Published in Eur J Biochem on October 01, 1999
Keap1 recruits Neh2 through binding to ETGE and DLG motifs: characterization of the two-site molecular recognition model. Mol Cell Biol (2006) 3.27
Expanding the proteome: disordered and alternatively folded proteins. Q Rev Biophys (2011) 1.60
Osmolyte perturbation reveals conformational equilibria in spin-labeled proteins. Protein Sci (2009) 1.60
SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment. J Biomol NMR (2001) 1.34
Sequence and structure relationships within von Willebrand factor. Blood (2012) 1.26
Resolving Conformational and Rotameric Exchange in Spin-Labeled Proteins Using Saturation Recovery EPR. Appl Magn Reson (2010) 1.10
Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces. Protein Sci (2004) 0.92
Mapping protein pockets through their potential small-molecule binding volumes: QSCD applied to biological protein structures. J Comput Aided Mol Des (2004) 0.75
1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR (1995) 15.76
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol (1999) 11.38
Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell (1997) 5.39
The effects of ibuprofen on the physiology and survival of patients with sepsis. The Ibuprofen in Sepsis Study Group. N Engl J Med (1997) 4.98
Zinc finger proteins: new insights into structural and functional diversity. Curr Opin Struct Biol (2001) 4.92
Three-dimensional solution structure of a single zinc finger DNA-binding domain. Science (1989) 4.57
Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc Natl Acad Sci U S A (1997) 4.10
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science (1993) 4.07
Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity. Proc Natl Acad Sci U S A (1996) 3.69
Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature (1995) 3.58
Structural characterization of a partly folded apomyoglobin intermediate. Science (1990) 3.53
Sequence-dependent correction of random coil NMR chemical shifts. J Am Chem Soc (2001) 3.42
Backbone dynamics in dihydrofolate reductase complexes: role of loop flexibility in the catalytic mechanism. Biochemistry (2001) 2.77
'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J Biomol NMR (1995) 2.54
Copper binding to the prion protein: structural implications of four identical cooperative binding sites. Proc Natl Acad Sci U S A (1999) 2.44
Recommendations for the presentation of NMR structures of proteins and nucleic acids. J Mol Biol (1998) 2.42
Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nat Struct Biol (1998) 2.36
Folding of immunogenic peptide fragments of proteins in water solution. II. The nascent helix. J Mol Biol (1988) 2.33
Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. J Mol Biol (1988) 2.30
Conformation of peptide fragments of proteins in aqueous solution: implications for initiation of protein folding. Biochemistry (1988) 2.21
Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J Biomol NMR (2000) 2.10
NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry (2001) 2.07
Dynamics of a flexible loop in dihydrofolate reductase from Escherichia coli and its implication for catalysis. Biochemistry (1994) 2.04
Is apomyoglobin a molten globule? Structural characterization by NMR. J Mol Biol (1996) 2.02
Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science (1995) 2.01
A trial of antioxidants N-acetylcysteine and procysteine in ARDS. The Antioxidant in ARDS Study Group. Chest (1997) 2.00
Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor. J Mol Biol (2000) 1.95
Solution structure of the first three zinc fingers of TFIIIA bound to the cognate DNA sequence: determinants of affinity and sequence specificity. J Mol Biol (1997) 1.89
Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. Biochemistry (1995) 1.86
Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J Mol Biol (2000) 1.83
Defining solution conformations of small linear peptides. Annu Rev Biophys Biophys Chem (1991) 1.80
High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. Structure (1994) 1.79
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin. J Mol Biol (1992) 1.79
Molecular basis for specific recognition of both RNA and DNA by a zinc finger protein. Science (1993) 1.75
Pulse methods for the simplification of protein NMR spectra. FEBS Lett (1975) 1.72
Absence of a stable intermediate on the folding pathway of protein A. Protein Sci (1997) 1.71
Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP. J Mol Biol (2000) 1.57
Structure of the retinoid X receptor alpha DNA binding domain: a helix required for homodimeric DNA binding. Science (1993) 1.56
Analysis of an activator:coactivator complex reveals an essential role for secondary structure in transcriptional activation. Mol Cell (1998) 1.56
Electrostatic calculations of side-chain pK(a) values in myoglobin and comparison with NMR data for histidines. Biochemistry (1993) 1.53
Equilibrium NMR studies of unfolded and partially folded proteins. Nat Struct Biol (1998) 1.51
Nuclear magnetic resonance methods for elucidation of structure and dynamics in disordered states. Methods Enzymol (2001) 1.50
Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. Biochemistry (1993) 1.49
DNA-induced alpha-helix capping in conserved linker sequences is a determinant of binding affinity in Cys(2)-His(2) zinc fingers. J Mol Biol (2000) 1.48
Role of secondary structure in discrimination between constitutive and inducible activators. Mol Cell Biol (1999) 1.47
Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. Biochemistry (1990) 1.46
Two different neurodegenerative diseases caused by proteins with similar structures. Proc Natl Acad Sci U S A (2001) 1.44
Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry (2000) 1.44
The radius of gyration of an apomyoglobin folding intermediate. Science (1995) 1.42
Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ. J Mol Biol (2000) 1.40
Functional role of a mobile loop of Escherichia coli dihydrofolate reductase in transition-state stabilization. Biochemistry (1992) 1.39
Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins. FEBS Lett (1997) 1.37
Local structural plasticity of the prion protein. Analysis of NMR relaxation dynamics. Biochemistry (2001) 1.37
Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. Eur J Biochem (1998) 1.37
SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment. J Biomol NMR (2001) 1.34
Structural analyses of CREB-CBP transcriptional activator-coactivator complexes by NMR spectroscopy: implications for mapping the boundaries of structural domains. J Mol Biol (1999) 1.34
The immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn. Nature (1986) 1.33
The solution structure of the Oct-1 POU-specific domain reveals a striking similarity to the bacteriophage lambda repressor DNA-binding domain. Cell (1993) 1.33
Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA. J Biomol NMR (1998) 1.32
1H and 15N resonance assignments and secondary structure of the carbon monoxide complex of sperm whale myoglobin. J Biomol NMR (1994) 1.30
Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB. FEBS Lett (1998) 1.29
Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. II. Plastocyanin. J Mol Biol (1992) 1.29
Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints. J Mol Biol (1994) 1.29
Specific interaction of the first three zinc fingers of TFIIIA with the internal control region of the Xenopus 5 S RNA gene. J Mol Biol (1992) 1.27
Recombinant soluble human tissue factor secreted by Saccharomyces cerevisiae and refolded from Escherichia coli inclusion bodies: glycosylation of mutants, activity and physical characterization. Biochem J (1995) 1.27
NMR solution structure of the inserted domain of human leukocyte function associated antigen-1. J Mol Biol (2000) 1.27
Mapping of the binding interfaces of the proteins of the bacterial phosphotransferase system, HPr and IIAglc. Biochemistry (1993) 1.26
Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements. Biochemistry (1992) 1.26
Proton sharing between cysteine thiols in Escherichia coli thioredoxin: implications for the mechanism of protein disulfide reduction. Biochemistry (1995) 1.25
Domain packing and dynamics in the DNA complex of the N-terminal zinc fingers of TFIIIA. Nat Struct Biol (1997) 1.25
DNA-induced conformational changes are the basis for cooperative dimerization by the DNA binding domain of the retinoid X receptor. J Mol Biol (1998) 1.22