Liming Li
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The organizations/institutes from the scholar's latest article
Research Subjects
Research Interests
Liming Li has a total of 2 co-authors. Here are the top co-authors by number of shared publications:
- J. Woodland Hastings
Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138-2020
1 shared publication Robert Hong
Department of Molecular and Cellular Biology, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138-2020
1 shared publication
Latest Publications
- Open Access
- 19 August 1997
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (17) , 8954-8958
Three functional luciferase domains in a single polypeptide chain
We report a unique case of a gene containing three homologous and contiguous repeat sequences, each of which, after excision, cloning, and expression in Escherichia coli, is shown to code for a peptide catalyzing the same reaction as the native protein, Gonyaulax polyedra luciferase (Mr = 137). This enzyme, which catalyzes the light-emitting oxidation of a linear tetrapyrrole (dinoflagellate luciferin), exhibits no sequence similarities to other luciferases in databases. Sequence analysis also reveals an unusual evolutionary feature of this gene: synonymous substitutions are strongly constrained in the central regions of each of the repeated coding sequences.
- 19 August 1997
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 94 (17) , 8954-8958
Open AccessThree functional luciferase domains in a single polypeptide chain
We report a unique case of a gene containing three homologous and contiguous repeat sequences, each of which, after excision, cloning, and expression in Escherichia coli, is shown to code for a peptide catalyzing the same reaction as the native protein, Gonyaulax polyedra luciferase (Mr = 137). This enzyme, which catalyzes the light-emitting oxidation of a linear tetrapyrrole (dinoflagellate luciferin), exhibits no sequence similarities to other luciferases in databases. Sequence analysis also reveals an unusual evolutionary feature of this gene: synonymous substitutions are strongly constrained in the central regions of each of the repeated coding sequences.