Literature DB >> 17592850

Exploiting temperature-dependent substrate promiscuity for nucleoside analogue activation by thymidine kinase from Thermotoga maritima.

Stefan Lutz1, Joseph Lichter, Lingfeng Liu.   

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Year:  2007        PMID: 17592850      PMCID: PMC2085358          DOI: 10.1021/ja0734391

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN: 0002-7863            Impact factor:   15.419


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8.  Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.

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1.  Quaternary structure change as a mechanism for the regulation of thymidine kinase 1-like enzymes.

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Review 2.  Protein promiscuity and its implications for biotechnology.

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3.  Engineering Kinases to Phosphorylate Nucleoside Analogs for Antiviral and Cancer Therapy.

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6.  Inactive-to-Active Transition of Human Thymidine Kinase 1 Revealed by Molecular Dynamics Simulations.

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