Timothy L. Tapley, Ph.D. - Publications
Affiliations: | 2005 | University of California, Irvine, Irvine, CA |
Area:
Biochemistry, General BiophysicsYear | Citation | Score | |||
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2010 | Tapley TL, Franzmann TM, Chakraborty S, Jakob U, Bardwell JC. 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. PMID 20080625 DOI: 10.1073/Pnas.0911610107 | 0.358 | |||
2009 | Tapley TL, Körner JL, Barge MT, Hupfeld J, Schauerte JA, Gafni A, Jakob U, Bardwell JC. 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. PMID 19321422 DOI: 10.1073/Pnas.0811811106 | 0.431 | |||
2006 | Tapley TL, Cupp-Vickery JR, Vickery LE. Structural determinants of HscA peptide-binding specificity. Biochemistry. 45: 8058-66. PMID 16800630 DOI: 10.1021/Bi0606187 | 0.714 | |||
2005 | Tapley TL, Cupp-Vickery JR, Vickery LE. Sequence-dependent peptide binding orientation by the molecular chaperone DnaK. Biochemistry. 44: 12307-15. PMID 16156644 DOI: 10.1021/Bi051145R | 0.694 | |||
2004 | Silberg JJ, Tapley TL, Hoff KG, Vickery LE. 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. PMID 15485839 DOI: 10.1074/Jbc.M410117200 | 0.641 | |||
2004 | Tapley TL, Vickery LE. Preferential substrate binding orientation by the molecular chaperone HscA. The Journal of Biological Chemistry. 279: 28435-42. PMID 15100228 DOI: 10.1074/Jbc.M400803200 | 0.733 | |||
2002 | Hoff KG, Ta DT, Tapley TL, Silberg JJ, Vickery LE. 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. PMID 11994302 DOI: 10.1074/Jbc.M202814200 | 0.672 | |||
2001 | Silberg JJ, Hoff KG, Tapley TL, Vickery LE. 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. PMID 11053447 DOI: 10.1074/Jbc.M009542200 | 0.634 | |||
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