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    وصف الملف: application/pdf

    Relation: Witucki, Laurie A.; Borowicz, Lauren Sanford; Pedley, Anthony M.; Curtis‐fisk, Jaime; Kuszpit, Elizabeth Girnys (2015). "Identification of FAK substrate peptides via colorimetric screening of a oneâ bead oneâ peptide combinatorial library." Journal of Peptide Science 21(4): 302-311.; http://hdl.handle.net/2027.42/110814; Journal of Peptide Science; Wu JJ, Afar DE, Phan H, Witte ON, Lam KS. Recognition of multiple substrate motifs by the c‐ABL protein tyrosine kinase. Comb. Chem. High Throughput Screen. 2002; 5: 83 – 91.; Infante JR, Camidge DR, Mileshkin LR, Chen EX, Hicks RJ, Rischin D, Fingert H, Pierce KJ, Xu H, Roberts WG, Shreeve SM, Burris HA, Siu LL. Safety, pharmacokinetic, and pharmacodynamic phase I dose‐escalation trial of PF‐00562271, an inhibitor of focal adhesion kinase, in advanced solid tumors. J. Clin. Oncol. 2012; 30: 1527 – 1533. DOI:10.1200/JCO.2011.38.9346.; Falciani C, Lozzi L, Pini A, Bracci L. Bioactive peptides from libraries. Chem. Biol. 2005; 12: 417 – 426. DOI:10.1016/j.chembiol.2005.02.009.; Lou Q, Leftwich ME, Lam KS. Identification of GIYWHHY as a novel peptide substrate for human p60 c‐src protein tyrosine kinase. Bioorg. Med. Chem. 1996; 4: 677 – 682. DOI:10.1016/0968-0896(96)00063-6.; Lam KS, Wu J, Lou Q. Identification and characterization of a novel synthetic peptide substrate specific for Src‐family protein tyrosine kinases. Int. J. Pept. Protein Res. 1995; 45: 587 – 592. DOI:10.1111/j.1399-3011.1995.tb01323.x.; Kim Y‐G, Shin D‐S, Kim E‐M, Park H‐Y, Lee C‐S, Kim J‐H, Lee B‐S, Lee Y‐S, Kim B‐G. High‐throughput identification of substrate specificity for protein kinase by using an improved one‐bead‐one‐compound library approach. Angew. Chem. 2007; 119: 5504 – 5507. DOI:10.1002/ange.200700195.; Lam KS, Salmon SE, Hersh EM, Hruby VJ, Kazmierski WM, Knapp RJ. A new type of synthetic peptide library for identifying ligand‐binding activity. Nature 1991; 354: 82 – 84. 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Biochemistry 2000; 39: 13251 – 13260.; Wavreille A‐S, Garaud M, Zhang Y, Pei D. Defining SH2 domain and PTP specificity by screening combinatorial peptide libraries. Methods 2007; 42: 207 – 219. DOI:10.1016/j.ymeth.2007.02.010.; Songyang Z, Carraway KL, III, Eck MJ, Harrison SC, Feldman RA, Mohammadi M, Schlessinger J, Hubbard SR, Smith DP, Eng C, Lorenzo MJ, Poner BAJ, Mayer BJ, Cantley LC. Catalytic specificity of protein‐tyrosine kinases is critical for selective signalling. Nature 1995; 373: 536 – 539.; Lam KS, Liu R, Miyamoto S, Lehman AL, Tuscano JM. Applications of one‐bead one‐compound combinatorial libraries and chemical microarrays in signal transduction research. Acc. Chem. Res. 2003; 36: 370 – 377. DOI:10.1021/ar0201299.; Kim M, Shin DS, Kim J, Lee YS. Substrate screening of protein kinases: detection methods and combinatorial peptide libraries. Biopolymers 2010; 94: 753 – 762. DOI:10.1002/bip.21506.; Martin SE, Peterson BR. 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DOI:10.1038/35010517.; Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT. Autophosphorylation of the focal adhesion kinase, pp125fak, directs SH2‐dependent binding of pp60src. Mol. Cell. Biol. 1994; 14: 1680 – 1688. DOI:10.1128/MCB.14.3.1680.; Xing Z, Chen HC, Nowlen JK, Taylor SJ, Shalloway D, Guan JL. Direct interaction of v‐Src with the focal adhesion kinase mediated by the Src SH2 domain. Mol. Biol. Cell 1994; 5: 413 – 421. DOI:10.1091/mbc.5.4.413.; Schlaepfer DD, Hanks SK, Hunter T, Geer P. Integrin‐mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994; 372: 786 – 791. DOI:10.1038/372786a0.; Schlaepfer DD, Jones KC, Hunter T. Multiple Grb2‐mediated integrin‐stimulated signaling pathways to ERK2/mitogen‐activated protein kinase: summation of both c‐Src‐ and focal adhesion kinase‐initiated tyrosine phosphorylation events. Mol. Cell. Biol. 1998; 18: 2571 – 2585.; Chan PC, Lai JF, Cheng CH, Tang MJ, Chiu CC, Chen HC. Suppression of ultraviolet irradiation‐induced apoptosis by overexpression of focal adhesion kinase in Madin‐Darby canine kidney cells. J. Biol. Chem. 1999; 274: 26901 – 26906.; Sonoda Y, Matsumoto Y, Funakoshi M, Yamamoto D, Hanks SK, Kasahara T. Anti‐apoptotic role of focal adhesion kinase (FAK). Induction of inhibitor‐of‐apoptosis proteins and apoptosis suppression by the overexpression of FAK in a human leukemic cell line, HL‐60. J. Biol. Chem. 2000; 275: 16309 – 16315.; Lim S‐T, Chen XL, Lim Y, Hanson DA, Vo T‐T, Howerton K, Larocque N, Fisher SJ, Schlaepfer DD, Ilic D. Nuclear FAK promotes cell proliferation and survival through FERM‐enhanced p53 degradation. Mol. Cell 2008; 29: 9 – 22. DOI:10.1016/j.molcel.2007.11.031.; Tremblay L, Hauck W, Aprikian AG, Begin LR, Chapdelaine A, Chevalier S. Focal adhesion kinase (pp125FAK) expression, activation and association with paxillin and p50CSK in human metastatic prostate carcinoma. Int. J. Cancer 1996; 68: 164 – 171.; Harte MT, Hildebrand JD, Burnham MR, Bouton AH, Parsons JT. P130Cas, a substrate associated with v‐Src and v‐Crk, localizes to focal adhesions and binds to focal adhesion kinase. J. Biol. Chem. 1996; 271: 13649 – 13655.; Shen Y, Schaller MD. Focal adhesion targeting: the critical determinant of FAK regulation and substrate phosphorylation. Mol. Biol. Cell 1999; 10: 2507 – 2518.; Tachibana K, Urano T, Fujita H, Ohashi Y, Kamiguchi K, Iwata S, Hirai H, Morimoto C. Tyrosine phosphorylation of Crk‐associated substrates by focal adhesion kinase: a putative mechanism for the integrin‐mediated tyrosine phosphorylation of Crk‐associated substrates. J. Biol. Chem. 1997; 272: 29083 – 29090. DOI:10.1074/jbc.272.46.29083.; Han DC, Shen T‐L, Guan J‐L. Role of Grb7 targeting to focal contacts and its phosphorylation by focal adhesion kinase in regulation of cell migration. J. Biol. Chem. 2000; 275: 28911 – 28917. DOI:10.1074/jbc.M001997200.; Golubovskaya VM, Kweh FA, Cance WG. Focal adhesion kinase and cancer. Histol. Histopathol. 2009; 24: 503 – 510.; Akasaka T, van Leeuwen RL, Yoshinaga IG, Mihm MC, Jr, Byers HR. Focal adhesion kinase (p125FAK) expression correlates with motility of human melanoma cell lines. J. Invest. Dermatol. 1995; 105: 104 – 108.; Cance WG, Harris JE, Iacocca MV, Roche E, Yang X, Chang J, Simkins S, Xu L. Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes. Clin. Cancer Res. 2000; 6: 2417 – 2423.; McCormack SJ, Brazinski SE, Moore JL, Jr, Werness BA, Goldstein DJ. Activation of the focal adhesion kinase signal transduction pathway in cervical carcinoma cell lines and human genital epithelial cells immortalized with human papillomavirus type 18. Oncogene 1997; 15: 265 – 274. DOI:10.1038/sj.onc.1201186.; McLean GW, Avizienyte E, Frame MC. Focal adhesion kinase as a potential target in oncology. Expert Opin. Pharmacother. 2003; 4: 227 – 234. DOI:10.1517/14656566.4.2.227.; Zhao J, Guan J‐L. Signal transduction by focal adhesion kinase in cancer. Cancer Metastasis Rev. 2009; 28: 35 – 49. DOI:10.1007/s10555-008-9165-4.; Judson PL, He X, Cance WG, Van Le L. Overexpression of focal adhesion kinase, a protein tyrosine kinase, in ovarian carcinoma. Cancer 1999; 86: 1551 – 1556.; Recher C, Ysebaert L, Beyne‐Rauzy O, Mas VM‐D, Ruidavets J‐B, Cariven P, Demur C, Payrastre B, Laurent G, Racaud‐Sultan C. Expression of focal adhesion kinase in acute myeloid leukemia is associated with enhanced blast migration, increased cellularity, and poor prognosis. Cancer Res. 2004; 64: 3191 – 3197. DOI:10.1158/0008-5472.CAN-03-3005.; Sulzmaier FJ, Jean C, Schlaepfer DD. FAK in cancer: mechanistic findings and clinical applications. Nat. Rev. Cancer 2014; 14: 598 – 610. DOI:10.1038/nrc3792.; Jean C, Chen XL, Nam J‐O, Tancioni I, Uryu S, Lawson C, Ward KK, Walsh CT, Miller NLG, Ghassemian M, Turowski P, Dejana E, Weis S, Cheresh DA, Schlaepfer DD. Inhibition of endothelial FAK activity prevents tumor metastasis by enhancing barrier function. J. Cell Biol. 2014; 204: 247 – 263. DOI:10.1083/jcb.201307067.; Hochwald SN, Nyberg C, Zheng M, Zheng D, Wood C, Massoll NA, Magis A, Ostrov D, Cance WG, Golubovskaya VM. A novel small molecule inhibitor of FAK decreases growth of human pancreatic cancer. Cell Cy. (Georgetown, Tex.) 2009; 8: 2435 – 2443.; Golubovskaya VM, Figel S, Ho BT, Johnson CP, Yemma M, Huang G, Zheng M, Nyberg C, Magis A, Ostrov DA, Gelman IH, Cance WG. A small molecule focal adhesion kinase (FAK) inhibitor, targeting Y397 site: 1‐(2‐hydroxyethyl)‐3, 5, 7‐triaza‐1‐azoniatricyclo [3.3. 1.13, 7] decane; bromide effectively inhibits FAK autophosphorylation activity and decreases cancer cell viability, clonogenicity and tumor growth in vivo. Carcinogenesis 2012; 33: 1004 – 1013. DOI:10.1093/carcin/bgs120.; Golubovskaya V, Beviglia L, Xu L‐H, Earp HS, Craven R, Cance W. Dual inhibition of focal adhesion kinase and epidermal growth factor receptor pathways cooperatively induces death receptor‐mediated apoptosis in human breast cancer cells. J. Biol. Chem. 2002; 277: 38978 – 38987. DOI:10.1074/jbc.M205002200.

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    المؤلفون: Yi Liu, Witucki, Laurie A.

    المصدر: Biochemistry; 11/28/2000, Vol. 39 Issue 47, p14400, 9p, 1 Color Photograph, 4 Black and White Photographs, 4 Diagrams, 4 Charts, 1 Graph

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    المصدر: Journal About Women in Higher Education; January 2008, Vol. 1 Issue: 1 p231-233, 3p

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    المصدر: Journal About Women in Higher Education; December 2009, Vol. 1 Issue: 1 p1015-1015, 1p

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