Results 191 to 200 of about 33,711 (238)

Mechanism of ribosome stalling by the AMD1 C-terminal tail arrest peptide. [PDF]

Sci Adv
Maldosevic E, Boiocchi FS, Swirski MI, Meiklejohn KA, Yordanova MM, Baranov PV, Jomaa A.   +6 more
europepmc   +1 more source

Mitochondrial translational control in cardiovascular diseases: from mechanisms to therapies. [PDF]

Redox Biol
Deng Y, Guo N, Li D, Wang Z.
europepmc   +1 more source

Cryo-EM reveals multiple mechanisms of ribosome inhibition by doxycycline

Stuart WS, Isupov MN, McLaren M, Jenkins CH, Monier A, Daum B, Norville IH, Gold VA, Harmer NJ.   +8 more
europepmc   +1 more source

Peptidyl transferase: ancient and exiguous [PDF]

Chemistry and Biology, 2000
The finding that the universal ribosomal peptidyl transferase is an RNA enzyme casts new light on its ancient origins, on the use of transition state analogues for ribozymes, and on the role of selection-amplification in studies of molecular evolution.
Michael Yarus
exaly   +3 more sources

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Peptidyl transferase and beyond

Biochemistry and Cell Biology, 1995
The peptidyl transferase center of the Escherichia coli ribosome encompasses a number of 50S-subunit proteins as well as several specific segments of the 23S rRNA. Although our knowledge of the role that both ribosomal proteins and 23S rRNA play in peptide bond formation has steadily increased, the location, organization, and molecular structure of ...
Wower, J, Wower, IK, Kirillov, SV, Rosen, KV, Hixson, SS, Zimmermann, RA   +5 more
openaire   +2 more sources

Transesterification by Peptidyl Transferase

Nature, 1970
Peptidyl transferase, the enzyme which catalyses formation of peptide bonds, can be stimulated by CCA, the 3′-terminus of tRNA, to catalyse also a transesterification reaction involving nucleophilic attack of Met-tRNAfMet by ethanol to yield fMet-ethyl ester.
E, Scolnick, G, Milman, M, Rosman, T, Caskey   +3 more
openaire   +2 more sources

Masking of peptidyl transferase activity in polyribosomes

Archives of Biochemistry and Biophysics, 1975
Abstract The peptidyl transferase activity of polysomes from Escherichia coli , rabbit reticulocytes and chick embryos, assayed in the fragment reaction, is 3- to 10-fold lower than the corresponding activity of single ribosomes. The polysomal peptidyl transferase activity is restored in full under conditions of in vitro protein synthesis that ...
V R, Leick, R F, Santerre, R, Kaempfer
openaire   +2 more sources

Molecular aspects of the ribosomal peptidyl transferase

Biochemical Society Transactions, 2002
The proteins in a living cell are synthesized on a large bipartite ribonucleoprotein complex termed the ribosome. The peptidyl transferase, which polymerizes amino acids to yield peptides, is localized on the large subunit. Biochemical investigations over the past 35 years have led to the hypothesis that rRNA has a major role in all ribosomal functions.
Barta, Andrea, Schulmeister, Ulrike, Polacek, Norbert, Panuschka, Claudia, Dorner, Silke   +4 more
openaire   +3 more sources

Peptidyl transferase: A new method for kinetic studies

Biochemical and Biophysical Research Communications, 1972
The reaction of N-Acetyl-phenylalanyl-t-RNA with E.coli ribosomes in the presence of poly Uridylic acid, guanosine 5′-triphosphate, and initiation factors (ribosomal wash), leads to the formation of N-Acetyl-phenylalanyl-RNA-ribosome-poly Uridylic acid complex, which can be isolated on a cellulose nitrate filter.
R, Fico, C, Coutsogeorgopoulos
openaire   +2 more sources

The presence of peptidyl transferase in wheat embryo ribosomes

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
Abstract Extensively washed wheat embryo ribosomes require a supernatant factor and GTP in order to synthesize the model peptide N-acetylphenylalanylpuromycin from N-acetylphenylalanyl-tRNA and puromycin. The reaction is inhibited by fusidic acid, suggesting a requirement for translocation.
M, Gatica, J E, Allende
openaire   +2 more sources