Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Roberta Carloni"'
Autor:
Fiona J. Flett, Emilija Ruksenaite, Lee A. Armstrong, Shipra Bharati, Roberta Carloni, Elizabeth R. Morris, C. Logan Mackay, Heidrun Interthal, Julia M. Richardson
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Human tyrosyl-DNA phosphodiesterase 1 (Tdp1) repairs covalently trapped topoisomerase 1B-DNA complexes and other lesions, and is a target for anticancer drug development. Here the authors use an integrated structural approach to shed light onto the m
Externí odkaz:
https://doaj.org/article/2dff6c27b8244f03bdfbb18f51738a7b
Autor:
Tatsiana Auchynnikava, Robin C. Allshire, Pin Tong, Desislava P. Staneva, A. Arockia Jeyaprakash, Roberta Carloni, Keith R. Matthews, Juri Rappsilber
Publikováno v:
Staneva, D, Carloni, R, Auchynnikava, T, Tong, P, Rappsilber, J, Jeyaprakash, A A, Matthews, K R & Allshire, R C 2021, ' A systematic analysis of Trypanosoma brucei chromatin factors identifies novel protein interaction networks associated with sites of transcription initiation and termination ', Genome Research, vol. 31, no. 11, pp. 2138-2154 . https://doi.org/10.1101/gr.275368.121
Nucleosomes composed of histones are the fundamental units around which DNA is wrapped to form chromatin. Transcriptionally active euchromatin or repressive heterochromatin is regulated in part by the addition or removal of histone post-translational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5574af1e474ac2fc1bf04d47a70b0d1e
https://doi.org/10.1101/2021.02.09.430399
https://doi.org/10.1101/2021.02.09.430399
Autor:
Desislava P, Staneva, Roberta, Carloni, Tatsiana, Auchynnikava, Pin, Tong, Juri, Rappsilber, A Arockia, Jeyaprakash, Keith R, Matthews, Robin C, Allshire
Publikováno v:
Genome Res
Nucleosomes composed of histones are the fundamental units around which DNA is wrapped to form chromatin. Transcriptionally active euchromatin or repressive heterochromatin is regulated in part by the addition or removal of histone post-translational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::79fb3298029f11579b6d4623ba4e3f1a
https://pubmed.ncbi.nlm.nih.gov/34407985
https://pubmed.ncbi.nlm.nih.gov/34407985
Autor:
Fiona J, Flett, Emilija, Ruksenaite, Lee A, Armstrong, Shipra, Bharati, Roberta, Carloni, Elizabeth R, Morris, C Logan, Mackay, Heidrun, Interthal, Julia M, Richardson
Publikováno v:
Nature Communications
Tyrosyl-DNA phosphodiesterase (Tdp1) is a DNA 3′-end processing enzyme that repairs topoisomerase 1B-induced DNA damage. We use a new tool combining site-specific DNA–protein cross-linking with mass spectrometry to identify Tdp1 interactions with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::48dec214d00824c13c0ed0e3bc8990f6
https://pubmed.ncbi.nlm.nih.gov/29295983
https://pubmed.ncbi.nlm.nih.gov/29295983