Literature DB >> 4897787

Substrate specificity of ribosomal peptidyl transferase: 2'(3')-O-aminoacyl nucleosides as acceptors of the peptide chain on the amino acid site.

I Rychlík, J Cerná, S Chládek, J Zemlicka, Z Haladová.   

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Year:  1969        PMID： 4897787     DOI： 10.1016/0022-2836(69)90075-8

Source DB:  PubMed          Journal:  J Mol Biol        ISSN： 0022-2836            Impact factor:   5.469


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  5 in total

1.  Hydrolysis of fMet-tRNA by peptidyl transferase.

Authors:  C T Caskey; A L Beaudet; E M Scolnick; M Rosman
Journal:  Proc Natl Acad Sci U S A       Date:  1971-12       Impact factor: 11.205

2.  Fluorescent 2'(3')-O-aminoacylnucleosides-acceptor substrates for ribosomal peptidyltransferase+.

Authors:  S Chládek; D Ringer; E M Abraham
Journal:  Nucleic Acids Res       Date:  1976-05       Impact factor: 16.971

3.  Mononucleotide derivatives as ribosomal P-site substrates reveal an important contribution of the 2'-OH to activity.

Authors:  Silke Dorner; Claudia Panuschka; Walther Schmid; Andrea Barta
Journal:  Nucleic Acids Res       Date:  2003-11-15       Impact factor: 16.971

4.  Influence of cholesteryl 14-methylhexadecanoate on some ribosomal functions required for peptide elongation.

Authors:  J Hradec; Z Dusek; O Mach
Journal:  Biochem J       Date:  1974-02       Impact factor: 3.857

5.  Induced fit of the peptidyl-transferase center of the ribosome and conformational freedom of the esterified amino acids.

Authors:  Jean Lehmann
Journal:  RNA       Date:  2016-11-22       Impact factor: 4.942
  5 in total

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