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Chapter 6: Identification of Protein–Protein Interactions with Glutathione-S-Transferase Fusion Proteins—References

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Bedouelle H. and Duplay P. 1988. Production in Escherichia coli and one-step purification of bifunctional hybrid proteins which bind maltose. Eur. J. Biochem. 171: 541–549.

Blackwood E.M. and Eisenman R.N. 1991. Max: A helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. Science 251: 1211–1217.

Blanar M.A. and Rutter W.J. 1992. Interaction cloning: Identification of a helix-loop-helix zipper protein that interacts with c-Fos. Science 256: 1014–1018.

Brehm M.A., Schreiber I., Bertsch U., Wegner A., and Mayr G.W. 2004. Identification of the actin-binding domain of Ins(1,4,5)P3-kinase isoform B(IP3K-B). Biochem. J. 382: 353–362.

Cao X., Cismowski M.J., Sato M., Blumer J.B., and Lanier S.M. 2004. Identification and characterization of AGS4: A protein containing three G-protein regulatory motifs that regulate the activation state of Giα. J. Biol. Chem. 279: 27567–27574.

Cox G.N., Pratt D., Smith D., McDermott M.J., and van der Slice R.W. 1999. Refolding and characterization of recombinant human soluble CTLA-4 expressed in Escherichia coli. Protein Expr. Purif. 17: 26–32.

Dignam J.D., Lebowitz R.M., and Roeder R.G. 1982. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11: 1475–1489.

Einarson M.B. and Chao M.V. 1995. Regulation of Id1 and its association with basic helix-loop-helix proteins during nerve growth factor-induced differentiation of PC12 cells. Mol. Cell. Biol. 15: 4175–4183.

Frangoni J.V. and Neel B.G. 1993. Solubilization and purification of enzymatically active glutathione-S-transferase (GEX) fusion proteins. Anal. Biochem. 210: 179–187.

Gentz R., Chen C.H., and Rosen C.A. 1989. Bioassay for trans-activation using purified human immuno-deficiency virus tat-encoded protein: Trans-activation requires mRNA synthesis. Proc. Natl. Acad. Sci. 86: 821–824.

Grgurevich S., Mikhael A., and McVicar D.W. 1999. The Csk homologous kinase, Chk, binds tyrosine phosphorylated paxillin in human blastic T cells. Biochem. Biophys. Res. Commun. 256: 668–675.

Guan C., Li P., Riggs P.D., and Inouye H. 1988. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose binding protein. Gene 67: 21–30.

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Hunter S., Burton E.A., Wu S.C., and Anderson S.M. 1999. Fyn associates with Cbl and phosphorylates tyrosine 731 in Cbl, a binding site for phosphatidylinositol 3-kinase. J. Biol. Chem. 274: 2097–2106.

Kaelin W.G., Pallas D.C., DeCaprio J.A., Kaye F.J., and Livingston D.M. 1991. Identification of cellular proteins that can interact specifically with the T/E1A binding region of the retinoblastoma gene product. Cell 64: 521–532.

Kaelin W.G., Krek W., Sellers W.R., DeCaprio J.A., Ajchenbaum F., Fuchs C.S., Chittenden T., Li Y., Farnham P.J., Blanar M.A., Livingston D.M., and Flemington E.K. 1992. Expression cloning of a cDNA encoding a retinoblastoma-binding protein with E2F-like properties. Cell 70: 351–364.

Li L. Xin H., Xu X., Huang M., Zhang X., Chen Y., Zhang S., Fu X.Y., and Chang Z. 2004. CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription. Mol. Cell. Biol. 24: 856–864.

Macgregor P.F., Abate C., and Curran T. 1990. Direct cloning of leucine zipper proteins: Jun binds cooperatively to the CRE with CRE-BP1. Oncogene 5: 451–458.

Maina C.V., Riggs P.D., Grandea A.G., III, Slatko B.E., Moran L.S., Tagliamonte J.A., McReynolds L.A., and Guan C. 1988. A vector to express and purify foreign proteins in Escherichia coli by fusion to, and separation from, maltose binding protein. Gene 74: 365–373.

Maiyar A.C., Leong M.L., and Firestone G.L. 2003. Importin-α mediates the regulated nuclear targeting of serum and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain. Mol. Biol. Cell 14: 1221–1239.

McDonald O.B., Chen W.J., Ellis B., Hoffman C., Overton L., Rink M., Smith A., Marshall C.J., and Wood E.R. 1999. A scintillation proximity assay for the Raf/MEK/ERK kinase cascade: High-throughput screening and identification of selective enzyme inhibitors. Anal. Biochem. 268: 318–329.

Min J.-H., Yang H., Ivan M., Gertler F., Kaelin W.G., and Pavletich N.P. 2002. Structure of an HIF-1α-pVHL complex: Hydroxyproline recognition in signaling. Science 296: 1886–1889.

Orlinick J.R. and Chao M.V. 1996. Interactions of the cellular polypeptides with the cytoplasmic domain of the mouse Fas antigen. J. Biol. Chem. 271: 8627–8632.

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Posern G., Zheng J., Knudsen B.S., Kardinal C., Muller K.B., Voss J., Sishido T., Cowburn D., Cheng G., Wang B., et al. 1998. Development of highly selective SH3 binding peptides for Crk and CRKL which disrupt Crk-complexes with DOCK180, SoS, and C3G. Oncogene 16: 1903–1912.

Ron D. and Dressler H. 1992. pGSTag—A versatile bacterial expression plasmid for enzymatic labeling of recombinant proteins. Biotechniques 13: 866–869.

Sambrook J. and Russell D. 2001. Molecular cloning: A laboratory manual, 3rd edition. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

Schober J.M., Lau L.F., Ugarova T.P., and Lam C.-T. 2003. Identification of a novel Integrin αMβ2 binding site in CCN1 (CYR61), a matricellular protein expressed in healing wounds and atherosclerotic lesions. J. Biol. Chem. 278: 25808–25815.

Skolnick E.Y., Margolis B., Mohammadi M., Lowenstein E., Fischer R., Drepps A., Ullrich A., and Schlessinger J. 1991. Cloning of PI3 kinase-associated p85 utilizing a novel method for expression/cloning of target proteins for receptor tyrosine kinases. Cell 65: 83–90.

Smith D.B. and Johnson K.S. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase. Gene 67: 31–40.

Spector D.L., Goldman R.D., and Leinwand L.A. 1998. Cells: A laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.

Sun Y., Liu X., Ng-Easton E., Lodish H.F., and Weinberg R.A. 1999. SnoN and Ski protooncoproteins are rapidly degraded in response to transforming growth factor β signaling. Proc. Natl. Acad. Sci. 96: 12442–12447.

Volkel D., Blankenfeldt W., and Schomburg D. 1998. Large-scale production, purification and refolding of the full-length cellular prion protein from Syrian golden hamster in Escherichia coli using glutathione S-transferase-fusion system. Eur. J. Biochem. 251: 462–471.

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