Zarin T, et al. (2021) Identifying molecular features that are associated with biological function of intrinsically disordered protein regions. Elife 10 PMID:33616531
Liu B, et al. (2014) The effect of intrachain electrostatic repulsion on conformational disorder and dynamics of the Sic1 protein. J Phys Chem B 118(15):4088-97 PMID:24673507
Stollar EJ, et al. (2012) Differential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysis. PLoS One 7(12):e51282 PMID:23251481
Tang X, et al. (2012) Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCFCdc4 ubiquitin ligase. Proc Natl Acad Sci U S A 109(9):3287-92 PMID:22328159
Mittag T, et al. (2010) Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 18(4):494-506 PMID:20399186
Stollar EJ, et al. (2009) Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p. J Biol Chem 284(39):26918-27 PMID:19590096
Mittag T, et al. (2008) Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proc Natl Acad Sci U S A 105(46):17772-7 PMID:19008353
Borg M, et al. (2007) Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proc Natl Acad Sci U S A 104(23):9650-5 PMID:17522259