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Lens Crystallins

Protein Aggregation & Misfolding

 

Formation of amyloid fribrils in vitro by human gamma D-crystallin and its isolated domains. Papanikolopoulou, K., Mills, I.A., Flaugh, S.L.., Wang, Y., Gross, A.A.R., Kirschner, D.A., Decatur, S.M. and King, J.A. (2008) Molecular Vision, 14, 81-89. http://www.molvis.org/molvis/v14/a10

Aggregation of graulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state. Raso, S.W., Abel, J., Barnes, J.M., Maloney, K.M., Pipes, G., Treuheit, M.J., King, J. and Brems, D.N. (2005) Protein Science, 14, 2246-2257.

Crystal cataracts: Human genetic cataract caused by protein crystallization. Pande. A., Pande, J., Asherie, N., Lomakin, A., Ogun, O., King, J., and Benedek, G.B. (2001) PNAS,98, 6116-6120.

Enhanced Crystallization of the Cys18 to Ser Mutant of Bovine B Crystallin. Asherie, N., Pande, J., Pande, A., Zarutskie, J.A., Lomakin, J., Lomakin, A., Ogun, O., Stern, L.J., King, J., Benedek, G.B. (2001) J. Mol.Biol., 314, 663-669.

Molecular basis of a progresssive juvenile-onset hereditary cataract. Pande, A., Pande, J., Aserie, N., Lomakin, A., Ogun, O., King, J., Lubsen, N., Walton, D. & Benedek, G. (2000) PNAS, 97, 1993-1998.

"Protein folding and human disease." Raso, S.W. and King, J. (2000) In, Frontiers in Molecular Biology: Mechanisms of Protein Folding, 2nd Edition (ed. R.H. Pain), Oxford University Press, 406-428. No abstract available.

Lattice simulations of aggregation funnels for protein folding. Istrail, S., Schwartz, R. and King, J. (1999) J. of Computational Biology, 6, 143-162.

There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike. Betts, S. and King, J. (1999) Structure, 7, R131-R139.
"Detection of early aggregation intermediates by native gel electrophoresis and native western blotting." Betts, S., Speed, M. and King, J. (1999) In, Amyloid, Prions, and Other Protein Aggregates (ed. R. Wetzel), Vol. 309 of "Methods in Enzymology," Academic Press, pp. 333-350. No abstract available.

Investigating temperature effects on refolding and aggregation of a large multimeric protein using capillary zone electrophoresis. Jensen, P.K., King, J. and Lee, C.S. (1998) Analytical Chemistry, 70, 730-736.

Cold rescue of the thermolabile tailspike intermediate at the junction between producitve folding and off-pathway aggregation. Betts, S. and King, J. (1998) Protein Sci., 7, 1516-1523.

The effects of Oxygen on Recombinant Protein Expression. Konz, J.O., King, J. and Cooney, C.L. (1998) Biotech. Progress, 14, 393-409.
 

Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Speed, M., Morshead, T., Wang, D. and King, J. (1997) Protein Science, 6, 99-108.

Polymerization Mechanism of Polypeptide Chain Aggregation." Speed, M., King, J. and Wang, D.I.C. (1997) Biotechnology and Bioengineering, 54, 333-343.

"Mutational effects on inclusion body formation." Betts, S., Haase-Pettingell, C., and King, J. (1997) In, Protein Misassembly (ed. R. Wetzel), Volume 50 of "Advances in Protein Chemistry," Academic Press, pp 243-264. No abstract available.

Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Speed, M., Wang, D. and King, J. (1996) Nature Biotechnology, 14, 1283-1287.

Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates. King, J., Haase-Pettingell, C., Robinson, A., Speed, M. A. and Mitraki, A. (1996) FASEB Journal, 10, 57-66.

Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Speed, M.A., Wang, D.I.C. and King, J. (1995) Protein Science, 4, 900-908.

"Protein misfolding and inclusion body formation in prokaryotes." King, J., Teschke, C.M., Haase-Pettingell, C. and Mitraki, A. (1993) 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. No abstract available.

Identifaction of global suppressors for temperature sensitive folding mutants of the P22 tailspike protein. Fane, B., Villafane, R., Mitraki, A., and King, J. (1991) J. Biol. Chem., 266, 11640-11648.

Global suppression of protein folding defects and inclusion body formation. Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J. and King, J. (1991) Science, 253, 54-58.

"Mechanisms of inclusion body formation." Mitraki, A., Haase-Pettingell, C., and King J. (1991) In Protein Refolding (G. Georgiou & E. de Bernardez-Clark, eds.) ACS Sympsosium Seris 470, American Chemical Society, Washington, D.C., pp. 35-49

"Mutations affecting protein folding and misfolding in vivo." Mitraki, A., Fane, B., Haase-Pettingell, C. and King, J. (1991) In Application in Enzyme Biotechnology (eds. T. Baldwin and J. Kelly) Plenum Press, pp. 129-136. No abstract available.

"Genetic analysis of polypeptide chain folding and misfolding in vivo." King, J., Fane, B., Haase-Pettingell, C., Mitraki, A. and Villafane, R. (1990) 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. No abstract available.

Protein folding intermediates and inclusion body formation. Mitraki, A. and King, J. (1989) Bio/technology, 7, 690-697.

Aggregate Formation from a Thermolabile Intermediate in the Maturation of the Thermostable P22 Tailspike Protein. King, J. and Haase-Pettingell, C. (1988) British Biochem. Society Transactions, 16(2), 105-108. No abstract available.

Formation of aggregates from a thermolabile in Vivo folding intermediate in P22 tailspike maturation: Model for inclusion body formation. Haase-Pettingell, C. and King, J. (1988) J. Biol. Chem., 263(10), 4977-4983.

Lens Crystallins

Formation of amyloid fribrils in vitro by human gamma D-crystallin and its isolated domains. Papanikolopoulou, K., Mills, I.A., Flaugh, S.L.., Wang, Y., Gross, A.A.R., Kirschner, D.A., Decatur, S.M. and King, J.A. (2008) Molecular Vision, 14, 81-89. http://www.molvis.org/molvis/v14/a10

Folding and stability of the isolated greek key domains of the long-lived human lens proteins, gamma D-crystallin and gamma S-crystallin. Mills, I.A., Flaugh, S.L., Kosinski-Collins, M.S. and King, J. (2007) Protein Science, 16, 2427-2444.

Glutamine deamidation destabilizes human gammaD-crystallin and lowers the kinetic barrier to unfolding. Flaugh, S.L., Mills, I.A. and King, J. (2006) J.Biol.Chem., 281, 30782-30793.

Mechanism of the highly efficient quenching of tryptophan fluorescence in human gammaD-crystallin. Chen, J., Flaugh, S.L., Callis, P.R. and King, J. (2006) Biochemsitry, 45, 11552-11563.

Interdomain side-chain interactions in human gammaD crystallin influencing folding and stability. Flaugh, S.L., Kosinski-Collins, M.S. and King, J (2005) Protein Science, 14, 2030-2043.

Contributions of hydrophobic domain interface interactions to the folding and stability of human gammaD-crystallin. Flaugh, S.L., Kosinski-Collins, M.S. and King, J (2005) Protein Science, 14, 569-581.

Probing folding and fluorescence quenching in Human gamma-D crystallin Greek key domains using Triple Tryptophan mutant proteins. Kosinski-Collins, M., Flaugh, S. & King, J. (2004) Protein Science, 13, 2223-2235.

In vitro unfolding and refolding of human gamma-D crystallin, a protein involved in cataract formation. Kosinski-Collins, M. & King, J. (2003) Protein Science, 12, 480-490.

Crystal cataracts: Human genetic cataract caused by protein crystallization. Pande. A., Pande, J., Asherie, N., Lomakin, A., Ogun, O., King, J., and Benedek, G.B. (2001) PNAS,98, 6116-6120.

Enhanced Crystallization of the Cys18 to Ser Mutant of Bovine B Crystallin. Asherie, N., Pande, J., Pande, A., Zarutskie, J.A., Lomakin, J., Lomakin, A., Ogun, O., Stern, L.J., King, J., Benedek, G.B. (2001) J. Mol.Biol., 314, 663-669.

Molecular basis of a progresssive juvenile-onset hereditary cataract. Pande, A., Pande, J., Aserie, N., Lomakin, A., Ogun, O., King, J., Lubsen, N., Walton, D. & Benedek, G. (2000) PNAS, 97, 1993-1998.

Virus Structure & Assembly

Backbone structure of the infectious e 15 virus capsid revealed by electron cryomicroscopy. Jiang, W., Baker, M.L., Jakana, J., Weigele, P.R., King, J. and Chiu, W. (2008) Nature, 451, 1130-1135.

Genomic and structural analysis of Syn9, a cyanophage infecting marine Prochlorococcus and Synechococcus. Weigele, P.R., Pedulla, M.L., Houtz, J.M., Smith, A.L., Conway, J.F., King, J., Hatfull, G.F., Lawrence, J.G. and Hendrix, R.W. (2007) Environ. Microbiol., 9, 1675-1695.

Genome sequence, structural proteins and capsid organization of the Cyanophage Syn5: A "Horned" bacteriophage of marine Synechococcus. Pope, W.H., Weigele, P.R., Chang, J., Pedulla, M.L., Ford, M.E., Houtz, J.M., Jiang, W., Chiu, W., Hatfull, G.F., Hendrix, R.W., and King, J. (2007) J. Mol. Biol., 368, 966-981.

Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Chang, J., Weigele, P., King, J., Chiu, W. and Jiang, W. (2006) Structure, 14, 1073-1082.

Structure of complete Epsilon 15 phage reveals organization of condensed DNA and DNA packaging/injection apparatus. Jiang, W., Chang J., Jakana, J., Weigele, P., King, J. and Chiu, W. (2006) Nature, 439, 612-616. [Download two supplements to the article. The first is in Word; second is in Powerpoint. Read a review in Microbe (ASM News), vol. 1, no. 4 (2006) by David Holzman.]

Lattice transformations and subunit conformational changes in phage capsid maturation. Gossard, D.C and King, J. (2005) J. of Theoretical Med., 6, 99-105.

Protein folding failure sets the high temperature limit on the growth of phage P22 in Salmonella serovar Typhimurium. Pope, W., Haase-Pettingell, C. and King, J. (2004) Applied & Environmental Microbiology, 70, 4840-4847.

Homo-trimeric, ß-stranded viral adhesins and tail proteins. Weigele, P.R., Scanlon, E. and King, J. (2003) J. Bacteriology, 185, 4022-4030.

Separating lysozyme from bacteriophage P22 in two-phase aqueous micellar systems. Kamei, D., King, J., Wang, D.I.C. & Blankschtein, D. (2002) Biotech & Bioeng, 80, 233-236.

Undertanding viral partitioning in two-phase aqueous nonionic micellar systems: 1. role of attractive interatctions between viruses and micelles. Kamei, D., Liu, C., Haase-Pettingell, C., King, J., Wang D.I.C. & Blancschtein, D. (2002) Biotech & Bioeng.,78, 190-202.

Understanding viral partitioning in two-phase aqueous nonionic micellar systems: 2.Effect of entrained micelle-poor domains. Kamei, D., Liu, C., Haase-Pettingell, C., King, J., Wang, D.I.C. & Blankschtein, D. (2002) Biotech & Bioeng, 78, 203-21

Visualization fo the maturation transition in bacteriophage P22 electron cryomicroscopy. Zhang,Z., Greene, B., Thuman-Commike, P.A., Jakana, J., Prevelige, P.E., King, J. and Chiu , W.(2000) J. Mol Biol., 297, 615-626.
Local Rule Mechanism for Selecting Icosahedral Shell Geometry. Bonnie Berger and J. King and R. S. Schwartz and Peter W. Shor (2000) Discrete Applied Mathematics, 105, 55-69.

In vitro unfolding/refolding of wild type phage P22 scaffolding protein reveals capsid binding domain. Greene, B. and King, J. (1999) J. Biol. Chem., 274, 16135-16140.
 
Folding and stability of mutant scaffolding proteins defective in phage capsid assembly. Greene, B. and King, J. (1999) J. Biol.Chem., 274, 16141-16146.
 
Solution X-ray scattering based estimation of electron cryomicroscopy imaging parameters for reconstruction of virus particles. Thuman-Commike, P.A., Tsuruta, H., Greene, B., Prevelige, P.E., King, J. and Chiu, W. (1999) Biophysical J., 76, 2249-2261.
 
Role of the Scaffolding Protein in P22 Procapsid Size Determination Suggested by T=4 and T=7 Procapsid Structures. Thuman-Commike, P.A., Greene, B., Malinski, J., King, J. and Chiu, W. (1998) Biophysical J., 74, 559-568.

Separation of proteins and viruses using two-phase aqueous micellar systems. Liu, C., Kamei, D.T., King, J., Wang, D.I.C. and Blankschtein, D. (1998) J. Chromatogr. B, 711(1-2), 127-138.

"The Procapsid to Capsid Transition in Double-stranded DNA Bacteriophages." King, J. and Chiu, W. (1997) In Structural Biology of Viruses (W. Chiu, R.M. Burnett and R. Garcea, eds.) Oxford University Press, pp. 288-311. No abstract available.

Three-dimensional Structure of Scaffolding-containing Phage P22 Procapsids by Electron Cryo-microscopy. Thuman-Commike, P., Greene, B., Jakana, J., Prasad, B.V.V., King, J., Prevelige, P.E., Chiu, W. (1996) J. Mol. Biol., 260, 85-98.

Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation. Greene, B. and King, J. (1996) Virology, 225, 82-96.

Role of entropic interactions in viral capsids: Single amino acid substitutins in P22 bacteriophage coat protein resulting in loss of capsid stability. Foguel, D., Teschke, C.M., Prevelige, Jr., P.E. and Silva, J.L. (1995) Biochem., 34, 1120-1126.

A local rule based theory of virus shell assembly. Berger, B, Shor, P.W., Tucker-Kellogg, L. and King, J. (1994) Proceedings of the National Academy of Sciences, 91, 7732-7736.

Binding of Scaffolding Subunits Within the P22 Procapsid Lattice. Greene, B. and King, J. (1994) Virology, 205, 188-197.

Pressure denaturation of the bacteriophage P22 coat protein and its entropic stabilization in icosahedral shells. Prevelige PE Jr, King J, Silva JL (1994) Biophys J., 66(5), 1631-1641.

Nucleation and Growth Phases in the Polymerization of Coat and Scaffolding Subunits into Icosahedral Procapsid Shells. Prevelige, P., Thomas, D. and King, J. (1993) Biophysical Journal, 64, 824-835.

"Assembly of Bacteriophage P22: A Model for sd-DNA Virus Assembly." Prevelige, P. & King, J. (1993) In: Progress in Medical Virology, Vol. 40 (ed. J.L. Melnick) Karger, Basel, pp. 206-221. No abstract available.

Temperature Sensitive Mutations in the P22 Coat Protein Which Interfere with Polypeptide Chain Folding. Gordon, C. and King, J. (1993) J. Biol. Chem., 268, 9358-9368.

Three Dimensional Transformation of Capsids Associated with Genome Packaging in a Bacterial Virus. Prasad, B.V., Prevelige, P., Marietta, E., Chen, R., Thomas, D., King, J. and Chiu, W. (1993) J. Mol. Biol., 231, 65-74.

Conformational Transformations in the Protein Lattice of Phage P22 Procapsids. Galisteo, M.L. and King, J. (1993) Biophysical Journal, 65, 227-235.

Folding of the Phage P22 Coat Protein in vitro. Teschke, C. and King, J. (1993) Biochemistry, 32, 10839-10847.

Inhibition of capsid assembly by 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid. Teschke, C.M., King, J. and Prevelige, P.E., Jr. (1993) Biochemistry, 32, 10658-10665.

A pilot protein participates in the initiation of P22 procapsid assembly. Thomas, D., and Prevelige, P. Jr. (1991)Virology, 182, 673-681.

Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly. Prevelige, P. E. Jr., Thomas, D., King, J., Towse, S. A., and Thomas, G. J. Jr. (1990) Biochem., 29, 5626-5633.

Novel second-site suppression of cold-sensitive defect in phage P22 procapsid assembly. Bazinet, C., Villafane, R. and King, J. (1990) J. Mol. Biol., 216, 701-716.

Purification and Organization of the Gene l Portal Protein Required for Phage P22 DNA Packaging Bazinet, C., Benbaset, J, King, J., Carazo, J. and Carrascosa, J. (1988) Biochem., 27, 1849-l856.

Initiation of P22 Procapsid Assembly in vivo. Bazinet, C., and King, J. (l988) J. Mol. Biol., 202, 77-86.

Scaffolding Protein Regulates the Polymerization of P22 Coat Subunits into Icosahedral Shells in vivo. Prevelige, P., Thomas, D. and King, J. (1988). J. Mol. Biol., 202: 743-757.

Identification of the 9-aminoacridine/DNA complex responsible for photodynamic inactivation of P22. Loechler, E.L. and King, J. (1986) Biochemistry, 25(20), 5858-64.

DNA injection apparatus of phage P22. Hartweig, E., Bazinet, C. and King, J. (1986) Biophys. J., 49, 24-26. No abstract available.

A late gene product of phage P22 affecting virus infectivity. Bazinet, C.W. and King, J. (1985) Virology, 143(2), 368-79.

The DNA translocating vertex of dsDNA bacteriophage. Bazinet, C. and King, J. (1985) Ann. Rev. Microbiol., 39, 109-129. No abstract available.

Assembly-controlled autogenous modulation of bacteriophage P22 scaffolding protein gene expression. Casjens, S., Adams, M.B, Hall, C. and King, J. (1985) J Virol, 53(1), 174-9.

DNA injection proteins are targets of acridine-sensitized photoinactivation of bacteriophage P22. Bryant, J.L., Jr. and King, J. (1984) J Mol Biol., 180(4), 837-63.

Steps in the stabilization of newly packaged DNA during phage P22 morphogenesis. Strauss, H. and King, J. (1984) J Mol Biol, 172(4), 523-43.

Structural studies of P22 phage, precursor particles, and proteins by laser Raman spectroscopy. Thomas, GJ, Jr., Li, Y, Fuller, MT and King, J. (1982) Biochemistry, 21(16), 3866-3878.

Assembly in Vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits. Fuller, MT and King, J. (1982) J Mol Biol., 156(3), 633-665.

Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22. Fuller, MT and King, J. (1981) Virology, 112(2), 529-547.

New genes in the left arm of the bacteriophage ø80 Chromosome. Youderian, P. and King J. (1981) J. Virology, 37, 976-986.

Investigations of bacteriophage P22 by laser Raman spectroscopy. Li, Y., Thomas, GJ, Jr., Fuller, MT and King, J. (1981) In: Bacteriophage Assembly (M. Dubow, ed) Alan R. Liss, Inc., NY, pp. 271-283.

Genetic control of organelle assembly at the molecular level: I. Introduction: from genes to organelles. J. King (1980) In: The Quarterly Review of Biology, vol 55, no. 4. The Stony Brook Foundation, NY, pp. 329-333. No abstract available.

Scaffolding proteins and the genetic control of virus shell assembly. King, J., Griffin-Shea, R. and Fuller, MT (1980) Q Rev Biol., 55(4), 369-93.

Investigation of secondary structures and macromolecular interactions in bacteriophage P22 by laser Raman spectoscopy. Fish, S.R., Hartman, K.A., Fuller, M.T., King, J. and thomas, G.J., Jr. (1980) Biophysical J., 32, 234-237.

Regulation of coat protein polymerization by the scaffolding protein of bacteriophage P22. Fuller, MT and King, J. (1980) Biophys J., 32(1), 381-401.

Regulation of structural protein interactions as revealed in phage morphogenesis. J. King (1980) In: Biological Regulation and Development, Vol. 2 (ed. R. F. Goldberger) Plenum Publishing Corp., pp. 101-132. No abstract available.

Genetic control of complex bacteriophage assembly. Wood, W.B. & King, J. (1979) In: Comprehensive Virology, vol 13: Structure & Assembly: Primary, Secondary, Tertiary, and Quaternary Structures (H. Fraenkel-Conrat and R.R. Wagner, eds.) Plenum Press, NY, pp. 581-633. No abstract available.

Structural studies of bacteriophage Lambda heads and proheads by small angle x-ray diffraction. Earnshaw, W.C., Hendrix, R.W. and King, J. (1979) J. Mol. Biol., 134, 575-594.

Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein. Earnshaw, W. and King, J. (1978) J Mol Biol., 126(4), 721-747.

Control of the synthesis of phage P22 scaffolding protein is coupled to capsid assembly. King, J., Hall, C. and Casjens, S. (1978) Cell, 15(2), 551-560.

Isolation and characterization of precursors in T4 baseplate assembly: The complex of gene 10 and gene 11 products. Berget, PB and King, J. (1978) J Mol Biol,. 124(3), 469-486.

The structural organization of DNA packaged within the heads of T4 wild-type, isometric and giant bacteriophages. Earnshaw WC, King J, Harrison SC, Eiserling FA (1978) Cell,14(3), 559-568.

The size of the bacteriophage T4 head in solution with comments about the dimension of virus particles as visualized by electron microscopy. Earnshaw WC, King J and Eiserling, FA (1978) J Mol Biol., 122(2), 247-253.

Antigenic gene products of bacteriophage T4 baseplates. Berget, PB and King, J. (1978) Virology, 86(2), 312-328.

Functions of two new genes in Salmonella phage P22 assembly. Poteete, AR and King, J. (1977) Virology, 76(2), 725-739.

Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4. Crowther, RA, Lenk, EV, Kikuchi, Y and King, J. (1977) J Mol Biol., 116(3), 489-523.

Structure and assembly of the capsid of bacteriophage P22. King J, Botstein D, Casjens S, Earnshaw W, Harrison S, Lenk E (1976) Philos Trans R Soc Lond B Biol Sci., 276, 37-49.

Assembly of the contractile tail of baceriophage T4. Kikuchi, Y. and King, J. (1976) Cell Motility, 71-91. No abstract available.

Intracellular visualization of precursor capsids in phage P22 mutant infected cells. Lenk, E., Casjens, S., Weeks, J. and King, J. (1975) Virology, 68(1), 182-99.

Genetic control of bacteriophage T4 baseplate morphogenesis. I. Sequential assembly of the major precursor, in vivo and in vitro. Kikuchi, Y and King, J. (1975) J Mol Biol., 99(4) 645-672.

Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate. Kikuchi, Y and King, J. (1975) J Mol Biol., 99(4) 673-694.

Genetic control of bacteriophage T4 baseplate morphogenesis. III. Formation of the central plug and overall assembly pathway. Kikuchi, Y and King, J. (1975) J Mol Biol., 99(4) 695-716.

Assembly of the tail of bacteriophage T4. Kikuchi, Y. and King, J. (1975) J Supramol Struct., 3(1), 24-38.

Virus Assembly. Casjens, S. and King, J. (1975) Ann. Rev. Biochemistry, 44, 555-611. No abstract available.

P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly. Casjens, S. and King, J. (1974) J Supramol Struct., 2(2-4), 202-24.

Catalytic head assembling protein in virus morphogenesis. King, J. and Casjens, S. (1974) Nature, 251, 112-119.

Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. II. Morphogenetic pathway. King, J., Lenk, EV and Botstein, D. (1973) J Mol Biol., 80(4), 697-731.

Mechanism of head assembly and DNA encapsulation in Salmonella phage p22. I. Genes, proteins, structures and DNA maturation. Botstein, D., Waddell, C.H. and King, J. (1973) J Mol Biol., 80(4), 669-695.

Bacteriophage T4 tail assembly: proteins of the sheath, core and baseplate. King, J. and Mykolajewycz, N. (1973) J Mol Biol., 75(2), 339-358.

Bacteriophage T4 tail assembly: structural proteins and their genetic identification. King, J. and Laemmli, U.K. (1973) J Mol Biol., 75(2), 315-337.

Genetic control of T4 tail assembly. King, J., Fitten, R., Mykolajewycz, N. and Floor, E. (1973) In: Virus Research (C.F. Fox and W.S. Robinson, eds.) Acdemic Press, NY, pp 259-277.

Polypeptides of the tail fibres of bacteriophage T4. King, J. and Laemmli, U.K. (1971) J Mol Biol. 62(3), 465-477.

Bacteriophage T4 tail assembly: four steps in core formation. King, J. (1971) J Mol Biol., 58(3), 693-709.

Steps in T4 tail core assembly. King, J. (1970) FEBS Symposium, 21, 171-180.

Assembly of bacteriophage T4 tail fibers: the sequence of gene product interaction. King, J and Wood, W.B. (1969) J Mol Biol., 39(3), 583-601.

Bacteriophage assembly. Wood, W.B., Edgar, R.S., King, J., Lielausis, I. and Henniger, M. (1968) Fed. Proc, 27, 1160-1166. No abstract available.

Assembly of the tail of bacteriophage T4. King, J. (1968) J Mol Biol., 32(2), 231-262. No abstract available.

Protein Folding & Stability

 

An elongated spine of buried core residues necessary for in vivo folding of the parallel b -helix of P22 tailspike adhesin. Simkovsky, R. and King, J. (2006) PNAS, 103, 3575-3580.

Stalled folding mutants in the triple beta-helix domain of the phage P22 tailspike adhesin. Weigele, P., Haase-Pettingell, C., Campbell, P.G., Gossard, D.C. and King, J. (2005) J.Mol.Biol., 354, 1103-1117.

Buried hydrophobic side chains essential for the folding of the parallel beta-helix domains of the P22 tailspike. Betts, S., Haase-Pettingell, C., Cook, K. and King, J. (2004) Protein Science, 13, 2291-2303.

Monoclonal epitope mapping describes tailspike beta-helix folding and aggregation intermediates. Jain, M., Evans, M.S., King, J. and Clark, P.L. (2005) J.Biol.Chem., 280, 23032-23040.

Homo-trimeric, ß-stranded viral adhesins and tail proteins. Weigele, P.R., Scanlon, E. and King, J. (2003) J. Bacteriology, 185, 4022-4030.

Protein Folding and Misfolding. King, J., Haase-Pettingell, C. & Gossard, D. (2002) American Scientist, 90, 445-453.

The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization. Kreisberg, J.F., Betts, S. D., Haase-Pettingell, C. and King, J. (2002) Protein Science, 11, 820-830.

Characterization of the protrimer intermediate in the folding pathway of the interdigitated ß-helix tailspike protein. Benton, C.B., Clark, P.L. and King, J. (2002) Biochemistry,41, 5093-5103.

A newly synthesized, Ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates. Clark, P.L. and King, J. (2001) J. Biol. Chem., 276, 25411-25420

ß-helix core packing within the triple-stranded oligomerizatin domain of the P22 tailspike. Kreisberg, J.F., Betts, S.D. & King, J. (2000) Protein Science, 9, 2338-2343.
In vitro unfolding/refolding of wild type phage P22 scaffolding protein reveals capsid binding domain. Greene, B. and King, J. (1999) J. Biol. Chem., 274, 16135-16140.

Folding and stability of mutant scaffolding proteins defective in phage capsid assembly. Greene, B. and King, J. (1999) J. Biol.Chem., 274, 16141-16146.

There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike. Betts, S. and King, J. (1999) Structure, 7, R131-R139.

A green light for protein folding. King, J. and Betts, S. (1999) Nature Biotech., 17, 637-638. No abstract available.

Cold rescue of the thermolabile tailspike intermediate at the junction between producitve folding and off-pathway aggregation. Betts, S. and King, J. (1998) Protein Sci., 7, 1516-1523.

The effects of Oxygen on Recombinant Protein Expression. Konz, J.O., King, J. and Cooney, C.L. (1998) Biotech. Progress, 14, 393-409.
Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Speed, M., Morshead, T., Wang, D. and King, J. (1997) Protein Science, 6, 99-108.

Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase. Haase-Pettingell, C. and King, J. (1997) J. Mol. Biol., 267, 88-102.

Refolding with a piece of the ring. King, J. (1997) Nature Biotechnology, 15, 514-515. No abstract available.

Disulfide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein. Robinson, A.S. and King, J. (1997) Nature Structural Biol., 4, 450-455.

Monitoring the refolding pathway for a large multimeric protein using capillary zone electrophoresis. Fan, Z.H., Jensen, P.K., King, J. and Lee, C.S. (1997) J. Chromatography, 769, 315-323.

Unexpected Pathways to protein stabilization. King, J. (1996) Nature Biotechnology, 14, 436. No abstract available.

Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates. King, J., Haase-Pettingell, C., Robinson, A., Speed, M. A. and Mitraki, A. (1996) FASEB Journal, 10, 57-66.

In Vitro folding of phage P22 coat protein with amino acid substitutions that confer in vivo tempertaure-sensitivity. Teschke, C.M. and King, J. (1995) Biochemistry, 34, 6815-6826.

Stability of wild-type and temperature-sensitive protein subunits of the phage P22 capsid. Galisteo, M.L., Gordon, C.L. and King, J. (1995) Biol. Chem., 270, 16595-16601.

Genetic properties of temperature sensitive folding mutants of the coat protein of phage P22. Gordon, C. and King, J. (1994) GENETICS, 136, 427-438.

In Vitro and ribosome bound folding intermediates of P22 tailspike protein detected with monoclonal antibodies. Friguet, B., Djavadi-Ohaniance, L., King, J. and Goldberg, M. (1994) J. Biol. Chem., 269, 15945-15949.

Intracellular Trapping of a Cytoplasmic folding Intermediate of the Phage P22 Tailspike Using Iodoacetamide. Sather, S. and King, J. (1994) J. Biol. Chem., 269, 25268-25276.

Selective In Vivo Rescue by GroEL/ES of Thermolabile Folding Intermediates of Phage P22 Structural Proteins. Gordon, C., Sather, S., Casjens, S. and King, J. (1994) J. Biol. Chem., 269, 27941-27951.

"Amino Acid Sequence Determinants of Polypeptide Chain Folding and Inclusion Body Formation." King, J., Haase-Pettingell, C., Gordon, C., Sather, S. and Mitraki, A. (1993) In Protein Folding: In Vivo and In Vitro (ed. J. Cleland) ACS Symposium Series 526, American Chemical Society, Washington, D.C., pp. 24-37.

Temperature Sensitive Mutations in the P22 Coat Protein Which Interfere with Polypeptide Chain Folding. Gordon, C. and King, J. (1993) J. Biol. Chem., 268, 9358-9368.

The Unfolding Puzzle of Protein Folding. King, J. (1993) Technology Review, 96(4), 54-61. No abstract available.

Folding of the Phage P22 Coat Protein in vitro. Teschke, C. and King, J. (1993) Biochemistry, 32, 10839-10847.

Temperature-sensitive Mutations and Second-site Suppressor Substitutions Affect Folding of the P22 Tailspike Protein in Vitro. Mitraki, A., Danner, M., King, J. and Seckler, R. (1993) J. Biol. Chem, 268, 20071-20075.

Amino acid substitutions influencing intracellular protein folding pathways. Mitraki, A. and King, J. (1992) FEBS Letters, 307, 20-25.

Folding and assembly of oligomeric proteins in Escherichia coli. Teschke, C. and King, J. (1992) Current Opinion in Biotechnology, 3, 468-473.

Intragenic suppressors of folding defects in the P22 tailspike protein. Fane, B. and King, J. (1991) Genetics, 127, 263-277.

Thermal unfolding pathway for the thermostable P22 tailspike endorhamnosidase. Chen, B. and King J. (1991)Biochemistry, 30, 6260-6269.

Identifaction of global suppressors for temperature sensitive folding mutants of the P22 tailspike protein. Fane, B., Villafane, R., Mitraki, A., and King, J. (1991) J. Biol. Chem., 261, 11640-11648.

Global suppression of protein folding defects and inclusion body formation. Mitraki, A., Fane, B., Haase-Pettingell, C., Sturtevant, J. and King, J. (1991) Science, 253, 54-58.

"Pathway for the thermal unfolding of wild type and mutant forms of the thermostable P22 tailspike endorhamnosidase." Chen, B. and King, J. (1991) In Protein Refolding (G. Georgiou & E. de Bernardez Clark, eds.) ACS Symposium Series 470, American Chemical Society, Washington, D.C., pp. 119-132.

"Mutations affecting protein folding and misfolding in vivo." Mitraki, A., Fane, B., Haase-Pettingell, C. and King, J. (1991) In Application in Enzyme Biotechnology (eds. T. Baldwin and J. Kelly) Plenum Press, pp. 129-136. No abstract available.

"Genetic analysis of polypeptide chain folding and misfolding in vivo." King, J., Fane, B., Haase-Pettingell, C., Mitraki, A. and Villafane, R. (1990) 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. No abstract available.

Conformational stability of P22 Tailspike Proteins Carrying Temperature Sensitive Folding Mutations. Thomas, G. J. Jr., Becka, R., Sargent, D., Yu, M-H, and King, J. (1990) Biochem., 29, 4181-4187.

Properties of monoclonal antibodies selected for probing the conformation of wild type and mutant forms of the P22 tailspike endorhamnosidase. Friguet, B., Djavadi-Ohaniance, L., Haase-Pettingell, C., King, J., and Goldberg, M. (1990) J. Biol. Chem., 265, 10347-10351.

Protein Folding: Deciphering the Second Half of the Genetic Code. Gierasch, L. A. and King, J. (1990) American Association for the Advancement of Science, Wash. D.C.

"Identification of amino acid sequences influencing intracellular folding pathways using temperature sensitive folding mutations." King, J., Fane, B., Haase-Pettingell, C., Mitraki, A., Villafane, R., and Yu, M-H. (1990) In Protein Folding: Deciphering the Second Half of the Genetic Code (L. A. Gierasch and J. King, eds.) AAAS, pp 225-240. No abstract available.

Protein folding intermediates and inclusion body formation. Mitraki, A. and King, J. (1989) Bio/technology, 7, 690-697.

Thermostability of temperature sensitive folding mutants of the P22 tailspike protein. Sturtevant, J., Yu, M-H, Haase-Pettingell, C. and King, J. (1989) J. Biol. Chem., 264, 10693 - 10698.

Deciphering the rules of protein folding. King, J. (1989) Chem. & Eng. News, 67, April 11, 32-54. No abstract available.

Reconstitution of the thermostable trimeric phage P22 tailspike protein from denatured chains in vitro. Seckler, R., Fuchs, A. King, J. and Jaenicke, R. (1989). J. Biol. Chem., 264, 11750-11753.

Surface Amino Acids as Sites of Temperature Sensitive Folding Mutations in the P22 Tailspike Protein Yu, M-h. and King, J. (1988) J. Biol. Chem., 263( 3), 1424-131.

Secondary Structure and Thermostability of the Phage P22 Tailspike: Analysis by Raman Spectroscopy of the Wild-Type Protein and a Temperature-Sensitive Folding Mutant. Sargent, D., Benevides, J. M., Yu, M-h., King, J. and Thomas, Jr., G. J. (1988) J. Mol. Biol., 199, 491-502.

Nature and Distribution of Sites of Temperature Sensitive Folding Mutations in the Gene for the P22 Tailspike Polypeptide Chain. Villafane, R. and King, J. (1988) J. Mol. Biol., 204, 607 - 619.

Temperature-sensitive mutations affecting kinetic steps in protein-folding pathways. King, J., Haase, C. and Yu, M-H (1987) In: Protein Engineering: Tutorials in molecular and cell biology (ed. D.L. Oxender and C.F. Fox)Alan R. Liss, Inc., NY, pp 109-121. No abstract available.

Identification of sites influencing the folding and subunit assembly of the P22 tailspike polypeptide chain using nonsense mutations. Fane, B. and King, J. (1987) Genetics, 117(2), 157-71.

Electron microscopy of nickel-containing methanogenic enzymes: methyl reductase and F420-reducing hydrogenase. Wackett, L.P., Hartwieg, E.A., King, J.A., Orme-Johnson, W.H. and Walsh, C.T. (1987) J. Bacteriol., 169, 718-727.

Genetic analysis of protein folding pathways. King, J. (1986) Bio/Technology, 4, 297-303.
Genetic identification of amino acid sequences infuencing protein folding. King, J., Yu, M-H., Siddiqi, J. and Haase, C. (1986) In: Protein Engineering: Applications in Science, Medicine, and Industry (ed. M. Inouye & R. Sarma) Academic Press, Inc., NY, pp 275-291. No abstract available.

Mutational analysis of protein folding pathways: the P22 tailspike endorhamnosidase. King, J. and Yu, M-H (1986) Methods Enzymol, 131, 250-66. No abstract available.
Single amino acid substitutions influencing the folding pathway of the phage P22 tailspike endorhamnosidase. Yu, M-H and King, J. (1984) Proc Natl Acad Sci U S A, 81(21), 6584-8.

Use of temperature sensitive mutants to dissect pathways of protein folding and subunit interaction. Smith, D.H., Goldenberg, D.P. and King, J. (1984) In:The Protein Folding Problem (ed. Donald B. Wetlaufer) AAAS Selected Symposium 89, pp 115-143. No abstract available.

Genetic analysis of the folding pathway for the tail spike protein of phage P22. Goldenberg, DP, Smith, DH and King, J. (1983) Proc Natl Acad Sci U S A., 80(23), 7060-4.

Genetic and biochemical anaylsis of in vivo protein folding and subunit assembly. Goldenberg, D.P., Smith, D.H. and King, J. (1983) Biopolymers, 22, 125-129.

Maturation of the tail spike endorhamnosidase of Salmonella phage P22. Goldenberg, DP, Berget, PB and King, J. (1982) J Biol Chem., 257(13), 7864-7871.

Trimeric intermediate in the in vivo folding and subunit assembly of the tailspike endorhamnosidase of bacteriophage P22. Goldenberg, D. and King, J. (1982) Proc Natl Acad Sci U S A, 79(11), 3403-3407.

Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tailspike protein. III. Inactive polypeptide chains synthesized at 39 degrees. C. Smith, DH and King, J. (1981) J Mol Biol., 145(4), 653-676.

Temperature-sensitive mutants blocked in the folding or subunit of the bacteriophage P22 tailspike protein. II. Active mutant proteins matured at 30° C. Goldenberg, DP and King, J. (1981) J. Mol Biol., 145(4), 633-651.

Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail-spike protein. I. Fine-structure mapping. Smith, DH, Berget, PB and King, J. (1980) Genetics, 96(2), 331-352.
 
 

Cysteine and Methionine

The reactivity and oxidation pathway of Cysteine 232 in Recombaninant human alpha1-Antitrypsin. Griffiths, S.W., King, J. & Cooney, C.L. (2002) J. Biol. Chem., 277, 25486-25492.
Distinct Cysteine sulfhydryl environments detected by analysis of Raman S-H markers of Cys –> Ser mutant proteins. Raso, S.W., Clark, P.L., Haase-Pettingell, C., King, J. and Thomas, G.J., Jr. (2001) J. Mol. Biol., 307, 899-911.

Role for Cysteine Residues in the In Vivo Folding and Assembly of the Phage P22 Tailspike. Cameron Haase-Pettingell, Scott Betts, Stephen W. Raso, Lisa Stuart, Anne Robinson and Jonathan King (2001) Protein Science, 10, 397-410.


Computational Biology

Fold recognition and accurate sequence-structure alignment of sequences directing beta-sheet proteins. McDonnell, A.V., Menke, M., Palmer, N., King, J., Cowen, L. and Berger, B. (2006) Proteins, 63, 976-985.

Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure. Schwartz, Russell and King, J. (2006) Protein Science, 15, 102-112.

Segmentation Conditional Random Fields (SCRFs): A New Approach for Protein Fold Recognition. Liu Y., Carbonell J. G., Weigele P. R., and Gopalakrishnan V. (2005) RECOMB 2005, 408-422.

Wrap and Pack: A new paradigm for beta structural motif recognition with application to recognizing beta trefoils. Menke, M., King, J., Berger, B. and Cowan, L. (2005) J. of Computational Biology, 12: 777-795.

Wrap and Pack: A New Paradigm for Beta Structural Motif Recognition with Application to Recognizing Beta Trefoils. Menke, M.,Scanlon, E., King, J., Berger, B. and Cowen, L. (2004) 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.

Predicting the Beta-helix fold from protein sequence data. Cowen, L., Bradley, P., Menke, M., King, J. and Berger, B. (2002) J. Comp. Biol., 9, 261-276.

BetaWrap: Successful prediction of parallel ß-helices from primary sequence reveals an association with many microbial pathogens. Bradley, P., Cowen, L., Menke, M., King, J. and Berger, B. (2001) PNAS, 98, 14819-14824.

"Predicting the Beta-Helix Fold from Protein Sequence Data." Bradley, P., Cowen, L.J., Menke, M., King, J. and Berger, B. (2001) In Proceedings of the Fifth Annual International Conference on Computational Molecular Biology, ACM Press, New York, pp. 59-67.

Frequencies of amino acid strings in globular protien sequences indicate suppression of blocks of consecutive hydrophobic residues. Schwartz, R., Istrail, S. And King, J. (2001) Protein Science, 10, 1023-1031.

Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life. Schwartz, R., Ting, C. and King, J. (2001) Genome Research, 11, 703-709.

Local Rule Mechanism for Selecting Icosahedral Shell Geometry. Bonnie Berger and J. King and R. S. Schwartz and Peter W. Shor (2000) Discrete Applied Mathematics, 105, 55-69.

Lattice simulations of aggregation funnels for protein folding. Istrail, S., Schwartz, R. and King, J. (1999) J. of Computational Biology, 6, 143-162.

A molecular thermodynamic model for helix-helix docking and protein aggregation. Chen, C-C., King, J. and Wang, D. (1995) AIChE Journal, 41, 1015-1024.

A local rule based theory of virus shell assembly. Berger, B, Shor, P.W., Tucker-Kellogg, L. and King, J. (1994) Proceedings of the National Academy of Sciences, 91, 7732-7736.

A molecular thermodynamic approach to predict the secondary structure of homo-polypeptides in aqueous systems. Chen, C.-C., Zhu, Y., King, J. and Evans, L. (1992) Biopolymers, 32, 1375-1392.

Molecular thermodynamic model to predict the alpha-helical secondary structure of polypeptide chains in solution. Zhu, Y., Chen, C.-C., King, J. and Evans, L. (1992) Biochemistry, 31, 10591-10601.

Photosynthetic Prokaryotes

 

Genomic and structural analysis of Syn9, a cyanophage infecting marine Prochlorococcus and Synechococcus. Weigele, P.R., Pedulla, M.L., Houtz, J.M., Smith, A.L., Conway, J.F., King, J., Hatfull, G.F., Lawrence, J.G. and Hendrix, R.W. (2007) Environ. Microbiol., 9, 1675-1695.

Genome sequence, structural proteins and capsid organization of the Cyanophage Syn5: A "Horned" bacteriophage of marine Synechococcus. Pope, W.H., Weigele, P.R., Chang, J., Pedulla, M.L., Ford, M.E., Houtz, J.M., Jiang, W., Chiu, W., Hatfull, G.F., Hendrix, R.W., and King, J. (2007) J. Mol. Biol., 368, 966-981.

Cyanobacterial photosynthesis in the oceans: the origins and significance of divergent light-harvesting strategies. Ting, C., Rocap, G., King, J. and Chisholm, S.W. (2002) Trends in Microbiology, 10, 134-142. [link is to PDF file.]

Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: Evidence for rapid evolution of genetic heterogeneity. Ting, C.S., Rocap, G., King, J. and Chisholm, S.W. (2001) Microbiology, 147, 3171-3182.

"Characterization of phycoerythrin genes in the chlorophyll a2/b2-containing prokaryote, Prochlorococcus sp. MIT9303." Ting, C., Rocap, G., King, J. and Chisholm, S.W. (1999) In: Photosynthesis: Mechanisms and Effects (G. Garab, ed.) Vol. I, Kluwer Academic Publishers, The Netherlands, pp. 225-228. No abstract available.

Soil microbial ecology of Wheeler Valley, Antarctica. Cameron, R.E., King, J. and David, C.N. (1970) Soil Science, 109, 110-120. No abstract available.

Microbiology, Ecology and microclimatology of soil sites in dry valleys of Southern Victoria Land, Antarctica. Cameron, R.E., King, J. and David, C.N. (1970) Antarctica Ecology, 2, 702-716. No abstract available.

Soil microbial and ecological studies in Southern Victoria Land. Cameron, R., King, J. and David, C. (1968) Antarctic J., July-August, 121-123. No abstract available.

Soil toxicity in Antarctic dry valleys. Cameron, R., David, C. and King, J. (1968) Antarctic J., Sept-Oct, 164-166. No abstract available.

Searching for life in Antarctica. David, C. and King, J. (1968) Engineering and Science, June, 14-18. No abstract available.


Biomedical Ethics, Integrity & Policy

The High Stakes in Science Education: Risking the Roots of American Productivity. King, J. (2007) Education Week, 26, pg. 34, 44.

"Environmental pollution and the emergence of new diseases." King, J. (2000) In, Environmental Evolution, 2nd Edition (ed. L. Margulis, C. Matthews & A. Haselton), MIT Press, pp 249-262. No abstract available.

"Biotechnology under globalisation: the corporate expropriation of plant, animal and microbial species." King, J. and Stabinsky, D. (1999) Race & Class, 40, 73-89. No abstract available.

"Patents on cells, genes, and organisms undermine the exchange of scientific ideas." King, J. and Stabinsky, D. (1999) The Chronicle of Higher Ed., Opinion & Arts, Feb. 5, 1999, pp. B6-B8. No abstract available.

The scientific endeavor is based on vigilance, not trust (commentary on Grinell). King J. (1999) Science & Eng. Ethics, 5, 215-217. No absract available.

Public resources, not corporate property. King, J. (1998) The Environmental Forum, 14, 40-41. No abstract available.

"The Biotechnology Revolution: Self-replicating Factories and the Ownership of Life Forms." King, J. (1997) In Cutting Edge: Technology, Information Capitalism and Social Revolution (J. Davis, T. Hirschl and M. Stack, eds.) Verso Press, pp 145-156. No abstract available.

"The end of work" and "The future before us". King, J. (1995) In: Job?Tech: The tecnological revolution and its impact on society. (Alkalimat, A., Gills, D. and Williams, K., eds.) Twenty-First Century Books and Publications, Chicago, IL, pp.22-26 and 52-58. No abstract available.

Patenting modified life forms: The case against. J. King (1982) Environment, 24, 38-41 & 57-58. No abstract available.

Science has always threatened values. J. King (1982) U.S. News & World Report, July 5, 48-49. No abstract available.

Arguments against patenting modified life forms. King, J. (1981) In: Patentability of Microorganisms: Issues and Questions. (R.F. Acker & M. Schaechter, eds) ASM, Washington, DC, pp. 36-41. No abstract available.

Biotechnology. King, J. and Orrego, C. In: McGraw-Hill Yearbook of Science and Technology 1980 Review/1981 Preview. No abstract available.

New diseases in new niches. J. King (1978) Nature, 276, 4-7. No abstract available. PDF at http://www.nature.com/nature/journal/v276/n5683/pdf/276004a0.pdf

Recombinant DNA and Autoimmune Disease. J. King (1978) J. Infectious Diseases, 137, 663 666. No abstract available.

Genetic Screening...Pitfalls. King, J., Beckwith, J. and Miller, L. (1976) The Science Teacher, Vol 43. No abstract available.

The XYY syndrome: a dangerous myth. Beckwith, J. and King, J. (1974) New Scientist,474-476.


 

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