메뉴 건너뛰기




Volumn 8, Issue 1, 2013, Pages

Purification and SAXS Analysis of the Integrin Linked Kinase, PINCH, Parvin (IPP) Heterotrimeric Complex

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA PARVIN; BINDING PROTEIN; INTEGRIN LINKED KINASE; PROTEIN PINCH1; UNCLASSIFIED DRUG;

EID: 84873138942     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0055591     Document Type: Article
Times cited : (12)

References (51)
  • 1
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger DS, Calderwood DA, (2009) Integrin signalling at a glance. J Cell Sci 122: 159-163.
    • (2009) J Cell Sci , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 3
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase
    • Hannigan GE, Leung-Hagesteijn C, Fitz-Gibbon L, Coppolino MG, Radeva G, et al. (1996) Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase. Nature 379: 91-96.
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1    Leung-Hagesteijn, C.2    Fitz-Gibbon, L.3    Coppolino, M.G.4    Radeva, G.5
  • 5
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu Y, Li F, Goicoechea S, Wu C, (1999) The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol Cell Biol 19: 2425-2434.
    • (1999) Mol Cell Biol , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 6
    • 0035895898 scopus 로고    scopus 로고
    • Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain
    • Velyvis A, Yang Y, Wu C, Qin J, (2001) Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain. J Biol Chem 276: 4932-4939.
    • (2001) J Biol Chem , vol.276 , pp. 4932-4939
    • Velyvis, A.1    Yang, Y.2    Wu, C.3    Qin, J.4
  • 7
    • 77950518387 scopus 로고    scopus 로고
    • Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase
    • Chiswell BP, Stiegler AL, Razinia Z, Nalibotski E, Boggon TJ, et al. (2010) Structural basis of competition between PINCH1 and PINCH2 for binding to the ankyrin repeat domain of integrin-linked kinase. J Struct Biol 170: 157-163.
    • (2010) J Struct Biol , vol.170 , pp. 157-163
    • Chiswell, B.P.1    Stiegler, A.L.2    Razinia, Z.3    Nalibotski, E.4    Boggon, T.J.5
  • 9
    • 71149097258 scopus 로고    scopus 로고
    • The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions
    • Fukuda K, Gupta S, Chen K, Wu C, Qin J, (2009) The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions. Mol Cell 36: 819-830.
    • (2009) Mol Cell , vol.36 , pp. 819-830
    • Fukuda, K.1    Gupta, S.2    Chen, K.3    Wu, C.4    Qin, J.5
  • 10
    • 79957552048 scopus 로고    scopus 로고
    • Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): cross-validation of the pseudokinase
    • Fukuda K, Knight JD, Piszczek G, Kothary R, Qin J, (2011) Biochemical, proteomic, structural, and thermodynamic characterizations of integrin-linked kinase (ILK): cross-validation of the pseudokinase. J Biol Chem 286: 21886-21895.
    • (2011) J Biol Chem , vol.286 , pp. 21886-21895
    • Fukuda, K.1    Knight, J.D.2    Piszczek, G.3    Kothary, R.4    Qin, J.5
  • 11
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y, Huang Y, Zhang Y, Hua Y, Wu C, (2001) A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J Cell Biol 153: 585-598.
    • (2001) J Cell Biol , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 12
    • 0035844879 scopus 로고    scopus 로고
    • A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
    • Yamaji S, Suzuki A, Sugiyama Y, Koide Y, Yoshida M, et al. (2001) A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J Cell Biol 153: 1251-1264.
    • (2001) J Cell Biol , vol.153 , pp. 1251-1264
    • Yamaji, S.1    Suzuki, A.2    Sugiyama, Y.3    Koide, Y.4    Yoshida, M.5
  • 13
    • 33644836716 scopus 로고    scopus 로고
    • The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction
    • Yoshimi R, Yamaji S, Suzuki A, Mishima W, Okamura M, et al. (2006) The gamma-parvin-integrin-linked kinase complex is critically involved in leukocyte-substrate interaction. J Immunol 176: 3611-3624.
    • (2006) J Immunol , vol.176 , pp. 3611-3624
    • Yoshimi, R.1    Yamaji, S.2    Suzuki, A.3    Mishima, W.4    Okamura, M.5
  • 14
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne M, Tan C, Gray V, Rue L, Woodgett J, et al. (1998) Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc Natl Acad Sci U S A 95: 11211-11216.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3    Rue, L.4    Woodgett, J.5
  • 15
    • 0037115611 scopus 로고    scopus 로고
    • Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • Zhang Y, Chen K, Tu Y, Velyvis A, Yang Y, et al. (2002) Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J Cell Sci 115: 4777-4786.
    • (2002) J Cell Sci , vol.115 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Velyvis, A.4    Yang, Y.5
  • 16
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos SN, Turner CE, (2000) Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J Cell Biol 151: 1435-1448.
    • (2000) J Cell Biol , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 17
    • 84866554447 scopus 로고    scopus 로고
    • Structural Basis for Paxillin Binding and Focal Adhesion Targeting of beta-Parvin
    • Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, et al. (2012) Structural Basis for Paxillin Binding and Focal Adhesion Targeting of beta-Parvin. J Biol Chem 287: 32566-32577.
    • (2012) J Biol Chem , vol.287 , pp. 32566-32577
    • Stiegler, A.L.1    Draheim, K.M.2    Li, X.3    Chayen, N.E.4    Calderwood, D.A.5
  • 18
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival
    • Fukuda T, Chen K, Shi X, Wu C, (2003) PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. J Biol Chem 278: 51324-51333.
    • (2003) J Biol Chem , vol.278 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3    Wu, C.4
  • 19
    • 69449100887 scopus 로고    scopus 로고
    • Molecular dissection of the ILK-PINCH-parvin triad reveals a fundamental role for the ILK kinase domain in the late stages of focal-adhesion maturation
    • Stanchi F, Grashoff C, Nguemeni Yonga CF, Grall D, Fassler R, et al. (2009) Molecular dissection of the ILK-PINCH-parvin triad reveals a fundamental role for the ILK kinase domain in the late stages of focal-adhesion maturation. J Cell Sci 122: 1800-1811.
    • (2009) J Cell Sci , vol.122 , pp. 1800-1811
    • Stanchi, F.1    Grashoff, C.2    Nguemeni Yonga, C.F.3    Grall, D.4    Fassler, R.5
  • 20
    • 0345103747 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation
    • Sakai T, Li S, Docheva D, Grashoff C, Sakai K, et al. (2003) Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev 17: 926-940.
    • (2003) Genes Dev , vol.17 , pp. 926-940
    • Sakai, T.1    Li, S.2    Docheva, D.3    Grashoff, C.4    Sakai, K.5
  • 21
    • 70350345546 scopus 로고    scopus 로고
    • Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling
    • Montanez E, Wickstrom SA, Altstatter J, Chu H, Fassler R, (2009) Alpha-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling. The EMBO journal 28: 3132-3144.
    • (2009) The EMBO Journal , vol.28 , pp. 3132-3144
    • Montanez, E.1    Wickstrom, S.A.2    Altstatter, J.3    Chu, H.4    Fassler, R.5
  • 22
    • 23744490092 scopus 로고    scopus 로고
    • PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage
    • Li S, Bordoy R, Stanchi F, Moser M, Braun A, et al. (2005) PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage. J Cell Sci 118: 2913-2921.
    • (2005) J Cell Sci , vol.118 , pp. 2913-2921
    • Li, S.1    Bordoy, R.2    Stanchi, F.3    Moser, M.4    Braun, A.5
  • 23
    • 16244413957 scopus 로고    scopus 로고
    • PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes
    • Liang X, Zhou Q, Li X, Sun Y, Lu M, et al. (2005) PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes. Molecular and cellular biology 25: 3056-3062.
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 3056-3062
    • Liang, X.1    Zhou, Q.2    Li, X.3    Sun, Y.4    Lu, M.5
  • 24
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon AC, Qadota H, Norman KR, Moerman DG, Williams BD, (2002) C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol 12: 787-797.
    • (2002) Curr Biol , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 25
    • 44149105411 scopus 로고    scopus 로고
    • Kindlin-2 controls bidirectional signaling of integrins
    • Montanez E, Ussar S, Schifferer M, Bosl M, Zent R, et al. (2008) Kindlin-2 controls bidirectional signaling of integrins. Genes Dev 22: 1325-1330.
    • (2008) Genes Dev , vol.22 , pp. 1325-1330
    • Montanez, E.1    Ussar, S.2    Schifferer, M.3    Bosl, M.4    Zent, R.5
  • 26
    • 11144225205 scopus 로고    scopus 로고
    • Integrin-linked kinase: a cancer therapeutic target unique among its ILK
    • Hannigan G, Troussard AA, Dedhar S, (2005) Integrin-linked kinase: a cancer therapeutic target unique among its ILK. Nat Rev Cancer 5: 51-63.
    • (2005) Nat Rev Cancer , vol.5 , pp. 51-63
    • Hannigan, G.1    Troussard, A.A.2    Dedhar, S.3
  • 27
    • 47749087950 scopus 로고    scopus 로고
    • Integrin-linked kinase-essential roles in physiology and cancer biology
    • McDonald PC, Fielding AB, Dedhar S, (2008) Integrin-linked kinase-essential roles in physiology and cancer biology. J Cell Sci 121: 3121-3132.
    • (2008) J Cell Sci , vol.121 , pp. 3121-3132
    • McDonald, P.C.1    Fielding, A.B.2    Dedhar, S.3
  • 28
    • 34248369857 scopus 로고    scopus 로고
    • Biological small-angle x-ray scattering facility at the Stanford synchrotron radiation laboratory
    • Smolsky IL, Liu P, Niebuhr M, Ito K, Weiss TM, et al. (2007) Biological small-angle x-ray scattering facility at the Stanford synchrotron radiation laboratory. Journal of Applied Crystallography 40: S453-S458.
    • (2007) Journal of Applied Crystallography , vol.40
    • Smolsky, I.L.1    Liu, P.2    Niebuhr, M.3    Ito, K.4    Weiss, T.M.5
  • 31
    • 62649139615 scopus 로고    scopus 로고
    • DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering
    • Franke D, Svergun DI, (2009) DAMMIF, a program for rapid ab-initio shape determination in small-angle scattering. Journal of Applied Crystallography 42: 342-346.
    • (2009) Journal of Applied Crystallography , vol.42 , pp. 342-346
    • Franke, D.1    Svergun, D.I.2
  • 32
    • 72449188596 scopus 로고    scopus 로고
    • NADPH oxidase activator P67(phox) behaves in solution as a multidomain protein with semi-flexible linkers
    • Durand D, Vives C, Cannella D, Perez J, Pebay-Peyroula E, et al. (2010) NADPH oxidase activator P67(phox) behaves in solution as a multidomain protein with semi-flexible linkers. Journal of Structural Biology 169: 45-53.
    • (2010) Journal of Structural Biology , vol.169 , pp. 45-53
    • Durand, D.1    Vives, C.2    Cannella, D.3    Perez, J.4    Pebay-Peyroula, E.5
  • 33
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing Flexible and Intrinsically Unstructured Biological Macromolecules by SAS Using the Porod-Debye Law
    • Rambo RP, Tainer JA, (2011) Characterizing Flexible and Intrinsically Unstructured Biological Macromolecules by SAS Using the Porod-Debye Law. Biopolymers 95: 559-571.
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 34
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI, (2003) Uniqueness of ab initio shape determination in small-angle scattering. Journal of Applied Crystallography 36: 860-864.
    • (2003) Journal of Applied Crystallography , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 35
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI, (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophysical Journal 76: 2879-2886.
    • (1999) Biophysical Journal , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 36
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI, (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophysical Journal 89: 1237-1250.
    • (2005) Biophysical Journal , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 37
    • 34247891557 scopus 로고    scopus 로고
    • Structural characterization of flexible proteins using small-angle X-ray scattering
    • Bernado P, Mylonas E, Petoukhov MV, Blackledge M, Svergun DI, (2007) Structural characterization of flexible proteins using small-angle X-ray scattering. J Am Chem Soc 129: 5656-5664.
    • (2007) J Am Chem Soc , vol.129 , pp. 5656-5664
    • Bernado, P.1    Mylonas, E.2    Petoukhov, M.V.3    Blackledge, M.4    Svergun, D.I.5
  • 38
    • 38549146411 scopus 로고    scopus 로고
    • Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering
    • Bernado P, Perez Y, Svergun DI, Pons M, (2008) Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering. Journal of Molecular Biology 376: 492-505.
    • (2008) Journal of Molecular Biology , vol.376 , pp. 492-505
    • Bernado, P.1    Perez, Y.2    Svergun, D.I.3    Pons, M.4
  • 39
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, Koch MHJ, (1995) CRYSOL- A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. Journal of Applied Crystallography 28: 768-773.
    • (1995) Journal of Applied Crystallography , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 40
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • Kozin MB, Svergun DI, (2001) Automated matching of high- and low-resolution structural models. Journal of Applied Crystallography 34: 33-41.
    • (2001) Journal of Applied Crystallography , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 41
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position-specific scoring matrices
    • Jones DT, (1999) Protein secondary structure prediction based on position-specific scoring matrices. Journal of Molecular Biology 292: 195-202.
    • (1999) Journal of Molecular Biology , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 42
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT, (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337: 635-645.
    • (2004) J Mol Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 43
    • 34547588389 scopus 로고    scopus 로고
    • PrDOS: prediction of disordered protein regions from amino acid sequence
    • Ishida T, Kinoshita K, (2007) PrDOS: prediction of disordered protein regions from amino acid sequence. Nucleic acids research 35: W460-464.
    • (2007) Nucleic Acids Research , vol.35
    • Ishida, T.1    Kinoshita, K.2
  • 44
    • 0242458482 scopus 로고    scopus 로고
    • Protein disorder prediction: implications for structural proteomics
    • Linding R, Jensen LJ, Diella F, Bork P, Gibson TJ, et al. (2003) Protein disorder prediction: implications for structural proteomics. Structure 11: 1453-1459.
    • (2003) Structure , vol.11 , pp. 1453-1459
    • Linding, R.1    Jensen, L.J.2    Diella, F.3    Bork, P.4    Gibson, T.J.5
  • 45
    • 65549125472 scopus 로고    scopus 로고
    • Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase
    • Yang Y, Wang X, Hawkins CA, Chen K, Vaynberg J, et al. (2009) Structural basis of focal adhesion localization of LIM-only adaptor PINCH by integrin-linked kinase. J Biol Chem 284: 5836-5844.
    • (2009) J Biol Chem , vol.284 , pp. 5836-5844
    • Yang, Y.1    Wang, X.2    Hawkins, C.A.3    Chen, K.4    Vaynberg, J.5
  • 46
    • 84867530808 scopus 로고    scopus 로고
    • Functional analysis of parvin and different modes of IPP-complex assembly at integrin sites during Drosophila development
    • Vakaloglou KM, Chountala M, Zervas CG, (2012) Functional analysis of parvin and different modes of IPP-complex assembly at integrin sites during Drosophila development. J Cell Sci.
    • (2012) J Cell Sci
    • Vakaloglou, K.M.1    Chountala, M.2    Zervas, C.G.3
  • 47
    • 4744340477 scopus 로고    scopus 로고
    • Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival
    • Zhang Y, Chen K, Tu Y, Wu C, (2004) Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival. J Biol Chem 279: 41695-41705.
    • (2004) J Biol Chem , vol.279 , pp. 41695-41705
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Wu, C.4
  • 48
    • 0037064063 scopus 로고    scopus 로고
    • Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration
    • Zhang Y, Chen K, Guo L, Wu C, (2002) Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration. J Biol Chem 277: 38328-38338.
    • (2002) J Biol Chem , vol.277 , pp. 38328-38338
    • Zhang, Y.1    Chen, K.2    Guo, L.3    Wu, C.4
  • 49
    • 34249851728 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of nuclear localization and functions of integrin-linked kinase
    • Acconcia F, Barnes CJ, Singh RR, Talukder AH, Kumar R, (2007) Phosphorylation-dependent regulation of nuclear localization and functions of integrin-linked kinase. Proc Natl Acad Sci U S A 104: 6782-6787.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6782-6787
    • Acconcia, F.1    Barnes, C.J.2    Singh, R.R.3    Talukder, A.H.4    Kumar, R.5
  • 50
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways
    • Tu Y, Li F, Wu C, (1998) Nck-2, a novel Src homology2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase-signaling pathways. Mol Biol Cell 9: 3367-3382.
    • (1998) Mol Biol Cell , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 51
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski TM, Noegel AA, Korenbaum E, (2001) Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J Cell Sci 114: 525-538.
    • (2001) J Cell Sci , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.