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Portal Protein: The Orchestrator of Capsid Assembly for the dsDNA Tailed Bacteriophages and Herpesviruses.

Dedeo CL, Cingolani G, Teschke CM.

Annu Rev Virol. 2019 Jul 23. doi: 10.1146/annurev-virology-092818-015819. [Epub ahead of print]


Of capsid structure and stability: The partnership between charged residues of E-loop and P-domain of the bacteriophage P22 coat protein.

Asija K, Teschke CM.

Virology. 2019 Aug;534:45-53. doi: 10.1016/j.virol.2019.05.021. Epub 2019 Jun 2.


A Hydrophobic Network: Intersubunit and Intercapsomer Interactions Stabilizing the Bacteriophage P22 Capsid.

Asija K, Teschke CM.

J Virol. 2019 Jun 28;93(14). pii: e00727-19. doi: 10.1128/JVI.00727-19. Print 2019 Jul 15.


The phage L capsid decoration protein has a novel OB-fold and an unusual capsid binding strategy.

Newcomer RL, Schrad JR, Gilcrease EB, Casjens SR, Feig M, Teschke CM, Alexandrescu AT, Parent KN.

Elife. 2019 Apr 4;8. pii: e45345. doi: 10.7554/eLife.45345.


The amazing HK97 fold: versatile results of modest differences.

Duda RL, Teschke CM.

Curr Opin Virol. 2019 Jun;36:9-16. doi: 10.1016/j.coviro.2019.02.001. Epub 2019 Mar 8. Review.


Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages.

Tripler TN, Kaplan AR, Alexandrescu AT, Teschke CM.

J Virol. 2019 Apr 17;93(9). pii: e00007-19. doi: 10.1128/JVI.00007-19. Print 2019 May 1.


Architect of Virus Assembly: the Portal Protein Nucleates Procapsid Assembly in Bacteriophage P22.

Motwani T, Teschke CM.

J Virol. 2019 Apr 17;93(9). pii: e00187-19. doi: 10.1128/JVI.00187-19. Print 2019 May 1.


NMR assignments for monomeric phage L decoration protein.

Newcomer RL, Belato HB, Teschke CM, Alexandrescu AT.

Biomol NMR Assign. 2018 Oct;12(2):339-343. doi: 10.1007/s12104-018-9836-1. Epub 2018 Aug 14.


Lessons from bacteriophages part 2: A saga of scientific breakthroughs and prospects for their use in human health.

Asija K, Teschke CM.

PLoS Pathog. 2018 May 17;14(5):e1006970. doi: 10.1371/journal.ppat.1006970. eCollection 2018 May. Review. No abstract available.


Lessons from bacteriophages part 1: Deriving utility from protein structure, function, and evolution.

Asija K, Teschke CM.

PLoS Pathog. 2018 May 17;14(5):e1006971. doi: 10.1371/journal.ppat.1006971. eCollection 2018 May. Review. No abstract available.


A viral scaffolding protein triggers portal ring oligomerization and incorporation during procapsid assembly.

Motwani T, Lokareddy RK, Dunbar CA, Cortines JR, Jarrold MF, Cingolani G, Teschke CM.

Sci Adv. 2017 Jul 26;3(7):e1700423. doi: 10.1126/sciadv.1700423. eCollection 2017 Jul.


Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation.

Lokareddy RK, Sankhala RS, Roy A, Afonine PV, Motwani T, Teschke CM, Parent KN, Cingolani G.

Nat Commun. 2017 Jan 30;8:14310. doi: 10.1038/ncomms14310.


NMR assignments for the insertion domain of bacteriophage Sf6 coat protein.

Tripler TN, Teschke CM, Alexandrescu AT.

Biomol NMR Assign. 2017 Apr;11(1):35-38. doi: 10.1007/s12104-016-9716-5. Epub 2016 Oct 31.


Localization of the Houdinisome (Ejection Proteins) inside the Bacteriophage P22 Virion by Bubblegram Imaging.

Wu W, Leavitt JC, Cheng N, Gilcrease EB, Motwani T, Teschke CM, Casjens SR, Steven AC.

MBio. 2016 Aug 9;7(4). pii: e01152-16. doi: 10.1128/mBio.01152-16.


Measurement of the accurate mass of a 50 MDa infectious virus.

Keifer DZ, Motwani T, Teschke CM, Jarrold MF.

Rapid Commun Mass Spectrom. 2016 Sep 15;30(17):1957-62. doi: 10.1002/rcm.7673.


Acquiring Structural Information on Virus Particles with Charge Detection Mass Spectrometry.

Keifer DZ, Motwani T, Teschke CM, Jarrold MF.

J Am Soc Mass Spectrom. 2016 Jun;27(6):1028-36. doi: 10.1007/s13361-016-1362-8. Epub 2016 Mar 28.


Contextual Role of a Salt Bridge in the Phage P22 Coat Protein I-Domain.

Harprecht C, Okifo O, Robbins KJ, Motwani T, Alexandrescu AT, Teschke CM.

J Biol Chem. 2016 May 20;291(21):11359-72. doi: 10.1074/jbc.M116.716910. Epub 2016 Mar 22.


Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.

Newcomer RL, Fraser LCR, Teschke CM, Alexandrescu AT.

Biophys J. 2015 Dec 15;109(12):2666-2677. doi: 10.1016/j.bpj.2015.11.010.


A method to investigate protein association with intact sealed mycobacterial membrane vesicles.

D'Lima NG, Teschke CM.

Anal Biochem. 2015 Sep 15;485:109-11. doi: 10.1016/j.ab.2015.06.023. Epub 2015 Jun 20.


Nature's favorite building block: Deciphering folding and capsid assembly of proteins with the HK97-fold.

Suhanovsky MM, Teschke CM.

Virology. 2015 May;479-480:487-97. doi: 10.1016/j.virol.2015.02.055. Epub 2015 Apr 8. Review.


NMR assignments for the insertion domain of bacteriophage CUS-3 coat protein.

Tripler TN, Maciejewski MW, Teschke CM, Alexandrescu AT.

Biomol NMR Assign. 2015 Oct;9(2):333-6. doi: 10.1007/s12104-015-9604-4. Epub 2015 Feb 19.


Multiple functional roles of the accessory I-domain of bacteriophage P22 coat protein revealed by NMR structure and CryoEM modeling.

Rizzo AA, Suhanovsky MM, Baker ML, Fraser LC, Jones LM, Rempel DL, Gross ML, Chiu W, Alexandrescu AT, Teschke CM.

Structure. 2014 Jun 10;22(6):830-41. doi: 10.1016/j.str.2014.04.003. Epub 2014 May 15.


ADP-dependent conformational changes distinguish Mycobacterium tuberculosis SecA2 from SecA1.

D'Lima NG, Teschke CM.

J Biol Chem. 2014 Jan 24;289(4):2307-17. doi: 10.1074/jbc.M113.533323. Epub 2013 Dec 2.


An intramolecular chaperone inserted in bacteriophage P22 coat protein mediates its chaperonin-independent folding.

Suhanovsky MM, Teschke CM.

J Biol Chem. 2013 Nov 22;288(47):33772-83. doi: 10.1074/jbc.M113.515312. Epub 2013 Oct 13.


NMR assignments for the telokin-like domain of bacteriophage P22 coat protein.

Rizzo AA, Fraser LC, Sheftic SR, Suhanovsky MM, Teschke CM, Alexandrescu AT.

Biomol NMR Assign. 2013 Oct;7(2):257-60. doi: 10.1007/s12104-012-9422-x. Epub 2012 Sep 18.


Themes and variations of viral small terminase proteins.

Teschke CM.

Structure. 2012 Aug 8;20(8):1291-2. doi: 10.1016/j.str.2012.07.007. No abstract available.


Unraveling the role of the C-terminal helix turn helix of the coat-binding domain of bacteriophage P22 scaffolding protein.

Padilla-Meier GP, Gilcrease EB, Weigele PR, Cortines JR, Siegel M, Leavitt JC, Teschke CM, Casjens SR.

J Biol Chem. 2012 Sep 28;287(40):33766-80. Epub 2012 Aug 9.


Stepwise molecular display utilizing icosahedral and helical complexes of phage coat and decoration proteins in the development of robust nanoscale display vehicles.

Parent KN, Deedas CT, Egelman EH, Casjens SR, Baker TS, Teschke CM.

Biomaterials. 2012 Aug;33(22):5628-37. doi: 10.1016/j.biomaterials.2012.04.026. Epub 2012 May 8.


The energetic contributions of scaffolding and coat proteins to the assembly of bacteriophage procapsids.

Zlotnick A, Suhanovsky MM, Teschke CM.

Virology. 2012 Jun 20;428(1):64-9. doi: 10.1016/j.virol.2012.03.017. Epub 2012 Apr 20.


Decoding bacteriophage P22 assembly: identification of two charged residues in scaffolding protein responsible for coat protein interaction.

Cortines JR, Weigele PR, Gilcrease EB, Casjens SR, Teschke CM.

Virology. 2011 Dec 5;421(1):1-11. doi: 10.1016/j.virol.2011.09.005. Epub 2011 Oct 4.


Bacteriophage P22 capsid size determination: roles for the coat protein telokin-like domain and the scaffolding protein amino-terminus.

Suhanovsky MM, Teschke CM.

Virology. 2011 Sep 1;417(2):418-29. doi: 10.1016/j.virol.2011.06.025. Epub 2011 Jul 23.


Conformational changes in bacteriophage P22 scaffolding protein induced by interaction with coat protein.

Padilla-Meier GP, Teschke CM.

J Mol Biol. 2011 Jul 8;410(2):226-40. doi: 10.1016/j.jmb.2011.05.006. Epub 2011 May 14.


Cryo-reconstructions of P22 polyheads suggest that phage assembly is nucleated by trimeric interactions among coat proteins.

Parent KN, Sinkovits RS, Suhanovsky MM, Teschke CM, Egelman EH, Baker TS.

Phys Biol. 2010 Dec 9;7(4):045004. doi: 10.1088/1478-3975/7/4/045004.


Determinants of bacteriophage P22 polyhead formation: the role of coat protein flexibility in conformational switching.

Suhanovsky MM, Parent KN, Dunn SE, Baker TS, Teschke CM.

Mol Microbiol. 2010 Sep;77(6):1568-82. doi: 10.1111/j.1365-2958.2010.07311.x. Epub 2010 Aug 18.


'Let the phage do the work': using the phage P22 coat protein structures as a framework to understand its folding and assembly mutants.

Teschke CM, Parent KN.

Virology. 2010 Jun 5;401(2):119-30. doi: 10.1016/j.virol.2010.02.017. Epub 2010 Mar 16. Review.


P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks.

Parent KN, Khayat R, Tu LH, Suhanovsky MM, Cortines JR, Teschke CM, Johnson JE, Baker TS.

Structure. 2010 Mar 10;18(3):390-401. doi: 10.1016/j.str.2009.12.014.


ATPase activity of Mycobacterium tuberculosis SecA1 and SecA2 proteins and its importance for SecA2 function in macrophages.

Hou JM, D'Lima NG, Rigel NW, Gibbons HS, McCann JR, Braunstein M, Teschke CM.

J Bacteriol. 2008 Jul;190(14):4880-7. doi: 10.1128/JB.00412-08. Epub 2008 May 16. Erratum in: J Bacteriol. 2009 Jun;191(12):4051.


Polyhead formation in phage P22 pinpoints a region in coat protein required for conformational switching.

Parent KN, Suhanovsky MM, Teschke CM.

Mol Microbiol. 2007 Sep;65(5):1300-10. Epub 2007 Aug 3.


GroEL/S substrate specificity based on substrate unfolding propensity.

Parent KN, Teschke CM.

Cell Stress Chaperones. 2007 Spring;12(1):20-32.


Phage P22 procapsids equilibrate with free coat protein subunits.

Parent KN, Suhanovsky MM, Teschke CM.

J Mol Biol. 2007 Jan 12;365(2):513-22. Epub 2006 Oct 4.


Molecular glue to cement a phage.

Teschke CM.

Structure. 2006 May;14(5):803-4. No abstract available.


Electrostatic interactions govern both nucleation and elongation during phage P22 procapsid assembly.

Parent KN, Doyle SM, Anderson E, Teschke CM.

Virology. 2005 Sep 15;340(1):33-45.


SecA folding kinetics: a large dimeric protein rapidly forms multiple native states.

Doyle SM, Bilsel O, Teschke CM.

J Mol Biol. 2004 Jul 30;341(1):199-214.


A concerted mechanism for the suppression of a folding defect through interactions with chaperones.

Doyle SM, Anderson E, Parent KN, Teschke CM.

J Biol Chem. 2004 Apr 23;279(17):17473-82. Epub 2004 Feb 4.


Rapid unfolding of a domain populates an aggregation-prone intermediate that can be recognized by GroEL.

Doyle SM, Anderson E, Zhu D, Braswell EH, Teschke CM.

J Mol Biol. 2003 Sep 26;332(4):937-51.


Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties.

Anderson E, Teschke CM.

Virology. 2003 Aug 15;313(1):184-97.

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