ATPase domain of DnaK, Escherichia coli Hsp70 Molecular Chaperone, Experiences pH-dependent ATPase Activity Upon Linker Binding Due to Asp194 and Glu171

Imamoglu Rahmi; Gunsel Umut; Balta Bulent; Dinler-Doganay Gizem

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ATPase domain of DnaK, Escherichia coli Hsp70 Molecular Chaperone, Experiences pH-dependent ATPase Activity Upon Linker Binding Due to Asp194 and Glu171

机译：DnaK，大肠杆菌Hsp70分子伴侣的ATPase结构域，由于Asp194和Glu171导致连接子结合后，会经历pH依赖性的ATPase活性。

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《Protein Science: A Publication of the Protein Society 》 |2014年第1期| 共2页
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Imamoglu Rahmi; Gunsel Umut; Balta Bulent; Dinler-Doganay Gizem;
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1. ATPase domain of DnaK, Escherichia coli Hsp70 Molecular Chaperone, Experiences pH-dependent ATPase Activity Upon Linker Binding Due to Asp194 and Glu171 [J] . Imamoglu Rahmi, Gunsel Umut, Balta Bulent, Protein Science: A Publication of the Protein Society . 2014 ,第Suppla1期

机译：DnaK，大肠杆菌Hsp70分子伴侣的ATPase结构域，由于Asp194和Glu171导致连接子结合后，会经历pH依赖性的ATPase活性。
2. Structure and Energetics of an Allele-Specific Genetic Interaction between dnaJ and dnaK: Correlation of Nuclear Magnetic Resonance Chemical Shift Perturbations in the J-Domain of Hsp40/DnaJ with Binding Affinity for the ATPase Domain of Hsp70/DnaK. [J] . Landry SJ Biochemistry . 2003 ,第17期

机译：dnaJ和dnaK之间的等位基因特异性遗传相互作用的结构和能量：Hsp40 / DnaJ的J-域中核磁共振化学位移扰动与Hsp70 / DnaK ATPase域的结合亲和力的相关性。
3. Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling. [J] . Montgomery DL, Morimoto RI, Gierasch LM Journal of Molecular Biology . 1999 ,第3期

机译：大肠杆菌70 kDa分子伴侣DnaK的底物结合域中的突变，可改变底物亲和力或域间偶联。
4. CONFORMATION-SPECIFIC INTERACTIONS WITH TOMM34 MODULATE HSP70 FOLDING AND ATPASE ACTIVITIES [C] . Jiri HAUSNER, Michal DURECH, Filip TRCKA, ASMS Conference on Mass Spectrometry and Allied Topics . 2016

机译：与Tomm34的构象特异性相互作用调节HSP70折叠和ATP酶活性
5. Kinetic characterization of the ATPase cycle of DnaK, an Escherichia coli molecular chaperone. [D] . Russell, Rick. 1998

机译：大肠杆菌分子伴侣DnaK ATPase循环的动力学表征。
6. Mutagenesis Reveals the Complex Relationships between ATPase Rate and the Chaperone Activities of Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK) [O] . Lyra Chang, Andrea D. Thompson, Peter Ung, 2010

机译：诱变揭示了ATP酶速率与大肠杆菌热激蛋白70（Hsp70 / DnaK）的伴侣活性之间的复杂关系。
7. Mutagenesis Reveals the Complex Relationships between ATPase Rate and the Chaperone Activities of Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK)* [O] . Chang, Lyra, Thompson, Andrea D., Ung, Peter, 2010

机译：诱变揭示了ATPase速率与大肠杆菌热激蛋白70（Hsp70 / DnaK）伴侣活性之间的复杂关系*

ATPase domain of DnaK, Escherichia coli Hsp70 Molecular Chaperone, Experiences pH-dependent ATPase Activity Upon Linker Binding Due to Asp194 and Glu171

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