Trapping and structure determination of an intermediate in the allosteric transition of aspartate transcarbamoylase
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference32 articles.
1. Amino acid substitutions which stabilize aspartate transcarbamoylase in the R state disrupt both homotropic and heterotropic effects
2. A solution NMR study showing that active site ligands and nucleotides directly perturb the allosteric equilibrium in aspartate transcarbamoylase
3. Changes in the X-ray solution scattering of aspartate transcarbamylase following the allosteric transition
4. Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R-State Bound to PALA, or to Product Analogues Citrate and Phosphate,
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1. Molecular Target Validation of Aspartate Transcarbamoylase from Plasmodium falciparum by Torin 2;ACS Infectious Diseases;2020-03-04
2. New regulatory mechanism‐based inhibitors of aspartate transcarbamoylase for potential anticancer drug development;The FEBS Journal;2020-02-04
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4. From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases;International Journal of Molecular Sciences;2015-08-12
5. Structural Characterisation of Non-Deamidated Acidic Variants of Erwinia chrysanthemi L-asparaginase Using Small-Angle X-ray Scattering and Ion-Mobility Mass Spectrometry;Pharmaceutical Research;2015-06-04
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