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Gu, H., Liang, Y., Mandel, G., Roizman, B. (2005) 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, 102 (21) 7571-7576 doi:10.1073/pnas.0502658102

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Reference TypeJournal (article/letter/editorial)
TitleComponents of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells
JournalProceedings of the National Academy of Sciences
AuthorsGu, H.Author
Liang, Y.Author
Mandel, G.Author
Roizman, B.Author
Year2005 (May 24)Volume102
Issue21
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.0502658102Search in ResearchGate
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Mindat Ref. ID1713426Long-form Identifiermindat:1:5:1713426:6
GUID0
Full ReferenceGu, H., Liang, Y., Mandel, G., Roizman, B. (2005) 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, 102 (21) 7571-7576 doi:10.1073/pnas.0502658102
Plain TextGu, H., Liang, Y., Mandel, G., Roizman, B. (2005) 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, 102 (21) 7571-7576 doi:10.1073/pnas.0502658102
In(2005, May) Proceedings of the National Academy of Sciences Vol. 102 (21) Proceedings of the National Academy of Sciences

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Gu, H., Roizman, B. (2007) 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, 104 (43) 17134-17139 doi:10.1073/pnas.0707266104
Du, T., Zhou, G., Khan, S., Gu, H., Roizman, B. (2010) 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, 107 (36) 15904-15909 doi:10.1073/pnas.1010741107
You, A., Tong, J. K., Grozinger, C. M., Schreiber, S. L. (2001) CoREST is an integral component of the CoREST- human histone deacetylase complex. Proceedings of the National Academy of Sciences, 98 (4) 1454-1458 doi:10.1073/pnas.98.4.1454
Zhou, G., Du, T., Roizman, B. (2013) HSV carrying WT REST establishes latency but reactivates only if the synthesis of REST is suppressed. Proceedings of the National Academy of Sciences, 110 (6) doi:10.1073/pnas.1222497110
Liang, Y., Kurakin, A., Roizman, B. (2005) Herpes simplex virus 1 infected cell protein 0 forms a complex with CIN85 and Cbl and mediates the degradation of EGF receptor from cell surfaces. Proceedings of the National Academy of Sciences, 102 (16) 5838-5843 doi:10.1073/pnas.0501253102
Taddeo, B., Luo, T. R., Zhang, W., Roizman, B. (2003) Activation of NF- B in cells productively infected with HSV-1 depends on activated protein kinase R and plays no apparent role in blocking apoptosis. Proceedings of the National Academy of Sciences, 100 (21) 12408-12413 doi:10.1073/pnas.2034952100
Yarden, R. I., Brody, L. C. (1999) BRCA1 interacts with components of the histone deacetylase complex. Proceedings of the National Academy of Sciences, 96 (9) 4983-4988 doi:10.1073/pnas.96.9.4983
Xu, Pei, Mallon, Stephen, Roizman, Bernard (2016) PML plays both inimical and beneficial roles in HSV-1 replication. Proceedings of the National Academy of Sciences, 113 (21) doi:10.1073/pnas.1605513113
Roizman, B. (1963) THE PROGRAMMING OF HERPES VIRUS MULTIPLICATION IN DOUBLY-INFECTED AND IN PUROMYCIN-TREATED CELLS. Proceedings of the National Academy of Sciences, 49 (2) 165-171 doi:10.1073/pnas.49.2.165
Kalamvoki, M., Roizman, B. (2009) ICP0 enables and monitors the function of D cyclins in herpes simplex virus 1 infected cells. Proceedings of the National Academy of Sciences, 106 (34) 14576-14580 doi:10.1073/pnas.0906905106
Ungerstedt, J. S., Sowa, Y., Xu, W.-S., Shao, Y., Dokmanovic, M., Perez, G., Ngo, L., Holmgren, A., Jiang, X., Marks, P. A. (2005) Role of thioredoxin in the response of normal and transformed cells to histone deacetylase inhibitors. Proceedings of the National Academy of Sciences, 102 (3) 673-678 doi:10.1073/pnas.0408732102
 
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