Jonathan A. King - Publications

Affiliations: 
Biology Massachusetts Institute of Technology, Cambridge, MA, United States 
Area:
Protein Folding
Website:
https://biology.mit.edu/people/jonathan_king

135 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2020 King J, Henry IM, Kosinski-Collins M, Thol S, Serebryany E. Buried Tryptophans Contributing to the High Kinetic Stability of the Long-lived Gamma Crystallins and their Oxidative Damage Opening the Pathway to the Aggregated State Associated with Cataracts Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.1105  0.52
2019 Sergeeva OA, Haase-Pettingell C, King JA. Co-expression of CCT subunits hints at TRiC assembly. Cell Stress & Chaperones. PMID 31410727 DOI: 10.1007/S12192-019-01028-5  0.52
2018 Dai W, Chen M, Myers C, Ludtke SJ, Montgomery Pettitt B, King JA, Schmid MF, Chiu W. Visualizing Individual RuBisCO and its Assembly into Carboxysomes in Marine Cyanobacteria by Cryo-Electron Tomography. Journal of Molecular Biology. PMID 30138616 DOI: 10.1016/J.Jmb.2018.08.013  0.32
2017 Pereira JH, McAndrew RP, Sergeeva OA, Ralston CY, King JA, Adams PD. Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy. Scientific Reports. 7: 3673. PMID 28623285 DOI: 10.1038/S41598-017-03825-3  0.52
2017 Hryc CF, Chen DH, Afonine PV, Jakana J, Wang Z, Haase-Pettingell C, Jiang W, Adams PD, King JA, Schmid MF, Chiu W. Accurate model annotation of a near-atomic resolution cryo-EM map. Proceedings of the National Academy of Sciences of the United States of America. PMID 28270620 DOI: 10.1073/Pnas.1621152114  0.32
2016 Serebryany E, Woodard JC, Adkar BV, Shabab M, King JA, Shakhnovich EI. An internal disulfide locks a misfolded aggregation-prone intermediate in cataract-linked mutants of human γD-crystallin. The Journal of Biological Chemistry. PMID 27417136 DOI: 10.1074/Jbc.M116.735977  0.52
2016 Serebryany E, Takata T, Erickson E, Schafheimer N, Wang Y, King JA. Aggregation of Trp>Glu Point Mutants of Human Gamma-D Crystallin Provides a Model for Hereditary or UV-Induced Cataract. Protein Science : a Publication of the Protein Society. PMID 26991007 DOI: 10.1002/Pro.2924  0.52
2015 Pintilie G, Chen DH, Haase-Pettingell CA, King JA, Chiu W. Resolution and Probabilistic Models of Components in CryoEM Maps of Mature P22 Bacteriophage. Biophysical Journal. PMID 26743049 DOI: 10.1016/J.Bpj.2015.11.3522  0.32
2015 Quintanar L, Domínguez-Calva JA, Serebryany E, Rivillas-Acevedo L, Haase-Pettingell C, Amero C, King JA. Copper and zinc ions specifically promote non-amyloid aggregation of the highly stable human γ-D crystallin. Acs Chemical Biology. PMID 26579725 DOI: 10.1021/Acschembio.5B00919  0.52
2015 Serebryany E, King JA. Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant. The Journal of Biological Chemistry. 290: 11491-503. PMID 25787081 DOI: 10.1074/Jbc.M114.621581  0.52
2015 Gipson P, Baker ML, Raytcheva D, Haase-Pettingell C, Piret J, King JA, Chiu W. Corrigendum: Protruding knob-like proteins violate local symmetries in an icosahedral marine virus. Nature Communications. 6: 6040. PMID 25581040 DOI: 10.1038/Ncomms7040  0.32
2015 Rivillas-Acevedo L, Quintanar L, King J, Amero C. Real Time NMR Folding Study of the Human Gamma D Crystallin in the Presence of Metal Ions Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.320  0.52
2015 King JA, Sergeeva O, Knee KM. How Do Group Ii Chaperonins Distinguish their Partially Folded Substrates from the Native States Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.319  0.52
2014 Dai W, Schmid MF, King JA, Chiu W. Identifying the assembly pathway of cyanophage inside the marine bacterium using electron cryo-tomography. Microbial Cell. 1: 45-47. PMID 25419524 DOI: 10.15698/Mic2014.01.125  0.32
2014 Sergeeva OA, Tran MT, Haase-Pettingell C, King JA. Biochemical characterization of mutants in chaperonin proteins CCT4 and CCT5 associated with hereditary sensory neuropathy. The Journal of Biological Chemistry. 289: 27470-80. PMID 25124038 DOI: 10.1074/Jbc.M114.576033  0.52
2014 Gipson P, Baker ML, Raytcheva D, Haase-Pettingell C, Piret J, King JA, Chiu W. Protruding knob-like proteins violate local symmetries in an icosahedral marine virus. Nature Communications. 5: 4278. PMID 24985522 DOI: 10.1038/Ncomms5278  0.52
2014 Serebryany E, King JA. The βγ-crystallins: native state stability and pathways to aggregation. Progress in Biophysics and Molecular Biology. 115: 32-41. PMID 24835736 DOI: 10.1016/J.Pbiomolbio.2014.05.002  0.52
2014 Sergeeva OA, Yang J, King JA, Knee KM. Group II archaeal chaperonin recognition of partially folded human γD-crystallin mutants. Protein Science : a Publication of the Protein Society. 23: 693-702. PMID 24615724 DOI: 10.1002/Pro.2452  0.52
2014 Yang Z, Xia Z, Huynh T, King JA, Zhou R. Dissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins. Nanoscale. 6: 1797-807. PMID 24352614 DOI: 10.1039/C3Nr03782G  0.52
2014 Raytcheva DA, Haase-Pettingell C, Piret J, King JA. Two novel proteins of cyanophage Syn5 compose its unusual horn structure. Journal of Virology. 88: 2047-55. PMID 24307583 DOI: 10.1128/Jvi.02479-13  0.52
2014 Chiu W, Dai W, Fu C, Raytcheva D, Flanagan J, Khant HA, Liu X, Rochat RH, Haase-Pettingell C, Piret J, Ludtke SJ, Nagayama K, Schmid MF, King JA. Visualizing virus assembly intermediates inside marine cyanobacteria by zernike phase contrast electron cryo-tomography Microscopy and Microanalysis. 20: 202-203. DOI: 10.1017/S1431927614002736  0.52
2013 Dai W, Fu C, Raytcheva D, Flanagan J, Khant HA, Liu X, Rochat RH, Haase-Pettingell C, Piret J, Ludtke SJ, Nagayama K, Schmid MF, King JA, Chiu W. Visualizing virus assembly intermediates inside marine cyanobacteria. Nature. 502: 707-10. PMID 24107993 DOI: 10.1038/Nature12604  0.52
2013 Baker ML, Hryc CF, Zhang Q, Wu W, Jakana J, Haase-Pettingell C, Afonine PV, Adams PD, King JA, Jiang W, Chiu W. Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling. Proceedings of the National Academy of Sciences of the United States of America. 110: 12301-6. PMID 23840063 DOI: 10.1073/Pnas.1309947110  0.52
2013 Sergeeva OA, Chen B, Haase-Pettingell C, Ludtke SJ, Chiu W, King JA. Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers. The Journal of Biological Chemistry. 288: 17734-44. PMID 23612981 DOI: 10.1074/Jbc.M112.443929  0.52
2013 Xia Z, Yang Z, Huynh T, King JA, Zhou R. UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding. Scientific Reports. 3: 1560. PMID 23532089 DOI: 10.1038/Srep01560  0.52
2013 Zhu B, Tabor S, Raytcheva DA, Hernandez A, King JA, Richardson CC. The RNA polymerase of marine cyanophage Syn5. The Journal of Biological Chemistry. 288: 3545-52. PMID 23258537 DOI: 10.1074/Jbc.M112.442350  0.52
2013 Knee KM, Sergeeva OA, King JA. Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro. Cell Stress & Chaperones. 18: 137-44. PMID 23011926 DOI: 10.1007/S12192-012-0357-Z  0.52
2012 Moreau KL, King JA. Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone. Plos One. 7: e37256. PMID 22655036 DOI: 10.1371/Journal.Pone.0037256  0.52
2012 Moreau KL, King JA. Protein misfolding and aggregation in cataract disease and prospects for prevention. Trends in Molecular Medicine. 18: 273-82. PMID 22520268 DOI: 10.1016/J.Molmed.2012.03.005  0.52
2012 Carvalho CM, Kropinski AM, Lingohr EJ, Santos SB, King J, Azeredo J. The genome and proteome of a Campylobacter coli bacteriophage vB_CcoM-IBB_35 reveal unusual features. Virology Journal. 9: 35. PMID 22284308 DOI: 10.1186/1743-422X-9-35  0.52
2012 Pereira JH, Ralston CY, Douglas NR, Kumar R, Lopez T, McAndrew RP, Knee KM, King JA, Frydman J, Adams PD. Mechanism of nucleotide sensing in group II chaperonins. The Embo Journal. 31: 731-40. PMID 22193720 DOI: 10.1038/Emboj.2011.468  0.52
2012 Pereira JH, Ralston CY, Douglas NR, Kumar R, Lopez T, McAndrew RP, Knee KM, King JA, Frydman J, Adams PD. Mechanism of nucleotide sensing in group II chaperonins: Corrigendum The Embo Journal. 31: 3949-3950. DOI: 10.1038/Emboj.2012.245  0.52
2011 Das P, King JA, Zhou R. Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands. Proceedings of the National Academy of Sciences of the United States of America. 108: 10514-9. PMID 21670251 DOI: 10.1073/Pnas.1019152108  0.52
2011 Goulet DR, Knee KM, King JA. Inhibition of unfolding and aggregation of lens protein human gamma D crystallin by sodium citrate. Experimental Eye Research. 93: 371-81. PMID 21600897 DOI: 10.1016/J.Exer.2011.04.011  0.52
2011 Chen DH, Baker ML, Hryc CF, DiMaio F, Jakana J, Wu W, Dougherty M, Haase-Pettingell C, Schmid MF, Jiang W, Baker D, King JA, Chiu W. Structural basis for scaffolding-mediated assembly and maturation of a dsDNA virus. Proceedings of the National Academy of Sciences of the United States of America. 108: 1355-60. PMID 21220301 DOI: 10.1073/Pnas.1015739108  0.52
2011 Raytcheva DA, Haase-Pettingell C, Piret JM, King JA. Intracellular assembly of cyanophage Syn5 proceeds through a scaffold-containing procapsid. Journal of Virology. 85: 2406-15. PMID 21177804 DOI: 10.1128/Jvi.01601-10  0.52
2011 Knee KM, Goulet DR, Zhang J, Chen B, Chiu W, King JA. The group II chaperonin Mm-Cpn binds and refolds human γD crystallin. Protein Science : a Publication of the Protein Society. 20: 30-41. PMID 20981710 DOI: 10.1002/Pro.531  0.52
2010 Chang JT, Schmid MF, Haase-Pettingell C, Weigele PR, King JA, Chiu W. Visualizing the structural changes of bacteriophage Epsilon15 and its Salmonella host during infection. Journal of Molecular Biology. 402: 731-40. PMID 20709082 DOI: 10.1016/J.Jmb.2010.07.058  0.52
2010 Murata K, Liu X, Danev R, Jakana J, Schmid MF, King J, Nagayama K, Chiu W. Zernike phase contrast cryo-electron microscopy and tomography for structure determination at nanometer and subnanometer resolutions. Structure (London, England : 1993). 18: 903-12. PMID 20696391 DOI: 10.1016/J.Str.2010.06.006  0.32
2010 Pereira JH, Ralston CY, Douglas NR, Meyer D, Knee KM, Goulet DR, King JA, Frydman J, Adams PD. Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle. The Journal of Biological Chemistry. 285: 27958-66. PMID 20573955 DOI: 10.1074/Jbc.M110.125344  0.52
2010 Wang Y, Petty S, Trojanowski A, Knee K, Goulet D, Mukerji I, King J. Formation of amyloid fibrils in vitro from partially unfolded intermediates of human gammaC-crystallin. Investigative Ophthalmology & Visual Science. 51: 672-8. PMID 19684009 DOI: 10.1167/Iovs.09-3987  0.52
2010 Acosta-Sampson L, King J. Chaperone Interactions of the Small Heat Shock Protein Human αb-Crystallin With Its Physiological Substrate γd-Crystallin and Its Isolated Domains Biophysical Journal. 98. DOI: 10.1016/J.Bpj.2009.12.194  0.52
2009 Xu J, Chen J, Toptygin D, Tcherkasskaya O, Callis P, King J, Brand L, Knutson JR. Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching. Journal of the American Chemical Society. 131: 16751-7. PMID 19919143 DOI: 10.1021/Ja904857T  0.52
2009 Chen J, Callis PR, King J. Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage. Biochemistry. 48: 3708-16. PMID 19358562 DOI: 10.1021/Bi802177G  0.52
2009 Jung J, Byeon IJL, Wang Y, King J, Gronenborn AM. The structure of the cataract-causing P23T mutant of human γD-crystallin exhibits distinctive local conformational and dynamic changes Biochemistry. 48: 2597-2609. PMID 19216553 DOI: 10.1021/Bi802292Q  0.52
2009 Jung J, Byeon I, Wang Y, King J, Gronenborn A. The structure of the cataract causing P23T mutant of human gamma-D crystallin Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr16173  0.52
2009 Acosta-Sampson LI, King J. HαB-Crystallin Suppresses The Aggregation Upon Refolding Of Its Physiological Substrates HγD-, HγC- And HγS-Crystallin Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.2222  0.52
2009 Knee KM, Goulet DR, Jameel S, King JA. Characterization of the Group II Chaperonin TriC derived from Human Cervical Adenocarcinoma (HeLa) Cells Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.2221  0.52
2009 Goulet DR, King JA, Knee KM. Characterization of Substrate Binding to the Group II Archael Chaperonin from Methanococcus maripaludis (Mm-Cpn) Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.2220  0.52
2009 Drahos KL, King J. Mutations Causing Early Cataract Development In Mice Destabilize Human gammaD-crystallin Biophysical Journal. 96. DOI: 10.1016/J.Bpj.2008.12.1676  0.52
2008 Chen J, Toptygin D, Brand L, King J. Mechanism of the efficient tryptophan fluorescence quenching in human gammaD-crystallin studied by time-resolved fluorescence. Biochemistry. 47: 10705-21. PMID 18795792 DOI: 10.1021/Bi800499K  0.52
2008 Jiang W, Baker ML, Jakana J, Weigele PR, King J, Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature. 451: 1130-4. PMID 18305544 DOI: 10.1038/Nature06665  0.52
2008 Drahos KL, King J. Mutations associated with early cataract development in mice destabilize human gammaD-crystallin The Faseb Journal. 22: 232-232. DOI: 10.1096/Fasebj.22.2_Supplement.232  0.52
2007 Weigele PR, Pope WH, Pedulla ML, Houtz JM, Smith AL, Conway JF, King J, Hatfull GF, Lawrence JG, Hendrix RW. Genomic and structural analysis of Syn9, a cyanophage infecting marine Prochlorococcus and Synechococcus. Environmental Microbiology. 9: 1675-95. PMID 17564603 DOI: 10.1111/J.1462-2920.2007.01285.X  0.52
2007 Pope WH, Weigele PR, Chang J, Pedulla ML, Ford ME, Houtz JM, Jiang W, Chiu W, Hatfull GF, Hendrix RW, King J. Genome sequence, structural proteins, and capsid organization of the cyanophage Syn5: a "horned" bacteriophage of marine synechococcus. Journal of Molecular Biology. 368: 966-81. PMID 17383677 DOI: 10.1016/J.Jmb.2007.02.046  0.52
2006 Chen J, Flaugh SL, Callis PR, King J. Mechanism of the highly efficient quenching of tryptophan fluorescence in human gammaD-crystallin. Biochemistry. 45: 11552-63. PMID 16981715 DOI: 10.1021/Bi060988V  0.52
2006 McDonnell AV, Menke M, Palmer N, King J, Cowen L, Berger B. Fold recognition and accurate sequence-structure alignment of sequences directing beta-sheet proteins. Proteins. 63: 976-85. PMID 16547930 DOI: 10.1002/Prot.20942  0.52
2006 Jiang W, Chang J, Jakana J, Weigele P, King J, Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus Nature. 439: 612-616. PMID 16452981 DOI: 10.1038/Nature04487  0.32
2005 Weigele PR, Haase-Pettingell C, Campbell PG, Gossard DC, King J. Stalled folding mutants in the triple beta-helix domain of the phage P22 tailspike adhesin. Journal of Molecular Biology. 354: 1103-17. PMID 16289113 DOI: 10.1016/J.Jmb.2005.10.007  0.52
2005 Raso SW, Abel J, Barnes JM, Maloney KM, Pipes G, Treuheit MJ, King J, Brems DN. Aggregation of granulocyte-colony stimulating factor in vitro involves a conformationally altered monomeric state. Protein Science : a Publication of the Protein Society. 14: 2246-57. PMID 16131655 DOI: 10.1110/Ps.051489405  0.52
2005 Jain M, Evans MS, King J, Clark PL. Monoclonal antibody epitope mapping describes tailspike beta-helix folding and aggregation intermediates. The Journal of Biological Chemistry. 280: 23032-40. PMID 15833745 DOI: 10.1074/Jbc.M501963200  0.52
2005 Gossard DC, King J. Lattice transformations and subunit conformational changes in phage capsid maturation Journal of Theoretical Medicine. 6: 99-105. DOI: 10.1080/10273660500149646  0.52
2004 Pope WH, Haase-Pettingell C, King J. Protein folding failure sets high-temperature limit on growth of phage P22 in Salmonella enterica serovar Typhimurium. Applied and Environmental Microbiology. 70: 4840-7. PMID 15294822 DOI: 10.1128/Aem.70.8.4840-4847.2004  0.52
2003 Weigele PR, Scanlon E, King J. Homotrimeric, beta-stranded viral adhesins and tail proteins. Journal of Bacteriology. 185: 4022-30. PMID 12837775 DOI: 10.1128/Jb.185.14.4022-4030.2003  0.52
2002 Kamei DT, King JA, Wang DI, Blankschtein D. Separating lysozyme from bacteriophage P22 in two-phase aqueous micellar systems. Biotechnology and Bioengineering. 80: 233-6. PMID 12209780 DOI: 10.1002/Bit.10377  0.52
2002 Cowen L, Bradley P, Menke M, King J, Berger B. Predicting the beta-helix fold from protein sequence data. Journal of Computational Biology : a Journal of Computational Molecular Cell Biology. 9: 261-76. PMID 12015881 DOI: 10.1089/10665270252935458  0.52
2002 Kamei DT, King JA, Wang DI, Blankschtein D. Understanding viral partitioning in two-phase aqueous nonionic micellar systems: 2. Effect of entrained micelle-poor domains. Biotechnology and Bioengineering. 78: 203-16. PMID 11870611 DOI: 10.1002/Bit.10194  0.52
2002 Kamei DT, Liu CL, Haase-Pettingell C, King JA, Wang DI, Blankschtein D. Understanding viral partitioning in two-phase aqueous nonionic micellar systems: 1. Role of attractive interactions between viruses and micelles. Biotechnology and Bioengineering. 78: 190-202. PMID 11870610 DOI: 10.1002/Bit.10193  0.52
2002 Ting CS, Rocap G, King J, Chisholm SW. Cyanobacterial photosynthesis in the oceans: the origins and significance of divergent light-harvesting strategies. Trends in Microbiology. 10: 134-42. PMID 11864823 DOI: 10.1016/S0966-842X(02)02319-3  0.52
2002 King J, Haase-Pettingell C, Gossard D. Protein Folding and Misfolding American Scientist. 90: 445-453. DOI: 10.1511/2002.33.790  0.52
2001 Bradley P, Cowen L, Menke M, King J, Berger B. BETAWRAP: successful prediction of parallel beta -helices from primary sequence reveals an association with many microbial pathogens. Proceedings of the National Academy of Sciences of the United States of America. 98: 14819-24. PMID 11752429 DOI: 10.1073/Pnas.251267298  0.52
2001 Asherie N, Pande J, Pande A, Zarutskie JA, Lomakin J, Lomakin A, Ogun O, Stern LJ, King J, Benedek GB. Enhanced crystallization of the Cys18 to Ser mutant of bovine gammaB crystallin. Journal of Molecular Biology. 314: 663-9. PMID 11733987 DOI: 10.1006/Jmbi.2001.5155  0.52
2001 Ting CS, Rocap G, King J, Chisholm SW. Phycobiliprotein genes of the marine photosynthetic prokaryote Prochlorococcus: evidence for rapid evolution of genetic heterogeneity. Microbiology (Reading, England). 147: 3171-82. PMID 11700369 DOI: 10.1099/00221287-147-11-3171  0.52
2001 Pande A, Pande J, Asherie N, Lomakin A, Ogun O, King J, Benedek GB. Crystal cataracts: human genetic cataract caused by protein crystallization. Proceedings of the National Academy of Sciences of the United States of America. 98: 6116-20. PMID 11371638 DOI: 10.1073/Pnas.101124798  0.52
2001 Clark PL, King J. A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates. The Journal of Biological Chemistry. 276: 25411-20. PMID 11319217 DOI: 10.1074/Jbc.M008490200  0.52
2001 Schwartz R, Istrail S, King J. Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues Protein Science. 10: 1023-1031. PMID 11316883 DOI: 10.1110/Ps.33201  0.52
2001 Raso SW, Clark PL, Haase-Pettingell C, King J, Thomas GJ. Distinct cysteine sulfhydryl environments detected by analysis of Raman S-hh markers of Cys-->Ser mutant proteins. Journal of Molecular Biology. 307: 899-911. PMID 11273709 DOI: 10.1006/Jmbi.2001.4476  0.52
2001 Schwartz R, Ting CS, King J. Whole proteome pI values correlate with subcellular localizations of proteins for organisms within the three domains of life. Genome Research. 11: 703-709. DOI: 10.1101/Gr.158701  0.52
2000 Zhang Z, Greene B, Thuman-Commike PA, Jakana J, Prevelige PE, King J, Chiu W. Visualization of the maturation transition in bacteriophage P22 by electron cryomicroscopy Journal of Molecular Biology. 297: 615-626. PMID 10731416 DOI: 10.1006/Jmbi.2000.3601  0.52
2000 Pande A, Pande J, Asherie N, Lomakin A, Ogun O, King JA, Lubsen NH, Walton D, Benedek GB. Molecular basis of a progressive juvenile-onset hereditary cataract. Proceedings of the National Academy of Sciences of the United States of America. 97: 1993-8. PMID 10688888 DOI: 10.1073/Pnas.040554397  0.52
1999 Istrail S, Schwartz R, King J. Lattice simulations of aggregation funnels for protein folding Journal of Computational Biology. 6: 143-162. PMID 10421520 DOI: 10.1089/Cmb.1999.6.143  0.52
1999 Greene B, King J. Folding and stability of mutant scaffolding proteins defective in P22 capsid assembly. Journal of Biological Chemistry. 274: 16141-16146. PMID 10347166 DOI: 10.1074/Jbc.274.23.16141  0.32
1999 Greene B, King J. In Vitro Unfolding/Refolding of Wild Type Phage P22 Scaffolding Protein Reveals Capsid-binding Domain Journal of Biological Chemistry. 274: 16135-16140. PMID 10347165 DOI: 10.1074/Jbc.274.23.16135  0.32
1999 Thuman-Commike PA, Tsuruta H, Greene B, Prevelige PE, King J, Chiu W. Solution x-ray scattering-based estimation of electron cryomicroscopy imaging parameters for reconstruction of virus particles Biophysical Journal. 76: 2249-2261. PMID 10096920 DOI: 10.1016/S0006-3495(99)77381-9  0.52
1999 King J, Stabinsky D. Biotechnology Under Globalisation : The Corporate Expropriation Of Plant, Animal And Microbial Species Race & Class. 40: 73-89. DOI: 10.1177/030639689904000206  0.52
1998 Liu CL, Kamei DT, King JA, Wang DI, Blankschtein D. Separation of proteins and viruses using two-phase aqueous micellar systems. Journal of Chromatography. B, Biomedical Sciences and Applications. 711: 127-38. PMID 9699982 DOI: 10.1016/S0378-4347(98)00013-9  0.52
1998 Thuman-Commike PA, Greene B, Malinski JA, King J, Chiu W. Role of the scaffolding protein in P22 procapsid size determination suggested by T = 4 and T = 7 procapsid structures. Biophysical Journal. 74: 559-68. PMID 9449356 DOI: 10.1016/S0006-3495(98)77814-2  0.32
1997 Robinson AS, King J. Disulphide-bonded intermediate on the folding and assembly pathway of a non-disulphide bonded protein. Nature Structural Biology. 4: 450-5. PMID 9187652 DOI: 10.1038/Nsb0697-450  0.4
1996 Greene B, King J. Scaffolding mutants identifying domains required for P22 procapsid assembly and maturation. Virology. 225: 82-96. PMID 8918536 DOI: 10.1006/Viro.1996.0577  0.32
1996 Thuman-Commike PA, Greene B, Jakana J, Prasad BVV, King J, Prevelige PE, Chiu W. Three-dimensional structure of scaffolding-containing phage P22 procapsids by electron cryo-microscopy Journal of Molecular Biology. 260: 85-98. PMID 8676394 DOI: 10.1006/Jmbi.1996.0383  0.52
1995 Galisteo ML, Gordon CL, King J. Stability of wild-type and temperature-sensitive protein subunits of the phage P22 capsid Journal of Biological Chemistry. 270: 16595-16601. PMID 7622466 DOI: 10.1074/Jbc.270.28.16595  0.52
1995 Chen C, King J, Wang DIC. Molecular thermodynamic model for Helix‐Helix docking and protein aggregation Aiche Journal. 41: 1015-1024. DOI: 10.1002/Aic.690410433  0.52
1994 Prevelige PE, King J, Silva JL. Pressure denaturation of the bacteriophage P22 coat protein and its entropic stabilization in icosahedral shells Biophysical Journal. 66: 1631-1641. PMID 8061212 DOI: 10.1016/S0006-3495(94)80955-5  0.52
1994 Greene B, King J. Binding of scaffolding subunits within the P22 procapsid lattice. Virology. 205: 188-97. PMID 7975215 DOI: 10.1006/Viro.1994.1634  0.32
1993 Prasad BVV, Prevelige PE, Marietta E, Chen RO, Thomas D, King J, Chiu W. Three-dimensional transformation of capsids associated with genome packaging in a bacterial virus Journal of Molecular Biology. 231: 65-74. PMID 8496966 DOI: 10.1006/Jmbi.1993.1257  0.52
1993 Prevelige PE, Thomas D, King J. Nucleation and growth phases in the polymerization of coat and scaffolding subunits into icosahedral procapsid shells Biophysical Journal. 64: 824-835. PMID 8471727 DOI: 10.1016/S0006-3495(93)81443-7  0.52
1993 King J. Folding of the phage P22 coat protein in vitro Biochemistry. 32: 10839-10847. PMID 8399234 DOI: 10.1021/Bi00091A040  0.52
1993 Teschke CM, King J, Prevelige PE. Inhibition of viral capsid assembly by 1,1′-bi(4-anilinonaphthalene-5-sulfonic acid) Biochemistry. 32: 10658-10665. PMID 8399211 DOI: 10.1021/Bi00091A016  0.52
1992 Teschke CM, King J. Folding and assembly of oligomeric proteins in Escherichia coli Current Opinion in Biotechnology. 3: 468-473. PMID 1368931 DOI: 10.1016/0958-1669(92)90073-R  0.52
1992 Teschke CM, King J. Folding and assembly of oligomeric proteins in Escherichia coli Current Biology. 2: 644. DOI: 10.1016/0960-9822(92)90108-M  0.52
1991 Mitraki A, Fane B, Haase-Pettingell C, Sturtevant J, King J. Global suppression of protein folding defects and inclusion body formation Science. 253: 54-58. PMID 1648264 DOI: 10.1126/Science.1648264  0.52
1990 Prevelige PE, Thomas D, King J, Towse SA, Thomas GJ. Conformational states of the bacteriophage P22 capsid subunit in relation to self-assembly Biochemistry. 29: 5626-5633. PMID 2386790 DOI: 10.1021/Bi00475A030  0.52
1990 Bazinet C, Villafane R, King J. Novel second-site suppression of a cold-sensitive defect in phage P22 procapsid assembly. Journal of Molecular Biology. 216: 701-16. PMID 2258936 DOI: 10.1016/0022-2836(90)90393-Z  0.52
1990 Thomas GJ, Becka R, Sargent D, Yu MH, King J. Conformational stability of P22 tailspike proteins carrying temperature-sensitive folding mutations. Biochemistry. 29: 4181-4187. PMID 2141794 DOI: 10.1021/Bi00469A022  0.32
1989 Mitraki A, King J. Protein folding intermediates and inclusion body formation Nature Biotechnology. 7: 690-697. DOI: 10.1038/Nbt0789-690  0.52
1989 King J. Deciphering the Rules of Protein Folding Chemical & Engineering News. 67: 32-54. DOI: 10.1021/Cen-V067N015.P032  0.52
1988 Bazinet C, Benbasat J, King J, Carazo JM, Carrascosa JL. Purification and organization of the gene 1 portal protein required for phage P22 DNA packaging. Biochemistry. 27: 1849-56. PMID 3288279 DOI: 10.1021/Bi00406A009  0.52
1988 Prevelige PE, Thomas D, King J. Scaffolding protein regulates the polymerization of P22 coat subunits into icosahedral shells in vitro Journal of Molecular Biology. 202: 743-757. PMID 3262767 DOI: 10.1016/0022-2836(88)90555-4  0.52
1988 Bazinet C, King J. Initiation of P22 procapsid assembly in vivo. Journal of Molecular Biology. 202: 77-86. PMID 3262766 DOI: 10.1016/0022-2836(88)90520-7  0.52
1988 Villafane R, King J. Nature and distribution of sites of temperature-sensitive folding mutations in the gene for the P22 Tailspike polypeptide chain Journal of Molecular Biology. 204: 607-619. PMID 3225847 DOI: 10.1016/0022-2836(88)90359-2  0.52
1988 Sargent D, Benevides JM, Yu M, King J, Thomas GJ. Secondary structure and thermostability of the phage P22 tailspike. XX. Analysis by Raman spectroscopy of the wild-type protein and a temperature-sensitive folding mutant. Journal of Molecular Biology. 199: 491-502. PMID 2965250 DOI: 10.1016/0022-2836(88)90620-1  0.32
1987 Wackett LP, Hartwieg EA, King JA, Orme-Johnson WH, Walsh CT. Electron microscopy of nickel-containing methanogenic enzymes: methyl reductase and F420-reducing hydrogenase. Journal of Bacteriology. 169: 718-27. PMID 3804976 DOI: 10.1128/Jb.169.2.718-727.1987  0.52
1986 Loechler EL, King J. Identification of the 9-aminoacridine/DNA complex responsible for photodynamic inactivation of P22 Biochemistry. 25: 5858-5864. PMID 3539179 DOI: 10.1021/Bi00368A004  0.52
1986 King J. Genetic analysis of protein folding pathways Bio/Technology. 4: 297-303. DOI: 10.1038/Nbt0486-297  0.52
1985 Bazinet CW, King J. A late gene product of phage P22 affecting virus infectivity. Virology. 143: 368-79. PMID 2998017 DOI: 10.1016/0042-6822(85)90377-0  0.52
1985 Bazinet C, King J. The DNA translocating vertex of dsDNA bacteriophage. Annual Review of Microbiology. 39: 109-29. PMID 2932996 DOI: 10.1146/Annurev.Mi.39.100185.000545  0.52
1984 Bryant JL, King J. DNA injection proteins are targets of acridine-sensitized photoinactivation of bacteriophage P22. Journal of Molecular Biology. 180: 837-63. PMID 6335533 DOI: 10.1016/0022-2836(84)90260-2  0.52
1982 Thomas GJ, Li Y, Fuller MT, King J. Structural studies of P22 phage, precursor particles, and proteins by laser Raman spectroscopy Biochemistry. 21: 3866-3878. PMID 7138810 DOI: 10.1021/Bi00259A023  0.52
1982 Fuller MT, King J. Assembly in vitro of bacteriophage P22 procapsids from purified coat and scaffolding subunits Journal of Molecular Biology. 156: 633-665. PMID 6750133 DOI: 10.1016/0022-2836(82)90270-4  0.52
1982 King J. The case against Environment. 24. DOI: 10.1080/00139157.1982.9929792  0.52
1982 Smith DH, King J. The Legal and Legislative Background Environment. 24: 24-36. DOI: 10.1080/00139157.1982.9929788  0.52
1981 Fuller MT, King J. Purification of the coat and scaffolding proteins from procapsids of bacteriophage P22 Virology. 112: 529-547. PMID 7257185 DOI: 10.1016/0042-6822(81)90300-7  0.52
1980 Fish SR, Hartman KA, Fuller MT, King J, Thomas GJ. Investigation of secondary structures and macromolecular interactions in bacteriophage p22 by laser Raman spectroscopy. Biophysical Journal. 32: 234-7. PMID 19431367 DOI: 10.1016/S0006-3495(80)84945-9  0.32
1980 King J, Griffin-Shea R, Fuller MT. Scaffolding proteins and the genetic control of virus shell assembly Quarterly Review of Biology. 55: 369-393. PMID 7267974 DOI: 10.1086/411981  0.52
1980 Fuller MT, King J. Regulation of coat protein polymerization by the scaffolding protein of bacteriophage P22 Biophysical Journal. 32: 381-401. PMID 7018607 DOI: 10.1016/S0006-3495(80)84963-0  0.52
1979 Earnshaw WC, Hendrix RW, King J. Structural studies of bacteriophage lambda heads and proheads by small angle X-ray diffraction. Journal of Molecular Biology. 134: 575-94. PMID 161330 DOI: 10.1016/0022-2836(79)90368-1  0.52
1978 Berget PB, King J. Isolation and characterization of precursors in T4 baseplate assembly. The complex of gene 10 and gene 11 products. Journal of Molecular Biology. 124: 469-86. PMID 712843 DOI: 10.1016/0022-2836(78)90182-1  0.52
1978 Earnshaw WC, King J, Harrison SC, Eiserling FA. The structural organization of DNA packaged within the heads of T4 wild-type, isometric and giant bacteriophages. Cell. 14: 559-68. PMID 688382 DOI: 10.1016/0092-8674(78)90242-8  0.48
1978 Earnshaw WC, King J, Eiserling FA. The size of the bacteriophage T4 head in solution with comments about the dimension of virus particles as visualized by electron microscopy. Journal of Molecular Biology. 122: 247-53. PMID 682194 DOI: 10.1016/0022-2836(78)90040-2  0.48
1978 Berget PB, King J. Antigenic gene products of bacteriophage T4 baseplates. Virology. 86: 312-28. PMID 664235 DOI: 10.1016/0042-6822(78)90073-9  0.52
1978 King J. Recombinant DNA and autoimmune disease Journal of Infectious Diseases. 137: 663-667. PMID 351083 DOI: 10.1093/Infdis/137.5.663  0.52
1975 Kikuchi Y, King J. Genetic control of bacteriophage T4 baseplate morphogenesis. II. Mutants unable to form the central part of the baseplate Journal of Molecular Biology. 99. PMID 765482 DOI: 10.1016/S0022-2836(75)80179-3  0.52
1971 King J. Bacteriophage T4 tail assembly: Four steps in core formation Journal of Molecular Biology. 58. PMID 4933424 DOI: 10.1016/0022-2836(71)90034-9  0.52
1970 Cameron RE, King J, David CN. Soil microbial ecology of wheeler valley, antarctica Soil Science. 109: 110-120. DOI: 10.1097/00010694-197002000-00006  0.52
1968 King J. Assembly of the tau of bacteriophage T4 Journal of Molecular Biology. 32. PMID 4868421 DOI: 10.1016/0022-2836(68)90007-7  0.52
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