Published in Proteins on December 09, 2016
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers (1983) 99.69
Structure validation by Calpha geometry: phi,psi and Cbeta deviation. Proteins (2003) 32.38
Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol (1978) 29.77
The penultimate rotamer library. Proteins (2000) 17.01
Areas, volumes, packing and protein structure. Annu Rev Biophys Bioeng (1977) 16.38
Stereochemistry of polypeptide chain configurations. J Mol Biol (1963) 14.20
Amino acid preferences for specific locations at the ends of alpha helices. Science (1988) 8.29
The importance of intrinsic disorder for protein phosphorylation. Nucleic Acids Res (2004) 8.23
Intrinsic disorder in cell-signaling and cancer-associated proteins. J Mol Biol (2002) 5.64
Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease. Nat Med (1998) 5.49
Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci U S A (1986) 5.42
Predicting the secondary structure of globular proteins using neural network models. J Mol Biol (1988) 5.13
Influence of proline residues on protein conformation. J Mol Biol (1991) 4.87
Random-coil behavior and the dimensions of chemically unfolded proteins. Proc Natl Acad Sci U S A (2004) 4.44
Helix capping. Protein Sci (1998) 4.18
Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry (1999) 4.12
Conformational preferences of amino acids in globular proteins. Biochemistry (1978) 4.00
AAindex: amino acid index database. Nucleic Acids Res (2000) 3.83
Thermodynamics of structural stability and cooperative folding behavior in proteins. Adv Protein Chem (1992) 3.24
Intrinsic disorder in transcription factors. Biochemistry (2006) 3.06
Reassessing random-coil statistics in unfolded proteins. Proc Natl Acad Sci U S A (2004) 2.93
A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation. Biochemistry (1997) 2.79
The characterization of amino acid sequences in proteins by statistical methods. J Theor Biol (1968) 2.75
Intrinsically disordered proteins in cellular signalling and regulation. Nat Rev Mol Cell Biol (2015) 2.69
Folding of polypeptide chains in proteins: a proposed mechanism for folding. Proc Natl Acad Sci U S A (1971) 2.68
THE SOLUBILITY OF AMINO ACIDS AND RELATED COMPOUNDS IN AQUEOUS UREA SOLUTIONS. J Biol Chem (1963) 2.64
Intrinsically disordered proteins: regulation and disease. Curr Opin Struct Biol (2011) 2.59
Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J Mol Biol (1996) 2.50
The crystal structure of staphylococcal nuclease refined at 1.7 A resolution. Proteins (1991) 2.50
Classification of intrinsically disordered regions and proteins. Chem Rev (2014) 2.48
From the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins. Proc Natl Acad Sci U S A (2010) 2.37
The heat capacity of proteins. Proteins (1995) 2.37
Structure-based calculation of the equilibrium folding pathway of proteins. Correlation with hydrogen exchange protection factors. J Mol Biol (1996) 2.29
The magnitude of the backbone conformational entropy change in protein folding. Proteins (1996) 2.18
Net charge per residue modulates conformational ensembles of intrinsically disordered proteins. Proc Natl Acad Sci U S A (2010) 2.16
Status of empirical methods for the prediction of protein backbone topography. Biochemistry (1976) 2.12
Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci (2012) 2.10
Biophysical characterization of intrinsically disordered proteins. Curr Opin Struct Biol (2009) 1.98
Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins (1994) 1.97
Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein. J Biol Chem (2008) 1.94
Conformational properties of amino acid residues in globular proteins. J Mol Biol (1976) 1.93
The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics. Proc Natl Acad Sci U S A (2015) 1.85
The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions. J Biol Chem (1970) 1.77
pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state. Biochemistry (2000) 1.73
Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues. Proc Natl Acad Sci U S A (2013) 1.71
A zinc-dependent adhesion module is responsible for intercellular adhesion in staphylococcal biofilms. Proc Natl Acad Sci U S A (2008) 1.70
Sequence determinants of compaction in intrinsically disordered proteins. Biophys J (2010) 1.66
Polyproline II propensities from GGXGG peptides reveal an anticorrelation with beta-sheet scales. Proc Natl Acad Sci U S A (2005) 1.64
Surface tension of amino acid solutions: a hydrophobicity scale of the amino acid residues. Arch Biochem Biophys (1974) 1.63
Dimensions of protein random coils. Biochemistry (1968) 1.50
Tuna cytochrome c at 2.0 A resolution. III. Coordinate optimization and comparison of structures. J Biol Chem (1977) 1.44
Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature (1990) 1.42
Prediction of protein function from sequence properties. Discriminant analysis of a data base. Biochim Biophys Acta (1984) 1.40
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation. J Mol Biol (1995) 1.38
Logical analysis of the mechanism of protein folding. I. Predictions of helices, loops and beta-structures from primary structure. J Mol Biol (1973) 1.37
Protein secondary structure. Studies on the limits of prediction accuracy. Int J Pept Protein Res (1982) 1.35
Energetics of hydrogen bonding in proteins: a model compound study. Protein Sci (1996) 1.31
Assemblages: functional units formed by cellular phase separation. J Cell Biol (2014) 1.30
Molecular basis of co-operativity in protein folding. III. Structural identification of cooperative folding units and folding intermediates. J Mol Biol (1992) 1.29
The intrinsic conformational propensities of the 20 naturally occurring amino acids and reflection of these propensities in proteins. Proc Natl Acad Sci U S A (2008) 1.26
Local hydrophobicity stabilizes secondary structures in proteins. Biopolymers (1980) 1.25
Backbone-driven collapse in unfolded protein chains. J Mol Biol (2011) 1.21
Structure based prediction of protein folding intermediates. J Mol Biol (1994) 1.20
Structure-based thermodynamic scale of alpha-helix propensities in amino acids. Biochemistry (1996) 1.20
Binding of natively unfolded HIF-1alpha ODD domain to p53. Mol Cell (2005) 1.18
Structure of bovine carbonic anhydrase II at 1.95 A resolution. Acta Crystallogr D Biol Crystallogr (2004) 1.18
Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1. J Biol Chem (1992) 1.18
Identification of a minimal myosin Va binding site within an intrinsically unstructured domain of melanophilin. J Biol Chem (2007) 1.15
Beyond the random coil: stochastic conformational switching in intrinsically disordered proteins. Structure (2011) 1.12
Calibration of effective van der Waals atomic contact radii for proteins and peptides. Proteins (1987) 1.09
Natively unfolded C-terminal domain of caldesmon remains substantially unstructured after the effective binding to calmodulin. Proteins (2003) 1.09
Host-guest scale of left-handed polyproline II helix formation. Proteins (2003) 1.08
Relating sequence encoded information to form and function of intrinsically disordered proteins. Curr Opin Struct Biol (2015) 1.06
Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos. Biochemistry (2000) 1.05
Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein. J Proteome Res (2003) 1.02
Intrinsically unstructured domains of Arf and Hdm2 form bimolecular oligomeric structures in vitro and in vivo. J Mol Biol (2008) 1.00
Physical reasons for secondary structure stability: alpha-helices in short peptides. Proteins (1991) 1.00
Statistical mechanical treatment of protein conformation. 5. A multistate model for specific-sequence copolymers of amino acids. Macromolecules (1977) 0.99
Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins. Proc Natl Acad Sci U S A (2007) 0.99
Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2. Proteins (2002) 0.98
Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases. Chem Rev (2014) 0.98
Main-chain conformational tendencies of amino acids. Proteins (2005) 0.98
Phase separation in biology; functional organization of a higher order. Cell Commun Signal (2016) 0.97
Human full-length Securin is a natively unfolded protein. Protein Sci (2005) 0.96
A propensity scale for type II polyproline helices (PPII): aromatic amino acids in proline-rich sequences strongly disfavor PPII due to proline-aromatic interactions. Biochemistry (2012) 0.96
Intrinsically disordered proteins drive membrane curvature. Nat Commun (2015) 0.96
The intrinsically disordered RNR inhibitor Sml1 is a dynamic dimer. Biochemistry (2008) 0.93
Biophysical constraints for protein structure prediction. J Proteome Res (2003) 0.93
Modeling the accessible conformations of the intrinsically unstructured transactivation domain of p53. Proteins (2008) 0.92
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations. J Inorg Biochem (2007) 0.89
Effects of zinc binding on the structure and dynamics of the intrinsically disordered protein prothymosin alpha: evidence for metalation as an entropic switch. Biochemistry (2007) 0.88
The cold denatured state is compact but expands at low temperatures: hydrodynamic properties of the cold denatured state of the C-terminal domain of L9. J Mol Biol (2007) 0.87
An unusual intrinsically disordered protein from the model legume Lotus japonicus stabilizes proteins in vitro. J Biol Chem (2008) 0.85
Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites. Protein Sci (2013) 0.85
Structural characterization of binding of Cu(II) to tau protein. Biochemistry (2008) 0.83
Temperature effects on the hydrodynamic radius of the intrinsically disordered N-terminal region of the p53 protein. Proteins (2013) 0.82
Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain. Protein Sci (2008) 0.80
Thermal unfolding of the N-terminal region of p53 monitored by circular dichroism spectroscopy. Protein Sci (2012) 0.79
Theory of protein molecule self-organization. II. A comparison of calculated thermodynamic parameters of local secondary structures with experiments. Biopolymers (1977) 0.79
The hydrodynamic and conformational properties of denatured proteins in dilute solutions. Protein Sci (2010) 0.78