Zobrazeno 1 - 10
of 38
pro vyhledávání: '"R J, Fletterick"'
Publikováno v:
Journal of molecular biology. 299(4)
Ecotin is a dimeric serine protease inhibitor from Escherichia coli which binds proteases to form a hetero-tetramer with three distinct interfaces: an ecotin-ecotin dimer interface, a larger primary ecotin-protease interface, and a smaller secondary
Autor:
Z F, Kanyo, K M, Pan, R A, Williamson, D R, Burton, S B, Prusiner, R J, Fletterick, F E, Cohen
Publikováno v:
Journal of molecular biology. 293(4)
The X-ray crystallographic structures of the anti-Syrian hamster prion protein (SHaPrP) monoclonal Fab 3F4 alone, as well as the complex with its cognate peptide epitope (SHaPrP 104-113), have been determined to atomic resolution. The conformation of
Publikováno v:
Journal of cellular biochemistry. 74(3)
A three-dimensional model for residues 142-427 of the ligand binding domain (LBD) of the human nuclear receptor for 1alpha, 25-dihydroxy-vitamin D(3) [VDR] has been generated based on the X-ray crystallographic atomic coordinates of the LBD of the ra
Publikováno v:
Journal of muscle research and cell motility. 19(8)
Recent studies have shown surprising structural and functional similarities between the motor domains of kinesin and myosin. Common features have also been described for motor proteins and G proteins. Despite these similarities, the evolutionary rela
Autor:
R C, Ribeiro, J W, Apriletti, R L, Wagner, B L, West, W, Feng, R, Huber, P J, Kushner, S, Nilsson, T, Scanlan, R J, Fletterick, F, Schaufele, J D, Baxter
Publikováno v:
Recent progress in hormone research. 53
This review summarizes the studies conducted in our laboratory on the mechanisms of thyroid hormone action over the past two decades. We have attempted to place our studies on thyroid hormone receptors (TRs) in perspective with the work conducted by
Publikováno v:
Biochemistry. 37(15)
Phosphotriesterase homology protein (PHP) is a member of a recently discovered family of proteins related to phosphotriesterase, a hydrolytic, bacterial enzyme with an unusual substrate specificity for synthetic organophosphate triesters and phosphor
Publikováno v:
The Journal of biological chemistry. 268(9)
The major cysteine protease of Trypanosoma cruzi, cruzain, has been previously expressed in Escherichia coli as a fusion polypeptide. The proteolytic processing events required to obtain active, mature cruzain from the recombinant expression system h
Publikováno v:
The Journal of biological chemistry. 266(24)
Liver and muscle glycogen phosphorylases, which are products of distinct genes, are both activated by covalent phosphorylation, but in the unphosphorylated (b) state, only the muscle isozyme is efficiently activated by the allosteric activator AMP. T
Publikováno v:
Journal of molecular biology. 219(3)
The X-ray crystal structure of trypsin-S195C, a rat anionic trypsin mutant in which the active site serine has been replaced by cysteine, was determined at -150 degrees C and room temperature to 1.6 A resolution, R = 15.4% and 1.8 A resolution, R = 1
Publikováno v:
Journal of molecular biology. 219(3)
The crystal structure of trypsin-G226A has been determined, in the presence of benzamidine, to a resolution of 1.75 A with an R-factor of 14.6%. The mutation was designed to alter substrate specificity by disrupting arginine binding, but was previous