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Structural analyses of NudT16-ADP-ribose complexes direct rational design of mutants with improved processing of poly(ADP-ribosyl)ated proteins.
Thirawatananond, Puchong; McPherson, Robert Lyle; Malhi, Jasmine; Nathan, Sara; Lambrecht, Michael J; Brichacek, Matthew; Hergenrother, Paul J; Leung, Anthony K L; Gabelli, Sandra B.
Afiliación
  • Thirawatananond P; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • McPherson RL; Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, 21205, USA.
  • Malhi J; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Nathan S; Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Lambrecht MJ; Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD, 21205, USA.
  • Brichacek M; Department of Chemistry, University of Illinois, Urbana, IL, 61801, USA.
  • Hergenrother PJ; Department of Chemistry, University of Illinois, Urbana, IL, 61801, USA.
  • Leung AKL; Department of Chemistry, University of Illinois, Urbana, IL, 61801, USA.
  • Gabelli SB; Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, 21205, USA. anleung@jhsph.edu.
Sci Rep ; 9(1): 5940, 2019 04 11.
Article en En | MEDLINE | ID: mdl-30976021
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Poli Adenosina Difosfato Ribosa / Pirofosfatasas / Procesamiento Proteico-Postraduccional / Poli(ADP-Ribosa) Polimerasas / Mutación Límite: Humans Idioma: En Revista: Sci Rep Año: 2019 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Poli Adenosina Difosfato Ribosa / Pirofosfatasas / Procesamiento Proteico-Postraduccional / Poli(ADP-Ribosa) Polimerasas / Mutación Límite: Humans Idioma: En Revista: Sci Rep Año: 2019 Tipo del documento: Article País de afiliación: Estados Unidos