King J - Search Results

1

Formation of amyloid fibrils in vitro by human gammaD-crystallin and its isolated domains.

Papanikolopoulou K, Mills-Henry I, Thol SL, Wang Y, Gross AA, Kirschner DA, Decatur SM, King J. Papanikolopoulou K, et al. Among authors: king j. Mol Vis. 2008 Jan 16;14:81-9. Mol Vis. 2008. PMID: 18253099 Free PMC article.

2

Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains.

Mills-Henry IA, Thol SL, Kosinski-Collins MS, Serebryany E, King JA. Mills-Henry IA, et al. Biophys J. 2019 Jul 23;117(2):269-280. doi: 10.1016/j.bpj.2019.06.006. Epub 2019 Jun 14. Biophys J. 2019. PMID: 31266635 Free PMC article.

3

Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin.

Wang Y, Petty S, Trojanowski A, Knee K, Goulet D, Mukerji I, King J. Wang Y, et al. Among authors: king j. Invest Ophthalmol Vis Sci. 2010 Feb;51(2):672-8. doi: 10.1167/iovs.09-3987. Epub 2009 Aug 13. Invest Ophthalmol Vis Sci. 2010. PMID: 19684009 Free PMC article.

4

Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.

Serebryany E, Takata T, Erickson E, Schafheimer N, Wang Y, King JA. Serebryany E, et al. Protein Sci. 2016 Jun;25(6):1115-28. doi: 10.1002/pro.2924. Epub 2016 Apr 18. Protein Sci. 2016. PMID: 26991007 Free PMC article.

5

The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes.

Jung J, Byeon IJ, Wang Y, King J, Gronenborn AM. Jung J, et al. Among authors: king j. Biochemistry. 2009 Mar 31;48(12):2597-609. doi: 10.1021/bi802292q. Biochemistry. 2009. PMID: 19216553 Free PMC article.

6

Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin.

Mills IA, Flaugh SL, Kosinski-Collins MS, King JA. Mills IA, et al. Protein Sci. 2007 Nov;16(11):2427-44. doi: 10.1110/ps.072970207. Epub 2007 Sep 28. Protein Sci. 2007. PMID: 17905830 Free PMC article.

7

Glutamine deamidation destabilizes human gammaD-crystallin and lowers the kinetic barrier to unfolding.

Flaugh SL, Mills IA, King J. Flaugh SL, et al. Among authors: king j. J Biol Chem. 2006 Oct 13;281(41):30782-93. doi: 10.1074/jbc.M603882200. Epub 2006 Aug 4. J Biol Chem. 2006. PMID: 16891314 Free article.

8

In vitro unfolding, refolding, and polymerization of human gammaD crystallin, a protein involved in cataract formation.

Kosinski-Collins MS, King J. Kosinski-Collins MS, et al. Among authors: king j. Protein Sci. 2003 Mar;12(3):480-90. doi: 10.1110/ps.0225503. Protein Sci. 2003. PMID: 12592018 Free PMC article.

9

Probing folding and fluorescence quenching in human gammaD crystallin Greek key domains using triple tryptophan mutant proteins.

Kosinski-Collins MS, Flaugh SL, King J. Kosinski-Collins MS, et al. Among authors: king j. Protein Sci. 2004 Aug;13(8):2223-35. doi: 10.1110/ps.04627004. Protein Sci. 2004. PMID: 15273315 Free PMC article.

10

Mechanism of the highly efficient quenching of tryptophan fluorescence in human gammaD-crystallin.

Chen J, Flaugh SL, Callis PR, King J. Chen J, et al. Among authors: king j. Biochemistry. 2006 Sep 26;45(38):11552-63. doi: 10.1021/bi060988v. Biochemistry. 2006. PMID: 16981715

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