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Phosphinic acid-based inhibitors of tubulin polyglycylation.
Zhuang, Zaile; Cummings, Steven W; Roll-Mecak, Antonina; Tanner, Martin E.
Afiliação
  • Zhuang Z; Department of Chemistry, University of British Columbia, Vancouver, BC, V6T 1Z1, Canada. mtanner@chem.ubc.ca.
  • Cummings SW; Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, and Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute, Bethesda, MD, 20892, USA. Antonina@nih.gov.
  • Roll-Mecak A; Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke, and Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute, Bethesda, MD, 20892, USA. Antonina@nih.gov.
  • Tanner ME; Department of Chemistry, University of British Columbia, Vancouver, BC, V6T 1Z1, Canada. mtanner@chem.ubc.ca.
Chem Commun (Camb) ; 58(45): 6530-6533, 2022 Jun 01.
Article em En | MEDLINE | ID: mdl-35579270
ABSTRACT
Tubulin polyglycylation is a posttranslational modification that occurs primarily on the axonemes of flagella and cilia and has been shown to be essential for proper sperm motility. Inhibitors of both the initiase and elongase ligases (TTLL8 and TTLL10) are shown to inhibit tubulin glycylation in the low micromolar range.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácidos Fosfínicos / Tubulina (Proteína) Limite: Humans / Male Idioma: En Revista: Chem Commun (Camb) Ano de publicação: 2022 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Ácidos Fosfínicos / Tubulina (Proteína) Limite: Humans / Male Idioma: En Revista: Chem Commun (Camb) Ano de publicação: 2022 Tipo de documento: Article