Challenges and approaches for assay development of membrane and membrane-associated proteins in drug discovery.
作者： Scott Gridley , Anthony L. Shrout , Edward A. Esposito
DOI: 10.1016/S1877-1173(10)91007-7
关键词:
摘要: In addition to its role as a barrier between the cytoplasm and extracellular milieu, cell membrane is scaffold for diverse collection of receptors enzymes. The organization afforded by this serves ensure an efficient interaction components membrane. desire maintain in solution challenge appropriate interrogation these biochemical components. This chapter will discuss strategies that allow analysis membrane-associated enzymes within standard reactions. advantages screening identifying valuable compounds from compound libraries understanding intricacies complex multiprotein complexes (i.e., chemotaxis) be discussed.
elsevier.com
sci-hub.se 参考文章(154)
Tony Pawson, Sh2 And Sh3 Domains In Signal Transduction Advances in Cancer Research. ,vol. 64, pp. 87- 110 ,(1994) , 10.1016/S0065-230X(08)60835-0
K L Carraway, J G Koland, R A Cerione, Visualization of epidermal growth factor (EGF) receptor aggregation in plasma membranes by fluorescence resonance energy transfer. Correlation of receptor activation with aggregation. Journal of Biological Chemistry. ,vol. 264, pp. 8699- 8707 ,(1989) , 10.1016/S0021-9258(18)81849-X
Joanne Crowe, Heinz Döbeli, Reiner Gentz, Erich Hochuli, Dietrich Stüber, Karsten Henco, 6xHis-Ni-NTA chromatography as a superior technique in recombinant protein expression/purification. Methods of Molecular Biology. ,vol. 31, pp. 371- 387 ,(1994) , 10.1385/0-89603-258-2:371
J.I. Yeh, H.P. Biemann, J. Pandit, D.E. Koshland, S.H. Kim, The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. Journal of Biological Chemistry. ,vol. 268, pp. 9787- 9792 ,(1993) , 10.1016/S0021-9258(18)98416-4
S Krishnaswamy, K.A. Field, T.S. Edgington, J.H. Morrissey, K.G. Mann, Role of the membrane surface in the activation of human coagulation factor X. Journal of Biological Chemistry. ,vol. 267, pp. 26110- 26120 ,(1992) , 10.1016/S0021-9258(18)35724-7
David J. Montefusco, Abdalin E. Asinas, Robert M. Weis, Liposome-mediated assembly of receptor signaling complexes. Methods in Enzymology. ,vol. 423, pp. 267- 298 ,(2007) , 10.1016/S0076-6879(07)23012-5
Dennis Bray, Matthew D. Levin, Carl J. Morton-Firth, Receptor clustering as a cellular mechanism to control sensitivity Nature. ,vol. 393, pp. 85- 88 ,(1998) , 10.1038/30018
E.G. Ninfa, A. Stock, S. Mowbray, J. Stock, Reconstitution of the bacterial chemotaxis signal transduction system from purified components. Journal of Biological Chemistry. ,vol. 266, pp. 9764- 9770 ,(1991) , 10.1016/S0021-9258(18)92886-3
John De Sena, Benjamin Mandel, Studies on the in vitro uncoating of poliovirus: I. Characterization of the modifying factor and the modifying reaction Virology. ,vol. 70, pp. 470- 483 ,(1976) , 10.1016/0042-6822(76)90288-9
P.F. Neuenschwander, J.H. Morrissey, Roles of the membrane-interactive regions of factor VIIa and tissue factor: The factor VIIa Gla domain is dispensable for binding to tissue factor but important for activation of factor X Journal of Biological Chemistry. ,vol. 269, pp. 8007- 8013 ,(1994) , 10.1016/S0021-9258(17)37152-1