Computational design and molecular dynamics simulations suggest the mode of substrate binding in ceramide synthases.
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| Title: | Computational design and molecular dynamics simulations suggest the mode of substrate binding in ceramide synthases. |
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| Authors: | Zelnik ID; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel., Mestre B; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel., Weinstein JJ; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel., Dingjan T; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel., Izrailov S; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel., Ben-Dor S; Life Sciences Core Facilities, Weizmann Institute of Science, Rehovot, 76100, Israel., Fleishman SJ; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel., Futerman AH; Department of Biomolecular Sciences, Weizmann Institute of Science, Rehovot, 76100, Israel. tony.futerman@weizmann.ac.il. |
| Source: | Nature communications [Nat Commun] 2023 Apr 22; Vol. 14 (1), pp. 2330. Date of Electronic Publication: 2023 Apr 22. |
| Publication Type: | Journal Article; Research Support, Non-U.S. Gov't |
| Journal Info: | Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE |
| Database: | MEDLINE Ultimate |
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| ISSN: | 2041-1723 |
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| DOI: | 10.1038/s41467-023-38047-x |
