메뉴 건너뛰기




Volumn 11, Issue 23, 2011, Pages 4588-4592

Analysis of protein networks in resting and collagen receptor (GPVI)-stimulated platelet sub-proteomes

Author keywords

Cell biology; GPVI signalling pathway; Platelet signalling; Platelet sub proteomes; Protein abundance

Indexed keywords

CELL MEMBRANE PROTEIN; CELL PROTEIN; COLLAGEN RECEPTOR; GLYCOPROTEIN VI; PROTEOME; TENEURIN 1; UNCLASSIFIED DRUG; VAN GOGH LIKE PROTEIN 1;

EID: 81855166736     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201100410     Document Type: Note
Times cited : (12)

References (24)
  • 1
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interactions: is GPVI the central receptor?
    • Nieswandt, B., Watson, S. P., Platelet-collagen interactions: is GPVI the central receptor? Blood 2003, 102, 449-461.
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 2
  • 4
    • 33749635803 scopus 로고    scopus 로고
    • A global proteomics approach identifies novel phosphorylated signalling proteins in GPVI-activated platelets: involvement of G6f, a novel platelet Grb2-binding membrane adapter
    • Garcia, A., Senis, Y. A., Antrobus, R., Hughes, C. E. et al., N., A global proteomics approach identifies novel phosphorylated signalling proteins in GPVI-activated platelets: involvement of G6f, a novel platelet Grb2-binding membrane adapter. Proteomics 2006, 6, 5332-5343.
    • (2006) Proteomics , vol.6 , pp. 5332-5343
    • Garcia, A.1    Senis, Y.A.2    Antrobus, R.3    Hughes, C.E.4
  • 5
    • 34147183885 scopus 로고    scopus 로고
    • A comprehensive proteomics and genomics analysis reveals novel transmembrane proteins in human platelets and mouse megakaryocytes including G6b-B, a novel immunoreceptor tyrosine-based inhibitory motif protein
    • Senis, Y. A., Tomlinson, M. G., Garcia, A., Dumon, S. et al., A comprehensive proteomics and genomics analysis reveals novel transmembrane proteins in human platelets and mouse megakaryocytes including G6b-B, a novel immunoreceptor tyrosine-based inhibitory motif protein. Mol. Cell. Proteomics 2007, 6, 548-564.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 548-564
    • Senis, Y.A.1    Tomlinson, M.G.2    Garcia, A.3    Dumon, S.4
  • 6
    • 66549093856 scopus 로고    scopus 로고
    • The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis
    • Senis, Y. A., Tomlinson, M. G., Ellison, S., Mazharian, A. et al., The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis. Blood 2009, 113, 4942-4954.
    • (2009) Blood , vol.113 , pp. 4942-4954
    • Senis, Y.A.1    Tomlinson, M.G.2    Ellison, S.3    Mazharian, A.4
  • 7
    • 67049125717 scopus 로고    scopus 로고
    • A functional proteomic method for the enrichment of peripheral membrane proteins reveals the collagen binding protein Hsp47 is exposed on the surface of activated human platelets
    • Kaiser, W. J., Holbrook, L. M., Tucker, K. L., Stanley, R. G., Gibbins, J. M., A functional proteomic method for the enrichment of peripheral membrane proteins reveals the collagen binding protein Hsp47 is exposed on the surface of activated human platelets. J. Proteome Res. 2009, 8, 2903-2914.
    • (2009) J. Proteome Res. , vol.8 , pp. 2903-2914
    • Kaiser, W.J.1    Holbrook, L.M.2    Tucker, K.L.3    Stanley, R.G.4    Gibbins, J.M.5
  • 8
    • 70349125020 scopus 로고    scopus 로고
    • Proteomic analysis of resting and thrombin-stimulated platelets reveals the translocation and functional relevance of HIP-55 in platelets
    • Tucker, K. L., Kaiser, W. J., Bergeron, A. L., Hu, H. et al., J. M., Proteomic analysis of resting and thrombin-stimulated platelets reveals the translocation and functional relevance of HIP-55 in platelets. Proteomics 2009, 9, 4340-4354.
    • (2009) Proteomics , vol.9 , pp. 4340-4354
    • Tucker, K.L.1    Kaiser, W.J.2    Bergeron, A.L.3    Hu, H.4
  • 9
    • 12144289394 scopus 로고    scopus 로고
    • Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins
    • Garcia, A., Prabhakar, S., Hughan, S., Anderson, T. W. et al., Differential proteome analysis of TRAP-activated platelets: involvement of DOK-2 and phosphorylation of RGS proteins. Blood 2004, 103, 2088-2095.
    • (2004) Blood , vol.103 , pp. 2088-2095
    • Garcia, A.1    Prabhakar, S.2    Hughan, S.3    Anderson, T.W.4
  • 10
    • 0029894287 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Fc receptor gamma-chain in collagen-stimulated platelets
    • Gibbins, J., Asselin, J., Farndale, R., Barnes, M. et al., Tyrosine phosphorylation of the Fc receptor gamma-chain in collagen-stimulated platelets. J. Biol. Chem. 1996, 271, 18095-18099.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18095-18099
    • Gibbins, J.1    Asselin, J.2    Farndale, R.3    Barnes, M.4
  • 12
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama, Y., Oda, Y., Tabata, T., Sato, T. et al., Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol. Cell. Proteomics 2005, 4, 1265-1272.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4
  • 13
    • 58149193234 scopus 로고    scopus 로고
    • STRING 8--a global view on proteins and their functional interactions in 630 organisms
    • Jensen, L. J., Kuhn, M., Stark, M., Chaffron, S. et al., STRING 8--a global view on proteins and their functional interactions in 630 organisms. Nucleic Acids Res. 2009, 37, D412-D416.
    • (2009) Nucleic Acids Res. , vol.37
    • Jensen, L.J.1    Kuhn, M.2    Stark, M.3    Chaffron, S.4
  • 14
    • 0032146135 scopus 로고    scopus 로고
    • ABH antigens on human platelets: expression on the glycosyl phosphatidylinositol-anchored protein CD109
    • Kelton, J. G., Smith, J. W., Horsewood, P., Warner, M. N. et al., ABH antigens on human platelets: expression on the glycosyl phosphatidylinositol-anchored protein CD109. J. Lab. Clin. Med. 1998, 132, 142-148.
    • (1998) J. Lab. Clin. Med. , vol.132 , pp. 142-148
    • Kelton, J.G.1    Smith, J.W.2    Horsewood, P.3    Warner, M.N.4
  • 15
    • 74249091561 scopus 로고    scopus 로고
    • Beta1 integrin establishes endothelial cell polarity and arteriolar lumen formation via a Par3-dependent mechanism
    • Zovein, A. C., Luque, A., Turlo, K. A., Hofmann, J. J. et al., Beta1 integrin establishes endothelial cell polarity and arteriolar lumen formation via a Par3-dependent mechanism. Dev. Cell 2010, 18, 39-51.
    • (2010) Dev. Cell , vol.18 , pp. 39-51
    • Zovein, A.C.1    Luque, A.2    Turlo, K.A.3    Hofmann, J.J.4
  • 16
    • 0035898658 scopus 로고    scopus 로고
    • The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)
    • Ebnet, K., Suzuki, A., Horikoshi, Y., Hirose, T. et al., The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). EMBO J. 2001, 20, 3738-3748.
    • (2001) EMBO J , vol.20 , pp. 3738-3748
    • Ebnet, K.1    Suzuki, A.2    Horikoshi, Y.3    Hirose, T.4
  • 17
    • 3543025190 scopus 로고    scopus 로고
    • Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa
    • Sobocka, M. B., Sobocki, T., Babinska, A., Hartwig, J. H. et al., Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa. J. Recept. Signal Tranduct. Res. 2004, 24, 85-105.
    • (2004) J. Recept. Signal Tranduct. Res , vol.24 , pp. 85-105
    • Sobocka, M.B.1    Sobocki, T.2    Babinska, A.3    Hartwig, J.H.4
  • 18
    • 67249084776 scopus 로고    scopus 로고
    • Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions: molecular structure and function of the tight junction
    • Fanning, A. S., Anderson, J. M., Zonula occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions: molecular structure and function of the tight junction. Ann. N. Y. Acad. Sci. 2009, 1165, 113-120.
    • (2009) Ann. N. Y. Acad. Sci. , vol.1165 , pp. 113-120
    • Fanning, A.S.1    Anderson, J.M.2
  • 19
    • 33747495972 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs) are differentially expressed in fibroblasts and co-localize with ZO-1 to adherens-like junctions
    • Morris, A. P., Tawil, A., Berkova, Z., Wible, L. et al., Junctional adhesion molecules (JAMs) are differentially expressed in fibroblasts and co-localize with ZO-1 to adherens-like junctions. Cell. Commun. Adhes. 2006, 13, 233-247.
    • (2006) Cell. Commun. Adhes. , vol.13 , pp. 233-247
    • Morris, A.P.1    Tawil, A.2    Berkova, Z.3    Wible, L.4
  • 20
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellen, L., Lindahl, U., Proteoglycans: Structures and interactions. Ann. Rev. Biochem. 1991, 60, 443-475.
    • (1991) Ann. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 21
    • 39149106427 scopus 로고    scopus 로고
    • Regulation of adaptor protein GIT1 in platelets, leading to the interaction between GIT1 and integrin alpha(IIb)beta3
    • Sato, H., Suzuki-Inoue, K., Inoue, O., Ozaki, Y., Regulation of adaptor protein GIT1 in platelets, leading to the interaction between GIT1 and integrin alpha(IIb)beta3. Biochem. Biophys. Res. Commun. 2008, 368, 157-161.
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 157-161
    • Sato, H.1    Suzuki-Inoue, K.2    Inoue, O.3    Ozaki, Y.4
  • 22
    • 0037416053 scopus 로고    scopus 로고
    • Integrin alpha2beta1 mediates outside-in regulation of platelet spreading on collagen through activation of Src kinases and PLCgamma2
    • Inoue, O., Suzuki-Inoue, K., Dean, W. L., Frampton, J., Watson, S. P., Integrin alpha2beta1 mediates outside-in regulation of platelet spreading on collagen through activation of Src kinases and PLCgamma2. J. Cell Biol. 2003, 160, 769-780.
    • (2003) J. Cell Biol. , vol.160 , pp. 769-780
    • Inoue, O.1    Suzuki-Inoue, K.2    Dean, W.L.3    Frampton, J.4    Watson, S.P.5
  • 23
    • 33646566846 scopus 로고    scopus 로고
    • GIT2 represses Crk- and Rac1-regulated cell spreading and Cdc42-mediated focal adhesion turnover
    • Frank, S. R., Adelstein, M. R., Hansen, S. H., GIT2 represses Crk- and Rac1-regulated cell spreading and Cdc42-mediated focal adhesion turnover. EMBO J. 2006, 25, 1848-1859.
    • (2006) EMBO J , vol.25 , pp. 1848-1859
    • Frank, S.R.1    Adelstein, M.R.2    Hansen, S.H.3
  • 24
    • 57149093203 scopus 로고    scopus 로고
    • FKBP family proteins: immunophilins with versatile biological functions
    • Kang, C. B., Hong, Y., Dhe-Paganon, S., Yoon, H. S., FKBP family proteins: immunophilins with versatile biological functions. Neurosignals 2008, 16, 318-325.
    • (2008) Neurosignals , vol.16 , pp. 318-325
    • Kang, C.B.1    Hong, Y.2    Dhe-Paganon, S.3    Yoon, H.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.