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Jonathan A. King Prof., Molecular Biology |
Updated: September 2009
Education
| Yale University, New Haven, CT. |
B.S. |
l962 |
Zoology |
| Caltech, Pasadena, CA |
PhD. |
l968 |
Genetics |
| British Medical
Research Council, |
Postdoc Fellow |
l969-70 |
Structural Biology |
| Associate Scientist, Jet Propulsion Laboratory, Pasadena CA, |
l968 |
| Assistant Professor, Department of Biology, M.I.T. |
l97l-73 |
| Associate Professor, Department of Biology, M.I.T. |
l974-78 |
| Director of Biomedical Electron Microscopy Lab., M.I.T. |
l97l-Present |
| Professor, Department of Biology, M.I.T. |
l979-Present |
| General Motors National Scholar |
l958-62 |
| B.S.magna
cum laude |
l962 |
| Woodrow Wilson National Fellow |
l962-63 |
| Jane Coffin Childs Fund Fellow |
l968-70 |
| U.S. Antarctic Service Medal |
l968 |
| Foundation Lecturer, ASM |
l983 |
| Fellow, AAAS |
l985 |
| Guggenheim Fellow |
l987 |
| NIH Merit Award |
1988-98 |
| President, Biophysical Society | 1999 |
| MIT Martin Luther King Leadership Award | 2003 |
| Distinguished Biology Award, 9th Annual International RECOMB Conference | 2005 |
| Chair, Massachusetts Darwin Bicentennial Project | 2008-present |
| Massachusetts Academy of Sciences, Board of Trustees | 2008-present |
| NEI Board of Scientific Counselors | 2005-08 |
| Chair, XVIII International Conference on Phage/Virus Assembly | 2003 |
| Executive Board Member, Biophysical Society |
1998-2000 |
| Joint Steering Committee for Public Policy Board Member |
1997-2000 |
| Technical Education Resource Center Board of Trustees |
1997-present |
| National Councillor, Biophysical Society |
1992-95 |
| FASEB Summer Research Conferences Advisory Committee |
1992-95 |
| Chair, Gordon Conference on Proteins |
1991 |
| Councillor, Am. Soc. Virology |
1990-92 |
| NIH Genetic Basis of Disease Study Section |
1990-93 |
| NIH Biotechnology Training Grant Study Section |
1990 |
| NIH Structural Biology Study Section |
1989-90 |
| Chair, FASEB Virus Assembly Conference |
1990 |
| Co-Chair, FASEB In Vivo Protein Folding Conf. |
1990 |
| Chair, AAAS Meeting on Protein Folding |
1987 |
| Editorial Board, Annual Reviews of Microbiology |
l986-90 |
| NIH
Microbial Physiology Study Section |
l98l-84 |
| Committee on Nominations, American Association for the Advancement of Science |
l985-87 |
| Chair, Bacterial Virus Division, American Society of Microbiology |
1982-83 |
65. Sargent, D., Benevides, J. M., Yu, M-h., King, J. and Thomas, Jr., G. J. "Secondary Structure and Thermostability of the Phage P22 Tailspike: Analysis of Raman Spectroscopy of the Wild-Type Protein and a Temperature-Sensitive Folding Mutant", (1988) J. Mol. Biol. 199: 491-502.
66. King, J. and Haase-Pettingell,
C. (l988) "Aggregate Formation from a Thermolabile Intermediate
in the Maturation of the Thermostable P22 Tailspike Protein." In British
Biochem. Society Transactions. 16, 2, 105.
67.
Bazinet, C., Benbaset, J, King, J., Carazo, J. and Carrascosa, J.
(1988) "Purification and Organization
of the Gene l Portal Protein Required for Phage P22 DNA Packaging", Biochem.
27: 1849-l856.
68. Haase-Pettingell, C. and King, J. (l988) "Aggregation of Thermolabile Intermediates in the Pathway of P22 Tailspike Maturation: Model for Inclusion Body Formation." J. Biol. Chem. 263, No. 10: 4977-4983.
69. Bazinet, C., and
King, J. (l988) Initiation of P22 "Procapsid Assembly" in vivo. J.
Mol. Biol. 202: 77-86
70. Prevelige, P., Thomas, D. and King, J. (1988) "Scaffolding Protein
Regulates the Polymerization of P22 Coat Subunits into Icosahedral Shells" in
vivo. J. Mol. Biol. 202: 743-757.
7l. Villafane, R. and King, J. (1988) "Nature and Distribution of Sites of Temperature Sensitive Folding Mutations in the Gene for the P22 Tailspike Polypeptide Chain". J. Mol. Biol., 204, 607 - 619.
72. Mitraki, A. and King, J. (1989) "Protein folding intermediates and inclusion body formation." Bio/technology, 7, 690 - 697.
73. Sturtevant, J,
Yu, M-h, Haase-Pettingell, C. and
King, J. (1989) "Thermostability of temperature sensitive folding mutants
of the P22 tailspike protein." J. Biol. Chem. 264, 10693
- 10698.
74. King, J. (1989) "Deciphering the rules of protein folding." Chem.
& Eng. News, April 11, 32-54.
75. Seckler, R., Fuchs, A. King, J. and Jaenicke, R. (1989). "Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains." in vitro. J. Biol. Chem., 264, 11750 - 11753.
76. King, J., Fane, B., Haase-Pettingell, C., Mitraki, A., Villafane, R., and Yu, M-H. (1989) "Identification of amino acid sequences influencing intracellular folding pathways using temperature sensitive folding mutations." In "Protein Folding: Deciphering the Second Half of the Genetic Code" (L. A. Gierasch and J. King, eds.) AAAS, pp 225-240.
77. King, J., Fane, B., Haase-Pettingell, C., Mitraki, A. and Villafane, R. (1990) "Genetic analysis of polypeptide chain folding and misfolding" in vivo. in "Protein Design and the Development of New Therapeutics and Vaccines." (Ed. Jerry Hook &;George Poste) Smith Kline and French Symposium, Plenum Press, 59-78.
78. Thomas, G. J. Jr., Becka, R., Sargent, D., Yu, M-H, and King, J. (1990) "Conformational stability of P22 Tailspike Proteins Carrying Temperature Sensitive Folding Mutations." Biochem., 29, 4181 - 4187.
79. Prevelige, P. E. Jr., Thomas, D., King, J., Towse, S. A., and Thomas, G. J. Jr. (1990) "Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly." Biochem., 29, 5626 - 5633.
80. Friguet, B., Djavadi-Ohaniance, L., Haase-Pettingell, C., King, J., and Goldberg, M. (1990) "Probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase with monoclonal antibodies." J. Biol. Chem., 265, 10347-10351.
81. Gierasch, L. A. and King, J. "Protein Folding: Deciphering the Second Half of the Genetic Code". (1990) American Association for the Advancement of Science, Wash. D.C.
82. Bazinet, C., Villafane, R. and King, J. (1990) "Novel second-site suppression of cold-sensitive defect in phage P22 procapsid assembly." J. Mol. Biol. 216, 701-716.
83. Fane, B. and King, J. (1991) "Intragenic suppressors of folding defects in the P22 tailspike protein." Genetics 127: 263-277.
84. Chen, B. and King J. (1991) "Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase." Biochemistry, 30, 6260-6269.
86. Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J. and King, J. (1991) "Global suppression of protein folding defects and inclusion body formation." Science, 253, 54-58.
87. Chen, B. and King, J. (1991) "Pathway for the thermal unfolding of wild type and mutant forms of the thermostable P22 tailspike endorhamnosidase." In "Protein Refolding" (G. Georgiou &;E. de Bernardez Clark, eds.) ACS Symposium Series 470, American Chemical Society, Washington, D.C., pp. 119-132.
88. Mitraki, A., Haase-Pettingell, C., and King J. (1991) "Mechanisms of inclusion body formation." In "Protein Refolding" (G. Georgiou & E. de Bernardez-Clark, eds.) ACS Sympsosium Seris 470, American Chemical Society, Washington, D.C., pp. 35-49.
89. Mitraki, A., Fane, B., Haase-Pettingell, C. and King, J. (1991) "Mutations affecting protein folding and misfolding in vivo." In "Application in Enzyme Biotechnology" (eds. T. Baldwin and J. Kelly) Plenum Press, pp. 129-136.
90. Chen, C.-C., Zhu, Y., King, J. and Evans, L. (1992) "A Molecular Thermodynamic Approach to Predict the Secondary structure of Homo-polypeptides in Aqueous Systems." Biopolymers, 32, 1375-1392.
91. Mitraki, A. and King, J. (1992) "Amino acid substitutions influencing intracellular protein folding pathways." FEBS Letters, 307, no. 1, 20-25.
92. Teschke, C. and King, J. (1992) "Folding and assembly of oligomeric proteins in Escherichia coli." Current Opinion in Biotechnology, 3, no. 5, 468-473.
93. Zhu, Y., Chen, C.-C., King, J. and Evans, L. (1992) "Molecular Thermodynamic Model To Predict the ÿ-Helical Secondary Structure of Polypeptide Chains in Solution." Biochemistry, 31, 10591-10601.
94. Prevelige, P., Thomas, D. and King, J. (1993) "Nucleation and Growth Phases in the Polymerization of Coat and Scaffolding Subunits into Icosahedral Procapsid Shells." Biophysical Journal, 64, 824-835.
95. King, J., Haase-Pettingell, C., Gordon, C., Sather, S. and Mitraki, A. (1993) "Amino Acid Sequence Determinants of Polypeptide Chain Folding and Inclusion Body Formation." In "Protein Folding: In Vivo and In Vitro" (ed. J. Cleland) ACS Symposium Series 526, American Chemical Society, Washington, D.C., pp. 24-37.
96. Prevelige, P. & King, J. (1993) "Assembly of Bacteriophage P22: A Model for sd-DNA Virus Assembly." In "Progress in Medical Virology, Vol. 40" (ed. J.L. Melnick) Karger, Basel, pp. 206-221.
97. Gordon, C. and King, J. (1993) "Temperature Sensitive Mutations in the P22 Coat Protein Which Interfere with Polypeptide Chain Folding." J. Biol. Chem., 268, 9358-9368.
98. King, J. (1993) "The Unfolding Puzzle of Protein Folding." Technology Review, 96: 4, pp. 54-61.
99.Prasad, B.V., Prevelige, P., Marietta, E., Chen, R., Thomas, D., King, J. and Chiu, W. (1993) "Three Dimensional Transformation of Capsids Associated with Genome Packaging in a Bacterial Virus." J. Mol. Biol., 231, 65-74.
100.Galisteo, M.L. and King, J. (1993) "Conformational Transformations in the Protein Lattice of Phage P22 Procapsids." Biophysical Journal, 65, 227-235.
101.Teschke, C. and King, J. (1993) "Folding of the Phage P22 Coat Protein in vitro." Biochemistry, 32, 10839-10847.
102.Mitraki, A., Danner, M., King, J. and Seckler, R. (1993) "Temperature-sensitive Mutations and Second-site Suppressor Substitutions Affect Folding of the P22 Tailspike Protein in Vitro." J. Biol. Chem, 268, 20071-20075.
103.Teschke, C.M., King, J. and Prevelige, P.E., Jr. (1993) "Inhibition of capsid assembly by 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid." Biochemistry, 32, 10658-10665.
104.King, J., Teschke, C.M., Haase-Pettingell, C. and Mitraki, A. (1993) "Protein misfolding and inclusion body formation in prokaryotes." In: Research Opportunities in Biomolecular Engineering: The Interface Between chemical Engineering and Biology. Proceedings of the National Institute of General Medical Sciences. ( G. Georgiou and I. Glowinski, eds.), Washington, D.C., pp.25-32.
105.Gordon, C. and King, J. (1994) "Genetic properties of temperature sensitive folding mutants of the coat protein of phage P22." GENETICS, 136, 427-438.
106.Berger, B, Shor, P.W., Tucker-Kellogg, L. and King, J. (1994) "A Local Rule Based Theory of Virus Shell Assembly." Proceedings of the National Academy of Sciences, 91, 7732-7736.
107.Friguet, B., Djavadi-Ohaniance, L., King, J. and Goldberg, M. (1994) "In Vitro and ribosome bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies." J. Biol. Chem., 269, 15945-15949.
108.Sather, S. and King, J. (1994) "Intracellular Trapping of a Cytoplasmic folding Intermediate of the Phage P22 Tailspike Using Iodoacetamide." J. Biol. Chem., 269, 25268-25276.
109.Gordon, C., Sather, S., Casjens, S. and King, J. (1994) "Selective In Vivo Rescue by GroEL/ES of Thermolabile Folding Intermediates of Phage P22 Structural Proteins." J. Biol. Chem., 269, 27941-27951.
110.Greene, B. and King, J. (1994) "Binding of Scaffolding Subunits Within the P22 Procapsid Lattice." Virology, 205, 188-197.
111.Chen, C-C., King, J. and Wang, D. (1995) "A Molecular Thermodynamic Model for Helix-Helix Docking and Protein Aggregation." AIChE Journal, 41, 1015-1024.
112.Teschke, C.M. and King, J. (1995) "In Vitro folding of Phage P22 Coat Protein with Amino Acid Substitutions that Confer In Vivo Tempertaure-Sensitivity." Biochemistry, 34, 6815-6826.
113. Speed, M.A., Wang, D.I.C. and King, J. (1995) "Multimeric Intermediates in the Pathway to the Aggregated Inclusion Body State for P22 Tailspike Polypeptide Chains." Protein Science, 4, 900-908.
114.Galisteo, M.L., Gordon, C.L. and King, J. (1995) "Stability of Wild-Type and Temperature-Sensitive Protein Subunits of the Phage P22 Capsid." J. Biol. Chem., 270, 16595-16601.
115.King, J., Haase-Pettingell, C., Robinson, A., Speed, M. A. and Mitraki, A. (1995) "Thermolabile Folding Intermediates: Inclusion Body Precursors and Chaperonin Substrates." FASEB Journal, 10, 57-66.
116.King, J. (1996) Unexpected Pathways to protein stabilization. Nature Biotechnology, 14, 436.
117.Thuman-Commike, P., Greene, B., Jakana, J., Prasad, B.V.V., King, J., Prevelige, P.E., Chiu, W. (1996) "Three-dimensional Structure of Scaffolding-containing Phage P22 Procapsids by Electron Cryo-microscopy." J. Mol. Biol., 260, 85-98.
118.Speed, M., Wang, D. and King, J. (1996) "Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition." Nature Biotechnology, 14, 1283-1287.
119.Greene, B. and King, J. (1996) "Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation." Virology, 225, 82-96.
120.Speed, M., Morshead, T., Wang, D. and King, J. (1997) "Conformation of Productive Folding Intermediates and off-Pathway Aggregation intermediates Probed by Monoclonal Antibodies." Protein Science, 6, 99-108.
121.Haase-Pettingell, C. and King, J. (1997) "Prevalence of Temperature Sensitive folding Mutations in the parallel Beta Coil Domain of the Phage P22 Tailspike Endorhamnosidase." J. Mol. Biol., 267, 88-102.
122.King, J. and Chiu, W. (1997) "The Procapsid to Capsid Transition in Double-stranded DNA Bacteriophages." In "Structural Biology of Viruses" (W. Chiu, R.M. Burnett and R. Garcea, eds.) Oxford University Press, pp. 288-311.
123.Speed, M., King, J. and Wang, D.I.C. (1997) "Polymerization Mechanism of Polypeptide Chain Aggregation." Biotechnology and Bioengineering, 54, 333-343.
124.King, J. (1997) "Refolding with a piece of the ring." Nature Biotechnology, 15, 7-8.
125.King, J. (1997) "The Biotechnology Revolution: Self-replicating Factories and the Ownership of Life Forms." In "Cutting Edge: Technology, Information Capitalism and Social Revolution" (J. Davis, T. Hirschl and M. Stack, eds.) Verso Press, pp 145-156.
126.Robinson, A.S. and King, J. (1997) "Disulfide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein." Nature Structural Biol., 4, 450-455.
127.Fan, Z.H., Jensen, P.K., King, J. and Lee, C.S. (1997) "Monitoring the refolding pathway for a large multimeric protein using capillary zone electrophoresis." J. Chromatography, 769, 315-323.
128.Betts, S., Haase-Pettingell, C., and King, J. (1997) "Mutational effects on inclusion body formation." In Protein Misassembly (ed. R. Wetzel), Volume 50 of "Advances in Protein Chemistry," Academic Press, pp 243-264.
129.Thuman-Commike, P.A., Greene, B., Malinski, J., King, J. and Chiu, W. (1998) "Role of the Scaffolding Protein in P22 Procapsid Size Determination Suggested by T=4 and T=7 Procapsid Structures." Biophysical J., 74, 559-568.
130.Jensen, P.K., King, J. and Lee, C.S. (1998) "Investigating temperature effects on refolding and aggregation of a large multimeric protein using capillary zone electrophoresis." Analytical Chemistry, 70, 730-736.
131.Liu, C., Kamei, D.T., King, J., Wang, D.I.C. and Blankschtein, D. (1998) Separation of proteins and viruses using two-phase aqueous micellar systems. J. Chromatogr. B, 711, Nos. 1+2, pp. 127-138.
132.Betts, S. and King, J. (1998) "Properties of the single chain tailspike intermediate at the junction between producitve folding and off-pathway aggregation." Protein Sci., 7, 1516-1523.
133.Konz, J.O., King, J. and Cooney, C.L. (1998) "The effects of Oxygen on Recombinant Protein Expression." Biotech. Progress, 14, 393-409.
134.King, J. (1998) public resources, not corporate property. The Environmental Forum, 14, 40-41.
135.Greene, B. and King, J. (1999) "In vitro unfolding/refolding of wild type phage P22 scaffolding protein reveals capsid binding domain." J. Biol. Chem., 274, 16135-16140.
156.Pande. A., Pande, J., Asherie, N., Lomakin, A., Ogun, O., King, J., and Benedek, G.B. (2001)Crystal cataracts: Human genetic cataract caused by protein crystallization. PNAS,98, 6116-6120.
157.Bradley, P., Cowen, L.J., Menke, M., King, J. and Berger, B. (2001) "Predicting the Beta-Helix Fold from Protein Sequence Data." In Proceedings of the Fifth Annual International Conference on Computational Molecular Biology, ACM Press, New York, pp. 59-67.
158.Clark, P.L. and King, J. (2001) A Newly Synthesized, Ribosome-Bound Polypeptide Chain adopts Conformations Dissimilar from Early In Vitro Refolding Intermediates. J. Biol.Chem., 276, 25411-25420.
159.Ting, C.S., Rocap, G., King, J. and Chisholm, S.W. (2001) Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: Evidence for rapid evolution of genetic heterogeneity. Microbiology, 147, 3171-3182 .
160. Bradley, P., Cowen, L., Menke, M., King, J. and Berger, B. (2001) BetaWrap: Successful prediction of parallel ß-helices from primary sequence reveals an association with many microbial pathogens. PNAS, 98, 14819-14824.
169.Kamei, D., King, J., Wang, D.I.C. & Blankschtein, D. (2002) Separating lysozyme from bacteriophage P22 in two-phase aqueous micellar systems. Biotech & Bioeng, 80, 233-236.
170.Griffiths, S.W., King, J. & Cooney, C.L. (2002) The reactivity and oxidation pathway of Cysteine 232 in Recombaninant human alpha1-Antitrypsin. J. Biol. Chem., 277:25486-25492.
171.Kosinski-Collins,
M. & King, J. (2003) In
vitro unfolding and refolding of human gamma-D crystallin, a
protein involved in cataract formation. Protein Science, 12,
480-490.
172.Weigele, P.R., Scanlon, E. and King, J. (2003) Homo-trimeric,
ß-stranded viral adhesins and tail proteins. J. Bacteriology,
185, 4022-4030.
173.Menke, M.,Scanlon, E., King, J., Berger, B. and Cowen, L. (2004) Wrap and Pack: A New Paradigm for Beta Structural Motif Recognition with Application to Recognizing Beta Trefoils. In Proceedings of the 8th Annual International Conference on Research in Computational Molecular Biology RECOMB, (P.E.Bourne and D. Gusfield, eds.). ACM Press, New York, pp. 298-307.
174.Kosinski-Collins, M., Flaugh, S. & King, J. (2004) Probing folding and fluorescence quenching in Human gamma-D crystallin Greek key domains using Triple Tryptophan mutant proteins. Protein Science, 13, 2223-2235.
175.Pope, W., Haase-Pettingell, C. & King, J. (2004) Protein folding failure sets the high temperature limit on the growth of phage P22 in Salmonella serovar Typhimurium. Applied & Environmental Microbiology, 70, 4840-4847 .
176.Betts, S., Haase-Pettingell, C., Cook, K. and King, J. (2004) Buried hydrophobic side chains essential for the folding of the parallel beta-helix domains of the P22 tailspike. Protein Science, 13, 2291-2303.
177.Flaugh, S.L., Kosinski-Collins, M.S. and King, J (2005) Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Protein Science, 14, 569-581 .
178.Jain, M., Evans, M.S., King, J. and Clark, P.L. (2005) Monoclonal epitope mapping describes tailspike beta-helix folding and aggregation intermediates. J.Biol.Chem., 280, 23032-23040 .
179.Gossard, D.C and King, J. (2005) Lattice transformations and subunit conformational changes in phage capsid maturation.J. of Theoretical Med., in press.
181..Menke, M.,Scanlon, E., King, J., Berger, B. and Cowen, L. (2005) Wrap and Pack: A New Paradigm for Beta Structural Motif Recognition with Application to Recognizing Beta Trefoils. J.Computational Biol., 12: 777-795.
182.Raso, S.W., Abel,
J., Barnes, J.M., Maloney, K.M., Pipes, G., Treuheit, M.J., King,
J. and Brems, D.N. (2005) Aggregation
of graulocyte-colony stimulating factor in vitro involves a conformationally
altered monomeric state. Protein Science, 14, 2246-2257.
183.Weigele, P., Haase-Pettingell,
C., Campbell, P.G., Gossard, D.C. and King, J. (2005) Stalled
folding mutants in the triple beta-helix domain of the phage P22 tailspike
adhesin. J.Mol.Biol., 354, 1103-1117.
184.Jiang, W., Chang J., Jakana, J., Weigele, P., King, J. and Chiu, W. (2006) Structure of complete Epsilon 15 phage reveals organization of condensed DNA and DNA packaging/injection apparatus. Nature, 439, 612-616.
185.Schwartz, Russell & King, J. (2006) Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure. Protein Science, 15, 102-112.
186.Simkovsky, R. and King, J. (2006) An elongated spine of buried core residues necessary for in vivo folding of the parallel b -helix of P22 tailspike adhesin. PNAS, 103, 3575-3580.
187.Chang, J., Weigele, P., King, J., Chiu, W. and Jiang, W. (2006) Cry-EM symmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure, 14, 1073-1082.
188.Chen, J., Flaugh, S.L., Callis, P.R. and King, J. (2006) Mechanism of the highly efficient quenching of tryptophan fluorescence in human gamma-D-crystallin. Biochemistry, 45, 1552-11563.
189.Flaugh, S.L., Mills, I.A. and King, J. (2006) Glutamine deamidation destabilizes human gamma-D-crystallin and lowers the kinetic barrier to unfolding. J.Biol.Chem., 281, 30782-30793.
190.McDonnell, A.V., Menke, M., Palmer, N., King, J., Cowen, L. and Berger, B. (2006) Fold recognition and accurate sequence-structure alignment of sequences directing beta-sheet proteins. Proteins, 63, 976-985.
191.Pope, WH, Weigele, PR, Chang, J, Pedulla, ML, Ford, ME, Houtz, JM, Jiang, W, Chiu, W, Hatfull, GF, Hendrix, RW and King, JA (2007), Genome sequence, structural proteins, and capsid organization of the cyanophage Syn5: a "horned" bacteriophage of marine Synechococcus. J. Mol. Biol., 368, 966-981.
192. Weigele, P.R., Pope, W.H., Pedulla, M.L., Houtz, J.M., Smith, A.L., King, J., Hatfull, G.F., Lawrence, J.G. and Hendrix, R.W. (2006) Genomic and structural analysis of Syn9, a cyanophage infecting marine prochlorococcus and synechococcus. Environmental Microbiology, 9, 1675-1695.
193. K. Papanikolopoulou, I.A. Mills, S.L Flaugh, Y. Wang, A.A.R. Gross, D.A. Kirschner, S.M. Decatur and J.A. King. (2007) Formation of Amyloid Fibrils In Vitro by Human gamma D-crystallin and its Isolated Domains. Molecular Vision, 14, 81-89.
194. Mills, I.A., Flaugh, S.L., Kosinski-Collins, M.S. and King, J. (2007) Folding and stability of the isolated greek key domains of the long-lived human lens proteins, gamma D-crystallin and gamma S-crystallin. Protein Science, 16, 2427-44.
195. King, J. (2007) The High Stakes in Science Education: Risking the Roots of American Productivity. Education Week, 26, pgs. 34, 44.
196. Jiang, W., Baker, M.L., Jakana, J., Weigele, P.R., King, J. and Chiu, W. (2008) Backbone structure of the infectious epsilon 15 virus capsid revealed by electron cryomicroscopy. Nature, 451, 1130-1135.
197. Wang, H., Duennwald, ML, Roberts, BE, Rozeboom, LM, Zhang, YL, Steele, AD, Krishnan, R, Su, LJ, Griffin, D., Mukhopadhyay, S, Hennessy, EJ, Weigele, P, Blanchard, BJ, King, J, Deniz, AA, Buchwald, SL, Ingram, VM, Lindquist, Sm and Shorter, J. (2008) Direct and selective elimination of specific prions and amyloids by 4,5-deanilinophthalimide and analogs. PNAS, 105, 7159-7164.
198. Chen, J., Toptygin, D., Brand, L. and King, J. (2008) Mechanism of the efficient tryptophan fluorescence quenching in human gamma d-crystallin studied by time-resolved fluorescence. Biochemistry, 47, 10705-10721.
199. Wang, Y. and King, J. (2009) Cataract as a protein aggregation disease. In, Protein Misfolding Diseases: Current and Emerging Principles and Therapies (Marina Ramirez-Alvarado, Jeffrey W. Kelly, and Christopher M. Dobson, eds.) John Wiley and Sons, Hoboken, NJ. In press.
200. Jung, J., Byeon, I-J.L., Wang, Y., King, J. and Gronenborn, A.M. (2009) The structure of the cataract causing P23T mutant of HgD-Crystallin exhibits local distinctive conformational and dynamic changes. Biochemistry, 48, 2597-2609.
201. Chen, J., Callis, P.R. and King, J. (2009) Mechanism of the very efficient quenching of tryptophan fluorescence in human gammaD- and gammaS-crystallins; the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage. Biochemistry, 48, 3708-3716.
202. Wang, Y., Petty, S.A., Trojanowski, A.T., Knee, K.M., Goulet, D.R., Mukerji, I. and King, J.A. (2009) Formation of amyloid fibrils in vitro from partially unfolded intermediates of Human gammaC-Crystallin. IOVS, in press.
203. Xu, Jianhua; Chen, Jiejin; Toptygin, Dmitri; Tcherkasskaya, Olga; Callis, Patrik; King, Jonathan; Brand, Ludwig; Knutson, Jay (2009) Femtosecond Fluorescence Spectra of Tryptophan in Human gamma-Crystallin Mutants: Site-Dependent Ultrafast Quenching. J.Am.Chem.Soc., in press.
204. Drahos, Kate and King, Jonathan (2009) Hydrophobic Core Mutations Associated with Cataract Development in Mice Destabilize Human gammaD-Crystallin. J.Biol.Chem, in press.
205.
Das, P., King, J.A. and Zhou, R. (2009) Interdomain interactions play a crucial role in folding and aggregation
of gammaD-crystallin. Protein Science, submitted.
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