Differential scanning calorimetric studies of E. coli aspartate transcarbamylase
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Biochemistry,Biophysics
Reference37 articles.
1. Escherichia coli Aspartate Transcarbamoylase: Structure, Energetics, and Catalytic and Regulatory Mechanisms
2. Escherichia coli Aspartate Transcarbamylase: the Relation Between Structure and Function
3. Can a simple model account for the allosteric transition of aspartate transcarbamoylase?
4. E. coli aspartate transcarbamylase: Part I: Catalytic and regulatory functions
5. E. coli aspartate transcarbamylase: Part II: Structure and allosteric interactions
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Structural Domain Organization of Gastric H+,K+-ATPase and Its Rearrangement during the Catalytic Cycle;Journal of Biological Chemistry;1997-01
2. [28] Thermodynamic approaches to understanding aspartate transcarbamylase;Methods in Enzymology;1995
3. Glutamic acid 86 is important for positioning the 80's loop and arginine 54 at the active site of Escherichia coli aspartate transcarbamoylase and for the structural stabilization of the C1-C2 interface.;Journal of Biological Chemistry;1994-10
4. Association of the catalytic subunit of aspartate transcarbamoylase with a zinc-containing polypeptide fragment of the regulatory chain leads to increases in thermal stability;Protein Science;1994-06
5. The conserved residues glutamate-37, aspartate-100, and arginine-269, are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase;Biochemistry;1993-09-28
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