| Year |
Citation |
Score |
| 2023 |
Iglesias SM, Lokareddy RK, Yang R, Li F, Yeggoni DP, David Hou CF, Leroux MN, Cortines JR, Leavitt JC, Bird M, Casjens SR, White S, Teschke CM, Cingolani G. Molecular Architecture of Salmonella Typhimurium Virus P22 Genome Ejection Machinery. Journal of Molecular Biology. 435: 168365. PMID 37952769 DOI: 10.1016/j.jmb.2023.168365 |
0.316 |
|
| 2023 |
Leavitt JC, Woodbury BM, Gilcrease EB, Bridges CM, Teschke CM, Casjens SR. Bacteriophage P22 SieA mediated superinfection exclusion. Biorxiv : the Preprint Server For Biology. PMID 37645741 DOI: 10.1101/2023.08.15.553423 |
0.459 |
|
| 2022 |
Woodbury BM, Motwani T, Leroux MN, Barnes LF, Lyktey NA, Banerjee S, Dedeo CL, Jarrold MF, Teschke CM. Tryptophan Residues Are Critical for Portal Protein Assembly and Incorporation in Bacteriophage P22. Viruses. 14. PMID 35891382 DOI: 10.3390/v14071400 |
0.6 |
|
| 2022 |
Whitehead RD, Teschke CM, Alexandrescu AT. Pulse-field gradient nuclear magnetic resonance of protein translational diffusion from native to non-native states. Protein Science : a Publication of the Protein Society. 31: e4321. PMID 35481638 DOI: 10.1002/pro.4321 |
0.312 |
|
| 2021 |
Leavitt JC, Gilcrease EB, Woodbury BM, Teschke CM, Casjens SR. Intravirion DNA Can Access the Space Occupied by the Bacteriophage P22 Ejection Proteins. Viruses. 13. PMID 34452369 DOI: 10.3390/v13081504 |
0.36 |
|
| 2020 |
Dedeo CL, Teschke CM, Alexandrescu AT. Keeping It Together: Structures, Functions, and Applications of Viral Decoration Proteins. Viruses. 12. PMID 33066635 DOI: 10.3390/v12101163 |
0.453 |
|
| 2020 |
Alexandrescu AT, Kaplan A, Tripler T, Teschke CM. NMR Structures of Closely Related Protein Conformations Biophysical Journal. 118: 23a. DOI: 10.1016/J.Bpj.2019.11.306 |
0.376 |
|
| 2019 |
Whitehead RD, Teschke CM, Alexandrescu AT. NMR Mapping of Disordered Segments from a Viral Scaffolding Protein Enclosed in a 23 MDa Procapsid. Biophysical Journal. 117: 1387-1392. PMID 31585705 DOI: 10.1016/J.Bpj.2019.08.038 |
0.324 |
|
| 2019 |
Dedeo CL, Cingolani G, Teschke CM. Portal Protein: The Orchestrator of Capsid Assembly for the dsDNA Tailed Bacteriophages and Herpesviruses. Annual Review of Virology. PMID 31337287 DOI: 10.1146/annurev-virology-092818-015819 |
0.395 |
|
| 2019 |
Asija K, Teschke CM. Of capsid structure and stability: The partnership between charged residues of E-loop and P-domain of the bacteriophage P22 coat protein. Virology. 534: 45-53. PMID 31176063 DOI: 10.1016/j.virol.2019.05.021 |
0.537 |
|
| 2019 |
Asija K, Teschke CM. A hydrophobic network: Intersubunit and intercapsomer interactions stabilizing the bacteriophage P22 capsid. Journal of Virology. PMID 31068429 DOI: 10.1128/JVI.00727-19 |
0.514 |
|
| 2019 |
Newcomer RL, Schrad JR, Gilcrease EB, Casjens SR, Feig M, Teschke CM, Alexandrescu AT, Parent KN. The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy. Elife. 8. PMID 30945633 DOI: 10.7554/Elife.45345 |
0.744 |
|
| 2019 |
Duda RL, Teschke CM. The amazing HK97 fold: versatile results of modest differences. Current Opinion in Virology. 36: 9-16. PMID 30856581 DOI: 10.1016/j.coviro.2019.02.001 |
0.628 |
|
| 2019 |
Tripler TN, Kaplan AR, Alexandrescu AT, Teschke CM. Conservation and divergence of the I-domain inserted into the ubiquitous HK97 coat protein fold in the P22-like bacteriophages. Journal of Virology. PMID 30787158 DOI: 10.1128/Jvi.00007-19 |
0.512 |
|
| 2019 |
Motwani T, Teschke CM. The architect of virus assembly: portal protein nucleates procapsid assembly in bacteriophage P22. Journal of Virology. PMID 30787152 DOI: 10.1128/Jvi.00187-19 |
0.496 |
|
| 2018 |
Newcomer RL, Belato HB, Teschke CM, Alexandrescu AT. NMR assignments for monomeric phage L decoration protein. Biomolecular Nmr Assignments. PMID 30109462 DOI: 10.1007/S12104-018-9836-1 |
0.391 |
|
| 2018 |
Asija K, Teschke CM. Lessons from bacteriophages part 1: Deriving utility from protein structure, function, and evolution. Plos Pathogens. 14: e1006971. PMID 29772002 DOI: 10.1371/journal.ppat.1006971 |
0.388 |
|
| 2018 |
Newcomer R, Belato H, Teschke C, Alexandrescu A. NMR assignments of Decorator, a phage-cementing 15 KDa monomer Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr27435 |
0.351 |
|
| 2018 |
Alexandrescu AT, Tripler TN, Kaplan AR, Parent KN, Teschke CM. IDP Segment Conservation and Divergence in I-Domains of the Phage Lambda Supercluster Biophysical Journal. 114: 67a. DOI: 10.1016/J.Bpj.2017.11.414 |
0.603 |
|
| 2017 |
Motwani T, Lokareddy RK, Dunbar CA, Cortines JR, Jarrold MF, Cingolani G, Teschke CM. A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly. Science Advances. 3: e1700423. PMID 28782023 DOI: 10.1126/Sciadv.1700423 |
0.421 |
|
| 2017 |
Lokareddy RK, Sankhala RS, Roy A, Afonine PV, Motwani T, Teschke CM, Parent KN, Cingolani G. Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation. Nature Communications. 8: 14310. PMID 28134243 DOI: 10.1038/Ncomms14310 |
0.774 |
|
| 2016 |
Tripler TN, Teschke CM, Alexandrescu AT. NMR assignments for the insertion domain of bacteriophage Sf6 coat protein. Biomolecular Nmr Assignments. PMID 27798771 DOI: 10.1007/s12104-016-9716-5 |
0.553 |
|
| 2016 |
Wu W, Leavitt JC, Cheng N, Gilcrease EB, Motwani T, Teschke CM, Casjens SR, Steven AC. Localization of the Houdinisome (Ejection Proteins) inside the Bacteriophage P22 Virion by Bubblegram Imaging. Mbio. 7. PMID 27507825 DOI: 10.1128/Mbio.01152-16 |
0.495 |
|
| 2016 |
Harprecht C, Okifo O, Robbins KJ, Motwani T, Alexandrescu AT, Teschke CM. Contextual Role of a Salt-Bridge in the Phage P22 Coat Protein I-Domain. The Journal of Biological Chemistry. PMID 27006399 DOI: 10.1074/Jbc.M116.716910 |
0.532 |
|
| 2015 |
Newcomer RL, Fraser LC, Teschke CM, Alexandrescu AT. Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding. Biophysical Journal. 109: 2666-77. PMID 26682823 DOI: 10.1016/J.Bpj.2015.11.010 |
0.373 |
|
| 2015 |
D'Lima NG, Teschke CM. A Molecular Staple: D-Loops in the I Domain of Bacteriophage P22 Coat Protein Make Important Intercapsomer Contacts Required for Procapsid Assembly. Journal of Virology. 89: 10569-79. PMID 26269173 DOI: 10.1128/JVI.01629-15 |
0.534 |
|
| 2015 |
Suhanovsky MM, Teschke CM. Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold. Virology. 479: 487-97. PMID 25864106 DOI: 10.1016/j.virol.2015.02.055 |
0.572 |
|
| 2015 |
Tripler TN, Maciejewski MW, Teschke CM, Alexandrescu AT. NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein. Biomolecular Nmr Assignments. 9: 333-6. PMID 25694158 DOI: 10.1007/S12104-015-9604-4 |
0.396 |
|
| 2014 |
Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM. Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling. Structure (London, England : 1993). 22: 830-41. PMID 24836025 DOI: 10.1016/J.Str.2014.04.003 |
0.507 |
|
| 2014 |
Cortines JR, Motwani T, Vyas AA, Teschke CM. Highly specific salt bridges govern bacteriophage P22 icosahedral capsid assembly: identification of the site in coat protein responsible for interaction with scaffolding protein. Journal of Virology. 88: 5287-97. PMID 24600011 DOI: 10.1128/Jvi.00036-14 |
0.683 |
|
| 2014 |
D'Lima NG, Teschke CM. ADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1. The Journal of Biological Chemistry. 289: 2307-17. PMID 24297168 DOI: 10.1074/jbc.M113.533323 |
0.412 |
|
| 2013 |
Suhanovsky MM, Teschke CM. An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding. The Journal of Biological Chemistry. 288: 33772-83. PMID 24126914 DOI: 10.1074/jbc.M113.515312 |
0.532 |
|
| 2013 |
Rizzo AA, Fraser LC, Sheftic SR, Suhanovsky MM, Teschke CM, Alexandrescu AT. NMR assignments for the telokin-like domain of bacteriophage P22 coat protein. Biomolecular Nmr Assignments. 7: 257-60. PMID 22987227 DOI: 10.1007/S12104-012-9422-X |
0.543 |
|
| 2012 |
Teschke CM. Themes and variations of viral small terminase proteins. Structure (London, England : 1993). 20: 1291-2. PMID 22884105 DOI: 10.1016/j.str.2012.07.007 |
0.419 |
|
| 2012 |
Padilla-Meier GP, Gilcrease EB, Weigele PR, Cortines JR, Siegel M, Leavitt JC, Teschke CM, Casjens SR. Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein. The Journal of Biological Chemistry. 287: 33766-80. PMID 22879595 DOI: 10.1074/Jbc.M112.393132 |
0.839 |
|
| 2012 |
Parent KN, Deedas CT, Egelman EH, Casjens SR, Baker TS, Teschke CM. Stepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles. Biomaterials. 33: 5628-37. PMID 22575828 DOI: 10.1016/J.Biomaterials.2012.04.026 |
0.766 |
|
| 2012 |
Zlotnick A, Suhanovsky MM, Teschke CM. The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids. Virology. 428: 64-9. PMID 22520942 DOI: 10.1016/J.Virol.2012.03.017 |
0.649 |
|
| 2011 |
Cortines JR, Weigele PR, Gilcrease EB, Casjens SR, Teschke CM. Decoding bacteriophage P22 assembly: identification of two charged residues in scaffolding protein responsible for coat protein interaction. Virology. 421: 1-11. PMID 21974803 DOI: 10.1016/J.Virol.2011.09.005 |
0.685 |
|
| 2011 |
Suhanovsky MM, Teschke CM. Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus. Virology. 417: 418-29. PMID 21784500 DOI: 10.1016/j.virol.2011.06.025 |
0.687 |
|
| 2011 |
Padilla-Meier GP, Teschke CM. Conformational changes in bacteriophage P22 scaffolding protein induced by interaction with coat protein. Journal of Molecular Biology. 410: 226-40. PMID 21605566 DOI: 10.1016/j.jmb.2011.05.006 |
0.834 |
|
| 2010 |
Parent KN, Sinkovits RS, Suhanovsky MM, Teschke CM, Egelman EH, Baker TS. Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins. Physical Biology. 7: 045004. PMID 21149969 DOI: 10.1088/1478-3975/7/4/045004 |
0.743 |
|
| 2010 |
Suhanovsky MM, Parent KN, Dunn SE, Baker TS, Teschke CM. Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching. Molecular Microbiology. 77: 1568-82. PMID 20659287 DOI: 10.1111/J.1365-2958.2010.07311.X |
0.843 |
|
| 2010 |
Teschke CM, Parent KN. 'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants. Virology. 401: 119-30. PMID 20236676 DOI: 10.1016/J.Virol.2010.02.017 |
0.805 |
|
| 2010 |
Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS. P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks. Structure (London, England : 1993). 18: 390-401. PMID 20223221 DOI: 10.1016/J.Str.2009.12.014 |
0.785 |
|
| 2008 |
Hou JM, D'Lima NG, Rigel NW, Gibbons HS, McCann JR, Braunstein M, Teschke CM. ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophages. Journal of Bacteriology. 190: 4880-7. PMID 18487341 DOI: 10.1128/Jb.00412-08 |
0.334 |
|
| 2007 |
Parent KN, Suhanovsky MM, Teschke CM. Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching. Molecular Microbiology. 65: 1300-10. PMID 17680786 DOI: 10.1111/J.1365-2958.2007.05868.X |
0.835 |
|
| 2007 |
Parent KN, Teschke CM. GroEL/S substrate specificity based on substrate unfolding propensity. Cell Stress & Chaperones. 12: 20-32. PMID 17441504 DOI: 10.1379/Csc-219R.1 |
0.834 |
|
| 2007 |
Parent KN, Suhanovsky MM, Teschke CM. Phage P22 procapsids equilibrate with free coat protein subunits. Journal of Molecular Biology. 365: 513-22. PMID 17067636 DOI: 10.1016/J.Jmb.2006.09.088 |
0.78 |
|
| 2006 |
Parent KN, Zlotnick A, Teschke CM. Quantitative analysis of multi-component spherical virus assembly: scaffolding protein contributes to the global stability of phage P22 procapsids. Journal of Molecular Biology. 359: 1097-106. PMID 16697406 DOI: 10.1016/J.Jmb.2006.03.068 |
0.817 |
|
| 2005 |
Parent KN, Doyle SM, Anderson E, Teschke CM. Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly. Virology. 340: 33-45. PMID 16045955 DOI: 10.1016/J.Virol.2005.06.018 |
0.831 |
|
| 2004 |
Parent KN, Ranaghan MJ, Teschke CM. A second-site suppressor of a folding defect functions via interactions with a chaperone network to improve folding and assembly in vivo. Molecular Microbiology. 54: 1036-50. PMID 15522085 DOI: 10.1111/J.1365-2958.2004.04326.X |
0.845 |
|
| 2004 |
Doyle SM, Bilsel O, Teschke CM. SecA folding kinetics: a large dimeric protein rapidly forms multiple native states. Journal of Molecular Biology. 341: 199-214. PMID 15312773 DOI: 10.1016/J.Jmb.2004.06.021 |
0.707 |
|
| 2004 |
Doyle SM, Anderson E, Parent KN, Teschke CM. A concerted mechanism for the suppression of a folding defect through interactions with chaperones. The Journal of Biological Chemistry. 279: 17473-82. PMID 14764588 DOI: 10.1074/Jbc.M400467200 |
0.85 |
|
| 2003 |
Doyle SM, Anderson E, Zhu D, Braswell EH, Teschke CM. Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL. Journal of Molecular Biology. 332: 937-51. PMID 12972263 DOI: 10.1016/S0022-2836(03)00955-0 |
0.806 |
|
| 2003 |
Anderson E, Teschke CM. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Virology. 313: 184-97. PMID 12951032 DOI: 10.1016/S0042-6822(03)00240-X |
0.623 |
|
| 2001 |
Aramli LA, Teschke CM. Alleviation of a defect in protein folding by increasing the rate of subunit assembly. The Journal of Biological Chemistry. 276: 25372-7. PMID 11304542 DOI: 10.1074/Jbc.M101759200 |
0.802 |
|
| 2000 |
de Beus MD, Doyle SM, Teschke CM. GroEL binds a late folding intermediate of phage P22 coat protein. Cell Stress & Chaperones. 5: 163-72. PMID 11005374 DOI: 10.1379/1466-1268(2000)005<0163:Gbalfi>2.0.Co;2 |
0.821 |
|
| 2000 |
Doyle SM, Braswell EH, Teschke CM. SecA folds via a dimeric intermediate. Biochemistry. 39: 11667-76. PMID 10995234 DOI: 10.1021/Bi000299Y |
0.699 |
|
| 2000 |
Capen CM, Teschke CM. Folding defects caused by single amino acid substitutions in a subunit are not alleviated by assembly Biochemistry. 39: 1142-1151. PMID 10653661 DOI: 10.1021/bi991956t |
0.653 |
|
| 1999 |
Aramli LA, Teschke CM. Single amino acid substitutions globally suppress the folding defects of temperature-sensitive folding mutants of phage P22 coat protein. The Journal of Biological Chemistry. 274: 22217-24. PMID 10428787 DOI: 10.1074/Jbc.274.32.22217 |
0.803 |
|
| 1999 |
Teschke CM. Aggregation and assembly of phage P22 temperature-sensitive coat protein mutants in vitro mimic the in vivo phenotype Biochemistry. 38: 2873-2881. PMID 10074339 DOI: 10.1021/bi982739f |
0.668 |
|
| 1998 |
Nakonechny WS, Teschke CM. GroEL and GroES control of substrate flux in the in vivo folding pathway of phage P22 coat protein Journal of Biological Chemistry. 273: 27236-27244. PMID 9765246 DOI: 10.1074/jbc.273.42.27236 |
0.667 |
|
| 1997 |
Fong DG, Doyle SM, Teschke CM. The folded conformation of phage P22 coat protein is affected by amino acid substitutions that lead to a cold-sensitive phenotype. Biochemistry. 36: 3971-80. PMID 9092827 DOI: 10.1021/Bi962188Y |
0.774 |
|
| 1996 |
Teschke CM, Fong DG. Interactions between coat and scaffolding proteins of phage P22 are altered in vitro by amino acid substitutions in coat protein that cause a cold-sensitive phenotype Biochemistry. 35: 14831-14840. PMID 8942646 DOI: 10.1021/bi960860l |
0.705 |
|
| 1995 |
Foguel D, Teschke CM, Prevelige PE, Silva JL. Role of entropic interactions in viral capsids: single amino acid substitutions in P22 bacteriophage coat protein resulting in loss of capsid stability. Biochemistry. 34: 1120-6. PMID 7827060 DOI: 10.1021/Bi00004A003 |
0.369 |
|
| 1995 |
Teschke CM. In vitro folding of phage p22 coat protein with amino acid substitutions that confer in vivo temperature sensitivity Biochemistry®. 34: 6815-6826. PMID 7756313 DOI: 10.1021/Bi00020A028 |
0.692 |
|
| 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 |
0.596 |
|
| 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 |
0.489 |
|
| 1991 |
Teschke CM, Kim J, Song T, Park S, Park C, Randall LL. Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. The Journal of Biological Chemistry. 266: 11789-96. PMID 1904869 |
0.653 |
|
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