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Patient mutations in human ATP:cob(I)alamin adenosyltransferase differentially affect its catalytic versus chaperone functions.
Gouda, Harsha; Mascarenhas, Romila; Pillay, Shubhadra; Ruetz, Markus; Koutmos, Markos; Banerjee, Ruma.
Affiliation
  • Gouda H; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
  • Mascarenhas R; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
  • Pillay S; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
  • Ruetz M; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA.
  • Koutmos M; Department of Chemistry, University of Michigan, Ann Arbor, Michigan, USA; Department of Biophysics, University of Michigan, Ann Arbor, Michigan, USA.
  • Banerjee R; Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan, USA. Electronic address: rbanerje@umich.edu.
J Biol Chem ; 297(6): 101373, 2021 12.
Article in En | MEDLINE | ID: mdl-34757128
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Triphosphate / Molecular Chaperones / Alkyl and Aryl Transferases / Mutation Limits: Humans Language: En Journal: J Biol Chem Year: 2021 Document type: Article Affiliation country: United States Country of publication: United States
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Adenosine Triphosphate / Molecular Chaperones / Alkyl and Aryl Transferases / Mutation Limits: Humans Language: En Journal: J Biol Chem Year: 2021 Document type: Article Affiliation country: United States Country of publication: United States