| Year |
Citation |
Score |
| 2023 |
Jan Fada B, Guha U, Zheng Y, Reward E, Kaadi E, Dourra A, Gu H. A Novel Recognition by the E3 Ubiquitin Ligase of HSV-1 ICP0 Enhances the Degradation of PML Isoform I to Prevent ND10 Reformation in Late Infection. Viruses. 15. PMID 37243155 DOI: 10.3390/v15051070 |
0.346 |
|
| 2021 |
Fada BJ, Reward E, Gu H. The Role of ND10 Nuclear Bodies in Herpesvirus Infection: A Frenemy for the Virus? Viruses. 13. PMID 33546431 DOI: 10.3390/v13020239 |
0.322 |
|
| 2020 |
Gu H, Jan Fada B. Specificity in Ubiquitination Triggered by Virus Infection. International Journal of Molecular Sciences. 21. PMID 32521668 DOI: 10.3390/Ijms21114088 |
0.43 |
|
| 2020 |
Jan Fada B, Kaadi E, Samrat S, Zheng Y, Gu H. Regulations of SUMO-SIM interaction on the ICP0-mediated degradation of PML isoform II and its associated proteins in HSV-1 infection. Journal of Virology. PMID 32295906 DOI: 10.1128/Jvi.00470-20 |
0.437 |
|
| 2018 |
Samrat SK, Gu H. Temporal Analysis of the Nuclear-to-cytoplasmic Translocation of a Herpes Simplex Virus 1 Protein by Immunofluorescent Confocal Microscopy. Journal of Visualized Experiments : Jove. PMID 30451237 DOI: 10.3791/58504 |
0.436 |
|
| 2017 |
Samrat SK, Ha BL, Zheng Y, Gu H. Characterization of Elements Regulating the Nuclear to Cytoplasmic Translocation of ICP0 in Late HSV-1 Infection. Journal of Virology. PMID 29093084 DOI: 10.1128/Jvi.01673-17 |
0.464 |
|
| 2016 |
Zheng Y, Samrat SK, Gu H. A Tale of Two PMLs: Elements Regulating the Differential Substrate Recognition by the HSV-1 ICP0 E3 Ubiquitin Ligase. Journal of Virology. PMID 27681131 DOI: 10.1128/Jvi.01636-16 |
0.47 |
|
| 2016 |
Gu H, Zheng Y. Role of ND10 nuclear bodies in the chromatin repression of HSV-1. Virology Journal. 13: 62. PMID 27048561 DOI: 10.1186/S12985-016-0516-4 |
0.434 |
|
| 2016 |
Gu H. Infected cell protein 0 functional domains and their coordination in herpes simplex virus replication. World Journal of Virology. 5: 1-13. PMID 26870669 DOI: 10.5501/Wjv.V5.I1.1 |
0.409 |
|
| 2015 |
Zheng Y, Gu H. Identification of three redundant segments responsible for herpes simplex virus 1 ICP0 to fuse with ND10 nuclear bodies. Journal of Virology. 89: 4214-26. PMID 25631093 DOI: 10.1128/Jvi.03658-14 |
0.461 |
|
| 2013 |
Gu H, Zheng Y, Roizman B. Interaction of herpes simplex virus ICP0 with ND10 bodies: a sequential process of adhesion, fusion, and retention. Journal of Virology. 87: 10244-54. PMID 23864622 DOI: 10.1128/Jvi.01487-13 |
0.412 |
|
| 2013 |
Zerboni L, Che X, Reichelt M, Qiao Y, Gu H, Arvin A. Herpes simplex virus 1 tropism for human sensory ganglion neurons in the severe combined immunodeficiency mouse model of neuropathogenesis. Journal of Virology. 87: 2791-802. PMID 23269807 DOI: 10.1128/Jvi.01375-12 |
0.332 |
|
| 2012 |
Kalamvoki M, Gu H, Roizman B. Overexpression of the ubiquitin-specific protease 7 resulting from transfection or mutations in the ICP0 binding site accelerates rather than depresses herpes simplex virus 1 gene expression. Journal of Virology. 86: 12871-8. PMID 22993145 DOI: 10.1128/Jvi.01981-12 |
0.451 |
|
| 2010 |
Du T, Zhou G, Khan S, Gu H, Roizman B. Disruption of HDAC/CoREST/REST repressor by dnREST reduces genome silencing and increases virulence of herpes simplex virus. Proceedings of the National Academy of Sciences of the United States of America. 107: 15904-9. PMID 20798038 DOI: 10.1073/Pnas.1010741107 |
0.395 |
|
| 2009 |
Gu H, Poon AP, Roizman B. During its nuclear phase the multifunctional regulatory protein ICP0 undergoes proteolytic cleavage characteristic of polyproteins. Proceedings of the National Academy of Sciences of the United States of America. 106: 19132-7. PMID 19850872 DOI: 10.1073/Pnas.0910920106 |
0.429 |
|
| 2009 |
Gu H, Roizman B. Engagement of the lysine-specific demethylase/HDAC1/CoREST/REST complex by herpes simplex virus 1. Journal of Virology. 83: 4376-85. PMID 19193804 DOI: 10.1128/Jvi.02515-08 |
0.407 |
|
| 2009 |
Gu H, Roizman B. The two functions of herpes simplex virus 1 ICP0, inhibition of silencing by the CoREST/REST/HDAC complex and degradation of PML, are executed in tandem. Journal of Virology. 83: 181-7. PMID 18945770 DOI: 10.1128/Jvi.01940-08 |
0.418 |
|
| 2007 |
Gu H, Roizman B. Herpes simplex virus-infected cell protein 0 blocks the silencing of viral DNA by dissociating histone deacetylases from the CoREST-REST complex. Proceedings of the National Academy of Sciences of the United States of America. 104: 17134-9. PMID 17939992 DOI: 10.1073/Pnas.0707266104 |
0.415 |
|
| 2006 |
Poon AP, Gu H, Roizman B. ICP0 and the US3 protein kinase of herpes simplex virus 1 independently block histone deacetylation to enable gene expression. Proceedings of the National Academy of Sciences of the United States of America. 103: 9993-8. PMID 16785443 DOI: 10.1073/Pnas.0604142103 |
0.413 |
|
| 2005 |
Roizman B, Gu H, Mandel G. The first 30 minutes in the life of a virus: unREST in the nucleus. Cell Cycle (Georgetown, Tex.). 4: 1019-21. PMID 16082207 DOI: 10.4161/Cc.4.8.1902 |
0.452 |
|
| 2005 |
Gu H, Liang Y, Mandel G, Roizman B. Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells. Proceedings of the National Academy of Sciences of the United States of America. 102: 7571-6. PMID 15897453 DOI: 10.1073/Pnas.0502658102 |
0.435 |
|
| 2003 |
Gu H, Schoenberg DR. U2AF modulates poly(A) length control by the poly(A)-limiting element. Nucleic Acids Research. 31: 6264-71. PMID 14576315 DOI: 10.1093/Nar/Gkg823 |
0.629 |
|
| 2003 |
Gu H, Roizman B. The degradation of promyelocytic leukemia and Sp100 proteins by herpes simplex virus 1 is mediated by the ubiquitin-conjugating enzyme UbcH5a. Proceedings of the National Academy of Sciences of the United States of America. 100: 8963-8. PMID 12855769 DOI: 10.1073/Pnas.1533420100 |
0.354 |
|
| 2001 |
Gupta JD, Gu H, Schoenberg DR. Position and sequence requirements for poly(A) length regulation by the poly(A) limiting element. Rna (New York, N.Y.). 7: 1034-42. PMID 11453064 DOI: 10.1017/S1355838201010329 |
0.637 |
|
| 1999 |
Gu H, Das Gupta J, Schoenberg DR. The poly(A)-limiting element is a conserved cis-acting sequence that regulates poly(A) tail length on nuclear pre-mRNAs. Proceedings of the National Academy of Sciences of the United States of America. 96: 8943-8. PMID 10430875 DOI: 10.1073/Pnas.96.16.8943 |
0.638 |
|
| 1998 |
Das Gupta J, Gu H, Chernokalskaya E, Gao X, Schoenberg DR. Identification of two cis-acting elements that independently regulate the length of poly(A) on Xenopus albumin pre-mRNA. Rna (New York, N.Y.). 4: 766-76. PMID 9671050 DOI: 10.1017/S1355838298971837 |
0.642 |
|
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