| Year |
Citation |
Score |
| 2022 |
King J. 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. PMID 36067882 DOI: 10.1016/j.jbc.2022.102463 |
0.333 |
|
| 2021 |
Takata T, Haase-Pettingell C, King J. The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly. Bacteriophage. 2: 36-49. PMID 22666655 DOI: 10.4161/bact.19775 |
0.303 |
|
| 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 |
0.318 |
|
| 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 |
0.38 |
|
| 2019 |
Mills-Henry IA, Thol SL, Kosinski-Collins MS, Serebryany E, King JA. Kinetic Stability of Long-Lived Human Lens γ-Crystallins and Their Isolated Double Greek Key Domains. Biophysical Journal. PMID 31266635 DOI: 10.1016/J.Bpj.2019.06.006 |
0.419 |
|
| 2018 |
Domínguez-Calva JA, Pérez-Vázquez ML, Serebryany E, King JA, Quintanar L. 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. PMID 30167892 DOI: 10.1007/S00775-018-1607-Z |
0.37 |
|
| 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 |
0.352 |
|
| 2018 |
Domínguez-Calva JA, Haase-Pettingell C, Serebryany E, King JA, Quintanar L. A Histidine Switch for Zn-Induced Aggregation of γ-Crystallins Reveals a Metal-Bridging Mechanism That Is Relevant to Cataract Disease. Biochemistry. PMID 30064223 DOI: 10.1021/Acs.Biochem.8B00436 |
0.384 |
|
| 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 |
0.414 |
|
| 2017 |
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 Gamma-D Crystallin Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.923 |
0.389 |
|
| 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 |
0.412 |
|
| 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 |
0.426 |
|
| 2016 |
Dominguez-Calva JA, Serebryany E, Haase-Pettingell C, King JA, Quintanar L. Elucidating the Coordination Features Associated to Copper and Zinc Induced Aggregation of Human γ-D Crystallin Biophysical Journal. 110. DOI: 10.1016/J.Bpj.2015.11.2095 |
0.353 |
|
| 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 |
0.401 |
|
| 2015 |
Darrow MC, Sergeeva OA, Isas JM, Galaz-Montoya J, King JA, Langen R, Schmid MF, Chiu W. Structural Mechanisms of Mutant Huntingtin Aggregation Suppression by Synthetic Chaperonin-like CCT5 Complex Explained by Cryo-electron Tomography. The Journal of Biological Chemistry. PMID 25995452 DOI: 10.1074/Jbc.M115.655373 |
0.408 |
|
| 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 |
0.457 |
|
| 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 |
0.335 |
|
| 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 |
0.374 |
|
| 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 |
0.784 |
|
| 2015 |
Knee KM, Patel D, Sergeeva O, Kelly JJ, Janz JM, King JA, Yue W, Bulawa C. CCT5: A Model Protein Folding Machine Biophysical Journal. 108: 52a. DOI: 10.1016/J.Bpj.2014.11.318 |
0.784 |
|
| 2015 |
Quintanar L, Serebryany E, Domínguez-Calva JA, Haasse-Pettingell C, King JA. Copper and Zinc Binding Specifically Induce the Aggregation of Human γ-D Crystallin Biophysical Journal. 108. DOI: 10.1016/J.Bpj.2014.11.2749 |
0.355 |
|
| 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 |
0.304 |
|
| 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 |
0.417 |
|
| 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 |
0.384 |
|
| 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 |
0.455 |
|
| 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 |
0.779 |
|
| 2014 |
Schafheimer N, Wang Z, Schey K, King J. Tyrosine/Cysteine Cluster Sensitizing Human γD-Crystallin to Ultraviolet Radiation-Induced Photoaggregation in Vitro Biochemistry. 53: 979-990. PMID 24410332 DOI: 10.1021/Bi401397G |
0.38 |
|
| 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 |
0.356 |
|
| 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 |
0.422 |
|
| 2014 |
Serebryany E, King JA. Aggregation of Oxidation-Mimicking Mutants of Gamma-D Crystallin Supports a Domain Swapping Model Biophysical Journal. 106. DOI: 10.1016/J.Bpj.2013.11.295 |
0.475 |
|
| 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 |
0.312 |
|
| 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 |
0.359 |
|
| 2013 |
Schafheimer N, King J. Tryptophan cluster protects human γD-crystallin from ultraviolet radiation-induced photoaggregation in vitro. Photochemistry and Photobiology. 89: 1106-1115. PMID 23683003 DOI: 10.1111/Php.12096 |
0.416 |
|
| 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 |
0.367 |
|
| 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 |
0.334 |
|
| 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 |
0.762 |
|
| 2013 |
Serebryany E, Schafheimer N, Lindquist SL, King JA. Aggregation of Trp>Glu Mutants of the Human Gamma-D Crystallin: A Model for Hereditary or UV-Induced Cataract Biophysical Journal. 104. DOI: 10.1016/J.Bpj.2012.11.307 |
0.482 |
|
| 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 |
0.405 |
|
| 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 |
0.445 |
|
| 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 |
0.765 |
|
| 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 |
0.703 |
|
| 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 |
0.408 |
|
| 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 |
0.768 |
|
| 2011 |
Kong F, King J. Contributions of aromatic pairs to the folding and stability of long-lived human γD-crystallin. Protein Science : a Publication of the Protein Society. 20: 513-28. PMID 21432932 DOI: 10.1002/Pro.583 |
0.434 |
|
| 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 |
0.482 |
|
| 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 |
0.437 |
|
| 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 |
0.782 |
|
| 2011 |
Acosta-Sampson L, King JA. Beta-Sheet Features in the Greek Key Gamma D-Crystallin Recognized by the Lens Chaperone Alpha B-Crystallin Biophysical Journal. 100. DOI: 10.1016/J.Bpj.2010.12.2322 |
0.474 |
|
| 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 |
0.326 |
|
| 2010 |
Acosta-Sampson L, King J. Partially Folded Aggregation Intermediates of Human γD-, γC- and γS-Crystallin Are Recognized and Bound by Human αB-crystallin Chaperone Journal of Molecular Biology. 401: 134-152. PMID 20621668 DOI: 10.1016/J.Jmb.2010.05.067 |
0.481 |
|
| 2010 |
Dudek EJ, Lampi KJ, Lampi JA, Shang F, King J, Wang Y, Taylor A. Ubiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidation. Investigative Ophthalmology & Visual Science. 51: 4164-73. PMID 20592226 DOI: 10.1167/Iovs.09-4087 |
0.447 |
|
| 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 |
0.773 |
|
| 2010 |
Das P, King JA, Zhou R. beta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallin. Protein Science : a Publication of the Protein Society. 19: 131-40. PMID 19937657 DOI: 10.1002/Pro.296 |
0.421 |
|
| 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 |
0.781 |
|
| 2010 |
Speed MA, King J, Wang DI. Polymerization mechanism of polypeptide chain aggregation. Biotechnology and Bioengineering. 54: 333-43. PMID 18634100 DOI: 10.1002/(Sici)1097-0290(19970520)54:4<333::Aid-Bit6>3.0.Co;2-L |
0.372 |
|
| 2010 |
Goulet DR, Knee KM, Mukerji I, King JA. Citrate Binding Stabilizes Human Gamma-Crystallin to Slow Unfolding and Inhibit Aggregation Biophysical Journal. 98: 614a. DOI: 10.1016/J.Bpj.2009.12.3350 |
0.812 |
|
| 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 |
0.468 |
|
| 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 |
0.34 |
|
| 2009 |
Moreau KL, King J. Hydrophobic core mutations associated with cataract development in mice destabilize human gammaD-crystallin. The Journal of Biological Chemistry. 284: 33285-95. PMID 19758984 DOI: 10.1074/Jbc.M109.031344 |
0.449 |
|
| 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 |
0.409 |
|
| 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 |
0.443 |
|
| 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 |
0.435 |
|
| 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 |
0.792 |
|
| 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 |
0.775 |
|
| 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 |
0.428 |
|
| 2009 |
Kong F, Chen J, King JA. Contributions of Tyrosine Residues to the Stability of Human γD-Crystallin Biophysical Journal. 96: 332. DOI: 10.1016/J.Bpj.2008.12.1674 |
0.413 |
|
| 2009 |
Chen J, Callis PR, King J. The γ-Crystallin Fold May Have Evolved To Protect Conserved Tryptophan Residues From UV Radiation Damage Through Efficient Quenching Biophysical Journal. 96: 47a. DOI: 10.1016/J.Bpj.2008.12.137 |
0.38 |
|
| 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 |
0.342 |
|
| 2008 |
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, et al. Direct and selective elimination of specific prions and amyloids by 4,5-dianilinophthalimide and analogs. Proceedings of the National Academy of Sciences of the United States of America. 105: 7159-64. PMID 18480256 DOI: 10.1073/Pnas.0801934105 |
0.38 |
|
| 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 |
0.425 |
|
| 2007 |
Mills IA, Flaugh SL, Kosinski-Collins MS, King JA. Folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin. Protein Science : a Publication of the Protein Society. 16: 2427-44. PMID 17905830 DOI: 10.1110/Ps.072970207 |
0.401 |
|
| 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 |
0.38 |
|
| 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 |
0.378 |
|
| 2007 |
Wang Y, Liu B, Liang JJ, King JA. Folding, unfolding, and fibril formation of human eye lens {gamma}C-crystallin The Faseb Journal. 21. DOI: 10.1096/Fasebj.21.5.A637-A |
0.317 |
|
| 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 |
0.344 |
|
| 2006 |
Flaugh SL, Mills IA, King J. Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding Journal of Biological Chemistry. 281: 30782-30793. PMID 16891314 DOI: 10.1074/Jbc.M603882200 |
0.419 |
|
| 2006 |
Chang J, Weigele P, King J, Chiu W, Jiang W. Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure (London, England : 1993). 14: 1073-82. PMID 16730179 DOI: 10.1016/J.Str.2006.05.007 |
0.367 |
|
| 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 |
0.304 |
|
| 2006 |
Simkovsky R, King J. An elongated spine of buried core residues necessary for in vivo folding of the parallel β-helix of P22 tailspike adhesin Proceedings of the National Academy of Sciences of the United States of America. 103: 3575-3580. PMID 16505375 DOI: 10.1073/Pnas.0509087103 |
0.409 |
|
| 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 |
0.378 |
|
| 2006 |
Schwartz R, King J. Frequencies of hydrophobic and hydrophilic runs and alternations in proteins of known structure. Protein Science : a Publication of the Protein Society. 15: 102-12. PMID 16373477 DOI: 10.1110/Ps.051741806 |
0.433 |
|
| 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 |
0.441 |
|
| 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 |
0.454 |
|
| 2005 |
Flaugh SL, Kosinski-Collins MS, King J. Interdomain side-chain interactions in human γD crystallin influencing folding and stability Protein Science. 14: 2030-2043. PMID 16046626 DOI: 10.1110/Ps.051460505 |
0.393 |
|
| 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 |
0.561 |
|
| 2005 |
Flaugh SL, Kosinski-Collins MS, King J. Contributions of hydrophobic domain interface interactions to the folding and stability of human γD-crystallin Protein Science. 14: 569-581. PMID 15722442 DOI: 10.1110/Ps.041111405 |
0.399 |
|
| 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 |
0.337 |
|
| 2004 |
Betts S, Haase-Pettingell C, Cook K, King J. Buried hydrophobic side-chains essential for the folding of the parallel β-helix domains of the P22 tailspike Protein Science. 13: 2291-2303. PMID 15322277 DOI: 10.1110/Ps.04676704 |
0.362 |
|
| 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 |
0.351 |
|
| 2004 |
Kosinski-Collins MS, Flaugh SL, King J. Probing folding and fluorescence quenching in human γD crystallin Greek key domains using triple tryptophan mutant proteins Protein Science. 13: 2223-2235. PMID 15273315 DOI: 10.1110/Ps.04627004 |
0.437 |
|
| 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 |
0.385 |
|
| 2003 |
Kosinski-Collins MS, King J. In vitro unfolding, refolding, and polymerization of human γD crystallin, a protein involved in cataract formation Protein Science. 12: 480-490. PMID 12592018 DOI: 10.1110/Ps.0225503 |
0.484 |
|
| 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 |
0.314 |
|
| 2002 |
Griffiths SW, King J, Cooney CL. The reactivity and oxidation pathway of cysteine 232 in recombinant human alpha 1-antitrypsin. The Journal of Biological Chemistry. 277: 25486-92. PMID 11991955 DOI: 10.1074/Jbc.M203089200 |
0.326 |
|
| 2002 |
Benton CB, King J, Clark PL. Characterization of the protrimer intermediate in the folding pathway of the interdigitated beta-helix tailspike protein. Biochemistry. 41: 5093-103. PMID 11955057 DOI: 10.1021/bi0115582 |
0.609 |
|
| 2002 |
Kreisberg JF, Betts SD, Haase-Pettingell C, King J. The interdigitated beta-helix domain of the P22 tailspike protein acts as a molecular clamp in trimer stabilization. Protein Science : a Publication of the Protein Society. 11: 820-30. PMID 11910025 DOI: 10.1110/Ps.3440102 |
0.409 |
|
| 2002 |
King J, Haase-Pettingell C, Gossard D. Protein Folding and Misfolding American Scientist. 90: 445-453. DOI: 10.1511/2002.33.790 |
0.443 |
|
| 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 |
0.309 |
|
| 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 |
0.368 |
|
| 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 |
0.384 |
|
| 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 |
0.58 |
|
| 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 |
0.392 |
|
| 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 |
0.567 |
|
| 2001 |
Haase-Pettingell C, Betts S, Raso SW, Stuart L, Robinson A, King J. Role for cysteine residues in the in vivo folding and assembly of the phage P22 tailspike. Protein Science. 10: 397-410. PMID 11266625 DOI: 10.1110/Ps.34701 |
0.658 |
|
| 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 |
0.329 |
|
| 2000 |
Kreisberg JF, Betts SD, King J. β-Helix core packing within the triple-stranded oligomerization domain of the P22 tailspike Protein Science. 9: 2338-2343. PMID 11206055 DOI: 10.1110/Ps.9.12.2338 |
0.314 |
|
| 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 |
0.642 |
|
| 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 |
0.414 |
|
| 1999 |
Betts S, Speed M, King J. [22] Detection of early aggregation intermediates by native gel electrophoresis and native Western blotting Methods in Enzymology. 309: 333-350. PMID 10507034 DOI: 10.1016/S0076-6879(99)09024-2 |
0.455 |
|
| 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 |
0.427 |
|
| 1999 |
King J, Betts S. A green light for protein folding. Nature Biotechnology. 17: 637-638. PMID 10409351 DOI: 10.1038/10848 |
0.364 |
|
| 1999 |
Betts S, King J. There's a right way and a wrong way: in vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike Structure. 7. PMID 10404587 DOI: 10.1016/S0969-2126(99)80078-1 |
0.41 |
|
| 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 |
0.454 |
|
| 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 |
0.457 |
|
| 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 |
0.546 |
|
| 1998 |
Betts SD, King J. Cold rescue of the thermolabile tailspike intermediate at the junction between productive folding and off-pathway aggregation. Protein Science. 7: 1516-1523. PMID 9684883 DOI: 10.1002/Pro.5560070704 |
0.444 |
|
| 1998 |
Konz JO, King J, Cooney CL. Effects of oxygen on recombinant protein expression. Biotechnology Progress. 14: 393-409. PMID 9622520 DOI: 10.1021/Bp980021L |
0.331 |
|
| 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 |
0.382 |
|
| 1998 |
Jensen PK, Lee CS, King JA. Temperature Effects on Refolding and Aggregation of a Large Multimeric Protein Using Capillary Zone Electrophoresis Analytical Chemistry. 70: 730-736. DOI: 10.1021/Ac970884D |
0.389 |
|
| 1997 |
Betts S, Haase-Pettingell C, King J. Mutational effects on inclusion body formation. Advances in Protein Chemistry. 50: 243-264. PMID 9338083 DOI: 10.1016/S0065-3233(08)60323-X |
0.391 |
|
| 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 |
0.637 |
|
| 1997 |
Haase-Pettingell C, King J. Prevalence of temperature sensitive folding mutations in the parallel beta coil domain of the phage P22 tailspike endorhamnosidase. Journal of Molecular Biology. 267: 88-102. PMID 9096209 DOI: 10.1006/Jmbi.1996.0841 |
0.399 |
|
| 1997 |
Speed MA, Morshead T, Wang DI, King J. Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies. Protein Science : a Publication of the Protein Society. 6: 99-108. PMID 9007981 DOI: 10.1002/Pro.5560060111 |
0.417 |
|
| 1997 |
Fan Z, Jensen PK, Lee CS, King J. Monitoring the refolding pathway for a large multimeric protein using capillary zone electrophoresis Journal of Chromatography A. 769: 315-323. DOI: 10.1016/S0021-9673(97)00046-0 |
0.411 |
|
| 1996 |
Speed MA, Wang DIC, King J. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition Nature Biotechnology. 14: 1283-1287. PMID 9631094 DOI: 10.1038/Nbt1096-1283 |
0.481 |
|
| 1996 |
King J. Unexpected pathways to protein stabilization Nature Biotechnology. 14: 436. PMID 9630915 DOI: 10.1038/Nbt0496-436 |
0.381 |
|
| 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 |
0.436 |
|
| 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 |
0.684 |
|
| 1996 |
King J, Haase-Pettingell C, Robinson AS, Speed M, Mitraki A. Thermolabile folding intermediates: inclusion body precursors and chaperonin substrates. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 10: 57-66. PMID 8566549 DOI: 10.1096/Fasebj.10.1.8566549 |
0.667 |
|
| 1995 |
Speed MA, Wang DI, King J. Multimeric intermediates in the pathway to the aggregated inclusion body state for P22 tailspike polypeptide chains. Protein Science : a Publication of the Protein Society. 4: 900-8. PMID 7663345 DOI: 10.1002/Pro.5560040509 |
0.427 |
|
| 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 |
0.453 |
|
| 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 |
0.436 |
|
| 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 |
0.603 |
|
| 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 |
0.412 |
|
| 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 |
0.608 |
|
| 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 |
0.643 |
|
| 1993 |
King J. Folding of the phage P22 coat protein in vitro Biochemistry. 32: 10839-10847. PMID 8399234 DOI: 10.1021/Bi00091A040 |
0.465 |
|
| 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 |
0.66 |
|
| 1993 |
Galisteo ML, King J. Conformational transformations in the protein lattice of phage P22 procapsids Biophysical Journal. 65: 227-235. PMID 8369433 DOI: 10.1016/S0006-3495(93)81073-7 |
0.455 |
|
| 1992 |
Mitraki A, King J. Amino acid substitutions influencing intracellular protein folding pathways. Febs Letters. 307: 20-25. PMID 1639189 DOI: 10.1016/0014-5793(92)80894-M |
0.42 |
|
| 1992 |
Chen CC, Zhu Y, King JA, Evans LB. A molecular thermodynamic approach to predict the secondary structure of homopolypeptides in aqueous systems. Biopolymers. 32: 1375-92. PMID 1420965 DOI: 10.1002/Bip.360321011 |
0.335 |
|
| 1992 |
Zhu Y, Chen CC, King JA, Evans LB. Molecular thermodynamic model to predict the alpha-helical secondary structure of polypeptide chains in solution. Biochemistry. 31: 10591-601. PMID 1420174 DOI: 10.1021/Bi00158A023 |
0.376 |
|
| 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 |
0.456 |
|
| 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 |
0.446 |
|
| 1991 |
Chen BL, King J. Thermal unfolding pathway for the thermostable p22 tailspike endorhamnosidase Biochemistry. 30: 6260-6269. PMID 2059632 DOI: 10.1021/Bi00239A026 |
0.407 |
|
| 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 |
0.454 |
|
| 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 |
0.666 |
|
| 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 |
0.405 |
|
| 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 |
0.434 |
|
| 1989 |
Mitraki A, King J. Protein folding intermediates and inclusion body formation Nature Biotechnology. 7: 690-697. DOI: 10.1038/Nbt0789-690 |
0.483 |
|
| 1989 |
King J. Deciphering the Rules of Protein Folding Chemical & Engineering News. 67: 32-54. DOI: 10.1021/Cen-V067N015.P032 |
0.392 |
|
| 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 |
0.41 |
|
| 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 |
0.629 |
|
| 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 |
0.456 |
|
| 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 |
0.357 |
|
| 1988 |
King J, Haase-Pettingell C. Aggregate formation from thermolabile intermediates in the maturation of the thermostable P22 tailspike. Biochemical Society Transactions. 16: 105-8. PMID 2967212 DOI: 10.1042/Bst0160105 |
0.328 |
|
| 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 |
0.407 |
|
| 1986 |
King J, Yu M. [13]Mutational analysis of protein folding pathways: The P22 tailspike endorhamnosidase Methods in Enzymology. 131: 250-266. PMID 3773760 DOI: 10.1016/0076-6879(86)31044-9 |
0.365 |
|
| 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 |
0.312 |
|
| 1986 |
King J. Genetic analysis of protein folding pathways Bio/Technology. 4: 297-303. DOI: 10.1038/Nbt0486-297 |
0.401 |
|
| 1985 |
Casjens S, Adams MB, Hall C, King J. Assembly-controlled autogenous modulation of bacteriophage P22 scaffolding protein gene expression. Journal of Virology. 53: 174-179. PMID 3880825 DOI: 10.1128/Jvi.53.1.174-179.1985 |
0.436 |
|
| 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 |
0.319 |
|
| 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 |
0.394 |
|
| 1984 |
Yu M, King J. Single amino acid substitutions influencing the folding pathway of the phage P22 tail spike endorhamnosidase Proceedings of the National Academy of Sciences of the United States of America. 81: 6584-6588. PMID 6387707 DOI: 10.1073/Pnas.81.21.6584 |
0.365 |
|
| 1984 |
Goldenberg DP, Smith DH, King J. Genetic and biochemical analysis of in vivo protein folding and subunit assembly. Biopolymers. 22: 125-9. PMID 6370323 DOI: 10.1002/Bip.360220120 |
0.446 |
|
| 1984 |
Strauss H, King J. Steps in the stabilization of newly packaged DNA during phage P22 morphogenesis. Journal of Molecular Biology. 172: 523-543. PMID 6363718 DOI: 10.1016/S0022-2836(84)80021-2 |
0.35 |
|
| 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 |
0.336 |
|
| 1984 |
Goldenberg DP, Smith DH, King J. Genetic analysis of the folding pathway for the tail spike protein of phage P22. Proceedings of the National Academy of Sciences of the United States of America. 80: 7060-4. PMID 6227917 DOI: 10.1073/Pnas.80.23.7060 |
0.412 |
|
| 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 |
0.656 |
|
| 1982 |
Goldenberg D, King J. Trimeric intermediate in the in vivo folding and subunit assembly of the tail spike endorhamnosidase of bacteriophage P22. Proceedings of the National Academy of Sciences of the United States of America. 79: 3403-7. PMID 6954486 DOI: 10.1073/Pnas.79.11.3403 |
0.453 |
|
| 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 |
0.625 |
|
| 1981 |
Smith DH, King J. Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein: III. Inactive polypeptide chains synthesized at 39 °C Journal of Molecular Biology. 145: 653-676. PMID 7265218 DOI: 10.1016/0022-2836(81)90308-9 |
0.422 |
|
| 1981 |
Goldenberg DP, King J. Temperature-sensitive mutants blocked in the folding or subunit assembly of the bacteriophage P22 tail spike protein: II. Active mutant proteins matured at 30 °C Journal of Molecular Biology. 145: 633-651. PMID 7265217 DOI: 10.1016/0022-2836(81)90307-7 |
0.425 |
|
| 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 |
0.634 |
|
| 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 |
0.614 |
|
| 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 |
0.647 |
|
| 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 |
0.663 |
|
| 1979 |
King J, Hall C, Casjens S. Control of the synthesis of phage P22 scaffolding protein is coupled to capsid assembly. Cell. 15: 551-60. PMID 719753 DOI: 10.1016/0092-8674(78)90023-5 |
0.447 |
|
| 1979 |
Earnshaw W, King J. Structure of phage P22 coat protein aggregates formed in the absence of the scaffolding protein. Journal of Molecular Biology. 126: 721-47. PMID 370407 DOI: 10.1016/0022-2836(78)90017-7 |
0.616 |
|
| 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 |
0.544 |
|
| 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 |
0.329 |
|
| 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 |
0.609 |
|
| 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 |
0.478 |
|
| 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 |
0.342 |
|
| 1977 |
Crowther RA, Lenk EV, Kikuchi Y, King J. Molecular reorganization in the hexagon to star transition of the baseplate of bacteriophage T4. Journal of Molecular Biology. 116: 489-523. PMID 592390 DOI: 10.1016/0022-2836(77)90081-X |
0.312 |
|
| 1977 |
Poteete AR, King J. Functions of two new genes in Salmonella phage P22 assembly Virology. 76: 725-739. PMID 320755 DOI: 10.1016/0042-6822(77)90254-9 |
0.343 |
|
| 1977 |
King J, Botstein D, Casjens S, Earnshaw W, Harrison S, Lenk E. Structure and assembly of the capsid of bacteriophage P22. Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 276: 37-49. PMID 13434 DOI: 10.1098/Rstb.1976.0096 |
0.628 |
|
| 1975 |
Kikuchi Y, King J. Assembly of the tail of bacteriophage T4. Journal of Supramolecular Structure. 3: 24-38. PMID 1152465 DOI: 10.1002/Jss.400030104 |
0.424 |
|
| 1975 |
Lenk E, Casjens S, Weeks J, King J. Intracellular visualization of precursor capsids in phage P22 mutant infected cells. Virology. 68: 182-199. PMID 1103445 DOI: 10.1016/0042-6822(75)90160-9 |
0.395 |
|
| 1975 |
Kikuchi Y, King J. Genetic control of bacteriophage T4 baseplate morphogenesis: III. Formation of the central plug and overall assembly pathway Journal of Molecular Biology. 99: 695-716. PMID 765483 DOI: 10.1016/S0022-2836(75)80180-X |
0.368 |
|
| 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 |
0.43 |
|
| 1975 |
Kikuchi Y, King J. Genetic control of bacteriophage T4 baseplate morphogenesis: I. Sequential assembly of the major precursor, in vivo and in vitro Journal of Molecular Biology. 99: 645-672. PMID 765481 DOI: 10.1016/S0022-2836(75)80178-1 |
0.461 |
|
| 1974 |
King J, Lenk EV, Botstein D. Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. II. Morphogenetic pathway. Journal of Molecular Biology. 80: 697-731. PMID 4773027 DOI: 10.1016/0022-2836(73)90205-2 |
0.426 |
|
| 1974 |
Botstein D, Waddell CH, King J. Mechanism of head assembly and DNA encapsulation in Salmonella phage p22. I. Genes, proteins, structures and DNA maturation. Journal of Molecular Biology. 80: 669-95. PMID 4773026 DOI: 10.1016/0022-2836(73)90204-0 |
0.385 |
|
| 1974 |
Casjens S, King J. P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly. Journal of Supramolecular Structure. 2: 202-224. PMID 4612247 DOI: 10.1002/Jss.400020215 |
0.452 |
|
| 1974 |
King J, Casjens S. Catalytic head assembling protein in virus morphogenesis Nature. 251: 112-119. PMID 4421992 DOI: 10.1038/251112A0 |
0.425 |
|
| 1973 |
King J, Mykolajewyoz N. Bacteriophage T4 tail assembly: Proteins of the sheath, core and baseplate Journal of Molecular Biology. 75: 339-358. PMID 4580680 DOI: 10.1016/0022-2836(73)90025-9 |
0.431 |
|
| 1973 |
King J, Laemmli UK. Bacteriophage T4 tail assembly: structural proteins and their genetic identification. Journal of Molecular Biology. 75: 315-37. PMID 4580679 DOI: 10.1016/0022-2836(73)90024-7 |
0.448 |
|
| 1971 |
King J, Laemmli UK. Polypeptides of the tail fibres of bacteriophage T4. Journal of Molecular Biology. 62: 465-77. PMID 5136579 DOI: 10.1016/0022-2836(71)90148-3 |
0.363 |
|
| 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 |
0.368 |
|
| 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 |
0.353 |
|
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