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The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability.
Vasu, Kommireddy; Ramachandiran, Iyappan; Terenzi, Fulvia; Khan, Debjit; China, Arnab; Khan, Krishnendu; Chechi, Aayushi; Baleanu-Gogonea, Camelia; Gogonea, Valentin; Fox, Paul L.
Affiliation
  • Vasu K; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Ramachandiran I; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Terenzi F; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Khan D; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • China A; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Khan K; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Chechi A; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Baleanu-Gogonea C; Department of Chemistry, Cleveland State University, Cleveland, OH, USA.
  • Gogonea V; Department of Cardiovascular and Metabolic Sciences, Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, OH, USA.
  • Fox PL; Department of Chemistry, Cleveland State University, Cleveland, OH, USA.
iScience ; 24(3): 102215, 2021 Mar 19.
Article in En | MEDLINE | ID: mdl-33748704
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Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: IScience Year: 2021 Type: Article Affiliation country: United States
Fulltext
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PubMed Links
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Full text: 1 Collection: 01-internacional Database: MEDLINE Language: En Journal: IScience Year: 2021 Type: Article Affiliation country: United States