Pages that link to "Q74325444"

The following pages link to Function of the homologous regions of the Escherichia coli DNA excision repair proteins UvrB and UvrC in stabilization of the UvrBC–DNA complex and in 3′-incision (Q74325444):

Displaying 17 items.

• Ultrafast evolution and loss of CRISPRs following a host shift in a novel wildlife pathogen, Mycoplasma gallisepticum (Q27334811) (← links)
• Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction (Q27620941) (← links)
• Crystal structure of the UvrB dimer: insights into the nature and functioning of the UvrAB damage engagement and UvrB-DNA complexes (Q27670608) (← links)
• The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands (Q28216179) (← links)
• Structural and functional divergence of MutS2 from bacterial MutS1 and eukaryotic MSH4-MSH5 homologs (Q28484788) (← links)
• Structural insights into the first incision reaction during nucleotide excision repair (Q28769998) (← links)
• The nucleotide excision repair protein UvrB, a helicase-like enzyme with a catch. (Q34006354) (← links)
• Cho, a second endonuclease involved in Escherichia coli nucleotide excision repair (Q34009802) (← links)
• Role of ATP hydrolysis by UvrA and UvrB during nucleotide excision repair (Q34290861) (← links)
• Robust incision of Benoz[a]pyrene-7,8-dihyrodiol-9,10-epoxide-DNA adducts by a recombinant thermoresistant interspecies combination UvrABC endonuclease system (Q36826082) (← links)
• NMR analysis of [methyl-13C]methionine UvrB from Bacillus caldotenax reveals UvrB-domain 4 heterodimer formation in solution (Q37060815) (← links)
• Dynamics of lesion processing by bacterial nucleotide excision repair proteins (Q37382348) (← links)
• Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot. (Q37614786) (← links)
• Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition. (Q41002702) (← links)
• Stimulation of UvrD helicase by UvrAB. (Q41960449) (← links)
• ClpC1 N-Terminal Domain Is Dispensable for Adaptor Protein-Dependent Allosteric Regulation (Q59795745) (← links)
• NMR assignments and secondary structure of the UvrC binding domain of UvrB (Q77889151) (← links)