PubRank

A M Stock

Author PubWeight™ 90.52‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 Protein phosphorylation and regulation of adaptive responses in bacteria. Microbiol Rev 1989 20.50
2 Histidine kinases and response regulator proteins in two-component signaling systems. Trends Biochem Sci 2001 6.27
3 The catalytic pathway of cytochrome p450cam at atomic resolution. Science 2000 5.42
4 Signal transduction in bacteria. Nature 1990 5.33
5 Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Proc Natl Acad Sci U S A 1992 4.88
6 Crystalline ribonuclease A loses function below the dynamical transition at 220 K. Nature 1992 4.80
7 Identification of the site of phosphorylation of the chemotaxis response regulator protein, CheY. J Biol Chem 1989 3.72
8 Bacterial chemotaxis and the molecular logic of intracellular signal transduction networks. Annu Rev Biophys Biophys Chem 1991 3.18
9 Structural relationships in the OmpR family of winged-helix transcription factors. J Mol Biol 1997 2.73
10 The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor. Structure 1997 2.63
11 Roles of the highly conserved aspartate and lysine residues in the response regulator of bacterial chemotaxis. J Biol Chem 1991 2.58
12 A tale of two components: a novel kinase and a regulatory switch. Nat Struct Biol 2000 2.39
13 Structural basis for methylesterase CheB regulation by a phosphorylation-activated domain. Proc Natl Acad Sci U S A 1998 2.10
14 Divalent metal ion binding to the CheY protein and its significance to phosphotransfer in bacterial chemotaxis. Biochemistry 1990 2.07
15 Purification and characterization of the S-adenosylmethionine:glutamyl methyltransferase that modifies membrane chemoreceptor proteins in bacteria. J Biol Chem 1987 1.94
16 Crystal structure of the chemotaxis receptor methyltransferase CheR suggests a conserved structural motif for binding S-adenosylmethionine. Structure 1997 1.66
17 Structural analysis of bacterial chemotaxis proteins: components of a dynamic signaling system. J Struct Biol 1998 1.66
18 Signal transduction in bacterial chemotaxis. J Biol Chem 1992 1.55
19 Purification and characterization of the CheZ protein of bacterial chemotaxis. J Bacteriol 1987 1.32
20 Chemotaxis receptor recognition by protein methyltransferase CheR. Nat Struct Biol 1998 1.30
21 Phosphorylation causes subtle changes in solvent accessibility at the interdomain interface of methylesterase CheB. J Mol Biol 2001 1.22
22 Activation of methylesterase CheB: evidence of a dual role for the regulatory domain. Biochemistry 1998 1.18
23 Signal transduction in bacteria: molecular mechanisms of stimulus-response coupling. Curr Opin Microbiol 1998 1.17
24 Orientation of OmpR monomers within an OmpR:DNA complex determined by DNA affinity cleaving. J Mol Biol 1999 1.17
25 Crystal structure of the catalytic domain of the chemotaxis receptor methylesterase, CheB. J Mol Biol 1995 1.16
26 Synthesis of [(32)P]phosphoramidate for use as a low molecular weight phosphodonor reagent. Anal Biochem 2000 0.93
27 Response-regulator phosphorylation and activation: a two-way street? Trends Microbiol 2000 0.90
28 Stabilization of the phospho-aspartyl residue in a two-component signal transduction system in Thermotoga maritima. Biochemistry 1998 0.87
29 The role of water in the catalytic efficiency of triosephosphate isomerase. Biochemistry 1999 0.85
30 A nonlinear stimulus-response relation in bacterial chemotaxis. Proc Natl Acad Sci U S A 1999 0.83
31 Characterization of the genes and proteins of a two-component system from the hyperthermophilic bacterium Thermotoga maritima. J Bacteriol 1996 0.83
32 Synthesis and biochemical characterization of a phosphorylated analogue of the response regulator CheB. Biochemistry 2001 0.80
33 Crystallization, X-ray studies, and site-directed cysteine mutagenesis of the DNA-binding domain of OmpR. Protein Sci 1996 0.79
34 High energy exchange: proteins that make or break phosphoramidate bonds. Structure 1999 0.76
35 Purification, crystallization, and preliminary X-ray diffraction analyses of the bacterial chemotaxis receptor modifying enzymes. Proteins 1995 0.75