Results 31 to 40 of about 33,711 (238)
Substrate Specificity of Escherichia coli Peptidyl‐Transferase [PDF]
European Journal of Biochemistry, 1970 The kinetics of the puromycin interaction with different ribosomal bound peptidyl‐tRNAs were studied. The rates of the puromycin reaction with AA‐Phe‐tRNA and AA2‐Phe‐tRNA using three different amino acids (AA) were compared. At 4° all the three dipeptidyl‐tRNAsPhe reacted considerably slower than the three tripeptidyl‐tRNAsPhe. Acetyl‐Phe‐tRNA reacted
Amos Panet, Nathan de Groot, Y. Lapidot
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Hydrolysis of fMet-tRNA by Peptidyl Transferase [PDF]
Proceedings of the National Academy of Sciences, 1971 Escherichia coli and rabbit reticulocyte (f[ 3 H]Met-tRNA·AUG·ribosome) intermediates undergo hydrolysis, with release of f[ 3 H]methionine, upon addition of tRNA or CpCpA in the presence of acetone.
C. Thomas Caskey +3 more
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Computational and Structural Biotechnology Journal, 2023 The central function of the large subunit of the ribosome is to catalyze peptide bond formation. This biochemical reaction is conducted at the peptidyl transferase center (PTC).
Marc Joiret +4 more
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Mapping of Complete Set of Ribose and Base Modifications of Yeast rRNA by RP-HPLC and Mung Bean Nuclease Assay. [PDF]
PLoS ONE, 2016 Ribosomes are large ribonucleoprotein complexes that are fundamental for protein synthesis. Ribosomes are ribozymes because their catalytic functions such as peptidyl transferase and peptidyl-tRNA hydrolysis depend on the rRNA.
Jun Yang +5 more
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Modulating the activity of the peptidyl transferase center of the ribosome. [PDF]
RNA, 2008 The peptidyl transferase (PT) center of the ribosome catalyzes two nucleophilic reactions, peptide bond formation between aminoacylated tRNA substrates and, together with release factor, peptide release. Structure and function of the PT center are modulated by binding of aminoacyl-tRNA or release factor, thus providing the basis for the specificity of ...
Beringer M.
europepmc +4 more sources
Atomic mutagenesis of stop codon nucleotides reveals the chemical prerequisites for release factor-mediated peptide release. [PDF]
, 2018 Termination of protein synthesis is triggered by the recognition of a stop codon at the ribosomal A site and is mediated by class I release factors (RFs).
Clementi, Nina +11 more
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Ribosomal history reveals origins of modern protein synthesis. [PDF]
PLoS ONE, 2012 The origin and evolution of the ribosome is central to our understanding of the cellular world. Most hypotheses posit that the ribosome originated in the peptidyl transferase center of the large ribosomal subunit.
Ajith Harish, Gustavo Caetano-Anollés
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Visualizing formation of the active site in the mitochondrial ribosome
eLife, 2021 Ribosome assembly is an essential and conserved process that is regulated at each step by specific factors. Using cryo-electron microscopy (cryo-EM), we visualize the formation of the conserved peptidyl transferase center (PTC) of the human mitochondrial
Viswanathan Chandrasekaran +6 more
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Extensive ribosome and RF2 rearrangements during translation termination
eLife, 2019 Protein synthesis ends when a ribosome reaches an mRNA stop codon. Release factors (RFs) decode the stop codon, hydrolyze peptidyl-tRNA to release the nascent protein, and then dissociate to allow ribosome recycling.
Egor Svidritskiy +4 more
doaj +1 more source
Liver transplantation for type IV glycogen storage disease [PDF]
, 1991 TYPE IV glycogen storage disease is a rare autosomal recessive disorder (also called Andersen's disease1 or amylopectinosis) in which the activity of branching enzyme alpha-1, 4-glucan: alpha-1, 4-glucan 6-glucosyltransferase is deficient in the liver as
Andreas Tzakis +17 more
core +1 more source