Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily.
By K. Hopfner, A. Karcher, D. Shin, L. Craig, L. Arthur, J. Carney, John A. Tainer. Cell, 2000
963 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/bb7a8916938f1fa13f8dea648eaa5766b5ecf80e
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In Molecular Biology
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Citations in the corpus
- Molecular basis of cholesterol efflux via ABCG subfamily transporters (2021, background): “After dimerization, the full transporter contains two nucleotidebinding sites (NBSs) that are formed by the Walker A (P loop), Q loop, and Walker B motifs from one protomer coupled with the signature motif from the other (10, 19, 20).”
- ABC multidrug transporters: structure, function and role in chemoresistance. (2008, background): “In the structures of BtuCD [19] and Rad50cd [35] (catalytic domains of a DNA repair enzyme) the two NBDs are in close contact to form a dimeric”
- Cohesin: its roles and mechanisms. (2009, background): “Like Rad50 (61) and an ABC ATPase transporter (156), the Smc1 NBD crystallizes as a dimer in the presence of the slowly hydrolysable ATP analog ATPγS (Figure 1c).”
- Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins. (2006, background): “The reason for this interdependence was initially suggested by the crystal structure of the soluble ABC-like protein Rad50, which dimerizes in the presence of ATP (189, 190).”
- SCOP database in 2002: refinements accommodate structural genomics (2002, methodology): “By the time of the next SCOP release, two new structures were solved: Rad50 ATPase (1f2t) (17) and SMC head domain (1e69) (18).”
- Recombination proteins in yeast. (2004, background): “PfRad50 forms homodimers in the presence of ATP (75, 78).”
- ABC transporters: physiology, structure and mechanism--an overview. (2001, background): “The crystal structures of several isolated ABC domains have now been determined and the structures of HisP, MalK, RbsA and the eukaryotic Rad50 published [2, 10, 21, 22], all of which (not unexpectedly) show very similar folds.”