Published in J Mol Biol on March 21, 2012
Within-population variability in a moth sex pheromone blend: genetic basis and behavioural consequences. Proc Biol Sci (2014) 0.93
Structural characterization of Staphylococcus aureus biotin protein ligase and interaction partners: an antibiotic target. Protein Sci (2013) 0.91
Protein:protein interactions in control of a transcriptional switch. J Mol Biol (2013) 0.76
A large solvent isotope effect on protein association thermodynamics. Biochemistry (2013) 0.76
Role of β-lactamase residues in a common interface for binding the structurally unrelated inhibitory proteins BLIP and BLIP-II. Protein Sci (2014) 0.75
Clustal W and Clustal X version 2.0. Bioinformatics (2007) 126.47
Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem (1989) 29.15
Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys J (1981) 5.57
Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea. Genome Res (2002) 3.26
Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc Natl Acad Sci U S A (1992) 2.89
Genetic and biochemical characterization of the birA gene and its product: evidence for a direct role of biotin holoenzyme synthetase in repression of the biotin operon in Escherichia coli. J Mol Biol (1981) 2.14
The birA gene of Escherichia coli encodes a biotin holoenzyme synthetase. J Mol Biol (1981) 2.02
THE ENZYMATIC SYNTHESIS OF HOLOTRANSCARBOXYLASE FROM APOTRANSCARBOXYLASE AND (+)-BIOTIN. II. INVESTIGATION OF THE REACTION MECHANISM. J Biol Chem (1964) 1.89
Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis. J Bacteriol (1993) 1.80
The diversity of ubiquitin recognition: hot spots and varied specificity. Mol Cell (2010) 1.63
Cooperative binding of the Escherichia coli repressor of biotin biosynthesis to the biotin operator sequence. Biochemistry (1993) 1.57
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure (1995) 1.49
Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J Biol Chem (1996) 1.45
Function of a conserved sequence motif in biotin holoenzyme synthetases. Protein Sci (2000) 1.44
Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J Mol Biol (2006) 1.41
Sedimentation equilibrium as thermodynamic tool. Methods Enzymol (1995) 1.38
Biotinyl 5'-adenylate: corepressor role in the regulation of the biotin genes of Escherichia coli K-12. Proc Natl Acad Sci U S A (1979) 1.33
Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination. J Biol Chem (1988) 1.29
Kinetics of biotinyl-5'-adenylate synthesis catalyzed by the Escherichia coli repressor of biotin biosynthesis and the stability of the enzyme-product complex. Biochemistry (1994) 1.26
Multiple disordered loops function in corepressor-induced dimerization of the biotin repressor. J Mol Biol (2000) 1.23
Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate. J Biol Chem (2008) 1.17
Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase. J Biol Chem (1999) 1.15
Dimerization of the Escherichia coli biotin repressor: corepressor function in protein assembly. Biochemistry (1999) 1.15
Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding. J Mol Biol (2003) 1.14
Built-in loops allow versatility in domain-domain interactions: lessons from self-interacting domains. Proc Natl Acad Sci U S A (2008) 1.09
Sedimentation equilibrium techniques: multiple speed analyses and an overspeed procedure. Biophys Chem (1976) 1.05
Nucleation of an allosteric response via ligand-induced loop folding. J Mol Biol (2007) 1.03
Structural and functional studies of the biotin protein ligase from Aquifex aeolicus reveal a critical role for a conserved residue in target specificity. J Mol Biol (2009) 1.01
Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase. J Mol Biol (2005) 0.97
Manipulating monomer-dimer equilibrium of bovine Beta -lactoglobulin by amino acid substitution. J Biol Chem (2002) 0.96
Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration. PLoS One (2010) 0.93
Thermodynamic and structural investigation of bispecificity in protein-protein interactions. J Mol Biol (2009) 0.92
In vivo tests of thermodynamic models of transcription repressor function. Biophys Chem (2011) 0.91
Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition. J Biol Chem (2009) 0.90
Multispecific recognition: mechanism, evolution, and design. Biochemistry (2011) 0.89
Biotinylation, a post-translational modification controlled by the rate of protein-protein association. J Biol Chem (2011) 0.82
Metal-binding loop length and not sequence dictates structure. Proc Natl Acad Sci U S A (2009) 0.78
Entropic switch regulates myristate exposure in the HIV-1 matrix protein. Proc Natl Acad Sci U S A (2003) 3.20
Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution. J Mol Biol (2006) 1.41
The biotin repressor: modulation of allostery by corepressor analogs. J Mol Biol (2004) 1.39
Use of binding enthalpy to drive an allosteric transition. Biochemistry (2005) 1.16
Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding. J Mol Biol (2003) 1.14
The biotin regulatory system: kinetic control of a transcriptional switch. Biochemistry (2006) 1.09
The biotin repressor: thermodynamic coupling of corepressor binding, protein assembly, and sequence-specific DNA binding. Biochemistry (2002) 1.09
Nucleation of an allosteric response via ligand-induced loop folding. J Mol Biol (2007) 1.03
Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics. J Mol Biol (2008) 1.02
Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch. J Mol Biol (2008) 1.02
Thermodynamic and structural investigation of bispecificity in protein-protein interactions. J Mol Biol (2009) 0.92
In vivo tests of thermodynamic models of transcription repressor function. Biophys Chem (2011) 0.91
Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition. J Biol Chem (2009) 0.90
Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase. Protein Sci (2002) 0.89
Nonenzymatic biotinylation of a biotin carboxyl carrier protein: unusual reactivity of the physiological target lysine. Protein Sci (2006) 0.88
Biochemical properties and biological function of a monofunctional microbial biotin protein ligase. Biochemistry (2010) 0.83
Protein-protein interactions dominate the assembly thermodynamics of a transcription repression complex. Biochemistry (2007) 0.83
Biotinylation, a post-translational modification controlled by the rate of protein-protein association. J Biol Chem (2011) 0.82
Metal-linked dimerization in the iron-dependent regulator from Mycobacterium tuberculosis. Biochemistry (2006) 0.80
Protein:protein interactions in control of a transcriptional switch. J Mol Biol (2013) 0.76
A large solvent isotope effect on protein association thermodynamics. Biochemistry (2013) 0.76
Selectivity in post-translational biotin addition to five human carboxylases. J Biol Chem (2011) 0.76
Sequence-function relationships in folding upon binding. Protein Sci (2014) 0.76