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July 1, 1984Proceedings of the National Academy of SciencesOpen Access

Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.

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Authors

HKHengming KeUniversity of North Carolina at Chapel HillRHRichard B. HonzatkoNovartis (Switzerland)WLWilliam N. LipscombUniversity of Stuttgart

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Ke et al. (1984) studied this question.

synapsesocial.com/papers/6a162555f9004307dec1eb91https://doi.org/10.1073/pnas.81.13.4037
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study.1982 · 38 citations
  2. 2Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli.1983 · 35 citations
  3. 3The Enzymology of Control by Feedback Inhibition1962 · 1,022 citations
  4. 4The 5.5 A Resolution Structure of the Regulatory Enzyme, Aspartate Transcarbamylase1972 · 44 citations
  5. 5Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation.1984 · 71 citations