Published in FEBS Lett on May 18, 1981
Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site. J Mol Biol (2000) 1.78
Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands. Protein Sci (1996) 1.13
Dimer state of protein L7/L12 and EF-G-dependent reactions of ribosomes. Eur J Biochem (1978) 1.05
The flexible region of protein L12 from bacterial ribosomes studied by proton nuclear magnetic resonance. J Biol Chem (1989) 1.03
Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure. Protein Eng (1994) 1.02
Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome. J Biol Chem (2000) 1.02
Stoichiometry and properties of the complex between ribosomal proteins L7 and L10 in solution. FEBS Lett (1978) 1.02
The structure and dynamics of ribosomal protein L12. Biochimie (1987) 0.98
Domain IV of elongation factor G from Thermus thermophilus is strictly required for translocation. FEBS Lett (1999) 0.96
[Enhanced resistance to phytopathogenic bacteria in transgenic tobacco plants with synthetic gene of antimicrobial peptide cecropin P1]. Genetika (2005) 0.95
An intact conformation at the tip of elongation factor G domain IV is functionally important. FEBS Lett (1998) 0.93
Elongation factor-dependent reactions of ribosomes deprived of proteins L7 and L12. FEBS Lett (1977) 0.92
Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid. J Biol Chem (2001) 0.91
Comparative evaluation of different methods for disulfide bond formation in synthesis of the HIV-2 antigenic determinant. J Pept Res (1997) 0.90
Conformational independence of N- and C-domains in ribosomal protein L7/L12 and in the complex with protein L10. FEBS Lett (1998) 0.89
Role of different regions of ribosomal proteins L7 and L10 in their complex formation and in the interaction with the ribosomal 50 S subunit. FEBS Lett (1980) 0.88
The N-terminal sequence protein of L7/L 12 is responsible for its dimerization. Eur J Biochem (1978) 0.87
Cell-free production of biologically active polypeptides: application to the synthesis of antibacterial peptide cecropin. Protein Expr Purif (2001) 0.86
Tertiary and quaternary structure for ribosomal protein L7 in solution. FEBS Lett (1977) 0.85
Specific interaction of the elongation factor EF-G with the ribosomal 23 S RNA from Escherichia coli. FEBS Lett (1982) 0.84
Direct expression of PCR products in a cell-free transcription/translation system: synthesis of antibacterial peptide cecropin. FEBS Lett (1997) 0.84
Topology of the secondary structure elements of ribosomal protein L7/L12 from E. coli in solution. FEBS Lett (1996) 0.84
A physical study of acidic ribosomal proteins from Artemia salina, Bacillus subtilis and Micrococcus lysodeikticus. FEBS Lett (1981) 0.82
Proton nuclear magnetic resonance study of the ribosomal protein L7/L12 in situ. FEBS Lett (1982) 0.82
Studies on the structure of protein L7/L12 from Escherichia coli ribosomes. Eur J Biochem (1978) 0.82
Comparative stability of dihydrofolate reductase mutants in vitro and in vivo. Protein Eng (1993) 0.81
Compact globular conformation of protein S4 from Escherichia coli ribosomes. J Mol Biol (1980) 0.80
Structure of protein-deficient 50 S ribosomal subunits. Particles without 5 S RNA-protein complex retain the L7/L12 stalk and associate with 30 S subunits. FEBS Lett (1986) 0.80
The L7/L12 proteins change their conformation upon interaction of EF-G with ribosomes. FEBS Lett (1984) 0.80
[Complex formation between L7 and L10 ribosomal proteins in solution]. Dokl Akad Nauk SSSR (1976) 0.78
[Role of the N-terminal sequence (1-26) in the dimerization of protein L7 in solution]. Mol Biol (Mosk) (1979) 0.78
The length of the interdomain region of the L7/L12 protein is important for its function. FEBS Lett (1992) 0.78
Structure of protein-deficient 50 S ribosomal subunits. Nine core proteins induce the compact conformation of 23 S ribosomal RNA. FEBS Lett (1986) 0.78
Elongation factors Tu and G change their conformation on interaction with ribosomes. Biomed Sci (1990) 0.78
Nuclear magnetic resonance techniques for studying structure and function of ribosomes. Methods Enzymol (1988) 0.78
[Structure of histone Hi and its Ser-38 phosphorylated derivative in complexes with DNA]. Dokl Akad Nauk SSSR (1976) 0.78
[Stability of the structure of KRP (kinase related protein) protein]. Mol Biol (Mosk) (1999) 0.77
[Synthesis and cardioprotective properties of apelin-12 and its structural analogs]. Bioorg Khim (2012) 0.77
[Peptide fragment 66-77 of monocyte chemoattractant protein 1 and its retro-enantio analogue inhibits the migration of cells in vitro and in vivo]. Bioorg Khim (2006) 0.77
The peptide of sequence 66-77 of monocytic chemotactic protein (MCP-1) inhibits inflammation in experimental animals. Dokl Biol Sci (2006) 0.77
[Solid-phase synthesis of peptides containing arginine with an unprotected guanidine group]. Bioorg Khim (2000) 0.76
[Mutation analysis of functional role of amino acid residues in domain IV of elongation factor G]. Mol Biol (Mosk) (2006) 0.76
C-H ... O hydrogen bonding in solutions of methylated nucleic acid base analogs as revealed by NMR. Biopolymers (1989) 0.76
Neutral glycolipids of atherosclerotic plaques and unaffected human aorta tissue. Eur J Biochem (1989) 0.76
Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain. Biochemistry (Mosc) (1998) 0.76
[Genomic instability in sunflower interspecific hybrids]. Genetika (2009) 0.75
Novel data on interactions of elongation factor Ts. Biochimie (1992) 0.75
[Letter: High-resolution nuclear magnetic study of the interaction between histones and DNA]. Biofizika (1975) 0.75
[Direct transition of S-acetamidomethyl-protected peptide 593-603 of HIV-2 gp41 into a cyclic disulfide using iodine. Study of side reactions]. Bioorg Khim (1996) 0.75
[NMR study of ricin conformation. High mobility of N-terminal regions of A- and B-subunits]. Mol Biol (Mosk) (1988) 0.75
Study of the secondary and tertiary structure of ribosomal protein S7 from Escherichia coli in solution. FEBS Lett (1981) 0.75
Globular structure of the small proteins L29 and L30 from Escherichia coli ribosomes. FEBS Lett (1982) 0.75
[Spatial structure of the cro-repressor in a solution. I. Identification of interaction in a hydrophobic cluster using the nuclear Overhauser effect]. Mol Biol (Mosk) (1986) 0.75
[Peptide fragments and structural analogues of chemokine MPC-1: synthesis and effect on the MPC-1-induced migration of monocytes]. Bioorg Khim (2004) 0.75
[Isolation of all proteins from the 50S subparticles of ribosomes of Escherichia coli]. Mol Biol (Mosk) (1982) 0.75
[Structure and density of ribosomal RNA and its complexes with proteins in a solution]. Mol Biol (Mosk) (1984) 0.75
[Nuclear magnetic resonance study of C--H...O type hydrogen bonds in analogs of nucleic acid base]. Mol Biol (Mosk) (1980) 0.75
[Penetrating peptide inhibitor of the myosin light chain kinase suppresses hyperpermeability of vascular endothelium]. Ross Fiziol Zh Im I M Sechenova (2009) 0.75
[Identification of signals in overlapping NMR spectra of proteins by the differential spin echo method]. Biofizika (1985) 0.75
[Solid phase synthesis of beta amyloid (1-42)]. Bioorg Khim (1997) 0.75
[Letter: Study of the interaction of histones F1, F2b, F2a1, F3 with nucleotides by the method of high resolution nuclear magnetic resonance]. Biofizika (1975) 0.75
Physical properties of ribosomal proteins isolated under different conditions from the Escherichia coli 50 S subunit. FEBS Lett (1983) 0.75
[Study by the proton magnetic resonance method of complex formation between nucleosides and compounds modeling amino acid residues of proteins in dimethyl sulfoxide]. Biofizika (1977) 0.75
[Study of carnosine complexes with nucleotides by the method of high resolution nuclear magnetic resonance]. Biokhimiia (1976) 0.75
[Studies of conformation of RNA-binding proteins from the small subparticle of Escherichia coli ribosomes by proton magnetic resonance]. Mol Biol (Mosk) (1982) 0.75
[Isolation of the postural asymmetry factor following right hemisection of the spinal cord]. Dokl Akad Nauk SSSR (1986) 0.75
[Secondary structure of total protein and 23S RNA in 50S ribosomal subunits and in the isolated state]. Mol Biol (Mosk) (1986) 0.75
[Physico-chemical characteristics of ribosomal proteins L10 and L11]. Mol Biol (Mosk) (1979) 0.75
Compact globular structure of protein S15 from Escherichia coli ribosomes. FEBS Lett (1979) 0.75
[Changes in the intramolecular mobility of protein L7/L12 resulting from the addition of elongation factor G to the ribosomes]. Dokl Akad Nauk SSSR (1985) 0.75
[Compact structure of the small proteins L 29 and L 30 from Escherichia coli ribosomes]. Dokl Akad Nauk SSSR (1982) 0.75
[NMR-intrascopy - new method of biophysical investigation]. Biofizika (1982) 0.75
A comparative study of structural properties of fibronectin and its 180 kDa fragment. FEBS Lett (1985) 0.75
[The synthesis of immunomodulating peptide alloferon, the active component of the antiviral drug allokine-alpha]. Bioorg Khim (2006) 0.75
Thermodynamic parameters of the helix-coil transition in polypeptide chains. III. Random copolymers of L-leucine and L-glutamic acid. Biopolymers (1975) 0.75
[Novel peptide inhibitors of the myosin light chain kinase suppress hyperpermeability of vascular endothelium]. Biofizika (2011) 0.75
[Structural changes of the ribosomes during interaction with the elongation factor Tu]. Dokl Akad Nauk SSSR (1988) 0.75
[Structural analysis of translating ribosomes. Proton magnetic resonance method]. Mol Biol (Mosk) (1988) 0.75
[1H-NMR study of protein L7/L12 from bacterial ribosomes]. Mol Biol (Mosk) (1989) 0.75
[Peptide inhibitors of myosin light chain kinase. Development of peptidase resistant analogues]. Bioorg Khim (2010) 0.75
[Comparison of the physical properties of ribosomal proteins from Escherichia coli 50S subparticles isolated by different methods]. Mol Biol (Mosk) (1984) 0.75
[Study of peptide degradation in the serum by 1H-NMR]. Bioorg Khim (1986) 0.75