메뉴 건너뛰기




Volumn 29, Issue 8, 2008, Pages 388-396

A new twist to adaptor proteins contributes to regulation of lymphocyte cell signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CRK LIKE PROTEIN; PEPTIDYLPROLYL ISOMERASE;

EID: 47749132965     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.it.2008.04.006     Document Type: Review
Times cited : (19)

References (70)
  • 1
    • 0026484261 scopus 로고
    • SH2 and SH3 domains: from structure to function
    • Pawson T., and Gish G.D. SH2 and SH3 domains: from structure to function. Cell 71 (1992) 359-362
    • (1992) Cell , vol.71 , pp. 359-362
    • Pawson, T.1    Gish, G.D.2
  • 2
    • 0028144080 scopus 로고
    • SH2 and SH3 domains in signal transduction
    • Pawson T. SH2 and SH3 domains in signal transduction. Adv. Cancer Res. 64 (1994) 87-110
    • (1994) Adv. Cancer Res. , vol.64 , pp. 87-110
    • Pawson, T.1
  • 3
    • 33745813187 scopus 로고    scopus 로고
    • Reading protein modifications with interaction domains
    • Seet B.T., et al. Reading protein modifications with interaction domains. Nat. Rev. Mol. Cell Biol. 7 (2006) 473-483
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 473-483
    • Seet, B.T.1
  • 4
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors-signalling complex formation and biological roles
    • Feller S.M. Crk family adaptors-signalling complex formation and biological roles. Oncogene 20 (2001) 6348-6371
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.M.1
  • 5
    • 0345257729 scopus 로고    scopus 로고
    • Involvement of crk adapter proteins in regulation of lymphoid cell functions
    • Gelkop S., et al. Involvement of crk adapter proteins in regulation of lymphoid cell functions. Immunol. Res. 28 (2003) 79-91
    • (2003) Immunol. Res. , vol.28 , pp. 79-91
    • Gelkop, S.1
  • 6
    • 33746220057 scopus 로고    scopus 로고
    • Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II
    • Muralidharan V., et al. Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry 45 (2006) 8874-8884
    • (2006) Biochemistry , vol.45 , pp. 8874-8884
    • Muralidharan, V.1
  • 7
    • 0036171759 scopus 로고    scopus 로고
    • Apoptotic regulation by the Crk adapter protein mediated by interactions with Wee1 and Crm1/exportin
    • Smith J.J., et al. Apoptotic regulation by the Crk adapter protein mediated by interactions with Wee1 and Crm1/exportin. Mol. Cell. Biol. 22 (2002) 1412-1423
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1412-1423
    • Smith, J.J.1
  • 8
    • 0028335709 scopus 로고
    • The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells
    • Ogawa S., et al. The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells. Oncogene 9 (1994) 1669-1678
    • (1994) Oncogene , vol.9 , pp. 1669-1678
    • Ogawa, S.1
  • 9
    • 0035098436 scopus 로고    scopus 로고
    • Mice lacking the homologue of the human 22q11.2 gene CRKL phenocopy neurocristopathies of DiGeorge syndrome
    • Guris D.L., et al. Mice lacking the homologue of the human 22q11.2 gene CRKL phenocopy neurocristopathies of DiGeorge syndrome. Nat. Genet. 27 (2001) 293-298
    • (2001) Nat. Genet. , vol.27 , pp. 293-298
    • Guris, D.L.1
  • 10
    • 29744440528 scopus 로고    scopus 로고
    • Crkl deficiency disrupts Fgf8 signaling in a mouse model of 22q11 deletion syndromes
    • Moon A.M., et al. Crkl deficiency disrupts Fgf8 signaling in a mouse model of 22q11 deletion syndromes. Dev. Cell 10 (2006) 71-80
    • (2006) Dev. Cell , vol.10 , pp. 71-80
    • Moon, A.M.1
  • 11
    • 33746970957 scopus 로고    scopus 로고
    • Cardiovascular and craniofacial defects in Crk-null mice
    • Park T.J., et al. Cardiovascular and craniofacial defects in Crk-null mice. Mol. Cell. Biol. 26 (2006) 6272-6282
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 6272-6282
    • Park, T.J.1
  • 12
    • 33748196233 scopus 로고    scopus 로고
    • The Cbl family proteins: ring leaders in regulation of cell signaling
    • Swaminathan G., and Tsygankov A.Y. The Cbl family proteins: ring leaders in regulation of cell signaling. J. Cell. Physiol. 209 (2006) 21-43
    • (2006) J. Cell. Physiol. , vol.209 , pp. 21-43
    • Swaminathan, G.1    Tsygankov, A.Y.2
  • 13
    • 32344451150 scopus 로고    scopus 로고
    • Regulating the regulator: negative regulation of Cbl ubiquitin ligases
    • Ryan P.E., et al. Regulating the regulator: negative regulation of Cbl ubiquitin ligases. Trends Biochem. Sci. 31 (2006) 79-88
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 79-88
    • Ryan, P.E.1
  • 14
    • 0028836129 scopus 로고
    • Crk interacts with tyrosine-phosphorylated p116 upon T cell activation
    • Sawasdikosol S., et al. Crk interacts with tyrosine-phosphorylated p116 upon T cell activation. J. Biol. Chem. 270 (1995) 2893-2896
    • (1995) J. Biol. Chem. , vol.270 , pp. 2893-2896
    • Sawasdikosol, S.1
  • 15
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • Reedquist K.A., et al. Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. J. Biol. Chem. 271 (1996) 8435-8442
    • (1996) J. Biol. Chem. , vol.271 , pp. 8435-8442
    • Reedquist, K.A.1
  • 16
    • 0029994305 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated Cbl binds to Crk after T cell activation
    • Sawasdikosol S., et al. Tyrosine-phosphorylated Cbl binds to Crk after T cell activation. J. Immunol. 157 (1996) 110-116
    • (1996) J. Immunol. , vol.157 , pp. 110-116
    • Sawasdikosol, S.1
  • 17
    • 0029664998 scopus 로고    scopus 로고
    • Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation
    • Buday L., et al. Interactions of Cbl with two adapter proteins, Grb2 and Crk, upon T cell activation. J. Biol. Chem. 271 (1996) 6159-6163
    • (1996) J. Biol. Chem. , vol.271 , pp. 6159-6163
    • Buday, L.1
  • 18
    • 0035965340 scopus 로고    scopus 로고
    • T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein
    • Gelkop S., et al. T cell activation induces direct binding of the Crk adapter protein to the regulatory subunit of phosphatidylinositol 3-kinase (p85) via a complex mechanism involving the Cbl protein. J. Biol. Chem. 276 (2001) 36174-36182
    • (2001) J. Biol. Chem. , vol.276 , pp. 36174-36182
    • Gelkop, S.1
  • 19
    • 0037592093 scopus 로고    scopus 로고
    • Negative regulation of T cell antigen receptor-mediated Crk-L-C3G signaling and cell adhesion by Cbl-b
    • Zhang W., et al. Negative regulation of T cell antigen receptor-mediated Crk-L-C3G signaling and cell adhesion by Cbl-b. J. Biol. Chem. 278 (2003) 23978-23983
    • (2003) J. Biol. Chem. , vol.278 , pp. 23978-23983
    • Zhang, W.1
  • 20
    • 0029990069 scopus 로고    scopus 로고
    • Adhesion through the interaction of lymphocyte function-associated antigen-1 with intracellular adhesion molecule-1 induces tyrosine phosphorylation of p130cas and its association with c-CrkII
    • Petruzzelli L., et al. Adhesion through the interaction of lymphocyte function-associated antigen-1 with intracellular adhesion molecule-1 induces tyrosine phosphorylation of p130cas and its association with c-CrkII. J. Biol. Chem. 271 (1996) 7796-7801
    • (1996) J. Biol. Chem. , vol.271 , pp. 7796-7801
    • Petruzzelli, L.1
  • 21
    • 0030871349 scopus 로고    scopus 로고
    • Ligation of the T cell antigen receptor induces tyrosine phosphorylation of p105CasL, a member of the p130Cas-related docking protein family, and its subsequent binding to the Src homology 2 domain of c-Crk
    • Kanda H., et al. Ligation of the T cell antigen receptor induces tyrosine phosphorylation of p105CasL, a member of the p130Cas-related docking protein family, and its subsequent binding to the Src homology 2 domain of c-Crk. Eur. J. Immunol. 27 (1997) 2113-2117
    • (1997) Eur. J. Immunol. , vol.27 , pp. 2113-2117
    • Kanda, H.1
  • 22
    • 0033214510 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration
    • Ohashi Y., et al. Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration. J. Immunol. 163 (1999) 3727-3734
    • (1999) J. Immunol. , vol.163 , pp. 3727-3734
    • Ohashi, Y.1
  • 23
    • 0032513128 scopus 로고    scopus 로고
    • T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G
    • Ohashi Y., et al. T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G. J. Biol. Chem. 273 (1998) 6446-6451
    • (1998) J. Biol. Chem. , vol.273 , pp. 6446-6451
    • Ohashi, Y.1
  • 24
    • 0036893185 scopus 로고    scopus 로고
    • DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines
    • Nishihara H., et al. DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines. Blood 100 (2002) 3968-3974
    • (2002) Blood , vol.100 , pp. 3968-3974
    • Nishihara, H.1
  • 25
    • 0032930551 scopus 로고    scopus 로고
    • Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase
    • Ling P., et al. Interaction of hematopoietic progenitor kinase 1 with adapter proteins Crk and CrkL leads to synergistic activation of c-Jun N-terminal kinase. Mol. Cell. Biol. 19 (1999) 1359-1368
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1359-1368
    • Ling, P.1
  • 26
    • 0033618287 scopus 로고    scopus 로고
    • T cell activation stimulates the association of enzymatically active tyrosine-phosphorylated ZAP-70 with the Crk adapter proteins
    • Gelkop S., and Isakov N. T cell activation stimulates the association of enzymatically active tyrosine-phosphorylated ZAP-70 with the Crk adapter proteins. J. Biol. Chem. 274 (1999) 21519-21527
    • (1999) J. Biol. Chem. , vol.274 , pp. 21519-21527
    • Gelkop, S.1    Isakov, N.2
  • 27
    • 29144441366 scopus 로고    scopus 로고
    • T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315
    • Gelkop S., et al. T cell activation-induced CrkII binding to the Zap70 protein tyrosine kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine 315. J. Immunol. 175 (2005) 8123-8132
    • (2005) J. Immunol. , vol.175 , pp. 8123-8132
    • Gelkop, S.1
  • 28
    • 0035353161 scopus 로고    scopus 로고
    • CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk
    • Oda A., et al. CrkL is an adapter for Wiskott-Aldrich syndrome protein and Syk. Blood 97 (2001) 2633-2639
    • (2001) Blood , vol.97 , pp. 2633-2639
    • Oda, A.1
  • 29
    • 0036928182 scopus 로고    scopus 로고
    • Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation
    • Sasahara Y., et al. Mechanism of recruitment of WASP to the immunological synapse and of its activation following TCR ligation. Mol. Cell 10 (2002) 1269-1281
    • (2002) Mol. Cell , vol.10 , pp. 1269-1281
    • Sasahara, Y.1
  • 30
    • 0035824685 scopus 로고    scopus 로고
    • T cell regulation of p62(dok) (Dok1) association with Crk-L
    • Martelli M.P., et al. T cell regulation of p62(dok) (Dok1) association with Crk-L. J. Biol. Chem. 276 (2001) 45654-45661
    • (2001) J. Biol. Chem. , vol.276 , pp. 45654-45661
    • Martelli, M.P.1
  • 31
    • 0030812812 scopus 로고    scopus 로고
    • Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1
    • Boussiotis V.A., et al. Maintenance of human T cell anergy: blocking of IL-2 gene transcription by activated Rap1. Science 278 (1997) 124-128
    • (1997) Science , vol.278 , pp. 124-128
    • Boussiotis, V.A.1
  • 32
    • 0030771490 scopus 로고    scopus 로고
    • Enhancement of guanine-nucleotide exchange activity of C3G for Rap1 by the expression of Crk, CrkL, and Grb2
    • Ichiba T., et al. Enhancement of guanine-nucleotide exchange activity of C3G for Rap1 by the expression of Crk, CrkL, and Grb2. J. Biol. Chem. 272 (1997) 22215-22220
    • (1997) J. Biol. Chem. , vol.272 , pp. 22215-22220
    • Ichiba, T.1
  • 33
    • 0242335092 scopus 로고    scopus 로고
    • T cell development and function in CrkL-deficient mice
    • Peterson A.C., et al. T cell development and function in CrkL-deficient mice. Eur. J. Immunol. 33 (2003) 2687-2695
    • (2003) Eur. J. Immunol. , vol.33 , pp. 2687-2695
    • Peterson, A.C.1
  • 34
    • 0028243505 scopus 로고
    • c-Abl kinase regulates the protein binding activity of c-Crk
    • Feller S.M., et al. c-Abl kinase regulates the protein binding activity of c-Crk. EMBO J. 13 (1994) 2341-2351
    • (1994) EMBO J. , vol.13 , pp. 2341-2351
    • Feller, S.M.1
  • 35
    • 0028181873 scopus 로고
    • Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites
    • Ren R., et al. Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites. Genes Dev. 8 (1994) 783-795
    • (1994) Genes Dev. , vol.8 , pp. 783-795
    • Ren, R.1
  • 36
    • 0031040941 scopus 로고    scopus 로고
    • Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site
    • de Jong R., et al. Tyrosine 207 in CRKL is the BCR/ABL phosphorylation site. Oncogene 14 (1997) 507-513
    • (1997) Oncogene , vol.14 , pp. 507-513
    • de Jong, R.1
  • 37
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopeptide sequences
    • Songyang Z., et al. SH2 domains recognize specific phosphopeptide sequences. Cell 72 (1993) 767-778
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1
  • 38
    • 0028916892 scopus 로고
    • Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein
    • Rosen M.K., et al. Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature 374 (1995) 477-479
    • (1995) Nature , vol.374 , pp. 477-479
    • Rosen, M.K.1
  • 39
    • 0029813117 scopus 로고    scopus 로고
    • A potential SH3 domain-binding site in the Crk SH2 domain
    • Anafi M., et al. A potential SH3 domain-binding site in the Crk SH2 domain. J. Biol. Chem. 271 (1996) 21365-21374
    • (1996) J. Biol. Chem. , vol.271 , pp. 21365-21374
    • Anafi, M.1
  • 40
    • 0028116526 scopus 로고
    • Identification of CRKL as the constitutively phosphorylated 39-kD tyrosine phosphoprotein in chronic myelogenous leukemia cells
    • Nichols G.L., et al. Identification of CRKL as the constitutively phosphorylated 39-kD tyrosine phosphoprotein in chronic myelogenous leukemia cells. Blood 84 (1994) 2912-2918
    • (1994) Blood , vol.84 , pp. 2912-2918
    • Nichols, G.L.1
  • 41
    • 0028024938 scopus 로고
    • Tyrosine phosphorylation of CRKL in Philadelphia+ leukemia
    • ten Hoeve J., et al. Tyrosine phosphorylation of CRKL in Philadelphia+ leukemia. Blood 84 (1994) 1731-1736
    • (1994) Blood , vol.84 , pp. 1731-1736
    • ten Hoeve, J.1
  • 42
    • 0028142490 scopus 로고
    • Crkl is the major tyrosine-phosphorylated protein in neutrophils from patients with chronic myelogenous leukemia
    • Oda T., et al. Crkl is the major tyrosine-phosphorylated protein in neutrophils from patients with chronic myelogenous leukemia. J. Biol. Chem. 269 (1994) 22925-22928
    • (1994) J. Biol. Chem. , vol.269 , pp. 22925-22928
    • Oda, T.1
  • 43
    • 0033952307 scopus 로고    scopus 로고
    • Enzymes that catalyse the restructuring of proteins
    • Schiene C., and Fischer G. Enzymes that catalyse the restructuring of proteins. Curr. Opin. Struct. Biol. 10 (2000) 40-45
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 40-45
    • Schiene, C.1    Fischer, G.2
  • 44
    • 33846059755 scopus 로고    scopus 로고
    • Immunophilins: for the love of proteins
    • Barik S. Immunophilins: for the love of proteins. Cell. Mol. Life Sci. 63 (2006) 2889-2900
    • (2006) Cell. Mol. Life Sci. , vol.63 , pp. 2889-2900
    • Barik, S.1
  • 45
    • 0026030568 scopus 로고
    • Chemistry and biology of the immunophilins and their immunosuppressive ligands
    • Schreiber S.L. Chemistry and biology of the immunophilins and their immunosuppressive ligands. Science 251 (1991) 283-287
    • (1991) Science , vol.251 , pp. 283-287
    • Schreiber, S.L.1
  • 46
    • 0008233581 scopus 로고    scopus 로고
    • Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent
    • Ranganathan R., et al. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell 89 (1997) 875-886
    • (1997) Cell , vol.89 , pp. 875-886
    • Ranganathan, R.1
  • 47
    • 0037133154 scopus 로고    scopus 로고
    • Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A
    • Brazin K.N., et al. Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1899-1904
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1899-1904
    • Brazin, K.N.1
  • 48
    • 4143074548 scopus 로고    scopus 로고
    • Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk
    • Colgan J., et al. Cyclophilin A regulates TCR signal strength in CD4+ T cells via a proline-directed conformational switch in Itk. Immunity 21 (2004) 189-201
    • (2004) Immunity , vol.21 , pp. 189-201
    • Colgan, J.1
  • 49
    • 0034235114 scopus 로고    scopus 로고
    • TCR/CD3-Induced activation and binding of Emt/Itk to linker of activated T cell complexes: requirement for the Src homology 2 domain
    • Ching K.A., et al. TCR/CD3-Induced activation and binding of Emt/Itk to linker of activated T cell complexes: requirement for the Src homology 2 domain. J. Immunol. 165 (2000) 256-262
    • (2000) J. Immunol. , vol.165 , pp. 256-262
    • Ching, K.A.1
  • 50
    • 0036895828 scopus 로고    scopus 로고
    • Structural characterization of a proline-driven conformational switch within the Itk SH2 domain
    • Mallis R.J., et al. Structural characterization of a proline-driven conformational switch within the Itk SH2 domain. Nat. Struct. Biol. 9 (2002) 900-905
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 900-905
    • Mallis, R.J.1
  • 51
    • 33344472738 scopus 로고    scopus 로고
    • Molecular details of Itk activation by prolyl isomerization and phospholigand binding: the NMR structure of the Itk SH2 domain bound to a phosphopeptide
    • Pletneva E.V., et al. Molecular details of Itk activation by prolyl isomerization and phospholigand binding: the NMR structure of the Itk SH2 domain bound to a phosphopeptide. J. Mol. Biol. 357 (2006) 550-561
    • (2006) J. Mol. Biol. , vol.357 , pp. 550-561
    • Pletneva, E.V.1
  • 52
    • 0345733987 scopus 로고    scopus 로고
    • Ligand specificity modulated by prolyl imide bond Cis/Trans isomerization in the Itk SH2 domain: a quantitative NMR study
    • Breheny P.J., et al. Ligand specificity modulated by prolyl imide bond Cis/Trans isomerization in the Itk SH2 domain: a quantitative NMR study. J. Am. Chem. Soc. 125 (2003) 15706-15707
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 15706-15707
    • Breheny, P.J.1
  • 53
    • 33745830461 scopus 로고    scopus 로고
    • Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1
    • Yu L., et al. Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1. J. Biol. Chem. 281 (2006) 18201-18207
    • (2006) J. Biol. Chem. , vol.281 , pp. 18201-18207
    • Yu, L.1
  • 54
    • 33750801024 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes
    • Esnault S., et al. The peptidyl-prolyl isomerase Pin1 regulates granulocyte-macrophage colony-stimulating factor mRNA stability in T lymphocytes. J. Immunol. 177 (2006) 6999-7006
    • (2006) J. Immunol. , vol.177 , pp. 6999-7006
    • Esnault, S.1
  • 55
    • 34548693416 scopus 로고    scopus 로고
    • Pin1 modulates the type 1 immune response
    • Esnault S., et al. Pin1 modulates the type 1 immune response. PLoS ONE 2 (2007) e226
    • (2007) PLoS ONE , vol.2
    • Esnault, S.1
  • 56
    • 38849085399 scopus 로고    scopus 로고
    • Pin1 regulates TGF-beta1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis
    • Shen Z.J., et al. Pin1 regulates TGF-beta1 production by activated human and murine eosinophils and contributes to allergic lung fibrosis. J. Clin. Invest. 118 (2008) 479-490
    • (2008) J. Clin. Invest. , vol.118 , pp. 479-490
    • Shen, Z.J.1
  • 57
    • 33744499683 scopus 로고    scopus 로고
    • Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1
    • Saitoh T., et al. Negative regulation of interferon-regulatory factor 3-dependent innate antiviral response by the prolyl isomerase Pin1. Nat. Immunol. 7 (2006) 598-605
    • (2006) Nat. Immunol. , vol.7 , pp. 598-605
    • Saitoh, T.1
  • 58
    • 0036302064 scopus 로고    scopus 로고
    • Peptidyl-prolyl isomerases: a new twist to transcription
    • Shaw P.E. Peptidyl-prolyl isomerases: a new twist to transcription. EMBO Rep. 3 (2002) 521-526
    • (2002) EMBO Rep. , vol.3 , pp. 521-526
    • Shaw, P.E.1
  • 59
    • 0036535975 scopus 로고    scopus 로고
    • Pinning down proline-directed phosphorylation signaling
    • Lu K.P., et al. Pinning down proline-directed phosphorylation signaling. Trends Cell Biol. 12 (2002) 164-172
    • (2002) Trends Cell Biol. , vol.12 , pp. 164-172
    • Lu, K.P.1
  • 60
    • 27444440554 scopus 로고    scopus 로고
    • Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1
    • Monje P., et al. Regulation of the transcriptional activity of c-Fos by ERK. A novel role for the prolyl isomerase PIN1. J. Biol. Chem. 280 (2005) 35081-35084
    • (2005) J. Biol. Chem. , vol.280 , pp. 35081-35084
    • Monje, P.1
  • 61
    • 33846688095 scopus 로고    scopus 로고
    • Proline cis-trans isomerization controls autoinhibition of a signaling protein
    • Sarkar P., et al. Proline cis-trans isomerization controls autoinhibition of a signaling protein. Mol. Cell 25 (2007) 413-426
    • (2007) Mol. Cell , vol.25 , pp. 413-426
    • Sarkar, P.1
  • 62
    • 33845266145 scopus 로고    scopus 로고
    • The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal
    • Harkiolaki M., et al. The C-terminal SH3 domain of CRKL as a dynamic dimerization module transiently exposing a nuclear export signal. Structure 14 (2006) 1741-1753
    • (2006) Structure , vol.14 , pp. 1741-1753
    • Harkiolaki, M.1
  • 63
    • 34249902061 scopus 로고    scopus 로고
    • Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK
    • Kobashigawa Y., et al. Structural basis for the transforming activity of human cancer-related signaling adaptor protein CRK. Nat. Struct. Mol. Biol. 14 (2007) 503-510
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 503-510
    • Kobashigawa, Y.1
  • 64
    • 34548660854 scopus 로고    scopus 로고
    • Prolyl cis-trans isomerization as a molecular timer
    • Lu K.P., et al. Prolyl cis-trans isomerization as a molecular timer. Nat. Chem. Biol. 3 (2007) 619-629
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 619-629
    • Lu, K.P.1
  • 65
    • 33846010183 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?
    • Shaw P.E. Peptidyl-prolyl cis/trans isomerases and transcription: is there a twist in the tail?. EMBO Rep. 8 (2007) 40-45
    • (2007) EMBO Rep. , vol.8 , pp. 40-45
    • Shaw, P.E.1
  • 66
    • 39349085931 scopus 로고    scopus 로고
    • Pinning down signaling in the immune system: the role of the peptidyl-prolyl isomerase pin1 in immune cell function
    • Esnault S., et al. Pinning down signaling in the immune system: the role of the peptidyl-prolyl isomerase pin1 in immune cell function. Crit. Rev. Immunol. 28 (2008) 45-60
    • (2008) Crit. Rev. Immunol. , vol.28 , pp. 45-60
    • Esnault, S.1
  • 67
    • 0025893168 scopus 로고
    • Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
    • Liu J., et al. Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes. Cell 66 (1991) 807-815
    • (1991) Cell , vol.66 , pp. 807-815
    • Liu, J.1
  • 68
    • 0027339327 scopus 로고
    • NF-ATp, a T lymphocyte DNA-binding protein that is a target for calcineurin and immunosuppressive drugs
    • McCaffrey P.G., et al. NF-ATp, a T lymphocyte DNA-binding protein that is a target for calcineurin and immunosuppressive drugs. J. Biol. Chem. 268 (1993) 3747-3752
    • (1993) J. Biol. Chem. , vol.268 , pp. 3747-3752
    • McCaffrey, P.G.1
  • 69
    • 0032741457 scopus 로고    scopus 로고
    • Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism
    • Zhou X.Z., et al. Phosphorylation-dependent prolyl isomerization: a novel signaling regulatory mechanism. Cell. Mol. Life Sci. 56 (1999) 788-806
    • (1999) Cell. Mol. Life Sci. , vol.56 , pp. 788-806
    • Zhou, X.Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.