Timothy L. Tapley, Ph.D.
Affiliations: | 2005 | University of California, Irvine, Irvine, CA |
Area:
Biochemistry, General BiophysicsGoogle:
"Timothy Tapley"Mean distance: (not calculated yet)
Parents
Sign in to add mentor| Larry Edward Vickery | grad student | 2005 | UC Irvine | |
| (Peptide and polypeptide substrate recognition by the Hsp70 molecular chaperones HscA and DnaK.) | ||||
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Publications
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| Tapley TL, Franzmann TM, Chakraborty S, et al. (2010) Protein refolding by pH-triggered chaperone binding and release. Proceedings of the National Academy of Sciences of the United States of America. 107: 1071-6 |
| Tapley TL, Körner JL, Barge MT, et al. (2009) Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proceedings of the National Academy of Sciences of the United States of America. 106: 5557-62 |
| Tapley TL, Cupp-Vickery JR, Vickery LE. (2006) Structural determinants of HscA peptide-binding specificity. Biochemistry. 45: 8058-66 |
| Tapley TL, Cupp-Vickery JR, Vickery LE. (2005) Sequence-dependent peptide binding orientation by the molecular chaperone DnaK. Biochemistry. 44: 12307-15 |
| Silberg JJ, Tapley TL, Hoff KG, et al. (2004) Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. The Journal of Biological Chemistry. 279: 53924-31 |
| Tapley TL, Vickery LE. (2004) Preferential substrate binding orientation by the molecular chaperone HscA. The Journal of Biological Chemistry. 279: 28435-42 |
| Hoff KG, Ta DT, Tapley TL, et al. (2002) Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. The Journal of Biological Chemistry. 277: 27353-9 |
| Silberg JJ, Hoff KG, Tapley TL, et al. (2001) The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. The Journal of Biological Chemistry. 276: 1696-700 |