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Structure (London, England : 1993)|January 27, 2015
Structural plasticity of helical nanotubes based on coiled-coil assembliesE H Egelman, C Xu, F DiMaio, et al.Nature Structural Biology|February 1, 1997
The RecA hexamer is a structural homologue of ring helicasesX Yu, E H EgelmanJournal of Molecular Biology|September 5, 1992
Structural data suggest that the active and inactive forms of the RecA filament are not simply interconvertibleX Yu, E H EgelmanJournal of Structural Biology|June 1, 1991
Removal of the RecA C-terminus results in a conformational change in the RecA-DNA filamentX Yu, E H EgelmanScience (New York, N.Y.)|July 28, 1989
The location of DNA in RecA-DNA helical filamentsE H Egelman, X YuJournal of Molecular Biology|July 5, 1993
DNA conformation induced by the bacteriophage T4 UvsX protein appears identical to the conformation induced by the Escherichia coli RecA proteinX Yu, E H EgelmanBiophysical Journal|March 1, 1990
Image analysis reveals that Escherichia coli RecA protein consists of two domainsX Yu, E H EgelmanJournal of Molecular Biology|May 5, 1993
The LexA repressor binds within the deep helical groove of the activated RecA filamentX Yu, E H EgelmanJournal of Molecular Biology|May 5, 1992
Direct visualization of dynamics and co-operative conformational changes within RecA filaments that appear to be associated with the hydrolysis of adenosine 5'-O-(3-thiotriphosphate)X Yu, E H EgelmanBiophysical Journal|February 1, 1994
Three-dimensional reconstruction of a co-complex of F-actin with antibody Fab fragments to actin's NH2 terminusA Orlova, X Yu, E H EgelmanPageof 797