Programmed remodeling of hyperacetylated histone H4 and H3 organization on the SV40 genome during lytic infection

Virology ◽

10.1016/j.virol.2005.01.025 ◽

2005 ◽

Vol 334 (1) ◽

pp. 111-123 ◽

Author(s):

Lata Balakrishnan ◽

Barry Milavetz

Keyword(s):

Lytic Infection ◽

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Temporal Control of Histone H4 methylation in SV40 minichromosomes during lytic infection

The FASEB Journal ◽

10.1096/fasebj.23.1_supplement.489.3 ◽

2009 ◽

Vol 23 (S1) ◽

Author(s):

Barry I Milavetz ◽

Amanda Gefroh ◽

Megan Hamling ◽

Lata Balakrishnan

Keyword(s):

Lytic Infection ◽

Temporal Control ◽

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Transcription of the SV40 Genome in Transformed Cells and during Lytic Infection

Cold Spring Harbor Symposia on Quantitative Biology ◽

10.1101/sqb.1970.035.01.097 ◽

1970 ◽

Vol 35 (0) ◽

pp. 823-831 ◽

Author(s):

S. Tonegawa ◽

G. Walter ◽

A. Bernardini ◽

R. Dulbecco

Keyword(s):

Lytic Infection ◽

Transformed Cells ◽

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Transcription of the SV40 Genome in Virus-transformed Cells and Early Lytic Infection

Cold Spring Harbor Symposia on Quantitative Biology ◽

10.1101/sqb.1980.044.01.006 ◽

1980 ◽

Vol 44 (0) ◽

pp. 31-39 ◽

Author(s):

P. K. Ghosh ◽

M. Piatak ◽

V. B. Reddy ◽

J. Swinscoe ◽

P. Lebowitz ◽

...

Keyword(s):

Lytic Infection ◽

Transformed Cells ◽

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Faculty Opinions recommendation of PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1007986.102715 ◽

2002 ◽

Author(s):

Patrick Matthias

Keyword(s):

Silent Chromatin ◽

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Faculty Opinions recommendation of PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1007986.99609 ◽

2002 ◽

Author(s):

Robin Allshire

Keyword(s):

Silent Chromatin ◽

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Faculty Opinions recommendation of The role of histone H2Av variant replacement and histone H4 acetylation in the establishment of Drosophila heterochromatin.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1023194.266686 ◽

2005 ◽

Author(s):

Dinah Singer

Keyword(s):

Histone H4 Acetylation ◽

Drosophila Heterochromatin

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Faculty Opinions recommendation of Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1061729.513646 ◽

2007 ◽

Author(s):

Michael Sattler

Keyword(s):

Structural Basis ◽

Methylation State ◽

Specific Recognition

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Faculty Opinions recommendation of Prognostic significance of the therapeutic targets histone deacetylase 1, 2, 6 and acetylated histone H4 in cutaneous T-cell lymphoma.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1160588.620958 ◽

2009 ◽

Author(s):

Janine Wechsler ◽

Dimitri Salameire

Keyword(s):

T Cell ◽

Histone Deacetylase ◽

Cell Lymphoma ◽

Prognostic Significance ◽

Therapeutic Targets ◽

T Cell Lymphoma ◽

Cutaneous T Cell Lymphoma ◽

Histone Deacetylase 1 ◽

Acetylated Histone H4

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UFL1 promotes histone H4 ufmylation and ATM activation

Nature Communications ◽

10.1038/s41467-019-09175-0 ◽

2019 ◽

Vol 10 (1) ◽

Author(s):

Bo Qin ◽

Jia Yu ◽

Somaira Nowsheen ◽

Minghui Wang ◽

Xinyi Tu ◽

...

Keyword(s):

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SIR2-Induced Inviability Is Suppressed by Histone H4 Overexpression

Genetics ◽

10.1093/genetics/162.2.973 ◽

2002 ◽

Vol 162 (2) ◽

pp. 973-976 ◽

Author(s):

Mirela Matecic ◽

Shelagh Stuart ◽

Scott G Holmes

Keyword(s):

Specific Interaction ◽

Yeast Cells ◽

High Expression ◽

Abstract We have identified histone H4 as a high-expression suppressor of Sir2-induced inviability in yeast cells. Overexpression of histone H3 does not suppress Sir2-induced lethality, nor does overexpression of histone H4 alleles associated with silencing defects. These results suggest a direct and specific interaction between Sir2 and H4 in the silencing mechanism.

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