Publications: Sandra K. Weller

• 2023

• Conformational exchange at a CH zinc-binding site facilitates redox sensing by the PML protein.
  Bregnard TA, Fairchild D, Erlandsen H, Semenova IV, Szczepaniak R, Ahmed A, Weller SK, Korzhnev DM, Bezsonova I
  Structure (London, England : 1993) (2023) 31(9):1086-1099.e6 PMC3855844 10.1038/nmeth.2019

• 2022

• Viral Nucleases from Herpesviruses and Coronavirus in Recombination and Proofreading: Potential Targets for Antiviral Drug Discovery.
  Wright LR, Wright DL, Weller SK
  Viruses (2022) 14(7): PMC8640510 10.1038/s41418-021-00900-1
• The B-box1 domain of PML mediates SUMO E2-E3 complex formation through an atypical interaction with UBC9.
  Bregnard T, Ahmed A, Semenova IV, Weller SK, Bezsonova I
  Biophysical chemistry (2022) 287:106827 PMC4393527 10.1093/bioinformatics/btu830
• Two-Metal Ion-Dependent Enzymes as Potential Antiviral Targets in Human Herpesviruses.
  DiScipio KA, Weerasooriya S, Szczepaniak R, Hazeen A, Wright LR, Wright DL, Weller SK
  mBio (2022) 13(1):e0322621 PMC2447070 10.1128/JVI.00455-08

• 2021

• New model integrates innate responses, PML-NB formation, epigenetic control and reactivation from latency.
  Weller SK, Deluca NA
  EMBO reports (2021) 22(9):e53496 PMC8419697 10.15252/embr.202153496
• Report of the National Institutes of Health SARS-CoV-2 Antiviral Therapeutics Summit.
  Hall MD, Anderson JM, Anderson A, Baker D, Bradner J, Brimacombe KR, Campbell EA, Corbett KS, Carter K, Cherry S, Chiang L, Cihlar T, de Wit E, Denison M, Disney M, Fletcher CV, Ford-Scheimer SL, Götte M, Grossman AC, Hayden FG, Hazuda DJ, Lanteri CA, Marston H, Mesecar AD, Moore S, Nwankwo JO, O'Rear J, Painter G, Singh Saikatendu K, Schiffer CA, Sheahan TP, Shi PY, Smyth HD, Sofia MJ, Weetall M, Weller SK, Whitley R, Fauci AS, Austin CP, Collins FS, Conley AJ, Davis MI
  The Journal of infectious diseases (2021) 224(Supplement):S1-S21 PMC8280938 10.1093/infdis/jiab305

• 2020

• Rising to the challenge: designing, implementing and reporting exercise oncology trials in understudied populations.
  Lahart IM, Weller SK, Kirkham AA
  British journal of cancer (2020) 123(2):173-175 PMC7374541 10.1016/j.tics.2019.07.009
• DNA Damage Kills Bacterial Spores and Cells Exposed to 222-Nanometer UV Radiation.
  Taylor W, Camilleri E, Craft DL, Korza G, Granados MR, Peterson J, Szczpaniak R, Weller SK, Moeller R, Douki T, Mok WWK, Setlow P
  Applied and environmental microbiology (2020) 86(8): PMC7117916 10.1128/AEM.03039-19

• 2019

• The Herpes Simplex Virus 1 Immediate Early Protein ICP22 Is a Functional Mimic of a Cellular J Protein.
  Adlakha M, Livingston CM, Bezsonova I, Weller SK
  Journal of virology (2019) 94(4): PMC6997750 10.1128/JVI.01564-19
• Herpes simplex virus 1 ICP8 mutant lacking annealing activity is deficient for viral DNA replication.
  Weerasooriya S, DiScipio KA, Darwish AS, Bai P, Weller SK
  Proceedings of the National Academy of Sciences of the United States of America (2019) 116(3):1033-1042 PMC6338833 10.1073/pnas.1817642116

• 2018

• Viral Proteins U41 and U70 of Human Herpesvirus 6A Are Dispensable for Telomere Integration.
  Wight DJ, Wallaschek N, Sanyal A, Weller SK, Flamand L, Kaufer BB
  Viruses (2018) 10(11): (PMC6267051) 10.3390/v10110656

• 2017

• The Exonuclease Activity of Herpes Simplex Virus 1 UL12 Is Required for Production of Viral DNA That Can Be Packaged To Produce Infectious Virus.
  Grady LM, Szczepaniak R, Murelli RP, Masaoka T, Le Grice SFJ, Wright DL, Weller SK
  J. Virol. (2017) 91(23): (PMC5686714) 10.1128/JVI.01380-17
• The UL8 subunit of the helicase-primase complex of herpes simplex virus promotes DNA annealing and has a high affinity for replication forks.
  Bermek O, Weller SK, Griffith JD
  J. Biol. Chem. (2017) 292(38):15611-15621 (PMC5612096) 10.1074/jbc.M117.799064

• 2016

• An Intrinsically Disordered Region of the DNA Repair Protein Nbs1 Is a Species-Specific Barrier to Herpes Simplex Virus 1 in Primates.
  Lou DI, Kim ET, Meyerson NR, Pancholi NJ, Mohni KN, Enard D, Petrov DA, Weller SK, Weitzman MD, Sawyer SL
  Cell Host Microbe (2016) 20(2):178-88 (PMC4982468) 10.1016/j.chom.2016.07.003

• 2015

• ICP8 Filament Formation Is Essential for Replication Compartment Formation during Herpes Simplex Virus Infection.
  Darwish AS, Grady LM, Bai P, Weller SK
  J. Virol. (2015) 90(5):2561-70 (PMC4810729) 10.1128/JVI.02854-15
• Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1.
  Pozhidaeva AK, Mohni KN, Dhe-Paganon S, Arrowsmith CH, Weller SK, Korzhnev DM, Bezsonova I
  J. Biol. Chem. (2015) 290(38):22907-18 (PMC4645603) 10.1074/jbc.M115.664805
• HSV-I and the cellular DNA damage response.
  Smith S, Weller SK
  Future Virol (2015) 10(4):383-397 (PMC4508672) 10.2217/fvl.15.18
• HSV cheats the executioner.
  Mossman KL, Weller SK
  Cell Host Microbe (2015) 17(2):148-51 10.1016/j.chom.2015.01.013

• 2014

• The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infection.
  Albright BS, Kosinski A, Szczepaniak R, Cook EA, Stow ND, Conway JF, Weller SK
  J. Virol. (2014) 89(1):443-53 (PMC4301124) 10.1128/JVI.01913-14
• Recombination promoted by DNA viruses: phage λ to herpes simplex virus.
  Weller SK, Sawitzke JA
  Annu. Rev. Microbiol. (2014) 68:237-58 (PMC4303060) 10.1146/annurev-micro-091313-103424
• Structure of the herpes simplex virus 1 genome: manipulation of nicks and gaps can abrogate infectivity and alter the cellular DNA damage response.
  Smith S, Reuven N, Mohni KN, Schumacher AJ, Weller SK
  J. Virol. (2014) 88(17):10146-56 (PMC4136335) 10.1128/JVI.01723-14
• HSV-1 protein expression using recombinant baculoviruses.
  Grady LM, Bai P, Weller SK
  Methods Mol. Biol. (2014) 1144:293-304 (PMC4427568) 10.1007/978-1-4939-0428-0_20

• 2013

• Herpes simplex virus type 1 single strand DNA binding protein and helicase/primase complex disable cellular ATR signaling.
  Mohni KN, Smith S, Dee AR, Schumacher AJ, Weller SK
  PLoS Pathog. (2013) 9(10):e1003652 (PMC3789782) 10.1371/journal.ppat.1003652
• The DNA helicase-primase complex as a target for herpes viral infection.
  Weller SK, Kuchta RD
  Expert Opin. Ther. Targets (2013) 17(10):1119-32 (PMC4098783) 10.1517/14728222.2013.827663

• 2012

• Efficient herpes simplex virus 1 replication requires cellular ATR pathway proteins.
  Mohni KN, Dee AR, Smith S, Schumacher AJ, Weller SK
  J. Virol. (2012) 87(1):531-42 (PMC3536419) 10.1128/JVI.02504-12
• Herpes simplex viruses: mechanisms of DNA replication.
  Weller SK, Coen DM
  Cold Spring Harb Perspect Biol (2012) 4(9):a013011 (PMC3428768) 10.1101/cshperspect.a013011
• The HSV-1 exonuclease, UL12, stimulates recombination by a single strand annealing mechanism.
  Schumacher AJ, Mohni KN, Kan Y, Hendrickson EA, Stark JM, Weller SK
  PLoS Pathog. (2012) 8(8):e1002862 (PMC3415443) 10.1371/journal.ppat.1002862

• 2011

• DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replication.
  Mohni KN, Mastrocola AS, Bai P, Weller SK, Heinen CD
  J. Virol. (2011) 85(23):12241-53 (PMC3209375) 10.1128/JVI.05487-11
• Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.
  Szczepaniak R, Nellissery J, Jadwin JA, Makhov AM, Kosinski A, Conway JF, Weller SK
  J. Virol. (2011) 85(17):8625-34 (PMC3165804) 10.1128/JVI.00214-11
• Disulfide bond formation in the herpes simplex virus 1 UL6 protein is required for portal ring formation and genome encapsidation.
  Albright BS, Nellissery J, Szczepaniak R, Weller SK
  J. Virol. (2011) 85(17):8616-24 (PMC3165836) 10.1128/JVI.00123-11

• 2010

• Herpes simplex virus reorganizes the cellular DNA repair and protein quality control machinery.
  Weller SK
  PLoS Pathog. (2010) 6(11):e1001105 (PMC2991270) 10.1371/journal.ppat.1001105
• Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation.
  Chen Y, Bai P, Mackay S, Korza G, Carson JH, Kuchta RD, Weller SK
  J. Virol. (2010) 85(2):968-78 (PMC3019990) 10.1128/JVI.01690-10
• Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex.
  Balasubramanian N, Bai P, Buchek G, Korza G, Weller SK
  J. Virol. (2010) 84(24):12504-14 (PMC3004347) 10.1128/JVI.01506-10
• ATR and ATRIP are recruited to herpes simplex virus type 1 replication compartments even though ATR signaling is disabled.
  Mohni KN, Livingston CM, Cortez D, Weller SK
  J. Virol. (2010) 84(23):12152-64 (PMC2976399) 10.1128/JVI.01643-10
• Identification of rep-associated factors in herpes simplex virus type 1-induced adeno-associated virus type 2 replication compartments.
  Nicolas A, Alazard-Dany N, Biollay C, Arata L, Jolinon N, Kuhn L, Ferro M, Weller SK, Epstein AL, Salvetti A, Greco A
  J. Virol. (2010) 84(17):8871-87 (PMC2919046) 10.1128/JVI.00725-10

• 2009

• Herpes simplex virus type 1 immediate-early protein ICP22 is required for VICE domain formation during productive viral infection.
  Bastian TW, Livingston CM, Weller SK, Rice SA
  J. Virol. (2009) 84(5):2384-94 (PMC2820935) 10.1128/JVI.01686-09
• Virus-Induced Chaperone-Enriched (VICE) domains function as nuclear protein quality control centers during HSV-1 infection.
  Livingston CM, Ifrim MF, Cowan AE, Weller SK
  PLoS Pathog. (2009) 5(10):e1000619 (PMC2752995) 10.1371/journal.ppat.1000619

• 2008

• Oligomerization of ICP4 and rearrangement of heat shock proteins may be important for herpes simplex virus type 1 prereplicative site formation.
  Livingston CM, DeLuca NA, Wilkinson DE, Weller SK
  J. Virol. (2008) 82(13):6324-36 (PMC2447070) 10.1128/JVI.00455-08

• 2007

• Direct interaction between the N- and C-terminal portions of the herpes simplex virus type 1 origin binding protein UL9 implies the formation of a head-to-tail dimer.
  Chattopadhyay S, Weller SK
  J. Virol. (2007) 81(24):13659-67 (PMC2168873) 10.1128/JVI.01204-07
• Enhanced phosphorylation of transcription factor sp1 in response to herpes simplex virus type 1 infection is dependent on the ataxia telangiectasia-mutated protein.
  Iwahori S, Shirata N, Kawaguchi Y, Weller SK, Sato Y, Kudoh A, Nakayama S, Isomura H, Tsurumi T
  J. Virol. (2007) 81(18):9653-64 (PMC2045397) 10.1128/JVI.00568-07
• A putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formation.
  Nellissery JK, Szczepaniak R, Lamberti C, Weller SK
  J. Virol. (2007) 81(17):8868-77 (PMC1951442) 10.1128/JVI.00739-07
• A mutation in the human herpes simplex virus type 1 UL52 zinc finger motif results in defective primase activity but can recruit viral polymerase and support viral replication efficiently.
  Chen Y, Livingston CM, Carrington-Lawrence SD, Bai P, Weller SK
  J. Virol. (2007) 81(16):8742-51 (PMC1951384) 10.1128/JVI.00174-07

• 2006

• Herpes simplex virus eliminates host mitochondrial DNA.
  Saffran HA, Pare JM, Corcoran JA, Weller SK, Smiley JR
  EMBO Rep. (2006) 8(2):188-93 (PMC1796774) 10.1038/sj.embor.7400878
• Herpes simplex virus type I disrupts the ATR-dependent DNA-damage response during lytic infection.
  Wilkinson DE, Weller SK
  J. Cell. Sci. (2006) 119(Pt 13):2695-703 (PMC4427570) 10.1242/jcs.02981
• The two helicases of herpes simplex virus type 1 (HSV-1).
  Chattopadhyay S, Chen Y, Weller SK
  Front. Biosci. (2006) 11:2213-23
• DNA binding activity of the herpes simplex virus type 1 origin binding protein, UL9, can be modulated by sequences in the N terminus: correlation between transdominance and DNA binding.
  Chattopadhyay S, Weller SK
  J. Virol. (2006) 80(9):4491-500 (PMC1471996) 10.1128/JVI.80.9.4491-4500.2006

• 2005

• Beta interferon and gamma interferon synergize to block viral DNA and virion synthesis in herpes simplex virus-infected cells.
  Pierce AT, DeSalvo J, Foster TP, Kosinski A, Weller SK, Halford WP
  J. Gen. Virol. (2005) 86(Pt 9):2421-32 (PMC1366490) 10.1099/vir.0.80979-0
• Herpes simplex virus type 1 DNA polymerase requires the mammalian chaperone hsp90 for proper localization to the nucleus.
  Burch AD, Weller SK
  J. Virol. (2005) 79(16):10740-9 (PMC1182622) 10.1128/JVI.79.16.10740-10749.2005
• Herpes simplex virus type 1 single-strand DNA binding protein ICP8 enhances the nuclease activity of the UL12 alkaline nuclease by increasing its processivity.
  Reuven NB, Weller SK
  J. Virol. (2005) 79(14):9356-8 (PMC1168754) 10.1128/JVI.79.14.9356-9358.2005
• Mutations in the putative zinc-binding motif of UL52 demonstrate a complex interdependence between the UL5 and UL52 subunits of the human herpes simplex virus type 1 helicase/primase complex.
  Chen Y, Carrington-Lawrence SD, Bai P, Weller SK
  J. Virol. (2005) 79(14):9088-96 (PMC1168741) 10.1128/JVI.79.14.9088-9096.2005
• Inhibition of the herpes simplex virus type 1 DNA polymerase induces hyperphosphorylation of replication protein A and its accumulation at S-phase-specific sites of DNA damage during infection.
  Wilkinson DE, Weller SK
  J. Virol. (2005) 79(11):7162-71 (PMC1112160) 10.1128/JVI.79.11.7162-7171.2005

• 2004

• Catalysis of strand exchange by the HSV-1 UL12 and ICP8 proteins: potent ICP8 recombinase activity is revealed upon resection of dsDNA substrate by nuclease.
  Reuven NB, Willcox S, Griffith JD, Weller SK
  J. Mol. Biol. (2004) 342(1):57-71 (PMC4412345) 10.1016/j.jmb.2004.07.012
• Nuclear sequestration of cellular chaperone and proteasomal machinery during herpes simplex virus type 1 infection.
  Burch AD, Weller SK
  J. Virol. (2004) 78(13):7175-85 (PMC421678) 10.1128/JVI.78.13.7175-7185.2004
• Recruitment of cellular recombination and repair proteins to sites of herpes simplex virus type 1 DNA replication is dependent on the composition of viral proteins within prereplicative sites and correlates with the induction of the DNA damage response.
  Wilkinson DE, Weller SK
  J. Virol. (2004) 78(9):4783-96 (PMC387708) 10.1128/jvi.78.9.4783-4796.2004
• The UL12.5 gene product of herpes simplex virus type 1 exhibits nuclease and strand exchange activities but does not localize to the nucleus.
  Reuven NB, Antoku S, Weller SK
  J. Virol. (2004) 78(9):4599-608 (PMC387724) 10.1128/jvi.78.9.4599-4608.2004

• 2003

• The Rep protein of adeno-associated virus type 2 interacts with single-stranded DNA-binding proteins that enhance viral replication.
  Stracker TH, Cassell GD, Ward P, Loo YM, van Breukelen B, Carrington-Lawrence SD, Hamatake RK, van der Vliet PC, Weller SK, Melendy T, Weitzman MD
  J. Virol. (2003) 78(1):441-53 (PMC303412) 10.1128/jvi.78.1.441-453.2004
• The role of DNA recombination in herpes simplex virus DNA replication.
  Wilkinson DE, Weller SK
  IUBMB Life (2003) 55(8):451-8 10.1080/15216540310001612237
• Existence of transdominant and potentiating mutants of UL9, the herpes simplex virus type 1 origin-binding protein, suggests that levels of UL9 protein may be regulated during infection.
  Marintcheva B, Weller SK
  J. Virol. (2003) 77(17):9639-51 (PMC187383) 10.1128/jvi.77.17.9639-9651.2003
• Point mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging.
  Przech AJ, Yu D, Weller SK
  J. Virol. (2003) 77(17):9613-21 (PMC187393) 10.1128/jvi.77.17.9613-9621.2003
• The herpes simplex virus type 1 alkaline nuclease and single-stranded DNA binding protein mediate strand exchange in vitro.
  Reuven NB, Staire AE, Myers RS, Weller SK
  J. Virol. (2003) 77(13):7425-33 (PMC164775) 10.1128/jvi.77.13.7425-7433.2003
• Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins.
  Carrington-Lawrence SD, Weller SK
  J. Virol. (2003) 77(7):4237-47 (PMC150627) 10.1128/jvi.77.7.4237-4247.2003
• Helicase motif Ia is involved in single-strand DNA-binding and helicase activities of the herpes simplex virus type 1 origin-binding protein, UL9.
  Marintcheva B, Weller SK
  J. Virol. (2003) 77(4):2477-88 (PMC141079) 10.1128/jvi.77.4.2477-2488.2003

• 2002

• The product of the UL12.5 gene of herpes simplex virus type 1 is not essential for lytic viral growth and is not specifically associated with capsids.
  Martinez R, Goldstein JN, Weller SK
  Virology (2002) 298(2):248-57

• 2001

• A tale of two HSV-1 helicases: roles of phage and animal virus helicases in DNA replication and recombination.
  Marintcheva B, Weller SK
  Prog. Nucleic Acid Res. Mol. Biol. (2001) 70:77-118
• The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid.
  Newcomb WW, Juhas RM, Thomsen DR, Homa FL, Burch AD, Weller SK, Brown JC
  J. Virol. (2001) 75(22):10923-32 (PMC114672) 10.1128/JVI.75.22.10923-10932.2001
• The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding.
  Biswas N, Weller SK
  J. Biol. Chem. (2001) 276(20):17610-9 10.1074/jbc.M010107200
• Interactions of herpes simplex virus type 1 with ND10 and recruitment of PML to replication compartments.
  Burkham J, Coen DM, Hwang CB, Weller SK
  J. Virol. (2001) 75(5):2353-67 (PMC114819) 10.1128/JVI.75.5.2353-2367.2001
• Herpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to its maturation.
  Sheaffer AK, Newcomb WW, Gao M, Yu D, Weller SK, Brown JC, Tenney DJ
  J. Virol. (2001) 75(2):687-98 (PMC113965) 10.1128/JVI.75.2.687-698.2001

• 2000

• Residues within the conserved helicase motifs of UL9, the origin-binding protein of herpes simplex virus-1, are essential for helicase activity but not for dimerization or origin binding activity.
  Marintcheva B, Weller SK
  J. Biol. Chem. (2000) 276(9):6605-15 10.1074/jbc.M007743200
• Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsids.
  Sheaffer AK, Newcomb WW, Brown JC, Gao M, Weller SK, Tenney DJ
  J. Virol. (2000) 74(15):6838-48 (PMC112201) 10.1128/jvi.74.15.6838-6848.2000
• Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.
  Newcomb WW, Trus BL, Cheng N, Steven AC, Sheaffer AK, Tenney DJ, Weller SK, Brown JC
  J. Virol. (2000) 74(4):1663-73 (PMC111641) 10.1128/jvi.74.4.1663-1673.2000

• 1999

• A mutation in the C-terminal putative Zn2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex.
  Biswas N, Weller SK
  J. Biol. Chem. (1999) 274(12):8068-76 10.1074/jbc.274.12.8068