Thermodynamic properties of nucleotide-free EF-Tu from Thermus thermophilus in the presence of low-molecular weight effectors of its GTPase activity
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference39 articles.
1. Modulation by monovalent and divalent cations of the guanosine-5'-triphosphatase activity dependent on elongation factor Tu
2. Hydrolysis of GTP by elongation factor Tu can be induced by monovalent cations in the absence of other effectors.
3. Kirromycin, an Inhibitor of Protein Biosynthesis that Acts on Elongation Factor Tu
4. Mg2+ Is Not Catalytically Required in the Intrinsic and Kirromycin-stimulated GTPase Action of Thermus thermophilus EF-Tu
5. MECHANISM OF ACTION OF KIRROMYCIN-LIKE ANTIBIOTICS
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1. Ion-Specific Protein/Water Interface Determines the Hofmeister Effect on the Kinetic Stability of Glucose Oxidase;The Journal of Physical Chemistry B;2019-09-11
2. Oxidation of a Cysteine Residue in Elongation Factor EF-Tu Reversibly Inhibits Translation in the Cyanobacterium Synechocystis sp. PCC 6803;Journal of Biological Chemistry;2016-03
3. Molecular Dynamics Simulations Predict a Favorable and Unique Mode of Interaction between Lithium (Li+) Ions and Hydrophobic Molecules in Aqueous Solution;Journal of Chemical Theory and Computation;2011-03-03
4. Flexibility and enzyme activity of NADH oxidase from Thermus thermophilus in the presence of monovalent cations of Hofmeister series;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2008-05
5. Modulation of activity of NADH oxidase fromThermus thermophilusthrough change in flexibility in the enzyme active site induced by Hofmeister series anions;European Journal of Biochemistry;2003-12-09
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