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Determining the differences in actin binding by human ADF and cofilin.
Yeoh S, Pope B, Mannherz HG, Weeds A. Yeoh S, et al. Among authors: pope b. J Mol Biol. 2002 Jan 25;315(4):911-25. doi: 10.1006/jmbi.2001.5280. J Mol Biol. 2002. PMID: 11812157
The C-terminal tail of UNC-60B (actin depolymerizing factor/cofilin) is critical for maintaining its stable association with F-actin and is implicated in the second actin-binding site.
Ono S, McGough A, Pope BJ, Tolbert VT, Bui A, Pohl J, Benian GM, Gernert KM, Weeds AG. Ono S, et al. Among authors: pope bj. J Biol Chem. 2001 Feb 23;276(8):5952-8. doi: 10.1074/jbc.M007563200. Epub 2000 Oct 24. J Biol Chem. 2001. PMID: 11050090
Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid beta-peptide of amyloid plaques.
Perutz MF, Pope BJ, Owen D, Wanker EE, Scherzinger E. Perutz MF, et al. Among authors: pope bj. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5596-600. doi: 10.1073/pnas.042681599. Proc Natl Acad Sci U S A. 2002. PMID: 11960015 Free PMC article.
Uncoupling actin filament fragmentation by cofilin from increased subunit turnover.
Pope BJ, Gonsior SM, Yeoh S, McGough A, Weeds AG. Pope BJ, et al. J Mol Biol. 2000 May 12;298(4):649-61. doi: 10.1006/jmbi.2000.3688. J Mol Biol. 2000. PMID: 10788327
Probing the effects of calcium on gelsolin.
Pope BJ, Gooch JT, Weeds AG. Pope BJ, et al. Biochemistry. 1997 Dec 16;36(50):15848-55. doi: 10.1021/bi972192p. Biochemistry. 1997. PMID: 9398317
The effect of two actin depolymerizing factors (ADF/cofilins) on actin filament turnover: pH sensitivity of F-actin binding by human ADF, but not of Acanthamoeba actophorin.
Maciver SK, Pope BJ, Whytock S, Weeds AG. Maciver SK, et al. Among authors: pope bj. Eur J Biochem. 1998 Sep 1;256(2):388-97. doi: 10.1046/j.1432-1327.1998.2560388.x. Eur J Biochem. 1998. PMID: 9760179
ADF decorates filaments below pH 7.3 and induces substantial depolymerization at higher pH values [Hawkins, M., Pope, B., Maciver, S. K. & Weeds, A. G. (1993) Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments, Biochemistry …
ADF decorates filaments below pH 7.3 and induces substantial depolymerization at higher pH values [Hawkins, M., Pope, B., Maci …
Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments.
Hawkins M, Pope B, Maciver SK, Weeds AG. Hawkins M, et al. Among authors: pope b. Biochemistry. 1993 Sep 28;32(38):9985-93. doi: 10.1021/bi00089a014. Biochemistry. 1993. PMID: 8399167
Characterisation of the F-actin binding domains of villin: classification of F-actin binding proteins into two groups according to their binding sites on actin.
Pope B, Way M, Matsudaira PT, Weeds A. Pope B, et al. FEBS Lett. 1994 Jan 24;338(1):58-62. doi: 10.1016/0014-5793(94)80116-9. FEBS Lett. 1994. PMID: 8307157
Identification of the trapped calcium in the gelsolin segment 1-actin complex: implications for the role of calcium in the control of gelsolin activity.
Weeds AG, Gooch J, McLaughlin P, Pope B, Bengtsdotter M, Karlsson R. Weeds AG, et al. Among authors: pope b. FEBS Lett. 1995 Mar 6;360(3):227-30. doi: 10.1016/0014-5793(95)00109-m. FEBS Lett. 1995. PMID: 7883037
Localization of the calcium-sensitive actin monomer binding site in gelsolin to segment 4 and identification of calcium binding sites.
Pope B, Maciver S, Weeds A. Pope B, et al. Biochemistry. 1995 Feb 7;34(5):1583-8. doi: 10.1021/bi00005a014. Biochemistry. 1995. PMID: 7849017
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