journal cover

Synthetic and editing mechanisms of aminoacyl-tRNA synthetases

Topics in Current Chemistry

Jul 16, 2013

John J Perona, Ita Gruic-Sovulj

Abstract

Aminoacyl-tRNA synthetases (aaRS) ensure the faithful transmission of genetic information in all living cells. The 24 known aaRS families are divided into 2 structurally distinct classes (class I and class II), each featuring a catalytic domain with a common fold that binds ATP, amino a...read more

Mentioned in this Paper

Enzymes, antithrombotic
Amino Acids, I.V. solution additive
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity
Transfer RNA
RNA Editing
Enzymes for Treatment of Wounds and Ulcers
Adenylate
Binding (Molecular Function)
Nucleotides
Paper Details
References
  • References
  • Citations24
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations24
123

Similar Papers Found In These Feeds

tRNA synthetases

Aminoacyl-tRNA synthetases, also known as tRNA-ligases, are enzymes that attaches the appropriate amino acid onto its transfer RNA. Mutations in these enzymes have been linked to several diseases including Charcot-Marie-Tooth and cancer. Here is the latest research.

Epigenome Engineering

Recent advances in epigenome engineering technologies allow now for the large-scale assessment of the functional relevance of dna methylation. Discover the latest research here.

Epigenome Engineering (Keystone)

Recent advances in epigenome engineering technologies allow now for the large-scale assessment of the functional relevance of DNA methylation. Discover the latest research here.

Related Papers

© 2020 Meta ULC. All rights reserved

Synthetic and editing mechanisms of aminoacyl-tRNA synthetases

Topics in Current Chemistry

Jul 16, 2013

John J Perona, Ita Gruic-Sovulj

PMID: 23852030

DOI: 10.1007/128_2013_456

Abstract

Aminoacyl-tRNA synthetases (aaRS) ensure the faithful transmission of genetic information in all living cells. The 24 known aaRS families are divided into 2 structurally distinct classes (class I and class II), each featuring a catalytic domain with a common fold that binds ATP, amino a...read more

Mentioned in this Paper

Enzymes, antithrombotic
Amino Acids, I.V. solution additive
MT-TA gene
Triplet Codon-amino Acid Adaptor Activity
Transfer RNA
RNA Editing
Enzymes for Treatment of Wounds and Ulcers
Adenylate
Binding (Molecular Function)
Nucleotides

Similar Papers Found In These Feeds

tRNA synthetases

Aminoacyl-tRNA synthetases, also known as tRNA-ligases, are enzymes that attaches the appropriate amino acid onto its transfer RNA. Mutations in these enzymes have been linked to several diseases including Charcot-Marie-Tooth and cancer. Here is the latest research.

Epigenome Engineering

Recent advances in epigenome engineering technologies allow now for the large-scale assessment of the functional relevance of dna methylation. Discover the latest research here.

Related Papers

Biochemistry

Structural diversity and protein engineering of the aminoacyl-tRNA synthetases

BiochemistryOctober 19, 2012
John J Perona, Andrew Hadd
Paper Details
References
  • References
  • Citations24
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
  • References
  • Citations24
123
/papers/synthetic-and-editing-mechanisms-of-aminoacyl-trna/23852030