Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Ruben Esse"'
Autor:
Ruben Esse, Alla Grishok
Publikováno v:
Cells, Vol 9, Iss 8, p 1846 (2020)
The methylation of histone H3 at lysine 79 is a feature of open chromatin. It is deposited by the conserved histone methyltransferase DOT1. Recently, DOT1 localization and H3K79 methylation (H3K79me) have been correlated with enhancers in C. elegans
Externí odkaz:
https://doaj.org/article/270efdad5a06415f879b9ee9ffb987f5
Publikováno v:
International Journal of Molecular Sciences, Vol 20, Iss 4, p 867 (2019)
Homocysteine (Hcy) is a sulfur-containing non-proteinogenic amino acid formed during the metabolism of the essential amino acid methionine. Hcy is considered a risk factor for atherosclerosis and cardiovascular disease (CVD), but the molecular basis
Externí odkaz:
https://doaj.org/article/fd19d69c380549519e468cb64f3b6995
Autor:
Ruben Esse, Tom Teerlink, Pieter Koolwijk, Isabel Tavares de Almeida, Henk J. Blom, Rita Castro
Publikováno v:
Nutrients, Vol 10, Iss 4, p 404 (2018)
Elevated plasma total homocysteine (tHcy) is associated with increased risk of cardiovascular disease, but the mechanisms underlying this association are not completely understood. Cellular hypomethylation has been suggested to be a key pathophysiolo
Externí odkaz:
https://doaj.org/article/3bf96b9a277e499db05ac59635a3f846
Autor:
Ruben Esse, Monica S Rocha, Madalena Barroso, Cristina Florindo, Tom Teerlink, Robert M Kok, Yvo M Smulders, Isabel Rivera, Paula Leandro, Pieter Koolwijk, Rita Castro, Henk J Blom, Isabel Tavares de Almeida
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e55483 (2013)
Methyltransferases use S-adenosylmethionine (AdoMet) as methyl group donor, forming S-adenosylhomocysteine (AdoHcy) and methylated substrates, including DNA and proteins. AdoHcy inhibits most methyltransferases. Accumulation of intracellular AdoHcy s
Externí odkaz:
https://doaj.org/article/841a09fd4f574ec8993de1f3fe8d9e03
Autor:
Ruben Esse, Monica S. Rocha, Madalena Barroso, Cristina Florindo, Tom Teerlink, Robert M. Kok, Yvo M. Smulders, Isabel Rivera, Paula Leandro, Pieter Koolwijk, Rita Castro, Henk J. Blom, Isabel Tavares de Almeida
Publikováno v:
PLoS ONE, Vol 8, Iss 10 (2013)
Externí odkaz:
https://doaj.org/article/2926133dcba94c76aa6b440ca99c5df0
Publikováno v:
Endocrine Abstracts.
Publikováno v:
RNA. 25:1259-1273
Methylation of histone H3 on lysine 79 (H3K79) by DOT1L is associated with actively transcribed genes. Earlier, we described that DOT-1.1, the Caenorhabditis elegans homolog of mammalian DOT1L, cooperates with the chromatin-binding protein ZFP-1 (AF1
Autor:
Alla Grishok, Ruben Esse
Publikováno v:
Cells, Vol 9, Iss 1846, p 1846 (2020)
Cells
Volume 9
Issue 8
Cells
Volume 9
Issue 8
The methylation of histone H3 at lysine 79 is a feature of open chromatin. It is deposited by the conserved histone methyltransferase DOT1. Recently, DOT1 localization and H3K79 methylation (H3K79me) have been correlated with enhancers in C. elegans
Methylation of histone H3 lysine 79 (H3K79) by DOT1L is associated with actively transcribed genes. We have previously demonstrated that DOT-1.1, the Caenorhabditis elegans DOT1L homologue, cooperates with the chromatin-binding protein ZFP-1 (homolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::265d015304f89791a0863afd7417fd88
Autor:
Pieter Koolwijk, Ruben Esse, Tom Teerlink, Rita Castro, Isabel Tavares de Almeida, Henk J. Blom
Publikováno v:
Nutrients, 10(4):404. Multidisciplinary Digital Publishing Institute (MDPI)
Esse, R, Teerlink, T, Koolwijk, P, Tavares de Almeida, I, Blom, H J & Castro, R 2018, ' Folinic acid increases protein arginine methylation in human endothelial cells ', Nutrients, vol. 10, no. 4, 404 . https://doi.org/10.3390/nu10040404
Nutrients
Nutrients; Volume 10; Issue 4; Pages: 404
Nutrients, Vol 10, Iss 4, p 404 (2018)
Esse, R, Teerlink, T, Koolwijk, P, Tavares de Almeida, I, Blom, H J & Castro, R 2018, ' Folinic acid increases protein arginine methylation in human endothelial cells ', Nutrients, vol. 10, no. 4, 404 . https://doi.org/10.3390/nu10040404
Nutrients
Nutrients; Volume 10; Issue 4; Pages: 404
Nutrients, Vol 10, Iss 4, p 404 (2018)
Elevated plasma total homocysteine (tHcy) is associated with increased risk of cardiovascular disease, but the mechanisms underlying this association are not completely understood. Cellular hypomethylation has been suggested to be a key pathophysiolo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbde419b2c5049ee859376b9f14990b4
https://research.vumc.nl/en/publications/5292a1f2-2740-4933-97fe-e57b9d89538f
https://research.vumc.nl/en/publications/5292a1f2-2740-4933-97fe-e57b9d89538f