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Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid.
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Mutations in isoleucyl tRNA synthetase (iars(y68)) leads to increased branching angiogenesis in developing zebrafish.
bi-allelic mutations in cytosolic isoleucyl-tRNA synthetase (IARS) have been described in three individuals with growth delay, hepatic dysfunction, and neurodevelopmental disabilities. Here we report an additional subject with this condition identified by whole-exome sequencing. Our findings support the association between this disorder and neonatal cholestasis with distinct liver pathology
Biallelic IARS Mutations Cause Growth Retardation with Prenatal Onset, Intellectual Disability, Muscular Hypotonia, and Infantile Hepatopathy
Aminoacyl-tRNA synthetases catalyze the aminoacylation of tRNA by their cognate amino acid. Because of their central role in linking amino acids with nucleotide triplets contained in tRNAS, aminoacyl-tRNA synthetases are thought to be among the first proteins that appeared in evolution. Isoleucine-tRNA synthetase belongs to the class-I aminoacyl-tRNA synthetase family and has been identified as a target of autoantibodies in the autoimmune disease polymyositis/dermatomyositis. Alternatively spliced transcript variants have been found.
isoleucyl-tRNA synthetase, cytoplasmic
, isoleucine tRNA synthetase
, isoleucyl-tRNA synthetase
, isoleucine--tRNA ligase, cytoplasmic
, isoleucine-tRNA synthetase
, isoleucyl tRNA synthetase
, isoleucine tRNA ligase 1, cytoplasmic