Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Matthew E Cockman"'
Autor:
Matthew E Cockman, Kerstin Lippl, Ya-Min Tian, Hamish B Pegg, William D Figg Jnr, Martine I Abboud, Raphael Heilig, Roman Fischer, Johanna Myllyharju, Christopher J Schofield, Peter J Ratcliffe
Publikováno v:
eLife, Vol 8 (2019)
Human and other animal cells deploy three closely related dioxygenases (PHD 1, 2 and 3) to signal oxygen levels by catalysing oxygen regulated prolyl hydroxylation of the transcription factor HIF. The discovery of the HIF prolyl-hydroxylase (PHD) enz
Externí odkaz:
https://doaj.org/article/70d88ea4f82c4443ab41453328102032
Autor:
Matthew E. Cockman, Yoichiro Sugimoto, Hamish B. Pegg, Norma Masson, Eidarus Salah, Anthony Tumber, Helen R. Flynn, Joanna M. Kirkpatrick, Christopher J. Schofield, Peter J. Ratcliffe
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 119(32)
The Jumonji domain–containing protein JMJD6 is a 2-oxoglutarate–dependent dioxygenase associated with a broad range of biological functions. Cellular studies have implicated the enzyme in chromatin biology, transcription, DNA repair, mRNA splicin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eafbca36a476f0147886ecdb4cf25a8e
https://pubmed.ncbi.nlm.nih.gov/35930668
https://pubmed.ncbi.nlm.nih.gov/35930668
Autor:
Mehdi Pirooznia, Komudi Singh, Marjan Gucek, Danielle A. Springer, Matthew E. Cockman, Angel Aponte, Junhui Sun, Karen J. Keeran, Elizabeth Murphy, Michael Harris, Leslie Kennedy
Publikováno v:
Cardiovasc Res
AIMS Prolyl hydroxylation is a post-translational modification that regulates protein stability, turnover, and activity. The proteins that catalyze prolyl hydroxylation belong to the 2-oxoglutarate- and iron-dependent oxygenase family of proteins. 2-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a42258a3dd425a7f6131f663c403b455
https://pubmed.ncbi.nlm.nih.gov/34668514
https://pubmed.ncbi.nlm.nih.gov/34668514
Autor:
Matthew E. Cockman, Peter J. Ratcliffe, Junhui Sun, Elizabeth Murphy, Leslie Kennedy, Michael Harris
Publikováno v:
Circulation Research. 127
Prolyl hydroxylation is a post-translational modification that is known to regulate several key cell functions including translation and protein stability. Enzymes that catalyze prolyl hydroxylation belong to the 2-oxoglutarate- and iron-dependent ox
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fecf71350f641c58f14ff7c261c4b303
https://doi.org/10.1161/res.127.suppl_1.317
https://doi.org/10.1161/res.127.suppl_1.317
Autor:
Steven C Clifford, Matthew E Cockman, Alan C Smallwood, David R Mole, Emma R Woodward, Patrick H Maxwell, Peter J Ratcliffe, Eamonn R Maher
Publikováno v:
Human Molecular Genetics. 30:844-845
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7c8c2b0345bf54d32d24aac00b83af2f
https://doi.org/10.1093/hmg/ddab037
https://doi.org/10.1093/hmg/ddab037
Autor:
Swaksha Rachuri, Riekelt H. Houtkooper, Roman Fischer, Marcin W. Wlodarski, Franca di Summa, Taco W. Kuijpers, Marieke von Lindern, Matthew E. Cockman, Susan J. Baserga, Jonathan D. Dinman, Martin Attwood, Peter J. Ratcliffe, Alyson W. MacInnes, Nahuel A. Paolini, Joseph Briggs, Pierre-Emmanuel Gleizes, Carolina Marques dos Santos Vieira, Anita M. van Adrichem, Marie-Françoise O'Donohue, Samuel B. Sondalle
Publikováno v:
American Journal of Human Genetics
American Journal of Human Genetics, Elsevier (Cell Press), 2017, 100 (3), pp.506-522. ⟨10.1016/j.ajhg.2017.01.034⟩
American journal of human genetics, 100(3), 506-522. Cell Press
American Journal of Human Genetics, Elsevier (Cell Press), 2017, 100 (3), pp.506-522. ⟨10.1016/j.ajhg.2017.01.034⟩
American journal of human genetics, 100(3), 506-522. Cell Press
Ribosomal protein (RP) gene mutations, mostly associated with inherited or acquired bone marrow failure, are believed to drive disease by slowing the rate of protein synthesis. Here de novo missense mutations in the RPS23 gene, which codes for uS12,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa037980b76c6bca03a9d4290f5a6685
https://doi.org/10.1016/j.ajhg.2017.01.034
https://doi.org/10.1016/j.ajhg.2017.01.034
Autor:
Johanna Myllyharju, Roman Fischer, William D Figg Jnr, Kerstin Lippl, Raphael Heilig, Christopher J. Schofield, Matthew E. Cockman, Ya-Min Tian, Martine I. Abboud, Hamish B Pegg, Peter J. Ratcliffe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8ed9be5c54cd1c00ac767438b749412d
https://doi.org/10.7554/elife.46490.072
https://doi.org/10.7554/elife.46490.072
Autor:
Danielle A. Springer, Elizabeth Murphy, Angel Aponte, Matthew E. Cockman, Marjan Gucek, Audrey Noguchi, Peter J. Ratcliffe, Junhui Sun, Leslie Kennedy
Publikováno v:
Journal of Molecular and Cellular Cardiology. 140:54
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2983747b2bde5c096268f28e60a489e7
https://doi.org/10.1016/j.yjmcc.2019.11.130
https://doi.org/10.1016/j.yjmcc.2019.11.130
Autor:
Pablo Wappner, Helen E McNeil, Robert K. Leśniak, Martine I. Abboud, Wei Ge, Rasheduzzaman Chowdhury, Simon J. Davis, Charlotte A. Hall, Weston B. Struwe, Ming Yang, Rebecca Konietzny, Peter J. Ratcliffe, Christopher J. Schofield, Sarah E. Wilkins, Charlotte D. Eaton, Roman Fischer, Suzana Markolovic, Maximiliano Javier Katz, Qinqin Zhuang, Justin L. P. Benesch, Benedikt M. Kessler, Mathew L. Coleman, Matthew E. Cockman
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Nature chemical biology
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Nature chemical biology
Biochemical, structural and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) to be a 2-oxoglutarate (2OG)-dependent oxygenase that catalyzes (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 to be more closely relat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a46c86c7038ec03a855bb818a0825bb
http://ora.ox.ac.uk/objects/uuid:
http://ora.ox.ac.uk/objects/uuid:
Autor:
Steven C. Clifford, Patrick H. Maxwell, David R. Mole, Eamonn R. Maher, Peter J. Ratcliffe, Matthew E. Cockman, Emma R. Woodward, Alan C Smallwood
The von Hippel-Lindau tumour suppressor gene product (pVHL) associates with the elongin B and C and Cul2 proteins to form a ubiquitin-ligase complex (VCBC). To date, the only VCBC substrates identified are the hypoxia-inducible factor alpha subunits
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fa0dca96efdd25f22ed62abcb939697
https://ora.ox.ac.uk/objects/uuid:79885dd6-7620-4a15-aae6-af32f19f2138
https://ora.ox.ac.uk/objects/uuid:79885dd6-7620-4a15-aae6-af32f19f2138