Common features in the unfolding and misfolding of PDZ domains and beyond: the modulatory effect of domain swapping and extra-elements.

Addressing the role of the α-helical extension in the folding of the third PDZ domain from PSD-95. Sci Rep (2017) 0.75

Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem (1989) 29.15

Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell (1996) 6.87

Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains. Cell (1996) 6.42

Experiment and theory highlight role of native state topology in SH3 folding. Nat Struct Biol (1999) 3.50

PDZ domain proteins: plug and play! Sci STKE (2003) 3.38

Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-syntrophin complex. Science (1999) 3.15

Important role of hydrogen bonds in the structurally polarized transition state for folding of the src SH3 domain. Nat Struct Biol (1998) 3.02

The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved. Nat Struct Biol (1999) 2.93

Obligatory steps in protein folding and the conformational diversity of the transition state. Nat Struct Biol (1998) 2.81

Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. J Mol Biol (2005) 2.10

Hidden dynamic allostery in a PDZ domain. Proc Natl Acad Sci U S A (2009) 1.93

PDZ domain of neuronal nitric oxide synthase recognizes novel C-terminal peptide sequences. Nat Biotechnol (1997) 1.68

Formation of nNOS/PSD-95 PDZ dimer requires a preformed beta-finger structure from the nNOS PDZ domain. J Mol Biol (2000) 1.43

Structures and target recognition modes of PDZ domains: recurring themes and emerging pictures. Biochem J (2013) 1.23

Plasticity of PDZ domains in ligand recognition and signaling. FEBS Lett (2012) 1.18

Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins. Proc Natl Acad Sci U S A (2008) 1.10

A conserved folding mechanism for PDZ domains. FEBS Lett (2007) 1.03

Kinetic folding mechanism of PDZ2 from PTP-BL. Protein Eng Des Sel (2005) 1.01

Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK). J Biol Chem (2011) 0.98

Structural diversity of PDZ-lipid interactions. Chembiochem (2010) 0.93

Novel conformational aspects of the third PDZ domain of the neuronal post-synaptic density-95 protein revealed from two 1.4A X-ray structures. J Struct Biol (2010) 0.86

An oligomeric equilibrium intermediate as the precursory nucleus of globular and fibrillar supramacromolecular assemblies in a PDZ domain. Biophys J (2010) 0.86

An expanded view of the protein folding landscape of PDZ domains. Biochem Biophys Res Commun (2012) 0.85

A thermodynamic study of the third PDZ domain of MAGUK neuronal protein PSD-95 reveals a complex three-state folding behavior. Biophys Chem (2013) 0.83

The interconversion between a flexible β-sheet and a fibril β-arrangement constitutes the main conformational event during misfolding of PSD95-PDZ3 domain. Biophys J (2012) 0.81

Post-translational modifications modulate ligand recognition by the third PDZ domain of the MAGUK protein PSD-95. PLoS One (2014) 0.81

The impact of extra-domain structures and post-translational modifications in the folding/misfolding behaviour of the third PDZ domain of MAGUK neuronal protein PSD-95. PLoS One (2014) 0.80