RAD53/YPL153C Literature Guide Help

Other names published for RAD53: LSD1, MEC2, SPK1, YPL153C

RAD53 - Protein/Nucleic Acid Structure (15)

ReferenceOther Genes Addressed
Jiao Y, et al.  (2012) Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction. Proc Natl Acad Sci U S A 109(8):2866-71
Matthews LA, et al.  (2012) Saccharomyces cerevisiae Dbf4 has unique fold necessary for interaction with Rad53 kinase. J Biol Chem 287(4):2378-87
Matsumura Y, et al.  (2010) alpha-Helical burst on the folding pathway of FHA domains from Rad53 and Ki67. Biochimie 92(8):1031-9
Lee H, et al.  (2008) Diphosphothreonine-specific interaction between an SQ/TQ cluster and an FHA domain in the Rad53-Dun1 kinase cascade. Mol Cell 30(6):767-78
Yongkiettrakul S, et al.  (2004) The ligand specificity of yeast Rad53 FHA domains at the +3 position is determined by nonconserved residues. Biochemistry 43(13):3862-9
Blanchard H, et al.  (2001) Crystallization and preliminary X-ray diffraction studies of FHA domains of Dun1 and Rad53 protein kinases. Acta Crystallogr D Biol Crystallogr 57(Pt 3):459-61
Brooksbank C  (2001) Protein-protein interactions: Phosphothreonine lego. Nat Rev Mol Cell Biol 2(1):5
Byeon IJ, et al.  (2001) Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes. J Mol Biol 314(3):577-88
Yuan C, et al.  (2001) Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. J Mol Biol 314(3):563-75
Durocher D, et al.  (2000) The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol Cell 6(5):1169-82
Frei C and Gasser SM  (2000) The yeast Sgs1p helicase acts upstream of Rad53p in the DNA replication checkpoint and colocalizes with Rad53p in S-phase-specific foci. Genes Dev 14(1):81-96
Liao H, et al.  (2000) Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9. J Mol Biol 304(5):941-51
Wang P, et al.  (2000) II. Structure and specificity of the interaction between the FHA2 domain of Rad53 and phosphotyrosyl peptides. J Mol Biol 302(4):927-40
Zhou MM  (2000) Phosphothreonine recognition comes into focus. Nat Struct Biol 7(12):1085-7
Liao H, et al.  (1999) Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53. J Mol Biol 294(4):1041-9