Protein-protein interaction. Complex flexibility.

Structure and interactions of the carboxyl terminus of striated muscle alpha-tropomyosin: it is important to be flexible. Biophys J (2002) 1.22

The X-ray structure of a growth hormone-prolactin receptor complex. Nature (1994) 2.39

Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Science (1985) 4.53

New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. Science (1993) 3.24

An alpha to beta conformational switch in EF-Tu. Structure (1996) 1.83

Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP. J Biol Chem (1984) 1.62

Functional implications of structure-based sequence alignment of proteins in the extracellular pectate lyase superfamily. Plant Physiol (1995) 1.51

Unusual structural features in the parallel beta-helix in pectate lyases. Structure (1993) 1.48

Kinetic studies of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate-aminoacyl-tRNA complexes. Biochemistry (1985) 1.41

Structure of a plant cell wall fragment complexed to pectate lyase C. Plant Cell (1999) 1.34

Protein motifs. 3. The parallel beta helix and other coiled folds. FASEB J (1995) 1.28

Structure and function of pectic enzymes: virulence factors of plant pathogens. Proc Natl Acad Sci U S A (2000) 1.25

The three-dimensional structure of c-H-ras p21: implications for oncogene and G protein studies. Trends Biochem Sci (1988) 1.15

The tree-dimensional structure of aspergillus niger pectin lyase B at 1.7-A resolution. Plant Physiol (1998) 1.08

Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu. Biochemistry (2000) 1.07

Biochemical and structural studies of the tetragonal crystalline modification of the Escherichia coli elongation factor Tu. J Biol Chem (1980) 1.05

A complex profile of protein elongation: translating chemical energy into molecular movement. Structure (1996) 1.04

Sequence profile of the parallel beta helix in the pectate lyase superfamily. J Struct Biol (1998) 1.02

Differential effect of site-directed mutations in pelC on pectate lyase activity, plant tissue maceration, and elicitor activity. J Biol Chem (1996) 1.00

Molecular approaches towards an anti-ras drug. Anticancer Drug Des (1987) 0.94

Structure-based multiple alignment of extracellular pectate lyase sequences. Mol Plant Microbe Interact (1995) 0.91

GE2270A-resistant mutations in elongation factor Tu allow productive aminoacyl-tRNA binding to EF-Tu.GTP.GE2270A complexes. J Mol Biol (2000) 0.91

Extension of the diffraction resolution of crystals. Acta Crystallogr D Biol Crystallogr (1994) 0.88

Preliminary X-ray study of leucine aminopeptidase (bpvine lens), and oligomeric metalloenzyme. J Mol Biol (1977) 0.85

Preliminary crystallographic analysis of a plant pathogenic factor: pectate lyase. J Mol Biol (1989) 0.84

Stabilization of the Escherichia coli elongation factor Tu-GTP-aminoacyl-tRNA complex. Arch Biochem Biophys (1991) 0.84

Circular dichroism of the parallel beta helical proteins pectate lyase C and E. Proteins (1995) 0.83

Elongation factor Tu ternary complex binds to small ribosomal subunits in a functionally active state. Biochemistry (1984) 0.83

Preliminary crystallographic analysis of the plant pathogenic factor, pectate lyase C from Erwinia chrysanthemi. J Biol Chem (1990) 0.82

Induction of elongation factor Tu-GDP crystal polymorphism by polyethylene glycol contaminants. J Mol Biol (1985) 0.81

Preliminary x-ray diffraction data for tetragonal crystals of trypsinized Escherichia coli elongation factor. J Mol Biol (1977) 0.81

Genetic engineering, isolation and characterization of a truncated Escherichia coli elongation factor Tu comprising domains 2 and 3. Biochim Biophys Acta (1990) 0.79

Structure of the DNA binding cleft of the gene 5 protein from bacteriophage fd. J Supramol Struct (1979) 0.79

Preliminary X-ray diffraction analysis of crystals of Bacillus thuringiensis toxin, a cell membrane disrupting protein. J Mol Biol (1987) 0.78

An isotope edited classical Raman difference spectroscopic study of the interactions of guanine nucleotides with elongation factor Tu and H-ras p21. Biochemistry (1991) 0.78

Effect of trypsin modification of the Escherichia coli elongation factor Tu on the ternary complex with aminoacyl-tRNA. J Biol Chem (1985) 0.78

Affinity purification of aminoacyl-tRNA. Anal Biochem (1984) 0.78

The structure of a DNA unwinding protein and its complexes with oligodeoxynucleotides by x-ray diffraction. Biophys J (1980) 0.77

Preparation of Escherichia coli elongation factor Tu-guanosine 5'-triphosphate analogs. Anal Biochem (1989) 0.77

Gene-V product of bacteriophage fd: structure of a DNA-unwinding protein and its complexes with DNA. Cold Spring Harb Symp Quant Biol (1979) 0.76

Structure of the gene 5 DNA binding protein from bacteriophage fd and its DNA binding cleft. Mol Biol Biochem Biophys (1980) 0.75

Preliminary crystallographic analysis of a complex between tetracycline and the trypsin-modified form of Escherichia coli elongation factor Tu. J Mol Biol (1990) 0.75

An improved bulk purification method for Escherichia coli elongation factor, Ts. Anal Biochem (1984) 0.75

Bulk preparation and crystallization of the Escherichia coli elongation factor Tu-Ts complex. Anal Biochem (1985) 0.75