Výsledky vyhledávání - "Lauren M Congdon"

Akademický článek

The UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression.

Autor: Tanya M Spektor, Lauren M Congdon, Chendhore S Veerappan, Judd C Rice

Publikováno v: PLoS ONE, Vol 6, Iss 7, p e22785 (2011)

PR-Set7/Set8/KMT5a is a chromatin-modifying enzyme that specifically monomethylates lysine 20 of histone H4 (H4K20me1). In this study we attempted to identify PR-Set7-interacting proteins reasoning that these proteins would provide important insights

Externí odkaz: https://doaj.org/article/ab6659dcc0eb4ad295609c4d3b4cdf88

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Concerted Activities of Distinct H4K20 Methyltransferases at DNA Double-Strand Breaks Regulate 53BP1 Nucleation and NHEJ-Directed Repair

Autor: Judd C. Rice, Lauren M. Congdon, Kyoko Yokomori, Xiaodong Kong, Gunnar Schotta, Shumin Wu, Creighton T. Tuzon, Tanya M. Spektor

Publikováno v: Cell Reports, Vol 8, Iss 2, Pp 430-438 (2014)
Cell reports, vol 8, iss 2
Tuzon, CT; Spektor, T; Kong, X; Congdon, LM; Wu, S; Schotta, G; et al.(2014). Concerted Activities of Distinct H4K20 Methyltransferases at DNA Double-Strand Breaks Regulate 53BP1 Nucleation and NHEJ-Directed Repair. Cell Reports, 8(2), 430-438. doi: 10.1016/j.celrep.2014.06.013. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/8j4860p6

Although selective binding of 53BP1 to dimethylated histone H4 lysine 20 (H4K20me2) at DNA double-strand breaks (DSBs) is a necessary and pivotal determinant of nonhomologous end joining (NHEJ)-directed repair, the enzymes that generate H4K20me2 at D

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::817f63953652abdbf9c40c4cef5ca962
http://www.sciencedirect.com/science/article/pii/S2211124714004811

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Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progression

Autor: Judd C. Rice, Weiping Wang, Xiangduo Kong, Shumin Wu, Kyoko Yokomori, Marc W. Kirschner, Lauren M. Congdon

Publikováno v: Genes & Development. 24:2531-2542

Although the PR-Set7/Set8/KMT5a histone H4 Lys 20 monomethyltransferase (H4K20me1) plays an essential role in mammalian cell cycle progression, especially during G2/M, it remained unknown how PR-Set7 itself was regulated. In this study, we discovered

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95b1795b8fad6c358e4a10f1db51bf67
https://doi.org/10.1101/gad.1984210

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The PR-Set7 binding domain of Riz1 is required for the H4K20me1-H3K9me1 trans-tail 'histone code' and Riz1 tumor suppressor function

Autor: Judd C. Rice, Jennifer K. Sims, Lauren M. Congdon, Creighton T. Tuzon

Publikováno v: Nucleic Acids Research

PR-Set7/Set8/KMT5a is the sole histone H4 lysine 20 monomethyltransferase (H4K20me1) in metazoans and is essential for proper cell division and genomic stability. We unexpectedly discovered that normal cellular levels of monomethylated histone H3 lys

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fb771f72a7638aedfdc98c2ac8e78f2
https://pubmed.ncbi.nlm.nih.gov/24423864

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The UBC9 E2 SUMO Conjugating Enzyme Binds the PR-Set7 Histone Methyltransferase to Facilitate Target Gene Repression

Autor: Judd C. Rice, Tanya M. Spektor, Lauren M. Congdon, Chendhore S. Veerappan

Publikováno v: PLoS ONE
PLoS ONE, Vol 6, Iss 7, p e22785 (2011)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cedd5f57db16369694085c7b98516d6
http://europepmc.org/articles/PMC3146489

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PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression

Autor: Lauren M. Congdon, Judd C. Rice, Chendhore S. Veerappan, Sabrina I. Houston, Tanya M. Spektor

Publikováno v: Journal of cellular biochemistry. 110(3)

Increasing evidence indicates that the post-translational modifications of the histone proteins play critical roles in all eukaryotic DNA-templated processes. To gain further biological insights into two of these modifications, the mono- and trimethy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d75669c82cb89c95c8d4800264c4d50
https://pubmed.ncbi.nlm.nih.gov/20512922

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Proteasomal inhibition stabilizes topoisomerase IIα protein and reverses resistance to the topoisomerase II poison ethonafide (AMP-53, 6-ethoxyazonafide)

Autor: Alan Pourpak, Aluvia M. Escalante, Robert T. Dorr, Terry H. Landowski, Lauren M. Congdon

Multiple myeloma (MM) is an incurable malignancy of plasma cells. Although multiple myeloma patients often respond to initial therapy, the majority of patients will relapse with disease that is refractory to further drug treatment. Thus, new therapeu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab80a634c13950681d87fbe2d75e30c1
https://europepmc.org/articles/PMC2271051/

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Abstract LB-133: Orchestrated recruitment of histone methyltransferases to DNA double strand breaks facilitates 53BP1 binding and proficient repair

Autor: Or Gozani, Judd C. Rice, Tanya M. Spektor, Alex J. Kuo, Kyoko Yokomori, Lauren M. Congdon, Xiaodong Kong, Creighton T. Tuzon, Peggie Cheung

Publikováno v: Cancer Research. 74:LB-133

While selective binding of the tandem tudor domains of p53 binding protein 1 (53BP1) to dimethylated histone H4 lysine 20 (H4K20me2) at DNA double strand breaks (DSBs) is well-documented to be an essential event for proficient DSB repair, the enzyme(

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::3ae488de62e695b8840b848eb75d5fb4
https://doi.org/10.1158/1538-7445.am2014-lb-133

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