Results 311 to 320 of about 345,668 (351)
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Biological Chemistry, 1999
AbstractHistidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS ...
W, Freist +4 more
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AbstractHistidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes.A compilation of currently known primary structures of HisRS ...
W, Freist +4 more
openaire +2 more sources
Biochemistry and Cell Biology, 1995
Direct measurements of the rates of dissociation of dipeptidyl-tRNA from the ribosome show that hyperaccurate SmP and SmD ribosomes have unstable A-site binding of peptidyl-tRNA, while P-site binding is extremely stable in relation to the wild type.
M, Ehrenberg +5 more
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Direct measurements of the rates of dissociation of dipeptidyl-tRNA from the ribosome show that hyperaccurate SmP and SmD ribosomes have unstable A-site binding of peptidyl-tRNA, while P-site binding is extremely stable in relation to the wild type.
M, Ehrenberg +5 more
openaire +2 more sources
Annual Review of Biophysics and Bioengineering, 1983
tRNA, because of its importance in gene translation, is widely studied. To date more than 200 primary structures are known (35), and the crystal structures of several tRNAs have been solved (61, 70, :83, 119, 120, 150, 154). From comparison of the nucleotide sequence aJ).d the tertiary structure of several tRNA species, features common to all tRNAs ...
R, Rigler, W, Wintermeyer
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tRNA, because of its importance in gene translation, is widely studied. To date more than 200 primary structures are known (35), and the crystal structures of several tRNAs have been solved (61, 70, :83, 119, 120, 150, 154). From comparison of the nucleotide sequence aJ).d the tertiary structure of several tRNA species, features common to all tRNAs ...
R, Rigler, W, Wintermeyer
openaire +2 more sources
Nature Chemical Biology, 2018
Fast, single-molecule tracking microscopy monitors transitions between mobile and ribosome-bound fluorescent tRNAs to achieve nucleotide-resolution measurements of translation rates in living cells.
Achillefs N, Kapanidis, Mathew, Stracy
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Fast, single-molecule tracking microscopy monitors transitions between mobile and ribosome-bound fluorescent tRNAs to achieve nucleotide-resolution measurements of translation rates in living cells.
Achillefs N, Kapanidis, Mathew, Stracy
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Journal of Biomolecular Structure and Dynamics, 2015
tRNAs are widely believed to segregate into two classes, I and II. Computational analysis of eukaryotic tRNA entries in Genomic tRNA Database, however, leads to new, albeit paradoxical, presence of more than a thousand class-I tRNAs with uncharacteristic long variable arms (V-arms), like in class-II.
Sanga, Mitra +4 more
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tRNAs are widely believed to segregate into two classes, I and II. Computational analysis of eukaryotic tRNA entries in Genomic tRNA Database, however, leads to new, albeit paradoxical, presence of more than a thousand class-I tRNAs with uncharacteristic long variable arms (V-arms), like in class-II.
Sanga, Mitra +4 more
openaire +2 more sources
Current Opinion in Structural Biology, 1995
Detailed mechanisms for each step of the reaction catalyzed by both class I and class II aminoacyl-tRNA synthetases have been proposed on the basis of crystallographic data of aminoacyl-tRNA synthetases in complex with their different substrates. Despite the very different topologies of the two classes, there are striking and unanticipated chemical ...
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Detailed mechanisms for each step of the reaction catalyzed by both class I and class II aminoacyl-tRNA synthetases have been proposed on the basis of crystallographic data of aminoacyl-tRNA synthetases in complex with their different substrates. Despite the very different topologies of the two classes, there are striking and unanticipated chemical ...
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Current Biology
Aminoacyl-tRNA synthetases hold the key to the genetic code and assign nucleic acid-based codons to amino acids, the building blocks of proteins. In their ability to recognize identity elements on transfer RNAs (tRNAs), some as simple as a single base pair, they ensure that the same proteins are formed each time information embedded in DNA is ...
Rasangi, Tennakoon, Haissi, Cui
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Aminoacyl-tRNA synthetases hold the key to the genetic code and assign nucleic acid-based codons to amino acids, the building blocks of proteins. In their ability to recognize identity elements on transfer RNAs (tRNAs), some as simple as a single base pair, they ensure that the same proteins are formed each time information embedded in DNA is ...
Rasangi, Tennakoon, Haissi, Cui
openaire +2 more sources
The expanding world of tRNA modifications and their disease relevance
Nature Reviews Molecular Cell Biology, 2021Tsutomu Suzuki
exaly
tRNA dysregulation and disease
Nature Reviews Genetics, 2022Esteban A Orellana, Richard I Gregory
exaly
Action mechanisms and research methods of tRNA-derived small RNAs
Signal Transduction and Targeted Therapy, 2020Junming Guo
exaly