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

32 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
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
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
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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  0.68
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