling. Mol Cell Proteomics 2015, 14:30-40.
    • (2015) Mol Cell Proteomics , vol.14 , pp. 30-40
    • Ji, Q.1    Ding, Y.2    Salomon, A.R.3
  • 5
    • 84881525417 scopus 로고    scopus 로고
    • Differential expression of proteins in naive and IL-2 stimulated primary human NK cells identified by global proteomic analysis
    • Ma D., Cao W., Kapur A., Felder M., Scarlett C.O., Patankar M.S., Li L. Differential expression of proteins in naive and IL-2 stimulated primary human NK cells identified by global proteomic analysis. J Proteomics 2013, 91:151-163.
    • (2013) J Proteomics , vol.91 , pp. 151-163
    • Ma, D.1    Cao, W.2    Kapur, A.3    Felder, M.4    Scarlett, C.O.5    Patankar, M.S.6    Li, L.7
  • 6
    • 84878413485 scopus 로고    scopus 로고
    • Proteomic analysis of NK92-MI cells activated by neuropeptide substance P
    • Diandong H., Kefeng S., Weixin F., Zaifu L. Proteomic analysis of NK92-MI cells activated by neuropeptide substance P. Neuropeptides 2013, 47:157-162.
    • (2013) Neuropeptides , vol.47 , pp. 157-162
    • Diandong, H.1    Kefeng, S.2    Weixin, F.3    Zaifu, L.4
  • 7
    • 67649429400 scopus 로고    scopus 로고
    • Functional regulation and proteomic characterization of human natural killer cells through recombinant human granulocyte-colony stimulating factor treatment
    • Chen Y.J., Yu C.C., Chen S.T., Chen T.Y., Liao H.F. Functional regulation and proteomic characterization of human natural killer cells through recombinant human granulocyte-colony stimulating factor treatment. Proteomics Clin Appl 2009, 3:563-573.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 563-573
    • Chen, Y.J.1    Yu, C.C.2    Chen, S.T.3    Chen, T.Y.4    Liao, H.F.5
  • 9
    • 84906921537 scopus 로고    scopus 로고
    • Proteomic changes during B cell maturation: 2D-DIGE approach
    • Salonen J., Ronnholm G., Kalkkinen N., Vihinen M. Proteomic changes during B cell maturation: 2D-DIGE approach. PLOS ONE 2013, 8:e77894.
    • (2013) PLOS ONE , vol.8
    • Salonen, J.1    Ronnholm, G.2    Kalkkinen, N.3    Vihinen, M.4
  • 11
    • 84883643051 scopus 로고    scopus 로고
    • Proteomic analysis of B-cell receptor signaling in chronic lymphocytic leukaemia reveals a possible role for kininogen
    • Kashuba E., Eagle G.L., Bailey J., Evans P., Welham K.J., Allsup D., Cawkwell L. Proteomic analysis of B-cell receptor signaling in chronic lymphocytic leukaemia reveals a possible role for kininogen. J Proteomics 2013, 91:478-485.
    • (2013) J Proteomics , vol.91 , pp. 478-485
    • Kashuba, E.1    Eagle, G.L.2    Bailey, J.3    Evans, P.4    Welham, K.J.5    Allsup, D.6    Cawkwell, L.7
  • 12
    • 71949127588 scopus 로고    scopus 로고
    • A comparison between protein profiles of B cell subpopulations and mantle cell lymphoma cells
    • Stranneheim H., Orre L.M., Lehtio J., Flygare J. A comparison between protein profiles of B cell subpopulations and mantle cell lymphoma cells. Proteome Sci 2009, 7:43.
    • (2009) Proteome Sci , vol.7 , pp. 43
    • Stranneheim, H.1    Orre, L.M.2    Lehtio, J.3    Flygare, J.4
  • 13
    • 84861157792 scopus 로고    scopus 로고
    • Super-SILAC allows classification of diffuse large B-cell lymphoma subtypes by their protein expression profiles
    • Deeb S.J., D'Souza R.C., Cox J., Schmidt-Supprian M., Mann M. Super-SILAC allows classification of diffuse large B-cell lymphoma subtypes by their protein expression profiles. Mol Cell Proteomics 2012, 11:77-89.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 77-89
    • Deeb, S.J.1    D'Souza, R.C.2    Cox, J.3    Schmidt-Supprian, M.4    Mann, M.5
  • 14
    • 71049123949 scopus 로고    scopus 로고
    • Protein profiling of plasma membranes defines aberrant signaling pathways in mantle cell lymphoma
    • Boyd R.S., Jukes-Jones R., Walewska R., Brown D., Dyer M.J., Cain K. Protein profiling of plasma membranes defines aberrant signaling pathways in mantle cell lymphoma. Mol Cell Proteomics 2009, 8:1501-1515.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 1501-1515
    • Boyd, R.S.1    Jukes-Jones, R.2    Walewska, R.3    Brown, D.4    Dyer, M.J.5    Cain, K.6
  • 15
    • 79953010049 scopus 로고    scopus 로고
    • Proteomic characterization of plasma membrane-proximal T cell activation responses
    • de Wet B., Zech T., Salek M., Acuto O., Harder T. Proteomic characterization of plasma membrane-proximal T cell activation responses. J Biol Chem 2011, 286:4072-4080.
    • (2011) J Biol Chem , vol.286 , pp. 4072-4080
    • de Wet, B.1    Zech, T.2    Salek, M.3    Acuto, O.4    Harder, T.5
  • 18
    • 79953693933 scopus 로고    scopus 로고
    • Effector granules in human T lymphocytes: proteomic evidence for two distinct species of cytotoxic effector vesicles
    • Schmidt H., Gelhaus C., Nebendahl M., Lettau M., Lucius R., Leippe M., Kabelitz D., Janssen O. Effector granules in human T lymphocytes: proteomic evidence for two distinct species of cytotoxic effector vesicles. J Proteome Res 2011, 10:1603-1620.
    • (2011) J Proteome Res , vol.10 , pp. 1603-1620
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Lettau, M.4    Lucius, R.5    Leippe, M.6    Kabelitz, D.7    Janssen, O.8
  • 19
    • 48949087726 scopus 로고    scopus 로고
    • 2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells
    • Schmidt H., Gelhaus C., Nebendahl M., Lettau M., Watzl C., Kabelitz D., Leippe M., Janssen O. 2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells. Proteomics 2008, 8:2911-2925.
    • (2008) Proteomics , vol.8 , pp. 2911-2925
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Lettau, M.4    Watzl, C.5    Kabelitz, D.6    Leippe, M.7    Janssen, O.8
  • 20
    • 84876541392 scopus 로고    scopus 로고
    • Direct proteomic quantification of the secretome of activated immune cells
    • Meissner F., Scheltema R.A., Mollenkopf H.J., Mann M. Direct proteomic quantification of the secretome of activated immune cells. Science 2013, 340:475-478.
    • (2013) Science , vol.340 , pp. 475-478
    • Meissner, F.1    Scheltema, R.A.2    Mollenkopf, H.J.3    Mann, M.4
  • 22
    • 80054029767 scopus 로고    scopus 로고
    • The Human Immunopeptidome Project, a suggestion for yet another postgenome next big thing
    • Admon A., Bassani-Sternberg M. The Human Immunopeptidome Project, a suggestion for yet another postgenome next big thing. Mol Cell Proteomics 2011, 10. O111 011833.
    • (2011) Mol Cell Proteomics
    • Admon, A.1    Bassani-Sternberg, M.2
  • 23
    • 79958769266 scopus 로고    scopus 로고
    • Insights into MHC class I antigen processing gained from large-scale analysis of class I ligands
    • Mester G., Hoffmann V., Stevanovic S. Insights into MHC class I antigen processing gained from large-scale analysis of class I ligands. Cell Mol Life Sci 2011, 68:1521-1532.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 1521-1532
    • Mester, G.1    Hoffmann, V.2    Stevanovic, S.3
  • 27
    • 84891938083 scopus 로고    scopus 로고
    • Alloreactive cytotoxic T cells provide means to decipher the immunopeptidome and reveal a plethora of tumor-associated self-epitopes
    • Kumari S., Walchli S., Fallang L.E., Yang W., Lund-Johansen F., Schumacher T.N., Olweus J. Alloreactive cytotoxic T cells provide means to decipher the immunopeptidome and reveal a plethora of tumor-associated self-epitopes. Proc Natl Acad Sci U S A 2014, 111:403-408.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 403-408
    • Kumari, S.1    Walchli, S.2    Fallang, L.E.3    Yang, W.4    Lund-Johansen, F.5    Schumacher, T.N.6    Olweus, J.7
  • 30
    • 84907424304 scopus 로고    scopus 로고
    • A mass spectrometry view of stable and transient protein interactions
    • Budayeva H.G., Cristea I.M. A mass spectrometry view of stable and transient protein interactions. Adv Exp Med Biol 2014, 806:263-282.
    • (2014) Adv Exp Med Biol , vol.806 , pp. 263-282
    • Budayeva, H.G.1    Cristea, I.M.2
  • 31
  • 32
    • 84871669469 scopus 로고    scopus 로고
    • Quantitative proteomics: a strategic ally to map protein interaction networks
    • Marcilla M., Albar J.P. Quantitative proteomics: a strategic ally to map protein interaction networks. IUBMB Life 2013, 65:9-16.
    • (2013) IUBMB Life , vol.65 , pp. 9-16
    • Marcilla, M.1    Albar, J.P.2
  • 33
    • 84871865189 scopus 로고    scopus 로고
    • Popular computational methods to assess multiprotein complexes derived from label-free affinity purification and mass spectrometry (AP-MS) experiments
    • Armean I.M., Lilley K.S., Trotter M.W. Popular computational methods to assess multiprotein complexes derived from label-free affinity purification and mass spectrometry (AP-MS) experiments. Mol Cell Proteomics 2013, 12:1-13.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 1-13
    • Armean, I.M.1    Lilley, K.S.2    Trotter, M.W.3
  • 34
    • 84862705739 scopus 로고    scopus 로고
    • Computational detection of protein complexes in AP-MS experiments
    • Choi H. Computational detection of protein complexes in AP-MS experiments. Proteomics 2012, 12:1663-1668.
    • (2012) Proteomics , vol.12 , pp. 1663-1668
    • Choi, H.1
  • 35
    • 84864619937 scopus 로고    scopus 로고
    • Beyond hairballs: the use of quantitative mass spectrometry data to understand protein-protein interactions
    • Gingras A.C., Raught B. Beyond hairballs: the use of quantitative mass spectrometry data to understand protein-protein interactions. FEBS Lett 2012, 586:2723-2731.
    • (2012) FEBS Lett , vol.586 , pp. 2723-2731
    • Gingras, A.C.1    Raught, B.2
  • 36
    • 84862684340 scopus 로고    scopus 로고
    • Affinity-purification coupled to mass spectrometry: basic principles and strategies
    • Dunham W.H., Mullin M., Gingras A.C. Affinity-purification coupled to mass spectrometry: basic principles and strategies. Proteomics 2012, 12:1576-1590.
    • (2012) Proteomics , vol.12 , pp. 1576-1590
    • Dunham, W.H.1    Mullin, M.2    Gingras, A.C.3
  • 38
    • 84894286325 scopus 로고    scopus 로고
    • Dynamic impacts of the inhibition of the molecular chaperone Hsp90 on the T-cell proteome have implications for anti-cancer therapy
    • Fierro-Monti I., Echeverria P., Racle J., Hernandez C., Picard D., Quadroni M. Dynamic impacts of the inhibition of the molecular chaperone Hsp90 on the T-cell proteome have implications for anti-cancer therapy. PLOS ONE 2013, 8:e80425.
    • (2013) PLOS ONE , vol.8
    • Fierro-Monti, I.1    Echeverria, P.2    Racle, J.3    Hernandez, C.4    Picard, D.5    Quadroni, M.6
  • 39
    • 84897046940 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of signalosome dynamics in primary T cells identifies the surface receptor CD6 as a Lat adaptor-independent TCR signaling hub
    • Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A., Kanduri K., Joly R., Malzac A., Lahdesmaki H., et al. Quantitative proteomics analysis of signalosome dynamics in primary T cells identifies the surface receptor CD6 as a Lat adaptor-independent TCR signaling hub. Nat Immunol 2014, 15:384-392.
    • (2014) Nat Immunol , vol.15 , pp. 384-392
    • Roncagalli, R.1    Hauri, S.2    Fiore, F.3    Liang, Y.4    Chen, Z.5    Sansoni, A.6    Kanduri, K.7    Joly, R.8    Malzac, A.9    Lahdesmaki, H.10
  • 41
    • 84880433886 scopus 로고    scopus 로고
    • ERK positive feedback regulates a widespread network of tyrosine phosphorylation sites across canonical T cell signaling and actin cytoskeletal proteins in Jurkat T cells
    • Helou Y.A., Nguyen V., Beik S.P., Salomon A.R. ERK positive feedback regulates a widespread network of tyrosine phosphorylation sites across canonical T cell signaling and actin cytoskeletal proteins in Jurkat T cells. PLOS ONE 2013, 8:e69641.
    • (2013) PLOS ONE , vol.8
    • Helou, Y.A.1    Nguyen, V.2    Beik, S.P.3    Salomon, A.R.4
  • 42
    • 84867429590 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics reveals SLP-76 dependent regulation of PAG and Src family kinases in T cells
    • Cao L., Ding Y., Hung N., Yu K., Ritz A., Raphael B.J., Salomon A.R. Quantitative phosphoproteomics reveals SLP-76 dependent regulation of PAG and Src family kinases in T cells. PLOS ONE 2012, 7:e46725.
    • (2012) PLOS ONE , vol.7
    • Cao, L.1    Ding, Y.2    Hung, N.3    Yu, K.4    Ritz, A.5    Raphael, B.J.6    Salomon, A.R.7
  • 44
    • 84905206969 scopus 로고    scopus 로고
    • Quantitative phosphoproteome analysis unveils LAT as a modulator of CD3zeta and ZAP-70 tyrosine phosphorylation
    • Salek M., McGowan S., Trudgian D.C., Dushek O., de Wet B., Efstathiou G., Acuto O. Quantitative phosphoproteome analysis unveils LAT as a modulator of CD3zeta and ZAP-70 tyrosine phosphorylation. PLOS ONE 2013, 8:e77423.
    • (2013) PLOS ONE , vol.8
    • Salek, M.1    McGowan, S.2    Trudgian, D.C.3    Dushek, O.4    de Wet, B.5    Efstathiou, G.6    Acuto, O.7
  • 47
    • 67651229135 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of tyrosine-phosphorylation induced by T-cell receptor or B-cell receptor activation reveals new signaling pathways
    • Matsumoto M., Oyamada K., Takahashi H., Sato T., Hatakeyama S., Nakayama K.I. Large-scale proteomic analysis of tyrosine-phosphorylation induced by T-cell receptor or B-cell receptor activation reveals new signaling pathways. Proteomics 2009, 9:3549-3563.
    • (2009) Proteomics , vol.9 , pp. 3549-3563
    • Matsumoto, M.1    Oyamada, K.2    Takahashi, H.3    Sato, T.4    Hatakeyama, S.5    Nakayama, K.I.6
  • 48
    • 33644554807 scopus 로고    scopus 로고
    • Quantitative analysis of phosphotyrosine signaling networks triggered by CD3 and CD28 costimulation in Jurkat cells
    • Kim J.E., White F.M. Quantitative analysis of phosphotyrosine signaling networks triggered by CD3 and CD28 costimulation in Jurkat cells. J Immunol 2006, 176:2833-2843.
    • (2006) J Immunol , vol.176 , pp. 2833-2843
    • Kim, J.E.1    White, F.M.2
  • 50
    • 84886923713 scopus 로고    scopus 로고
    • Integrated phosphoproteomic and metabolomic profiling reveals NPM-ALK-mediated phosphorylation of PKM2 and metabolic reprogramming in anaplastic large cell lymphoma
    • McDonnell S.R., Hwang S.R., Rolland D., Murga-Zamalloa C., Basrur V., Conlon K.P., Fermin D., Wolfe T., Raskind A., Ruan C., et al. Integrated phosphoproteomic and metabolomic profiling reveals NPM-ALK-mediated phosphorylation of PKM2 and metabolic reprogramming in anaplastic large cell lymphoma. Blood 2013, 122:958-968.
    • (2013) Blood , vol.122 , pp. 958-968
    • McDonnell, S.R.1    Hwang, S.R.2    Rolland, D.3    Murga-Zamalloa, C.4    Basrur, V.5    Conlon, K.P.6    Fermin, D.7    Wolfe, T.8    Raskind, A.9    Ruan, C.10
  • 51
    • 70350462371 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions
    • Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal 2009, 2:ra46.
    • (2009) Sci Signal , vol.2 , pp. ra46
    • Mayya, V.1    Lundgren, D.H.2    Hwang, S.I.3    Rezaul, K.4    Wu, L.5    Eng, J.K.6    Rodionov, V.7    Han, D.K.8
  • 52
    • 84903747405 scopus 로고    scopus 로고
    • Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers
    • Jayasundera K.B., Iliuk A.B., Nguyen A., Higgins R., Geahlen R.L., Tao W.A. Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers. Anal Chem 2014, 86:6363-6371.
    • (2014) Anal Chem , vol.86 , pp. 6363-6371
    • Jayasundera, K.B.1    Iliuk, A.B.2    Nguyen, A.3    Higgins, R.4    Geahlen, R.L.5    Tao, W.A.6
  • 54
    • 80052164672 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics revealed interplay between Syk and Lyn in the resistance to nilotinib in chronic myeloid leukemia cells
    • Gioia R., Leroy C., Drullion C., Lagarde V., Etienne G., Dulucq S., Lippert E., Roche S., Mahon F.X., Pasquet J.M. Quantitative phosphoproteomics revealed interplay between Syk and Lyn in the resistance to nilotinib in chronic myeloid leukemia cells. Blood 2011, 118:2211-2221.
    • (2011) Blood , vol.118 , pp. 2211-2221
    • Gioia, R.1    Leroy, C.2    Drullion, C.3    Lagarde, V.4    Etienne, G.5    Dulucq, S.6    Lippert, E.7    Roche, S.8    Mahon, F.X.9    Pasquet, J.M.10
  • 56
    • 84861136348 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis reveals a role for serine and threonine kinases in the cytoskeletal reorganization in early T cell receptor activation in human primary T cells
    • Ruperez P., Gago-Martinez A., Burlingame A.L., Oses-Prieto J.A. Quantitative phosphoproteomic analysis reveals a role for serine and threonine kinases in the cytoskeletal reorganization in early T cell receptor activation in human primary T cells. Mol Cell Proteomics 2012, 11:171-186.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 171-186
    • Ruperez, P.1    Gago-Martinez, A.2    Burlingame, A.L.3    Oses-Prieto, J.A.4
  • 57
    • 79952962027 scopus 로고    scopus 로고
    • Phosphoproteomic analysis reveals an intrinsic pathway for the regulation of histone deacetylase 7 that controls the function of cytotoxic T lymphocytes
    • Navarro M.N., Goebel J., Feijoo-Carnero C., Morrice N., Cantrell D.A. Phosphoproteomic analysis reveals an intrinsic pathway for the regulation of histone deacetylase 7 that controls the function of cytotoxic T lymphocytes. Nat Immunol 2011, 12:352-361.
    • (2011) Nat Immunol , vol.12 , pp. 352-361
    • Navarro, M.N.1    Goebel, J.2    Feijoo-Carnero, C.3    Morrice, N.4    Cantrell, D.A.5
  • 60
    • 0000109995 scopus 로고
    • Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
    • Hunter T., Sefton B.M. Transforming gene product of Rous sarcoma virus phosphorylates tyrosine. Proc Natl Acad Sci U S A 1980, 77:1311-1315.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 1311-1315
    • Hunter, T.1    Sefton, B.M.2
  • 61
    • 77954572010 scopus 로고    scopus 로고
    • Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant mice
    • Iwai L.K., Benoist C., Mathis D., White F.M. Quantitative phosphoproteomic analysis of T cell receptor signaling in diabetes prone and resistant mice. J Proteome Res 2010, 9:3135-3145.
    • (2010) J Proteome Res , vol.9 , pp. 3135-3145
    • Iwai, L.K.1    Benoist, C.2    Mathis, D.3    White, F.M.4
  • 62
    • 79953184690 scopus 로고    scopus 로고
    • Multiple hypothesis testing in proteomics: a strategy for experimental work
    • Diz A.P., Carvajal-Rodriguez A., Skibinski D.O. Multiple hypothesis testing in proteomics: a strategy for experimental work. Mol Cell Proteomics 2011, 10. M110 004374.
    • (2011) Mol Cell Proteomics
    • Diz, A.P.1    Carvajal-Rodriguez, A.2    Skibinski, D.O.3
  • 64
    • 0345822598 scopus 로고    scopus 로고
    • The positive false discovery rate: a Bayesian interpretation and the q-value
    • Storey J.D. The positive false discovery rate: a Bayesian interpretation and the q-value. Ann Stat 2003, 31:2013-2035.
    • (2003) Ann Stat , vol.31 , pp. 2013-2035
    • Storey, J.D.1
  • 65
    • 84889805348 scopus 로고    scopus 로고
    • Staurosporine-derived inhibitors broaden the scope of analog-sensitive kinase technology
    • Lopez M.S., Choy J.W., Peters U., Sos M.L., Morgan D.O., Shokat K.M. Staurosporine-derived inhibitors broaden the scope of analog-sensitive kinase technology. J Am Chem Soc 2013, 135:18153-18159.
    • (2013) J Am Chem Soc , vol.135 , pp. 18153-18159
    • Lopez, M.S.1    Choy, J.W.2    Peters, U.3    Sos, M.L.4    Morgan, D.O.5    Shokat, K.M.6
  • 66
    • 84892719664 scopus 로고    scopus 로고
    • Inhibition of the kinase Csk in thymocytes reveals a requirement for actin remodeling in the initiation of full TCR signaling
    • Tan Y.X., Manz B.N., Freedman T.S., Zhang C., Shokat K.M., Weiss A. Inhibition of the kinase Csk in thymocytes reveals a requirement for actin remodeling in the initiation of full TCR signaling. Nat Immunol 2014, 15:186-194.
    • (2014) Nat Immunol , vol.15 , pp. 186-194
    • Tan, Y.X.1    Manz, B.N.2    Freedman, T.S.3    Zhang, C.4    Shokat, K.M.5    Weiss, A.6
  • 69
    • 79959735228 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells
    • Kettenbach A.N., Schweppe D.K., Faherty B.K., Pechenick D., Pletnev A.A., Gerber S.A. Quantitative phosphoproteomics identifies substrates and functional modules of Aurora and Polo-like kinase activities in mitotic cells. Sci Signal 2011, 4:rs5.
    • (2011) Sci Signal , vol.4 , pp. rs5
    • Kettenbach, A.N.1    Schweppe, D.K.2    Faherty, B.K.3    Pechenick, D.4    Pletnev, A.A.5    Gerber, S.A.6
  • 71
  • 74
    • 84896708757 scopus 로고    scopus 로고
    • A comparative study of ATP analogs for phosphorylation-dependent kinase-substrate crosslinking
    • Garre S., Senevirathne C., Pflum M.K. A comparative study of ATP analogs for phosphorylation-dependent kinase-substrate crosslinking. Bioorg Med Chem 2014, 22:1620-1625.
    • (2014) Bioorg Med Chem , vol.22 , pp. 1620-1625
    • Garre, S.1    Senevirathne, C.2    Pflum, M.K.3
  • 75
    • 84885115150 scopus 로고    scopus 로고
    • Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomics
    • Xue L., Geahlen R.L., Tao W.A. Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomics. Mol Cell Proteomics 2013, 12:2969-2980.
    • (2013) Mol Cell Proteomics , vol.12 , pp. 2969-2980
    • Xue, L.1    Geahlen, R.L.2    Tao, W.A.3
  • 76
    • 84910626377 scopus 로고    scopus 로고
    • Identification of ERK1 direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics
    • Xue L., Wang P., Cao P., Zhu J.K., Tao W.A. Identification of ERK1 direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics. Mol Cell Proteomics 2014, 13:3199-3210.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 3199-3210
    • Xue, L.1    Wang, P.2    Cao, P.3    Zhu, J.K.4    Tao, W.A.5
  • 77
    • 84899929564 scopus 로고    scopus 로고
    • Heterogeneity in immune responses: from populations to single cells
    • Satija R., Shalek A.K. Heterogeneity in immune responses: from populations to single cells. Trends Immunol 2014, 35:219-229.
    • (2014) Trends Immunol , vol.35 , pp. 219-229
    • Satija, R.1    Shalek, A.K.2
  • 78
    • 84884138622 scopus 로고    scopus 로고
    • Single-cell mass cytometry for analysis of immune system functional states
    • Bjornson Z.B., Nolan G.P., Fantl W.J. Single-cell mass cytometry for analysis of immune system functional states. Curr Opin Immunol 2013, 25:484-494.
    • (2013) Curr Opin Immunol , vol.25 , pp. 484-494
    • Bjornson, Z.B.1    Nolan, G.P.2    Fantl, W.J.3
  • 82
    • 84896503384 scopus 로고    scopus 로고
    • Antigen-dependent integration of opposing proximal TCR-signaling cascades determines the functional fate of T lymphocytes
    • Wolchinsky R., Hod-Marco M., Oved K., Shen-Orr S.S., Bendall S.C., Nolan G.P., Reiter Y. Antigen-dependent integration of opposing proximal TCR-signaling cascades determines the functional fate of T lymphocytes. J Immunol 2014, 192:2109-2119.
    • (2014) J Immunol , vol.192 , pp. 2109-2119
    • Wolchinsky, R.1    Hod-Marco, M.2    Oved, K.3    Shen-Orr, S.S.4    Bendall, S.C.5    Nolan, G.P.6    Reiter, Y.7


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