Carolyn Teschke - Publications

Affiliations: 
Molecular and Cell Biology University of Connecticut, Storrs, CT, United States 
Area:
General Biophysics

57 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 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  0.36
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  1
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  0.36
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  0.36
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  1
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  1
2016 Keifer DZ, Motwani T, Teschke CM, Jarrold MF. Measurement of the accurate mass of a 50 MDa infectious virus. Rapid Communications in Mass Spectrometry : Rcm. 30: 1957-62. PMID 27501430 DOI: 10.1002/rcm.7673  0.36
2016 Keifer DZ, Motwani T, Teschke CM, Jarrold MF. Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry. Journal of the American Society For Mass Spectrometry. PMID 27020925 DOI: 10.1007/s13361-016-1362-8  1
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  1
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  1
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  1
2015 D'Lima NG, Teschke CM. A method to investigate protein association with intact sealed mycobacterial membrane vesicles. Analytical Biochemistry. 485: 109-11. PMID 26099936 DOI: 10.1016/j.ab.2015.06.023  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  0.8
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2009 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 (2008) 190, 14, (4880-4887)) Journal of Bacteriology. 191: 4051. DOI: 10.1128/JB.00468-09  1
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  1
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  1
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  1
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  1
2006 Teschke CM. Molecular glue to cement a phage. Structure (London, England : 1993). 14: 803-4. PMID 16698540 DOI: 10.1016/j.str.2006.05.003  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2003 Teschke CM, McGough A, Thuman-Commike PA. Penton release from P22 heat-expanded capsids suggests importance of stabilizing penton-hexon interactions during capsid maturation. Biophysical Journal. 84: 2585-92. PMID 12668466 DOI: 10.1016/S0006-3495(03)75063-2  1
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  1
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  1
2000 Doyle SM, Braswell EH, Teschke CM. SecA folds via a dimeric intermediate. Biochemistry. 39: 11667-76. PMID 10995234 DOI: 10.1021/bi000299y  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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