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Action at a distance: mutations of peripheral residues transform rapid reversible inhibitors to slow, tight binders of cyclooxygenase-2.
Blobaum, Anna L; Xu, Shu; Rowlinson, Scott W; Duggan, Kelsey C; Banerjee, Surajit; Kudalkar, Shalley N; Birmingham, William R; Ghebreselasie, Kebreab; Marnett, Lawrence J.
Afiliación
  • Blobaum AL; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Xu S; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Rowlinson SW; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Duggan KC; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Banerjee S; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, and Northeastern Collaborative Access Team, Argonne National Laboratory, Argonne, Illinois 60439.
  • Kudalkar SN; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Birmingham WR; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Ghebreselasie K; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
  • Marnett LJ; From the A. B. Hancock, Jr. Memorial Laboratory for Cancer Research, Departments of Biochemistry, Chemistry, and Pharmacology, Vanderbilt Institute of Chemical Biology, Center in Molecular Toxicology, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Nashville Tennessee 3723
J Biol Chem ; 290(20): 12793-803, 2015 May 15.
Article en En | MEDLINE | ID: mdl-25825493
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Mutación Missense / Ciclooxigenasa 2 / Inhibidores de la Ciclooxigenasa 2 Límite: Animals Idioma: En Revista: J Biol Chem Año: 2015 Tipo del documento: Article
Texto completo
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Mutación Missense / Ciclooxigenasa 2 / Inhibidores de la Ciclooxigenasa 2 Límite: Animals Idioma: En Revista: J Biol Chem Año: 2015 Tipo del documento: Article