Publications

2020

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Draganova E.B., Thorsen M.K. and Heldwein E.E. (2020). Nuclear Egress. In "Alphaherpesviruses: Molecular Biology, Host Interactions and Control", E.E Heldwein and G.A. Smith, Eds. Caister Academic Press. doi: https://doi.org/10.21775/9781913652555.08

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White E.M., Stampfer S.D., and Heldwein E.E. (2020). Expression, purification, and crystallization of HSV-1 glycoproteins for structure determination. In “Methods in Molecular Biology: Herpes Simplex Virus: Methods and Protocols”, R. Diefenbach and C. Fraefel, Eds. Springer Science and Business Media. 2060:377-393. doi: 10.1007/978-1-4939-9814-2_23

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Cooper R.S. and Heldwein E.E. (2020). Expression, purification, and crystallization of full-length HSV-1 gB for structure determination. In “Methods in Molecular Biology: Herpes Simplex Virus: Methods and Protocols”, R. Diefenbach and C. Fraefel, Eds. Springer Science and Business Media. 2060:395-407. doi: 10.1007/978-1-4939-9814-2_24

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Draganova E.B. and Heldwein E.E. (2020). Virally derived peptide inhibitors of the herpes simplex virus type 1 nuclear egress complex. BIORXIV/2020/168898. doi: https://doi.org/10.1101/2020.06.24.168898
 

Metrick, C.M., Koenigsberg, A.L., Heldwein, E.E. (2020) Conserved outer-tegument component UL11 from herpes simplex virus type 1 is an intrinsically disordered, RNA-binding protein. mBio. https://mbio.asm.org/content/11/3/e00810-20.

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Koenigsberg, A.L., Pitts, J.D. and Heldwein, E.E. (2020). Identification of buffer conditions for optimal thermostability and solubility of herpesviral protein UL37 using the Thermofluor assay. Bio-protocol. 10: e3662. doi: 10.21769/BioProtoc.3662

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Draganova, E.B., Zhang, J., Zhou, Z.H., Heldwein, E.E. (2020) Structural basis for capsid recruitment and coat formation during HSV-1 nuclear egress. bioRxiv. https://www.biorxiv.org/content/10.1101/2020.03.11.988170v1.

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Hilterbrand, A.T., Daly, R., Heldwein, E.E. (2020) Contributions of the four essential entry glycoproteins to HSV-1 tropism and the selection of entry routes. bioRxiv. https://www.biorxiv.org/content/10.1101/2020.03.10.985325v1

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2019

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Hilterbrand, A.T. and Heldwein, E.E. (2019) Go go gadget glycoprotein!: HSV-1 draws on its sizeable glycoprotein tool kit to customize its diverse entry routes. PLoS Pathog. 15(5), e1007660. PMC6508585.

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2018

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Koenigsberg, A.L., and Heldwein, E.E. (2018) The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J. Biol Chem. 293(41), 15827-15839. PMC6187633.

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Cooper R.S, Georgieva E.R., Borbat P.P., Freed J.H., Heldwein E.E. (2018) Structural basis for membrane anchoring and fusion regulation of the herpes simplex virus fusogen gB.  Nature Structural & Molecular Biology, Volume 25, pages 416–424 (2018). PMC5942590. 

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Heldwein E.E. (2018)  Up close with herpesviruses. Science. Vol. 360, Issue 6384, pp. 34-35,  06 April 2018. PMID: 29622644. 

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2017

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Richards, A.L., Sollars, P.J., Pitts, P.D., Stults, A.M., Heldwein, E.E., Pickard, G.E. and Smith, G.A. (2017) The pUL37 tegument protein guides alpha-herpesvirus retrograde axonal transport to promote neuroinvasion. PLoS Pathog 13(12): e1006741. PMC5749899. 

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Koenigsberg A.L. and  Heldwein E.E. (2017) Crystal structure of the N-terminal half of the traffic controller UL37 from Herpes Simplex virus Type 1. J. Virol. 2017 Sep 27;91(20), Print 2017 Oct 15. PMC5625493.

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Wang, P., Yu, Z., Santangelo, T.J., Olesik, J., Wang, Y., Heldwein, E. and Li, X. (2017) BosR is a novel Fur family member responsive to copper and regulating copper homeostasis in Borrelia burgdorferi. J Bacteriol 199(16); e00276-17. PMC5527378.

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Bigalke J.M. and Heldwein E.E. (2017). Have NEC Coat, Will Travel: Structural Basis of Membrane Budding During Nuclear Egress in Herpesviruses. Adv Virus Res. 97, 107-141. PMC5367388.

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2016

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Rogalin H.B. and Heldwein E.E. Characterization of VSV pseudotypes bearing essential entry glycoproteins gB, gD, gH, and gL of Herpes Simplex virus Type 1. J. Virol. 90, 10321-10328. PMC5105666.

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Bigalke J.M. and Heldwein E.E. (2016). Expression, Purification and Crystallization of the Herpesvirus Nuclear Egress Complex (NEC). Bio-protocol. 6:e1872. PMC5199029.

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Meyer PA, Socias S, Key J, Ransey E, Tjon EC, Buschiazzo A, Lei M, Botka C, Withrow J, Neau D, Rajashankar K, Anderson KS, Baxter RH, Blacklow SC, Boggon TJ, Bonvin AM, Borek D, Brett TJ, Caflisch A, Chang CI, Chazin WJ, Corbett KD, Cosgrove MS, Crosson S, Dhe-Paganon S, Di Cera E, Drennan CL, Eck MJ, Eichman BF, Fan QR, Ferré-D’Amaré AR, Christopher Fromme J, Garcia KC, Gaudet R, Gong P, Harrison SC, Heldwein EE, Jia Z, Keenan RJ, Kruse AC, Kvansakul M, McLellan JS, Modis Y, Nam Y, Otwinowski Z, Pai EF, Pereira PJ, Petosa C, Raman CS, Rapoport TA, Roll-Mecak A, Rosen MK, Rudenko G, Schlessinger J, Schwartz TU, Shamoo Y, Sondermann H, Tao YJ, Tolia NH, Tsodikov OV, Westover KD, Wu H, Foster I, Fraser JS, Maia FR, Gonen T, Kirchhausen T, Diederichs K, Crosas M, Sliz P. (2016). Data publication with the structural biology data grid supports live analysis. Nat Commun. 7, 10882. PMC4786681.

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Bigalke, J.M. and Heldwein E.E. (2016). Nuclear Exodus: Herpesviruses Lead the Way. Annu Rev Virol. 3, 387-409. PMC5065387.

Metrick, C.M. and Heldwein E.E. (2016). Novel Structure and Unexpected RNA-Binding Ability of the C-Terminal Domain of Herpes Simplex Virus 1 Tegument Protein UL21. J Virol.  90, 5759-5769. PMC4886797.

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Heldwein E.E. (2016). gH/gL supercomplexes at early stages of herpesvirus entry. Curr Opin Virol.  18, 1-8. PMC4970976.

2015

Cooper, R.S. and Heldwein E.E. (2015). Herpesvirus gB: A Finely Tuned Fusion Machine. Viruses.  7, 6552-6569. PMC4690880.

Bigalke, J.M. and Heldwein E.E. (2015). Structural basis of membrane budding by the nuclear egress complex of herpesviruses. EMBO J.  34, 2921-2936. PMC4687684.

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Burke H.G. and Heldwein E.E. (2015). Crystal Structure of the Human Cytomegalovirus Glycoprotein B. PLoS Pathog.  11, e1005227. PMC4617298.

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Rogalin H.B. and Heldwein E.E. (2015). The interplay between the HSV-1 gB cytodomains and the gH cytotail during cell-cell fusion. J. Virol.  89, 12262-12272. PMC4665236.

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Bigalke J.M. and Heldwein E.E. (2015). The great (nuclear) escape: new insights into the role of the nuclear egress complex of herpesviruses. J. Virol. 89, 9150-9153. PMC4542350.

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Metrick C.M., Chadha P., and Heldwein E.E. (2015). The unusual fold of Herpes Simplex Virus 1 UL21, a multifunctional tegument protein. J. Virol. 89, 2979-2984. PMC4325721.

2014

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Bigalke J.M., Heuser T., Nicastro D., and Heldwein E.E. (2014). Membrane deformation and scission by the HSV-1 nuclear egress complex. Nat. Commun. 5, 4131. PMC41105210.

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Pitts J.D., Klabis J., Richards A.L., Smith G.A., and Heldwein E.E. (2014). Crystal structure of the herpesvirus inner tegument protein UL37 supports its essential role in control of viral trafficking. J. Virol. 88, 5462-5473. PMC4019128.

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Stampfer S.D. and Heldwein E.E. (2014). Expression, Purification, and Crystallization of HSV-1 Glycoproteins for Structure Determination. Methods Mol. Biol. 1144, 249-263. PMID: 24671689.

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2013

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Silverman J.L. and Heldwein E.E. (2013). Mutations in the cytoplasmic tail of HSV-1 gH reduce the fusogenicity of gB in transfected cells. J. Virol. 87, 10139-47. PMC3753984.

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Stampfer S.D. and Heldwein E.E. (2013). Stuck in the middle: structural insights into the role of gH/gL heterodimer in herpesvirus entry. Curr. Opin. Virol. 3, 13-19. PMCID: PMC3562363.

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Vitu E., Sharma S., Stampfer S.D., and Heldwein E.E. (2013). Extensive mutagenesis of the HSV-1 gB ectodomain reveals remarkable stability of its postfusion form. J. Mol. Biol. 425, 2056-2071. PMC3655159.

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Sharma S., Wisner T.W., Johnson D.C., and Heldwein E.E. (2013). HCMV gB shares structural and biochemical properties with gB proteins from other herpesviruses. Virology 435, 239-249. PMC3534942.

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2012

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Silverman J.L., Greene N.G., King D.S., and Heldwein E.E. (2012). Membrane requirement for the folding of the HSV-1 gB cytodomain suggests a unique mechanism of fusion regulation. J. Virol. 86, 8171-8184. PMC3421659.

2011

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Eisenberg R.J., Heldwein E.E., Cohen G.H., and Krummenacher C. Recent progress in understanding herpes simplex virus entry: relationship of structure to function. In: “Alpha Herpesviruses: Molecular Virology”, S.K. Weller, Ed. Caister Academic Press. March 2011.

Cairns T.M., Whitbeck J.C., Lou H., Heldwein E.E., Chowdary T.K., Eisenberg R.J., and Cohen G.H. (2011). Capturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment. J. Virol. 85, 6175-6184. PMC3126480.

2010

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Stampfer S.D., Lou H., Cohen G.H., Eisenberg R.J., and Heldwein E.E. (2010). Structural basis of local, pH-dependent conformational changes in glycoprotein B from Herpes Simplex virus 1. J. Virol. 84, 12924-12933. PMC3004323.

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Chowdary T.K., Cairns T.M., Atanasiu D., Cohen G.H., Eisenberg R.J., and Heldwein E.E. (2010). Crystal structure of the conserved herpesvirus fusion regulator complex gH–gL. Nat. Struct. Mol. Biol. 17, 882-888. PMC2921994.

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Chowdary T.K. and Heldwein E.E. (2010). Syncytial phenotype of HSV-1 gB is associated with diminished membrane interactions. J. Virol. 84, 4923-4935. PMC2863819.

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Silverman J.L., Sharma S., Cairns T.M., and Heldwein E.E. (2010). Fusion-null insertion mutants of HSV-1 gB adopt the trimeric postfusion conformation. J. Virol. 84, 2001-2012. PMC2812406.

2009

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Heldwein E.E. (2009). Entry of herpesviruses into cells: more than one way to pull the trigger. Structure. 17, 147-149. PMID: 19217384.

2008

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Heldwein E.E. and Krummenacher C. (2008). Entry of herpesviruses into mammalian cells. Cell. and Mol. Life Sciences 65, 1653-1668. PMID: 18351291.

2007

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Hannah B.P., Heldwein E.E., Bender F.C., Cohen G.H., and Eisenberg R.J. (2007). Mutational Evidence of Internal Fusion Loops in HSV glycoprotein B. J. Virol. 81, 4858-4865. PMC1900191.

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Bender F.C., Samanta M., Heldwein E.E., deLeon M.P., Lou H., Bilman E., Whitbeck J.C., Eisenberg R.J., and Cohen G.H. (2007). Antigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regions. J. Virol. 81, 3827-3841. PMC1866100.

2004-2006

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Heldwein E.E., Lou H., Bender F.C., Cohen G.H., Eisenberg R.J., and HarrisonS.C. (2006). Crystal structure of glycoprotein B from Herpes Simplex Virus 1. Science 313, 217-220. PMID: 16840698.

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Heldwein E.E., Macia E., Wang J., Yin H.L., Kirchhausen T.K., and Harrison S.C. (2004). Crystal structure of the clathrin adaptor AP-1 core. Proc. Natl. Acad. Sci. USA 101, 14108-14113. PMC521094.

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Heldwein E. This one goes to eleven (hundred) – data collection on crystals with a very long unit cell. CHESS News Magazine 2004:58-60.

1996-2002

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Godsey M.H., Heldwein E.E., and Brennan R.G. (2002). Structural biology of bacterial multidrug resistance gene regulators. J. Biol. Chem. 277, 40169-40172.

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Heldwein E.E. and Brennan R.G. (2001). Crystal structure of the transcription activator BmrR bound to DNA and a drug. Nature 409, 378-382.

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Zheleznova E.E., Crosa J.H., and Brennan R.G. (2000). Characterization of DNA and metal binding properties of Vibrio anguillarum Fur. J. Bacteriol. 182, 6264-6267.

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Vazquez-Laslop N., Zheleznova E.E., Markham P.N., Brennan R.G., and Neyfakh A.A. (2000). Recognition of multiple drugs by a single protein: a trivial solution of an old paradox. Biochem. Soc. Trans. 28, 517-520.

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Jardim A., Liu W., Zheleznova E., and Ullman B. (2000). Peroxisomal Targeting Signal-1 Receptor Protein PEX5 from Leishmania donovani. MOLECULAR, BIOCHEMICAL, AND IMMUNOCYTOCHEMICAL CHARACTERIZATION. J. Biol. Chem. 275, 13637-13644.

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Zheleznova E.E., Markham P.N., Edgar R., Bibi E., Neyfakh A.A., and Brennan R.G. (2000). A Structure-based Mechanism for Drug Binding by Multidrug Transporters. TiBS 25, 39-43.

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Zheleznova E.E., Markham P.N., Neyfakh A.A., and Brennan R.G. (1999). Structural Basis of Multidrug Recognition by BmrR, a Transcription Activator of a Multidrug Transporter. Cell 96, 353-362.

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Zheleznova E.E., Markham P.N., Neyfakh A.A., and Brennan R.G. (1997). Preliminary Structural Studies on the Multi-ligand Binding Domain of the Transcription Activator, BmrR, from Bacillus subtilis. Protein Science 6, 2465-2468.

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Schumacher M.A., Zheleznova E.E., Poundstone K.S., Kluger R., Jones R.T., and Brennan R.G. (1997). Allosteric Intermediates Indicate R2 is the Liganded Hemoglobin End State. Proc. Natl. Acad. Sci. USA 94, 7841-7844.

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Dement’eva E.I., Zheleznova E.E., Kutuzova G.D., Lundovskih I.A., and Ugarova N.N. (1996). Physicochemical Properties of Recombinant Luciferase Luciola mingrelica and its Mutant Forms [Russian]. Biokhimiia 61, 152-159.