Results 201 to 210 of about 33,890 (233)

Genetic characteristics of novel extreme alkaline-inducible promoter located in five prime upstream region of peptidyl-prolyl cis/trans isomerase from Vibrio anguillarum. [PDF]

Sci Rep
Kim DG, Kim GM, Oh DN, Kim YS, Lee JM.
europepmc   +1 more source

Detection of <i>Helicobacter pylori</i> and the Genotypes of Resistance to Clarithromycin, Fluoroquinolones, and Metronidazole in Gastric Biopsies: An In Silico Analysis to Help Understand Antibiotic Resistance. [PDF]

Curr Issues Mol Biol
Valada P, Mata A, Brito RMM, Gonçalves T, Medeiros JA, Nogueira C.   +5 more
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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

Horizontal transfer of post-translational modifiers brings evolutionary opportunity and challenges to a conserved translation factor

Brewer TE, Kielkowski P, Stritzel J, Meier-Rosar F, Schlundt A, Lassak J.   +5 more
europepmc   +1 more source

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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
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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
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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
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Affinity labelling of yeast ribosomal peptidyl transferase

Molecular and General Genetics MGG, 1978
Using p-nitrophenylcarbamyl-phenylalanyl-tRNA (PNPC-Phe-tRNA) and N-Iodoacetylphenylalanyl-tRNA as affinity labels we have attempted to identify the components of the aminoacyl-tRNA binding sites located in the vicinity of the peptidyl transferase centre of the yeast ribosome. Both Phe-tRNA derivatives bind to the ribosomal A-site in the presence of 20
M, Pérez-Gosálbez, D, Vázquez, J P, Ballesta   +2 more
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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
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SPARK: A New Peptidyl Transferase Activity Assay

2008
The formation of peptide bonds is the central chemical reaction during protein synthesis and is catalyzed by the peptidyl transferase center residing in the large ribosomal subunit. This active site is composed of universally conserved rRNA nucleosides.
Alexander S, Mankin, Norbert, Polacek
openaire   +2 more sources