메뉴 건너뛰기




Volumn 30, Issue 8, 2016, Pages 2640-2650

CIB1: A small protein with big ambitions

Author keywords

Cancer; Cardiovascular; Kinase; Signaling; Structure

Indexed keywords

BINDING PROTEIN; CALCIUM AND INTEGRIN BINDING PROTEIN 1; INTEGRIN; UNCLASSIFIED DRUG; CALCIUM BINDING PROTEIN; CIB1 PROTEIN, HUMAN;

EID: 84980373486     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.201500073R     Document Type: Review
Times cited : (58)

References (100)
  • 1
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain
    • Naik, U. P., Patel, P. M., Parise, L. V. (1997) Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain. J. Biol. Chem. 272, 4651-4654
    • (1997) J. Biol. Chem. , vol.272 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 2
    • 17744392416 scopus 로고    scopus 로고
    • The crystal structure of calcium-and integrin-binding protein 1: Insights into redox regulated functions
    • Blamey, C. J., Ceccarelli, C., Naik, U. P., Bahnson, B. J. (2005) The crystal structure of calcium-and integrin-binding protein 1: insights into redox regulated functions. Protein Sci. 14, 1214-1221
    • (2005) Protein Sci. , vol.14 , pp. 1214-1221
    • Blamey, C.J.1    Ceccarelli, C.2    Naik, U.P.3    Bahnson, B.J.4
  • 3
    • 14844282775 scopus 로고    scopus 로고
    • Structural and biochemical characterization of CIB1 delineates a new family of EF-handcontaining proteins
    • Gentry, H. R., Singer, A. U., Betts, L., Yang, C., Ferrara, J. D., Sondek, J., Parise, L. V. (2005) Structural and biochemical characterization of CIB1 delineates a new family of EF-handcontaining proteins. J. Biol. Chem. 280, 8407-8415
    • (2005) J. Biol. Chem. , vol.280 , pp. 8407-8415
    • Gentry, H.R.1    Singer, A.U.2    Betts, L.3    Yang, C.4    Ferrara, J.D.5    Sondek, J.6    Parise, L.V.7
  • 4
    • 79955768339 scopus 로고    scopus 로고
    • Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain
    • Huang, H., Ishida, H., Yamniuk, A. P., Vogel, H. J. (2011) Solution structures of Ca2+-CIB1 and Mg2+-CIB1 and their interactions with the platelet integrin alphaIIb cytoplasmic domain. J. Biol. Chem. 286, 17181-17192
    • (2011) J. Biol. Chem. , vol.286 , pp. 17181-17192
    • Huang, H.1    Ishida, H.2    Yamniuk, A.P.3    Vogel, H.J.4
  • 5
    • 84863272301 scopus 로고    scopus 로고
    • Structural basis for the activation of platelet integrin aIIbb3 by calcium-and integrin-binding protein 1
    • Huang, H., Vogel, H. J. (2012) Structural basis for the activation of platelet integrin aIIbb3 by calcium-and integrin-binding protein 1. J. Am. Chem. Soc. 134, 3864-3872
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3864-3872
    • Huang, H.1    Vogel, H.J.2
  • 6
    • 0034060568 scopus 로고    scopus 로고
    • Structures of the platelet calcium-and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; Homology modelling and NMR studies
    • Hwang, P. M., Vogel, H. J. (2000) Structures of the platelet calcium-and integrin-binding protein and the alphaIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies. J. Mol. Recognit. 13, 83-92
    • (2000) J. Mol. Recognit. , vol.13 , pp. 83-92
    • Hwang, P.M.1    Vogel, H.J.2
  • 7
    • 0037307080 scopus 로고    scopus 로고
    • Protein conformational changes studied by diffusion NMR spectroscopy: Application to helix-loop-helix calcium binding proteins
    • Weljie, A.M., Yamniuk, A. P., Yoshino, H., Izumi, Y., Vogel, H. J. (2003) Protein conformational changes studied by diffusion NMR spectroscopy: application to helix-loop-helix calcium binding proteins. Protein Sci. 12, 228-236
    • (2003) Protein Sci. , vol.12 , pp. 228-236
    • Weljie, A.M.1    Yamniuk, A.P.2    Yoshino, H.3    Izumi, Y.4    Vogel, H.J.5
  • 8
    • 68849122052 scopus 로고    scopus 로고
    • Auxiliary Ca2+ binding sites can influence the structure of CIB1
    • Yamniuk, A. P., Anderson, K.L., Fraser, M.E., Vogel, H. J. (2009) Auxiliary Ca2+ binding sites can influence the structure of CIB1. Protein Sci. 18, 1128-1134
    • (2009) Protein Sci. , vol.18 , pp. 1128-1134
    • Yamniuk, A.P.1    Anderson, K.L.2    Fraser, M.E.3    Vogel, H.J.4
  • 9
    • 38949178847 scopus 로고    scopus 로고
    • Effects of metal-binding loop mutations on ligand binding to calcium-and integrin-bindingprotein1.Evolutionof theEF-hand
    • Yamniuk, A. P., Gifford, J.L., Linse, S., Vogel, H. J. (2008)Effects of metal-binding loop mutations on ligand binding to calcium-and integrin-bindingprotein1.Evolutionof theEF-hand Biochemistry 47, 1696-1707
    • (2008) Biochemistry , vol.47 , pp. 1696-1707
    • Yamniuk, A.P.1    Gifford, J.L.2    Linse, S.3    Vogel, H.J.4
  • 10
    • 33748750710 scopus 로고    scopus 로고
    • The interaction between calcium-and integrin-binding protein 1 and the alphaIIb integrin cytoplasmic domain involves a novel C-terminal displacement mechanism
    • Yamniuk, A. P., Ishida, H., Vogel, H. J. (2006) The interaction between calcium-and integrin-binding protein 1 and the alphaIIb integrin cytoplasmic domain involves a novel C-terminal displacement mechanism. J. Biol. Chem. 281, 26455-26464
    • (2006) J. Biol. Chem. , vol.281 , pp. 26455-26464
    • Yamniuk, A.P.1    Ishida, H.2    Vogel, H.J.3
  • 11
    • 34250888729 scopus 로고    scopus 로고
    • Domain stability and metal-induced folding of calcium-and integrin-binding protein 1
    • Yamniuk, A. P., Silver, D. M., erson, K. L., Martin, S. R., Vogel, H. J. (2007) Domain stability and metal-induced folding of calcium-and integrin-binding protein 1. Biochemistry 46, 7088-7098
    • (2007) Biochemistry , vol.46 , pp. 7088-7098
    • Yamniuk, A.P.1    Silver, D.M.2    Erson, K.L.3    Martin, S.R.4    Vogel, H.J.5
  • 12
    • 22444443424 scopus 로고    scopus 로고
    • Calcium-and magnesium dependent interactions between calcium-and integrin-binding protein and the integrinalphaIIbcy to plasmic domain
    • Yamniuk, A. P., Vogel, H. J. (2005) Calcium-andmagnesiumdependent interactions between calcium-and integrin-binding proteinandthe integrinalphaIIbcytoplasmicdomain. ProteinSci. 14, 1429-1437
    • (2005) Protein Sci. , vol.14 , pp. 1429-1437
    • Yamniuk, A.P.1    Vogel, H.J.2
  • 13
    • 0033568191 scopus 로고    scopus 로고
    • Calcium-dependent properties ofCIBbindingto the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton
    • Shock, D.D., Naik, U. P., Brittain, J. E., Alahari, S. K., Sondek, J., Parise, L.V. (1999)Calcium-dependent properties ofCIBbindingto the integrin alphaIIb cytoplasmic domain and translocation to the platelet cytoskeleton. Biochem. J. 342, 729-735
    • (1999) Biochem. J. , vol.342 , pp. 729-735
    • Shock, D.D.1    Naik, U.P.2    Brittain, J.E.3    Alahari, S.K.4    Sondek, J.5    Parise, L.V.6
  • 14
    • 0032895315 scopus 로고    scopus 로고
    • Intracellular neuronal calcium sensor proteins: A family of EF-hand calciumbinding proteins in search of a function
    • Braunewell, K. H., Gundelfinger, E. D. (1999) Intracellular neuronal calcium sensor proteins: a family of EF-hand calciumbinding proteins in search of a function. Cell Tissue Res. 295, 1-12
    • (1999) Cell Tissue Res. , vol.295 , pp. 1-12
    • Braunewell, K.H.1    Gundelfinger, E.D.2
  • 15
    • 0015919772 scopus 로고
    • Carpmuscle calciumbinding protein. II. Structure determination and general description
    • Kretsinger, R. H., Nockolds, C. E. (1973) Carpmuscle calciumbinding protein. II. Structure determination and general description. J. Biol. Chem. 248, 3313-3326
    • (1973) J. Biol. Chem. , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 16
    • 79955665185 scopus 로고    scopus 로고
    • Insights intomodulationof calciumsignaling by magnesium in calmodulin, troponin C and related EF-hand proteins
    • Grabarek, Z. (2011) Insights intomodulationof calciumsignaling by magnesium in calmodulin, troponin C and related EF-hand proteins. Biochim. Biophys. Acta 1813, 913-921
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 913-921
    • Grabarek, Z.1
  • 17
    • 1542357645 scopus 로고    scopus 로고
    • Metal ion binding properties and conformational states of calciumand integrin-binding protein
    • Yamniuk, A. P., Nguyen, L. T., Hoang, T.T., Vogel, H. J. (2004) Metal ion binding properties and conformational states of calciumand integrin-binding protein. Biochemistry 43, 2558-2568
    • (2004) Biochemistry , vol.43 , pp. 2558-2568
    • Yamniuk, A.P.1    Nguyen, L.T.2    Hoang, T.T.3    Vogel, H.J.4
  • 18
    • 84885454396 scopus 로고    scopus 로고
    • Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): Structural and thermodynamic basis of CIB1 promiscuity
    • Freeman, T. C., Jr., Black, J. L., Bray, H. G., Dagliyan, O., Wu, Y. I., Tripathy, A., Dokholyan, N. V., Leisner, T. M., Parise, L. V. (2013) Identification of novel integrin binding partners for calcium and integrin binding protein 1 (CIB1): structural and thermodynamic basis of CIB1 promiscuity. Biochemistry 52, 7082-7090
    • (2013) Biochemistry , vol.52 , pp. 7082-7090
    • Freeman, T.C.1    Black, J.L.2    Bray, H.G.3    Dagliyan, O.4    Wu, Y.I.5    Tripathy, A.6    Dokholyan, N.V.7    Leisner, T.M.8    Parise, L.V.9
  • 19
    • 49549123609 scopus 로고    scopus 로고
    • Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP3-dependent Ca2+ release in vivo
    • Hennigs, J. K., Burhenne, N., Stähler, F., Winnig, M., Walter, B., Meyerhof, W., Schmale, H. (2008) Sweet taste receptor interacting protein CIB1 is a general inhibitor of InsP3-dependent Ca2+ release in vivo. J. Neurochem. 106, 2249-2262
    • (2008) J. Neurochem. , vol.106 , pp. 2249-2262
    • Hennigs, J.K.1    Burhenne, N.2    Stähler, F.3    Winnig, M.4    Walter, B.5    Meyerhof, W.6    Schmale, H.7
  • 20
    • 73649108890 scopus 로고    scopus 로고
    • Translocation of sphingosine kinase 1 to the plasma membrane is mediated by calcium-and integrin-binding protein 1
    • Jarman, K. E., Moretti, P. A., Zebol, J. R., Pitson, S. M. (2010) Translocation of sphingosine kinase 1 to the plasma membrane is mediated by calcium-and integrin-binding protein 1. J. Biol. Chem. 285, 483-492
    • (2010) J. Biol. Chem. , vol.285 , pp. 483-492
    • Jarman, K.E.1    Moretti, P.A.2    Zebol, J.R.3    Pitson, S.M.4
  • 22
    • 34548658230 scopus 로고    scopus 로고
    • Heat shock factor 1 is a power ful multi face ted modifier of carcinogenesis
    • Dai, C., Whitesell, L., Rogers, A. B., Lindquist, S. (2007) Heat shock factor 1 is a powerfulmultifacetedmodifier of carcinogenesis. Cell 130, 1005-1018
    • (2007) Cell , vol.130 , pp. 1005-1018
    • Dai, C.1    Whitesell, L.2    Rogers, A.B.3    Lindquist, S.4
  • 24
    • 0033546169 scopus 로고    scopus 로고
    • Divalent cations differentially regulate integrin alphaIIb cytoplasmic tail binding to beta3 and to calcium-and integrin-binding protein
    • Vallar, L., Melchior, C., Plançon, S., Drobecq, H., Lippens, G., Regnault, V., Kieffer, N. (1999) Divalent cations differentially regulate integrin alphaIIb cytoplasmic tail binding to beta3 and to calcium-and integrin-binding protein. J. Biol. Chem. 274, 17257-17266
    • (1999) J. Biol. Chem. , vol.274 , pp. 17257-17266
    • Vallar, L.1    Melchior, C.2    Plançon, S.3    Drobecq, H.4    Lippens, G.5    Regnault, V.6    Kieffer, N.7
  • 25
    • 29644434488 scopus 로고    scopus 로고
    • Ca2+-independent binding and cellular expression profiles question a significant role of calmyrin in transduction of Ca2+-signals to Alzheimer's disease-related presenilin 2 in forebrain
    • Blazejczyk, M., Wojda, U., Sobczak, A., Spilker, C., Bernstein, H. G., Gundelfinger, E. D., Kreutz, M. R., Kuznicki, J. (2006) Ca2+-independent binding and cellular expression profiles question a significant role of calmyrin in transduction of Ca2+-signals to Alzheimer's disease-related presenilin 2 in forebrain. Biochim. Biophys. Acta 1762, 66-72
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 66-72
    • Blazejczyk, M.1    Wojda, U.2    Sobczak, A.3    Spilker, C.4    Bernstein, H.G.5    Gundelfinger, E.D.6    Kreutz, M.R.7    Kuznicki, J.8
  • 26
    • 78649838512 scopus 로고    scopus 로고
    • Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells
    • Naik, M.U., Pham, N.T., Beebe, K., Dai, W., Naik, U. P. (2011) Calcium-dependent inhibition of polo-like kinase 3 activity by CIB1 in breast cancer cells. Int. J. Cancer 128, 587-596
    • (2011) Int. J. Cancer , vol.128 , pp. 587-596
    • Naik, M.U.1    Pham, N.T.2    Beebe, K.3    Dai, W.4    Naik, U.P.5
  • 28
    • 48049116376 scopus 로고    scopus 로고
    • Identification of residues of functional importance within the central turn motifs present in the cytoplasmic tails of integrin alphaIIb and alphaV subunits
    • Haas, T. A., Taherian, A., Berry, T., Ma, X. (2008) Identification of residues of functional importance within the central turn motifs present in the cytoplasmic tails of integrin alphaIIb and alphaV subunits. Thromb. Res. 122, 507-516
    • (2008) Thromb. Res. , vol.122 , pp. 507-516
    • Haas, T.A.1    Taherian, A.2    Berry, T.3    Ma, X.4
  • 29
    • 76349120580 scopus 로고    scopus 로고
    • Differential binding of IClninplatelets to integrin-derived activating and inhibitory peptides
    • Raab, M., Parthasarathi, L., Treumann, A., Moran, N., Daxecker, H. (2010) Differential binding of IClninplatelets to integrin-derived activating and inhibitory peptides. Biochem. Biophys. Res. Commun. 392, 258-263
    • (2010) Biochem. Biophys. Res. Commun. , vol.392 , pp. 258-263
    • Raab, M.1    Parthasarathi, L.2    Treumann, A.3    Moran, N.4    Daxecker, H.5
  • 30
    • 0037127264 scopus 로고    scopus 로고
    • Calciumintegrin-binding protein activates platelet integrin alpha IIbbeta 3
    • Tsuboi, S. (2002)Calciumintegrin-binding protein activates platelet integrin alpha IIbbeta 3. J. Biol. Chem. 277, 1919-1923
    • (2002) J. Biol. Chem. , vol.277 , pp. 1919-1923
    • Tsuboi, S.1
  • 31
    • 33746339970 scopus 로고    scopus 로고
    • CIB1, a ubiquitously expressed Ca2+-binding protein ligand of the InsP3 receptor Ca2+ release channel
    • White, C., Yang, J., Monteiro, M. J., Foskett, J. K. (2006)CIB1, a ubiquitously expressed Ca2+-binding protein ligand of the InsP3 receptor Ca2+ release channel. J. Biol. Chem. 281, 20825-20833
    • (2006) J. Biol. Chem. , vol.281 , pp. 20825-20833
    • White, C.1    Yang, J.2    Monteiro, M.J.3    Foskett, J.K.4
  • 32
    • 84901022639 scopus 로고    scopus 로고
    • Reduced IRE1amediates apoptotic cell death by disrupting calcium homeostasis via the InsP3 receptor
    • Son, S. M., Byun, J., Roh, S. E., Kim, S. J., Mook-Jung, I. (2014) Reduced IRE1amediates apoptotic cell death by disrupting calcium homeostasis via the InsP3 receptor. Cell Death Dis. 5, e1188
    • (2014) Cell Death Dis. , vol.5 , pp. e1188
    • Son, S.M.1    Byun, J.2    Roh, S.E.3    Kim, S.J.4    Mook-Jung, I.5
  • 34
    • 84862596361 scopus 로고    scopus 로고
    • Inhibition of protein N-myristoylation: A therapeutic protocol in developing anticancer agents
    • Das, U., Kumar, S., Dimmock, J. R., Sharma, R. K. (2012) Inhibition of protein N-myristoylation: a therapeutic protocol in developing anticancer agents. Curr. Cancer Drug Targets 12, 667-692
    • (2012) Curr. Cancer Drug Targets , vol.12 , pp. 667-692
    • Das, U.1    Kumar, S.2    Dimmock, J.R.3    Sharma, R.K.4
  • 37
    • 0033553908 scopus 로고    scopus 로고
    • A myristoylated calcium-binding protein that preferentially interactswiththeAlzheimer's diseasepresenilin 2 protein
    • Stabler, S. M., Ostrowski, L. L., Janicki, S. M., Monteiro, M. J. (1999) A myristoylated calcium-binding protein that preferentially interactswiththeAlzheimer's diseasepresenilin 2 protein. J.Cell Biol. 145, 1277-1292
    • (1999) J.Cell Biol. , vol.145 , pp. 1277-1292
    • Stabler, S.M.1    Ostrowski, L.L.2    Janicki, S.M.3    Monteiro, M.J.4
  • 39
    • 79953230120 scopus 로고    scopus 로고
    • Structural analysis of Mg2+ and Ca2+ binding, myristoylation, and dimerization of the neuronal calcium sensor and visinin-like protein 1 (VILIP-1)
    • Li, C., Pan, W., Braunewell, K. H., Ames, J. B. (2011) Structural analysis of Mg2+ and Ca2+ binding, myristoylation, and dimerization of the neuronal calcium sensor and visinin-like protein 1 (VILIP-1). J. Biol. Chem. 286, 6354-6366
    • (2011) J. Biol. Chem. , vol.286 , pp. 6354-6366
    • Li, C.1    Pan, W.2    Braunewell, K.H.3    Ames, J.B.4
  • 41
    • 84922272377 scopus 로고    scopus 로고
    • Integrin activation
    • Ginsberg, M. H. (2014) Integrin activation. BMB Rep. 47, 655-659
    • (2014) BMB Rep. , vol.47 , pp. 655-659
    • Ginsberg, M.H.1
  • 42
    • 84920285138 scopus 로고    scopus 로고
    • Targeting integrin and integrin signaling in treating thrombosis
    • Estevez, B., Shen, B., Du, X. (2015) Targeting integrin and integrin signaling in treating thrombosis. Arterioscler. Thromb. Vasc. Biol. 35, 24-29
    • (2015) Arterioscler. Thromb. Vasc. Biol. , vol.35 , pp. 24-29
    • Estevez, B.1    Shen, B.2    Du, X.3
  • 45
    • 33745185800 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein is involved in alphaIIb beta3-mediated cell adhesion
    • Tsuboi, S., Nonoyama, S., Ochs, H. D. (2006) Wiskott-Aldrich syndrome protein is involved in alphaIIb beta3-mediated cell adhesion. EMBO Rep. 7, 506-511
    • (2006) EMBO Rep. , vol.7 , pp. 506-511
    • Tsuboi, S.1    Nonoyama, S.2    Ochs, H.D.3
  • 46
    • 70449431471 scopus 로고    scopus 로고
    • CIB1 deficiency results in impaired thrombosis: The potential role of CIB1 in outside-in signaling through integrin alpha IIb beta 3
    • Naik, M. U., Nigam, A., Manrai, P., Millili, P., Czymmek, K., Sullivan, M., Naik, U. P. (2009) CIB1 deficiency results in impaired thrombosis: the potential role of CIB1 in outside-in signaling through integrin alpha IIb beta 3. J. Thromb. Haem. 7, 1906-1914
    • (2009) J. Thromb. Haem. , vol.7 , pp. 1906-1914
    • Naik, M.U.1    Nigam, A.2    Manrai, P.3    Millili, P.4    Czymmek, K.5    Sullivan, M.6    Naik, U.P.7
  • 47
    • 55549097150 scopus 로고    scopus 로고
    • Characterization of calcium-and integrin-binding protein 1 (CIB1) knockout platelets: Potential compensation byCIB family members
    • Denofrio, J. C., Yuan, W., Temple, B. R., Gentry, H. R., Parise, L. V. (2008) Characterization of calcium-and integrin-binding protein 1 (CIB1) knockout platelets: potential compensation byCIB family members. Thromb. Haemost. 100, 847-856
    • (2008) Thromb. Haemost. , vol.100 , pp. 847-856
    • Denofrio, J.C.1    Yuan, W.2    Temple, B.R.3    Gentry, H.R.4    Parise, L.V.5
  • 48
    • 0037041030 scopus 로고    scopus 로고
    • The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading
    • Haataja, L., Kaartinen, V., Groffen, J., Heisterkamp, N. (2002) The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin alpha(IIb)beta(3)-mediated adhesion and spreading. J. Biol. Chem. 277, 8321-8328
    • (2002) J. Biol. Chem. , vol.277 , pp. 8321-8328
    • Haataja, L.1    Kaartinen, V.2    Groffen, J.3    Heisterkamp, N.4
  • 49
    • 2442694279 scopus 로고    scopus 로고
    • Determination of N-and C-terminal borders of the transmembrane domain of integrin subunits
    • Stefansson, A., Armulik, A., Nilsson, I., von Heijne, G., Johansson, S. (2004) Determination of N-and C-terminal borders of the transmembrane domain of integrin subunits. J. Biol. Chem. 279, 21200-21205
    • (2004) J. Biol. Chem. , vol.279 , pp. 21200-21205
    • Stefansson, A.1    Armulik, A.2    Nilsson, I.3    Von Heijne, G.4    Johansson, S.5
  • 50
    • 70449566822 scopus 로고    scopus 로고
    • Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation
    • Yang, J., Ma, Y.Q., Page, R.C., Misra, S., Plow, E. F., andQin, J.(2009) Structure of an integrin alphaIIb beta3 transmembrane-cytoplasmic heterocomplex provides insight into integrin activation. Proc. Natl. Acad. Sci. USA 106, 17729-17734
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17729-17734
    • Yang, J.1    Ma, Y.Q.2    Page, R.C.3    Misra, S.4    Plow, E.F.5    Qin, J.6
  • 51
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau, T. L., Kim, C., Ginsberg, M. H., Ulmer, T. S. (2009) The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBOJ. 28, 1351-1361
    • (2009) EMBOJ. , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 52
    • 0242579243 scopus 로고    scopus 로고
    • Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen
    • Naik, M. U., Naik, U. P. (2003) Calcium-and integrin-binding protein regulates focal adhesion kinase activity during platelet spreading on immobilized fibrinogen. Blood 102, 3629-3636
    • (2003) Blood , vol.102 , pp. 3629-3636
    • Naik, M.U.1    Naik, U.P.2
  • 53
    • 80054982154 scopus 로고    scopus 로고
    • Contra-regulation of calcium-and integrin-binding protein 1-induced cell migration on fibronectin by PAK1 and MAP kinase signaling
    • Naik, M.U., Naik, U.P. (2011) Contra-regulation of calcium-and integrin-binding protein 1-induced cell migration on fibronectin by PAK1 and MAP kinase signaling. J. Cell. Biochem. 112, 3289-3299
    • (2011) J. Cell. Biochem. , vol.112 , pp. 3289-3299
    • Naik, M.U.1    Naik, U.P.2
  • 54
    • 23744432051 scopus 로고    scopus 로고
    • Essential role of CIB1 in regulating PAK1 activation and cell migration
    • Leisner, T. M., Liu, M., Jaffer, Z. M., Chernoff, J., Parise, L. V. (2005) Essential role of CIB1 in regulating PAK1 activation and cell migration. J. Cell Biol. 170, 465-476
    • (2005) J. Cell Biol. , vol.170 , pp. 465-476
    • Leisner, T.M.1    Liu, M.2    Jaffer, Z.M.3    Chernoff, J.4    Parise, L.V.5
  • 56
    • 84856068314 scopus 로고    scopus 로고
    • Calcium-and integrin-binding protein 1 regulates megakaryocyte ploidy, adhesion, and migration
    • Kostyak, J. C., Naik, M. U., Naik, U. P. (2012) Calcium-and integrin-binding protein 1 regulates megakaryocyte ploidy, adhesion, and migration. Blood 119, 838-846
    • (2012) Blood , vol.119 , pp. 838-846
    • Kostyak, J.C.1    Naik, M.U.2    Naik, U.P.3
  • 57
    • 0033577902 scopus 로고    scopus 로고
    • P21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts
    • Sells, M.A., Boyd, J.T., Chernoff, J. (1999)p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts. J. Cell Biol. 145, 837-849
    • (1999) J. Cell Biol. , vol.145 , pp. 837-849
    • Sells, M.A.1    Boyd, J.T.2    Chernoff, J.3
  • 58
    • 2542451854 scopus 로고    scopus 로고
    • Constitutive p21-activated kinase (PAK) activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions
    • Stofega, M. R., Sanders, L. C., Gardiner, E.M., Bokoch, G.M. (2004) Constitutive p21-activated kinase (PAK) activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions. Mol. Biol. Cell 15, 2965-2977
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2965-2977
    • Stofega, M.R.1    Sanders, L.C.2    Gardiner, E.M.3    Bokoch, G.M.4
  • 62
    • 84883145808 scopus 로고    scopus 로고
    • CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell death via AKT and ERK signaling
    • Leisner, T.M., Moran, C., Holly, S. P., Parise, L. V. (2013) CIB1 prevents nuclear GAPDH accumulation and non-apoptotic tumor cell death via AKT and ERK signaling. Oncogene 32, 4017-4027
    • (2013) Oncogene , vol.32 , pp. 4017-4027
    • Leisner, T.M.1    Moran, C.2    Holly, S.P.3    Parise, L.V.4
  • 63
    • 84906987368 scopus 로고    scopus 로고
    • DNA-PKcs-interacting protein KIP binding to TRF2 is required for the maintenance of functional telomeres
    • Khadka, P., Lee, J. H., Baek, S. H., Oh, S. Y., Chung, I. K. (2014) DNA-PKcs-interacting protein KIP binding to TRF2 is required for the maintenance of functional telomeres. Biochem. J. 463, 19-30
    • (2014) Biochem. J. , vol.463 , pp. 19-30
    • Khadka, P.1    Lee, J.H.2    Baek, S.H.3    Oh, S.Y.4    Chung, I.K.5
  • 64
    • 84895729227 scopus 로고    scopus 로고
    • CIB1 synergizes with EphrinA2 to regulate Kaposi's sarcoma-associated herpesvirus macropinocytic entry in human microvascular dermal endothelial cells
    • Bandyopadhyay, C., Valiya-Veettil, M., Dutta, D., Chakraborty, S., Chandran, B. (2014)CIB1 synergizes with EphrinA2 to regulate Kaposi's sarcoma-associated herpesvirus macropinocytic entry in human microvascular dermal endothelial cells. PLoS Pathog. 10, e1003941
    • (2014) PLoS Pathog. , vol.10 , pp. e1003941
    • Bandyopadhyay, C.1    Valiya-Veettil, M.2    Dutta, D.3    Chakraborty, S.4    Chandran, B.5
  • 66
    • 0034643903 scopus 로고    scopus 로고
    • Human sphingosine kinase:molecular cloning, functional characterization and tissue distribution
    • Melendez, A. J., Carlos-Dias, E., Gosink, M., Allen, J.M., Takacs, L. (2000)Human sphingosine kinase:molecular cloning, functional characterization and tissue distribution. Gene 251, 19-26
    • (2000) Gene , vol.251 , pp. 19-26
    • Melendez, A.J.1    Carlos-Dias, E.2    Gosink, M.3    Allen, J.M.4    Takacs, L.5
  • 67
    • 84897385973 scopus 로고    scopus 로고
    • Synergistic anti-tumor effects of combined gemcitabine and cisplatin nanoparticles in a stroma-rich bladder carcinoma model
    • Zhang, J., Miao, L., Guo, S., Zhang, Y., Zhang, L., Satterlee, A., Kim, W. Y., Huang, L. (2014) Synergistic anti-tumor effects of combined gemcitabine and cisplatin nanoparticles in a stroma-rich bladder carcinoma model. J. Control. Release 182, 90-96
    • (2014) J. Control. Release , vol.182 , pp. 90-96
    • Zhang, J.1    Miao, L.2    Guo, S.3    Zhang, Y.4    Zhang, L.5    Satterlee, A.6    Kim, W.Y.7    Huang, L.8
  • 69
    • 84900796050 scopus 로고    scopus 로고
    • Apoptosis signalregulating kinase 1 as a therapeutic target
    • Kawarazaki, Y., Ichijo, H., Naguro, I. (2014) Apoptosis signalregulating kinase 1 as a therapeutic target. Expert Opin. Ther. Targets 18, 651-664
    • (2014) Expert Opin. Ther. Targets , vol.18 , pp. 651-664
    • Kawarazaki, Y.1    Ichijo, H.2    Naguro, I.3
  • 70
    • 77950547739 scopus 로고    scopus 로고
    • The roles of ASK family proteins in stress responses and diseases
    • Hattori, K., Naguro, I., Runchel, C., Ichijo, H. (2009) The roles of ASK family proteins in stress responses and diseases. Cell Commun. Signal. 7, 9
    • (2009) Cell Commun. Signal. , vol.7 , pp. 9
    • Hattori, K.1    Naguro, I.2    Runchel, C.3    Ichijo, H.4
  • 72
    • 84874532079 scopus 로고    scopus 로고
    • Death in the United States 2010
    • Minino, A.M., Murphy, S. L. (2012) Death in theUnited States, 2010. NCHS Data Brief 99, 1-8
    • (2012) NCHS Data Brief , vol.99 , pp. 1-8
    • Minino, A.M.1    Murphy, S.L.2
  • 73
    • 84859926397 scopus 로고    scopus 로고
    • Cancer cell differentiation heterogeneity and aggressive behavior in solid tumors
    • Jögi, A., Vaapil, M., Johansson, M., Pahlman, S. (2012) Cancer cell differentiation heterogeneity and aggressive behavior in solid tumors. Ups. J. Med. Sci. 117, 217-224
    • (2012) Ups. J. Med. Sci. , vol.117 , pp. 217-224
    • Jögi, A.1    Vaapil, M.2    Johansson, M.3    Pahlman, S.4
  • 74
    • 61449182121 scopus 로고    scopus 로고
    • Principles of cancer therapy: Oncogene and non-oncogene addiction
    • Luo, J., Solimini, N. L., Elledge, S. J. (2009) Principles of cancer therapy: oncogene and non-oncogene addiction. Cell 136, 823-837
    • (2009) Cell , vol.136 , pp. 823-837
    • Luo, J.1    Solimini, N.L.2    Elledge, S.J.3
  • 75
    • 80054687126 scopus 로고    scopus 로고
    • Overexpression of hepatoma-derived growth factor in melanocytes does not lead to oncogenic transformation
    • Sedlmaier, A., Wernert, N., Gallitzendörfer, R., Abouzied, M. M., Gieselmann, V., Franken, S. (2011) Overexpression of hepatoma-derived growth factor in melanocytes does not lead to oncogenic transformation. BMC Cancer 11, 457
    • (2011) BMC Cancer , vol.11 , pp. 457
    • Sedlmaier, A.1    Wernert, N.2    Gallitzendörfer, R.3    Abouzied, M.M.4    Gieselmann, V.5    Franken, S.6
  • 77
    • 84896689604 scopus 로고    scopus 로고
    • A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis
    • Armacki, M., Joodi, G., Nimmagadda, S. C., de Kimpe, L., Pusapati, G. V., Vandoninck, S., Van Lint, J., Illing, A., Seufferlein, T. (2014) A novel splice variant of calcium and integrin-binding protein 1 mediates protein kinase D2-stimulated tumour growth by regulating angiogenesis. Oncogene 33, 1167-1180
    • (2014) Oncogene , vol.33 , pp. 1167-1180
    • Armacki, M.1    Joodi, G.2    Nimmagadda, S.C.3    De Kimpe, L.4    Pusapati, G.V.5    Vandoninck, S.6    Van Lint, J.7    Illing, A.8    Seufferlein, T.9
  • 78
    • 84930960105 scopus 로고    scopus 로고
    • Interaction of human tumor viruses with host cell surface receptors and cell entry
    • Schäfer, G., Blumenthal, M. J., Katz, A. A. (2015) Interaction of human tumor viruses with host cell surface receptors and cell entry. Viruses 7, 2592-2617
    • (2015) Viruses , vol.7 , pp. 2592-2617
    • Schäfer, G.1    Blumenthal, M.J.2    Katz, A.A.3
  • 79
    • 0030002580 scopus 로고    scopus 로고
    • The progression from hypertension to congestive heart failure
    • Levy, D., Larson, M. G., Vasan, R. S., Kannel, W. B., Ho, K. K. (1996) The progression from hypertension to congestive heart failure. JAMA 275, 1557-1562
    • (1996) JAMA , vol.275 , pp. 1557-1562
    • Levy, D.1    Larson, M.G.2    Vasan, R.S.3    Kannel, W.B.4    Ho, K.K.5
  • 83
    • 84888331632 scopus 로고    scopus 로고
    • Expression of genes encoding the calcium signalosome in cellular and transgenic models of Huntington's disease
    • Czeredys, M., Gruszczynska-Biegala, J., Schacht, T., Methner, A., Kuznicki, J. (2013) Expression of genes encoding the calcium signalosome in cellular and transgenic models of Huntington's disease. Front. Mol. Neurosci. 6, 42
    • (2013) Front. Mol. Neurosci. , vol.6 , pp. 42
    • Czeredys, M.1    Gruszczynska-Biegala, J.2    Schacht, T.3    Methner, A.4    Kuznicki, J.5
  • 84
    • 84901278110 scopus 로고    scopus 로고
    • Calcium-and integrin-binding protein-1 is down-regulated in the sperm of patients with oligoasthenozoospermia: CIB1 expression in patients with oligoasthenozoospermia
    • Sun, W., Guan, Q., Wen, J., Zhang, Q., Yang, W., Zhang, B., Cui, W., Zou, Z., Yu, Y. (2014)Calcium-and integrin-binding protein-1 is down-regulated in the sperm of patients with oligoasthenozoospermia: CIB1 expression in patients with oligoasthenozoospermia. J. Assist. Reprod. Genet. 31, 541-547
    • (2014) J. Assist. Reprod. Genet. , vol.31 , pp. 541-547
    • Sun, W.1    Guan, Q.2    Wen, J.3    Zhang, Q.4    Yang, W.5    Zhang, B.6    Cui, W.7    Zou, Z.8    Yu, Y.9
  • 85
    • 77955385274 scopus 로고    scopus 로고
    • The interaction between AID and CIB1 is nonessential for antibody gene diversification by gene conversion or class switch recombination
    • Demorest, Z.L., MacDuff, D.A., Brown, W.L., Morham, S. G., Parise, L. V., Harris, R. S. (2010) The interaction between AID and CIB1 is nonessential for antibody gene diversification by gene conversion or class switch recombination. PLoS One 5, e11660
    • (2010) PLoS One , vol.5 , pp. e11660
    • Demorest, Z.L.1    MacDuff, D.A.2    Brown, W.L.3    Morham, S.G.4    Parise, L.V.5    Harris, R.S.6
  • 86
    • 0030680162 scopus 로고    scopus 로고
    • Interaction between DNAdependent protein kinase and a novel protein
    • Wu, X., Lieber, M. R. (1997) Interaction between DNAdependent protein kinase and a novel protein, KIP. Mutat. Res. 385, 13-20
    • (1997) KIP. Mutat. Res. , vol.385 , pp. 13-20
    • Wu, X.1    Lieber, M.R.2
  • 87
    • 4544379480 scopus 로고    scopus 로고
    • DNA-protein kinase catalytic subunit-interacting protein KIP binds telomerase by interacting with human telomerase reverse transcriptase
    • Lee, G. E., Yu, E. Y., Cho, C.H., Lee, J., Muller, M.T., Chung, I.K. (2004)DNA-protein kinase catalytic subunit-interacting protein KIP binds telomerase by interacting with human telomerase reverse transcriptase. J. Biol. Chem. 279, 34750-34755
    • (2004) J. Biol. Chem. , vol.279 , pp. 34750-34755
    • Lee, G.E.1    Yu, E.Y.2    Cho, C.H.3    Lee, J.4    Muller, M.T.5    Chung, I.K.6
  • 89
    • 0037066571 scopus 로고    scopus 로고
    • The EF-hand calcium-binding protein calmyrin inhibits the transcriptional and DNA-binding activity of Pax3
    • Hollenbach, A. D., McPherson, C. J., Lagutina, I., Grosveld, G. (2002) The EF-hand calcium-binding protein calmyrin inhibits the transcriptional and DNA-binding activity of Pax3. Biochim. Biophys. Acta 1574, 321-328
    • (2002) Biochim. Biophys. Acta , vol.1574 , pp. 321-328
    • Hollenbach, A.D.1    McPherson, C.J.2    Lagutina, I.3    Grosveld, G.4
  • 91
    • 0034737397 scopus 로고    scopus 로고
    • Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity
    • Ito, A., Uehara, T., Nomura, Y. (2000) Isolation of Ich-1S (caspase-2S)-binding protein that partially inhibits caspase activity. FEBS Lett. 470, 360-364
    • (2000) FEBS Lett. , vol.470 , pp. 360-364
    • Ito, A.1    Uehara, T.2    Nomura, Y.3
  • 92
    • 13044313478 scopus 로고    scopus 로고
    • The polo-like protein kinases Fnk and Snk associate with a Ca2+-and integrin-binding protein and are regulated dynamically with synaptic plasticity
    • Kauselmann, G., Weiler, M., Wulff, P., Jessberger, S., Konietzko, U., Scafidi, J., Staubli, U., Bereiter-Hahn, J., Strebhardt, K., Kuhl, D. (1999) The polo-like protein kinases Fnk and Snk associate with a Ca2+-and integrin-binding protein and are regulated dynamically with synaptic plasticity. EMBO J. 18, 5528-5539
    • (1999) EMBO J. , vol.18 , pp. 5528-5539
    • Kauselmann, G.1    Weiler, M.2    Wulff, P.3    Jessberger, S.4    Konietzko, U.5    Scafidi, J.6    Staubli, U.7    Bereiter-Hahn, J.8    Strebhardt, K.9    Kuhl, D.10
  • 94
    • 63149152651 scopus 로고    scopus 로고
    • The oncoprotein LMO3 interacts with calcium-and integrin-binding protein CIB
    • Hui, L., Ji, C., Hui, B., Lv, T., Ha, X., Yang, J., Cai, W. (2009)The oncoprotein LMO3 interacts with calcium-and integrin-binding protein CIB. Brain Res. 1265, 24-29
    • (2009) Brain Res. , vol.1265 , pp. 24-29
    • Hui, L.1    Ji, C.2    Hui, B.3    Lv, T.4    Ha, X.5    Yang, J.6    Cai, W.7
  • 96
    • 0036159744 scopus 로고    scopus 로고
    • NBR1 interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB) and shows developmentally restricted expression in the neural tube
    • Whitehouse, C., Chambers, J., Howe, K., Cobourne, M., Sharpe, P., Solomon, E. (2002) NBR1 interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB) and shows developmentally restricted expression in the neural tube. Eur. J. Biochem. 269, 538-545
    • (2002) Eur. J. Biochem. , vol.269 , pp. 538-545
    • Whitehouse, C.1    Chambers, J.2    Howe, K.3    Cobourne, M.4    Sharpe, P.5    Solomon, E.6
  • 98
    • 0037359602 scopus 로고    scopus 로고
    • The seruminducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium-and integrin-binding protein CIB
    • Ma, S., Liu, M. A., Yuan, Y. L., Erikson, R. L. (2003) The seruminducible protein kinase Snk is a G1 phase polo-like kinase that is inhibited by the calcium-and integrin-binding protein CIB. Mol. Cancer Res. 1, 376-384
    • (2003) Mol. Cancer Res. , vol.1 , pp. 376-384
    • Ma, S.1    Liu, M.A.2    Yuan, Y.L.3    Erikson, R.L.4
  • 99
    • 84980417241 scopus 로고    scopus 로고
    • Interaction of calcium-and integrin-binding protein 1 with integrin a11 and its possible involvement in pulmonary fibrosis
    • Yoshida, K., Park, A., Ozaki, S., Munakata, H. (2014) Interaction of calcium-and integrin-binding protein 1 with integrin a11 and its possible involvement in pulmonary fibrosis. Adv. Biol. Chem. 4, 59-66
    • (2014) Adv. Biol. Chem. , vol.4 , pp. 59-66
    • Yoshida, K.1    Park, A.2    Ozaki, S.3    Munakata, H.4
  • 100
    • 0035871099 scopus 로고    scopus 로고
    • The interaction of the calcium-andintegrin-binding protein (CIBP) with the coagulation factor VIII
    • Fang, X., Chen, C., Wang, Q., Gu, J., Chi, C. (2001) The interaction of the calcium-andintegrin-binding protein (CIBP) with the coagulation factor VIII. Thromb. Res. 102, 177-185
    • (2001) Thromb. Res. , vol.102 , pp. 177-185
    • Fang, X.1    Chen, C.2    Wang, Q.3    Gu, J.4    Chi, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.