Zobrazeno 1 - 10
of 59
pro vyhledávání: '"Robert Gourlay"'
Autor:
Seraina Blümli, Nicola Wiechens, Meng-Ying Wu, Vijender Singh, Marek Gierlinski, Gabriele Schweikert, Nick Gilbert, Catherine Naughton, Ramasubramanian Sundaramoorthy, Joby Varghese, Robert Gourlay, Renata Soares, David Clark, Tom Owen-Hughes
Publikováno v:
Cell Reports, Vol 37, Iss 5, Pp 109943- (2021)
Summary: The ARID1A subunit of SWI/SNF chromatin remodeling complexes is a potent tumor suppressor. Here, a degron is applied to detect rapid loss of chromatin accessibility at thousands of loci where ARID1A acts to generate accessible minidomains of
Externí odkaz:
https://doaj.org/article/04921146582c4b71a0ec2443dd1ee13e
Autor:
Kevin Z.L. Wu, Rebecca A. Jones, Theresa Tachie-Menson, Thomas J. Macartney, Nicola T. Wood, Joby Varghese, Robert Gourlay, Renata F. Soares, James C. Smith, Gopal P. Sapkota
Publikováno v:
Wellcome Open Research, Vol 4 (2020)
Background: Two recessive mutations in the FAM83G gene, causing A34E and R52P amino acid substitutions in the DUF1669 domain of the PAWS1 protein, are associated with palmoplantar keratoderma (PPK) in humans and dogs respectively. We have previously
Externí odkaz:
https://doaj.org/article/6d803ddfa9804a42b43f77a667ddecfe
Autor:
Kevin Z.L. Wu, Rebecca A. Jones, Theresa Tachie-Menson, Thomas J. Macartney, Nicola T. Wood, Joby Varghese, Robert Gourlay, Renata F. Soares, James C. Smith, Gopal P. Sapkota
Publikováno v:
Wellcome Open Research, Vol 4 (2019)
Background: Two recessive mutations in the FAM83G gene, causing A34E and R52P amino acid substitutions in the DUF1669 domain of the PAWS1 protein, are associated with palmoplantar keratoderma (PPK) in humans and dogs respectively. We have previously
Externí odkaz:
https://doaj.org/article/825b99f7ce8c4131b3178e4180dfa8e2
Autor:
Janis Vogt, Kevin S. Dingwell, Lina Herhaus, Robert Gourlay, Thomas Macartney, David Campbell, James C. Smith, Gopal P. Sapkota
Publikováno v:
Open Biology, Vol 4, Iss 2 (2014)
Bone morphogenetic proteins (BMPs) control multiple cellular processes in embryos and adult tissues. BMPs signal through the activation of type I BMP receptor kinases, which then phosphorylate SMADs 1/5/8. In the canonical pathway, this triggers the
Externí odkaz:
https://doaj.org/article/cd09befeb687451bb7705bf7e0827b03
Autor:
Veerle De Wever, David C Lloyd, Isha Nasa, Mhairi Nimick, Laura Trinkle-Mulcahy, Robert Gourlay, Nick Morrice, Greg B G Moorhead
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e39510 (2012)
Metazoan mitosis requires remodelling of sub-cellular structures to ensure proper division of cellular and genetic material. Faults often lead to genomic instability, cell cycle arrests and disease onset. These key structural changes are under tight
Externí odkaz:
https://doaj.org/article/b674daa69e1f4f0c8d8b023cea388afa
Autor:
Chandana Kondapalli, Agne Kazlauskaite, Ning Zhang, Helen I. Woodroof, David G. Campbell, Robert Gourlay, Lynn Burchell, Helen Walden, Thomas J. Macartney, Maria Deak, Axel Knebel, Dario R. Alessi, Miratul M. K. Muqit
Publikováno v:
Open Biology, Vol 2, Iss 5 (2012)
Summary Missense mutations in PTEN-induced kinase 1 (PINK1) cause autosomal-recessive inherited Parkinson's disease (PD). We have exploited our recent discovery that recombinant insect PINK1 is catalytically active to test whether PINK1 directly phos
Externí odkaz:
https://doaj.org/article/a7ccab88220e49e2ad360b217db36be0
Autor:
Andrew D. Waddell, Hina Ojha, Shalini Agarwal, Christopher J. Clarke, Ana Terriente-Felix, Houjiang Zhou, Poonam Kakade, Axel Knebel, Andrew M. Shaw, Robert Gourlay, Joby Varghese, Renata F. Soares, Rachel Toth, Thomas Macartney, Patrick A. Eyers, Nick Morrice, Richard Bayliss, Alexander J. Whitworth, Claire E. Eyers, Miratul M. K. Muqit
Loss-of-function mutations in the human PINK1 kinase (hPINK1) are causative of early-onset Parkinson’s disease (PD). Activation of hPINK1 induces phosphorylated ubiquitin to initiate removal of damaged mitochondria by autophagy. Previously we solve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e0e00472b151d1285b844ca753507a62
https://doi.org/10.1101/2023.03.31.534916
https://doi.org/10.1101/2023.03.31.534916
Publikováno v:
The Biochemical journal. 479(20)
SummaryADP-heptose activates the protein kinase ALPK1 triggering TIFA phosphorylation at Thr9, the recruitment of TRAF6 and the subsequent production of inflammatory mediators. Here, we demonstrate that ADP-heptose also stimulates the formation of Ly