Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Lysine chemistry"'
Autor:
Fujiwara, Y., Yamanashi, Y., Fujimura, A., Sato, Y., Kujirai, T., Kurumizaka, H., Kimura, Hiroshi, Yamatsugu, K., Kawashima, S. A., Kanai, M.
Publikováno v:
Proc Natl Acad Sci U S A
Chemical modifications of histones, such as lysine acetylation and ubiquitination, play pivotal roles in epigenetic regulation of gene expression. Methods to alter the epigenome thus hold promise as tools for elucidating epigenetic mechanisms and as
Autor:
Lia Vanzetti, Cristina Potrich, Lorenzo Lunelli, Cecilia Pederzolli, Salvatore Iannotta, Paolo Macchi, L. Pasquardini, Sandra Dirè, Valentina Prusakova, Alessandro Roncador
Publikováno v:
Colloids and surfaces. B, Biointerfaces
204 (2021). doi:10.1016/j.colsurfb.2021.111787
info:cnr-pdr/source/autori:Pasquardini L.; Roncador A.; Prusakova V.; Vanzetti L.; Potrich C.; Lunelli L.; Pederzolli C.; Iannotta S.; Macchi P.; Dire S./titolo:Functionalization of TiO2 sol-gel derived films for cell confinement/doi:10.1016%2Fj.colsurfb.2021.111787/rivista:Colloids and surfaces. B, Biointerfaces (Print)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:204
204 (2021). doi:10.1016/j.colsurfb.2021.111787
info:cnr-pdr/source/autori:Pasquardini L.; Roncador A.; Prusakova V.; Vanzetti L.; Potrich C.; Lunelli L.; Pederzolli C.; Iannotta S.; Macchi P.; Dire S./titolo:Functionalization of TiO2 sol-gel derived films for cell confinement/doi:10.1016%2Fj.colsurfb.2021.111787/rivista:Colloids and surfaces. B, Biointerfaces (Print)/anno:2021/pagina_da:/pagina_a:/intervallo_pagine:/volume:204
The neuroscience field has increased enormously over the last decades, achieving the possible real application of neuronal cultures not only for reproducing neural architectures resembling in vivo tissues, but also for the development of functional d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b43abc7639008404662a111ff0dfeb9
https://publications.cnr.it/doc/458071
https://publications.cnr.it/doc/458071
Akademický článek
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Autor:
Bush, J, Lesniak, R, Yeh, T, Belle, R, Kramer, H, Tumber, A, Chowdhury, R, Flashman, E, Mecinovic, J, Schofield, C
Publikováno v:
Bush, J T, Leśniak, R K, Yeh, T L, Belle, R, Kramer, H, Tumber, A, Chowdhury, R, Flashman, E, Mecinović, J & Schofield, C J 2019, ' Small-molecules that covalently react with a human prolyl hydroxylase-towards activity modulation and substrate capture ', Chemical Communications, vol. 55, no. 8, pp. 1020-1023 . https://doi.org/10.1039/c8cc07706a
We describe covalently binding modulators of the activity of human prolyl hydroxylase domain 2 (PHD2) and studies towards a strategy for photocapture of PHD2 substrates. Reversible active site binding of electrophile bearing compounds enables susbseq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::c51852a308e76e7b3e7f5727fcc6d0bd
https://findresearcher.sdu.dk:8443/ws/files/145976068/c8cc07706a.pdf
https://findresearcher.sdu.dk:8443/ws/files/145976068/c8cc07706a.pdf
Autor:
Markus Kaiser, Xavier Guillory, Jeroen Briels, Christian Ottmann, Elvan Yilmaz, David Bier, Yasser B. Ruiz-Blanco, Elsa Sanchez-Garcia
Publikováno v:
Chemistry : A European Journal, 24(52), 13807-13814. Wiley-VCH Verlag
Previous studies have indicated the presence of defined interactions between oligo or poly(ethylene glycol) (OEG or PEG) and lysine residues. In these interactions, the OEG or PEG residues “wrap around” the lysine amino group, thereby enabling co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c447d84e65f0a0eb6743f8629a201266
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85053043365
https://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&origin=inward&scp=85053043365
Autor:
Robert A. Hipskind, Manuel S. Rodriguez, Guillaume Bossis, Rosa Farràs, Elisabetta Andermarcher, Stefan Müller, Marc Piechaczyk, Isabelle Jariel-Encontre, Darja Schmidt, Cécile E. Malnou
Publikováno v:
Molecular and Cellular Biology
Molecular and Cellular Biology, American Society for Microbiology, 2005, 25 (16), pp.6964--79. ⟨10.1128/MCB.25.16.6964-6979.2005⟩
Molecular and Cellular Biology, American Society for Microbiology, 2005, 25 (16), pp.6964--79. ⟨10.1128/MCB.25.16.6964-6979.2005⟩
The inducible transcriptional complex AP-1, composed of c-Fos and c-Jun proteins, is crucial for cell adaptation to many environmental changes. While its mechanisms of activation have been extensively studied, how its activity is restrained is poorly
Autor:
Sanjeev Khosla, Tamzin E. Randall, Bryan M. Turner, Robert Feil, Laura P. O'Neill, Cécile Fournier, Richard I. Gregory
Publikováno v:
J Biol Chem
J Biol Chem, 2002, 277 (14), pp.11728--34. ⟨10.1074/jbc.M105775200 M105775200 [pii]⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2002, 277 (14), pp.11728--34. ⟨10.1074/jbc.M105775200⟩
J Biol Chem, 2002, 277 (14), pp.11728--34. ⟨10.1074/jbc.M105775200 M105775200 [pii]⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2002, 277 (14), pp.11728--34. ⟨10.1074/jbc.M105775200⟩
International audience; Most loci that are regulated by genomic imprinting have differentially methylated regions (DMRs). Previously, we showed that the DMRs of the mouse Snrpn and U2af1-rs1 genes have paternal allele-specific patterns of acetylation
Publikováno v:
Journal of the American Chemical Society. 134(4)
Post-translational modifications (PTMs) (e.g., acetylation, methylation, and phosphorylation) play crucial roles in regulating the diverse protein-protein interactions involved in essentially every cellular process. While significant progress has bee
Autor:
Hirsch, Brett M.
Silent information regulator 2 (Sir2) enzymes or sirtuins are a family of intracellular protein deacetylases that can catalyze the beta-nicotinamide adenine dinucleotide (beta-NAD+)-dependent deacetylation of N(epsilon)-acetyl-lysine on protein subst
Externí odkaz:
http://rave.ohiolink.edu/etdc/view?acc_num=akron1302055499
Autor:
Hidetoshi Saze, Jerzy Paszkowski, Jacek Lichota, Muhammad Tariq, Yoshiki Habu, Aline V. Probst
Publikováno v:
Tariq, M, Saze, H, Probst, A, Lichota, J, Habu, Y & Paszkowski, JK 2003, ' Erasure of CpG methylation in Arabidopsis alters patterns of histone H3 methylation in heterochromatin ', Proceedings of the National Academy of Science of the United States of America, vol. 100, no. 15, pp. 8823-8827 . https://doi.org/10.1073/pnas.1432939100
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2003, 100 (15), pp.8823-7. ⟨10.1073/pnas.1432939100⟩
Proceedings of the National Academy of Sciences, Vol. 100, No 15 (2003) pp. 8823-7
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2003, 100 (15), pp.8823-7. ⟨10.1073/pnas.1432939100⟩
Proceedings of the National Academy of Sciences, Vol. 100, No 15 (2003) pp. 8823-7
In mammals and plants, formation of heterochromatin is associated with hypermethylation of DNA at CpG sites and histone H3 methylation at lysine 9. Previous studies have revealed that maintenance of DNA methylation in Neurospora and Arabidopsis requi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5181bc179658ef18e9fbadac5f552360
https://vbn.aau.dk/da/publications/af75e4b0-b774-11db-8b72-000ea68e967b
https://vbn.aau.dk/da/publications/af75e4b0-b774-11db-8b72-000ea68e967b