Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Anna Plechanovová"'
Autor:
Paul Murphy, Yingqi Xu, Sarah L. Rouse, Ellis G. Jaffray, Anna Plechanovová, Steve J. Matthews, J. Carlos Penedo, Ronald T. Hay
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
RNF4 is a prototypical single-subunit E3 enzyme that can bind both substrate and ubiquitin-loaded E2. Here, the authors show that the RNF4 N-terminal region, although lacking a defined secondary structure, maintains a compact global conformation to f
Externí odkaz:
https://doaj.org/article/c9de74e062a44078a1b0ae8e8b67bf15
Autor:
Ellis Jaffray, Steve Matthews, Anna Plechanovová, Paul Murphy, Yingqi Xu, Ronald T. Hay, Sarah L. Rouse, J. Carlos Penedo
Publikováno v:
Nature Communications
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
The human genome contains an estimated 600 ubiquitin E3 ligases, many of which are single-subunit E3s (ssE3s) that can bind to both substrate and ubiquitin-loaded E2 (E2~Ub). Within ssE3s structural disorder tends to be located in substrate binding a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf5806855838dded5420bcf80b7148d4
http://europepmc.org/articles/PMC7393505
http://europepmc.org/articles/PMC7393505
Publikováno v:
Methods in enzymology. 618
Posttranslational modification with small ubiquitin-like modifier (SUMO) plays an important role in many biological processes. SUMO-targeted ubiquitin E3 ligases (STUbLs) are part of the really interesting new gene (RING)-type family of ubiquitin E3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::79ce08d20e559f02ed1ff3b6950adfcf
https://pubmed.ncbi.nlm.nih.gov/30850055
https://pubmed.ncbi.nlm.nih.gov/30850055
Posttranslational modification with small ubiquitin-like modifier (SUMO) plays an important role in many biological processes. SUMO-targeted ubiquitin E3 ligases (STUbLs) are part of the really interesting new gene (RING)-type family of ubiquitin E3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f5fc42649a9fae76d2ba0e39cf43d9b
https://doi.org/10.1016/bs.mie.2018.11.005
https://doi.org/10.1016/bs.mie.2018.11.005
Publikováno v:
Nature
Ubiquitin modification is mediated by a large family of specificity determining ubiquitin E3 ligases. To facilitate ubiquitin transfer, RING E3 ligases bind both substrate and a ubiquitin E2 conjugating enzyme linked to ubiquitin via a thioester bond
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::69fbc764309d091dca3c1d044a189aa0
http://europepmc.org/articles/PMC3442243
http://europepmc.org/articles/PMC3442243
Autor:
Kenneth A. Johnson, Ronald T. Hay, Stephen A. McMahon, Ellis Jaffray, Iva Navratilova, James H. Naismith, Anna Plechanovová
Publikováno v:
Nature Structural & Molecular Biology. 18:1052-1059
Mammalian RNF4 is a dimeric RING ubiquitin E3 ligase that ubiquitylates poly-SUMOylated proteins. We found that RNF4 bound ubiquitin-charged UbcH5a tightly but free UbcH5a weakly. To provide insight into the mechanism of RING-mediated ubiquitylation,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c6c1a7a20db867c56e715e049f2c385
https://doi.org/10.1038/nsmb.2108
https://doi.org/10.1038/nsmb.2108
Autor:
Ronald T. Hay, Amit K. Garg, Anna Plechanovová, Roland Bruderer, Ivan Matic, Michael H. Tatham
Publikováno v:
EMBO Rep
The small ubiquitin-like modifier (SUMO) can undergo self-modification to form polymeric chains that have been implicated in cellular processes such as meiosis, genome maintenance and stress response. Investigations into the biological role of polyme
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ad086ae5ba6f2e2a0c573e887e05398
https://doi.org/10.1038/embor.2010.206
https://doi.org/10.1038/embor.2010.206
Publikováno v:
Traffic (Copenhagen, Denmark)
Cystatin F is a cysteine protease inhibitor that is selectively expressed in immune cells and unlike other cystatin family members is targeted to a significant extent to intracellular compartments. Initially made as an inactive glycosylated disulfide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f946c48b72786f5f863254c99c14519
http://europepmc.org/articles/PMC2691902
http://europepmc.org/articles/PMC2691902
Autor:
Neil Hattersley, Anna Plechanovová, Jorma J. Palvimo, Marie-Claude Geoffroy, Ellis Jaffray, Michael H. Tatham, Ronald T. Hay, Linnan Shen
Publikováno v:
Nature Cell Biology
Nature Cell Biology, Nature Publishing Group, 2008, 10, pp.538-546. ⟨10.1038/ncb1716⟩
Nature Cell Biology, Nature Publishing Group, 2008, 10, pp.538-546. ⟨10.1038/ncb1716⟩
International audience; In acute promyelocytic leukaemia (APL), promyelocytic leukaemia (PML) protein is fused to the retinoic acid receptor α (RAR). This disease can be treated effectively with arsenic, which induces PML modification by small ubiqu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab364d6461b8035a57c6054a0ad4cdea
https://doi.org/10.1038/ncb1716
https://doi.org/10.1038/ncb1716
Autor:
Cyril Bařinka, Jan Konvalinka, Lubomír Rulíšek, Daruka Mahadevan, Petra Mlčochová, Anna Plechanovová, José W. Saldanha
Publikováno v:
FEBS Journal. 274:4731-4741
Human glutamate carboxypeptidase II [GCPII (EC 3.4.17.21)] is recognized as a promising pharmacological target for the treatment and imaging of various pathologies, including neurological disorders and prostate cancer. Recently reported crystal struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::15ba45cb1e05324bfb0b88cda766ef7b
https://doi.org/10.1111/j.1742-4658.2007.06021.x
https://doi.org/10.1111/j.1742-4658.2007.06021.x