Search Results - "Seit Nebi, A S"
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Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro
Published in Biochemistry (Moscow) (01-02-2008)“…Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is…”
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2
Suppression of nonsense mutations in the Dystrophin gene by a suppressor tRNA gene
Published in Molecular biology (New York) (01-01-2002)“…Nonsense mutations in the dystrophin gene are the cause of Duchenne muscular dystrophy (DMD) in 10-15% of patients. In such an event, one approach to gene…”
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3
Phosphorylation by cyclic AMP-dependent protein kinase inhibits chaperone-like activity of human HSP22 in vitro
Published in Biochemistry (Moscow) (01-02-2008)“…Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is…”
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Journal Article -
4
Some properties of human small heat shock protein Hsp22 (H11 or HspB8)
Published in Biochemical and biophysical research communications (19-03-2004)“…Untagged recombinant human small heat shock protein with apparent molecular mass 22 kDa (Hsp22) was obtained in homogeneous state. Size exclusion…”
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5
The problem of protein kinase activity of small heat shock protein Hsp22 (H11 or HspB8)
Published in Biochemical and biophysical research communications (17-12-2004)“…The recently described protein denoted H11, Hsp22 or HspB8 seems to participate in regulation of proliferation, apoptosis, and cardiac hypertrophy. Mutation of…”
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6
Some properties of human small heat shock protein Hsp20 (HspB6)
Published in European journal of biochemistry (01-01-2004)“…Human heat shock protein of apparent molecular mass 20 kDa (Hsp20) and its mutant, S16D, mimicking phosphorylation by cyclic nucleotide‐dependent protein…”
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7
A new method to measure the functional activity of class-1 translation termination factor eRF1
Published in Molekuliarnaia biologiia (01-01-2002)“…Termination of protein synthesis (hydrolysis of the last peptidyl-tRNA on the ribosome) takes place when the ribosomal A site is occupied simultaneously by one…”
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