Jonathan A. King
Affiliations: | Biology | Massachusetts Institute of Technology, Cambridge, MA, United States |
Area:
Protein FoldingWebsite:
https://biology.mit.edu/people/jonathan_kingGoogle:
"Jonathan A. King"Bio:
http://web.mit.edu/king-lab/www/
http://web.mit.edu/king-lab/www/people/JKing/JKing.html
http://www.biophysics.org/LinkClick.aspx?fileticket=Nt6zF95ju0Q%3D&tabid=524
http://resolver.caltech.edu/CaltechETD:etd-09242002-105334
Mean distance: 8.46 | S | N | B | C | P |
Parents
Sign in to add mentor| Robert S. Edgar | grad student | 1968 | Caltech | |
| (Steps in the assembly of bacteriophage T4 ) | ||||
| Aaron Klug | post-doc | 1970 | MRC-LMB | |
Children
Sign in to add trainee| William C. Earnshaw | grad student | MIT (Neurotree) | |
| Margaret T. (Minx) Fuller | grad student | 1980 | MIT (FlyTree) |
| Peter E. Prevelige | post-doc | 1985-1993 | MIT (Microtree) |
| Anne Skaja Robinson | post-doc | 1994-1997 | (E-Tree) |
| Patricia L. Clark | post-doc | 2001 | MIT |
| Kelly M. Knee | post-doc | 2007-2011 | MIT (Physics Tree) |
BETA: Related publications
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Publications
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| King J. (2022) Using T4 Genetics and Laemmli's Development of High Resolution SDS Gel Electrophoresis to Reveal Structural Protein Interactions Controlling Protein Folding and Phage Self-Assembly. The Journal of Biological Chemistry. 102463 |
| Takata T, Haase-Pettingell C, King J. (2021) The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly. Bacteriophage. 2: 36-49 |
| King J, Henry IM, Kosinski-Collins M, et al. (2020) 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 |
| Sergeeva OA, Haase-Pettingell C, King JA. (2019) Co-expression of CCT subunits hints at TRiC assembly. Cell Stress & Chaperones |
| Mills-Henry IA, Thol SL, Kosinski-Collins MS, et al. (2019) Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains. Biophysical Journal |
| Domínguez-Calva JA, Pérez-Vázquez ML, Serebryany E, et al. (2018) Mercury-induced aggregation of human lens γ-crystallins reveals a potential role in cataract disease. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry |
| Dai W, Chen M, Myers C, et al. (2018) Visualizing Individual RuBisCO and its Assembly into Carboxysomes in Marine Cyanobacteria by Cryo-Electron Tomography. Journal of Molecular Biology |
| Domínguez-Calva JA, Haase-Pettingell C, Serebryany E, et al. (2018) A Histidine Switch for Zn-Induced Aggregation of γ-Crystallins Reveals a Metal-Bridging Mechanism That Is Relevant to Cataract Disease. Biochemistry |
| Pereira JH, McAndrew RP, Sergeeva OA, et al. (2017) Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy. Scientific Reports. 7: 3673 |
| Serebryany E, Woodard JC, Adkar BV, et al. (2017) An Internal Disulfide Locks a Misfolded Aggregation-Prone Intermediate in Cataract-Linked Mutants of Human Gamma-D Crystallin Biophysical Journal. 112 |