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Biochemistry|January 31, 1998
Probing the effects of calcium on gelsolinB J Pope, J T Gooch, A G WeedsNature|August 19, 1993
Structure of gelsolin segment 1-actin complex and the mechanism of filament severingP J McLaughlin, J T Gooch, H G Mannherz, et al.European Journal of Biochemistry|October 6, 1998
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 actophorinS K Maciver, B J Pope, S Whytock, et al.Journal of Molecular Biology|May 2, 2000
Uncoupling actin filament fragmentation by cofilin from increased subunit turnoverB J Pope, S M Gonsior, S Yeoh, et al.European Journal of Biochemistry|November 17, 1986
Binding of pig plasma gelsolin to F-actin and partial fractionation into calcium-dependent and calcium-independent formsB Pope, A G WeedsAnnual Review of Biophysics and Biomolecular Structure|January 1, 1995
Actin-binding protein complexes at atomic resolutionP J McLaughlin, A G WeedsFEBS Letters|May 7, 1984
The rate constant for ATP hydrolysis by polymerized actinT D Pollard, A G WeedsThe Journal of Biological Chemistry|October 26, 2000
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 siteS Ono, A McGough, B J Pope, et al.Pageof 5