Structural basis for catalysis and substrate specificity of human ACAT1
By H. Qian, Xin Zhao, R. Yan, X. Yao, Shuai Gao, Xue Sun, Ximing Du, Hongyuan Yang, Catherine C. L. Wong, Nieng Yan. 2020
90 citations recorded by the source corpus.
Subfields: Molecular Biology
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- Claire E. Coupland
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- Thomas Lanyon-Hogg
Citations in the corpus
- Structural model of PORCN illuminates disease-associated variants and drug binding sites (2021, unknown): “The CoA moiety anchors in a pocket on the cytoplasmic face (Figure 3C), similar to how it interacts with ACAT1 (Qian et al., 2020) and DGAT1 (Sui et al., 2020; Wang et al., 2020).”
- Structure, mechanism, and inhibition of Hedgehog acyltransferase (2021, background): “The majority of MBOATs 16, 2021 Crown Copyright ª 2021 Published by Elsevier Inc. 5025 er the CC BY license (http://creativecommons.org/licenses/by/4.0/). catalyze lipid chain transfer to small-molecule lipid substrates; however, HHAT, alongside porcupine acyltransferase (PORCN) and ghrelin O-acyltr”