Published in Protein Sci on July 05, 2006
A promiscuous biotin ligase fusion protein identifies proximal and interacting proteins in mammalian cells. J Cell Biol (2012) 3.32
The Thermoplasma acidophilum LplA-LplB complex defines a new class of bipartite lipoate-protein ligases. J Biol Chem (2009) 1.07
Nonenzymatic biotinylation of histone H2A. Protein Sci (2009) 1.02
Crystallization and preliminary X-ray crystallographic studies of the biotin carboxyl carrier protein and biotin protein ligase complex from Pyrococcus horikoshii OT3. Acta Crystallogr Sect F Struct Biol Cryst Commun (2007) 0.79
Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem (1987) 59.79
MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph (1996) 39.73
THE ENZYMATIC SYNTHESIS OF HOLOTRANSCARBOXYLASE FROM APOTRANSCARBOXYLASE AND (+)-BIOTIN. II. INVESTIGATION OF THE REACTION MECHANISM. J Biol Chem (1964) 1.89
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
Use of streptavidin to detect biotin-containing proteins in plants. Anal Biochem (1985) 1.42
The biotin repressor: modulation of allostery by corepressor analogs. J Mol Biol (2004) 1.39
The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins. Anal Chem (1999) 1.30
Promiscuous protein biotinylation by Escherichia coli biotin protein ligase. Protein Sci (2004) 1.22
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor. Protein Sci (2001) 1.21
Analysis of microbial biotin proteins. Methods Enzymol (1979) 1.19
Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry (1997) 1.17
Purification and properties of clostridiopeptidase B (Clostripain). J Biol Chem (1968) 1.14
Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains. J Biol Chem (2000) 1.09
High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry (2000) 1.01
Rhodopsin's carboxyl-terminal threonines are required for wild-type arrestin-mediated quench of transducin activation in vitro. Biochemistry (1999) 0.94
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
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
Functional versatility of a single protein surface in two protein:protein interactions. J Mol Biol (2012) 0.81
Metal-linked dimerization in the iron-dependent regulator from Mycobacterium tuberculosis. Biochemistry (2006) 0.80
A large solvent isotope effect on protein association thermodynamics. Biochemistry (2013) 0.76
Sequence-function relationships in folding upon binding. Protein Sci (2014) 0.76
Protein:protein interactions in control of a transcriptional switch. J Mol Biol (2013) 0.76
Selectivity in post-translational biotin addition to five human carboxylases. J Biol Chem (2011) 0.76