يعرض 1 - 1 نتائج من 1 نتيجة بحث عن '"KTG, Lys497Thr498Gly499"', وقت الاستعلام: 0.54s تنقيح النتائج
  1. 1
    Mutations in PBP2 from ceftriaxone-resistant Neisseria gonorrhoeae alter the dynamics of the β3-β4 loop to favor a low-affinity drug-binding state

    المؤلفون: Carly A. Sciandra, Joshua Tomberg, Pei Zhou, Benjamin A. Fenton, Robert A. Nicholas, Christopher Davies

    المصدر: The Journal of Biological Chemistry

    مصطلحات موضوعية: antibiotic resistance, conformational dynamics, Protein Data Bank (RCSB PDB), Mutation, Missense, medicine.disease_cause, Biochemistry, Protein Structure, Secondary, Antibiotic resistance, PDB, Protein Data Bank, Drug Resistance, Bacterial, medicine, KTG, Lys497Thr498Gly499, Molecular Biology, TPase, transpeptidase, Binding Sites, Strain (chemistry), Chemistry, ITC, isothermal titration calorimetry, PBP2, penicillin-binding protein 2, Ceftriaxone, Pathogenic bacteria, Isothermal titration calorimetry, Cell Biology, computer.file_format, PBP2, Protein Data Bank, Serine-Type D-Ala-D-Ala Carboxypeptidase, BTFA, bromotrifluoroacetone, Neisseria gonorrhoeae, Amino Acid Substitution, ESC, extended-spectrum cephalosporin, Biophysics, beta-lactam, computer, medicine.drug, Research Article

    URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6559d2a270ae356593cb5d2525a831f3
    https://pubmed.ncbi.nlm.nih.gov/34529975

    View record in OpenAIRE

    أضف إلى المفضلة
أدوات البحث: أحصل على تغذية RSS – أرسل هذا البحث بالبريد الإلكتروني – حفظ البحث – جدول التنبيهات: لا شيء