Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Dionne Turnbull"'
Publikováno v:
BioTechniques, Vol 62, Iss 2, Pp 69-75 (2017)
S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl g
Externí odkaz:
https://doaj.org/article/314315093c43443bbafe979ff037d8cc
Autor:
Charlotte H. Hurst, Dionne Turnbull, Kaltra Xhelilaj, Sally Myles, Robin L. Pflughaupt, Michaela Kopischke, Paul Davies, Susan Jones, Silke Robatzek, Cyril Zipfel, Julien Gronnier, Piers A. Hemsley
Plant receptor kinases are key transducers of extracellular stimuli, such as the presence of beneficial or pathogenic microbes or secreted signaling molecules. Receptor kinases are regulated by numerous post-translational modifications.1,2,3 Here, us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e30aae23269ac572fbaf969ea678dbb1
https://doi.org/10.5167/uzh-233956
https://doi.org/10.5167/uzh-233956
Autor:
Dionne Turnbull, Sally M Myles, Charlotte H. Hurst, Julien Gronnier, Susan Jones, Piers A. Hemsley, Cyril Zipfel, Paul Davies, Silke Robatzek, Michaela Kopischke, Robin L. Pflughaupt
SummaryPlant receptor kinases are key transducers of extracellular stimuli, such as the presence of beneficial or pathogenic microbes or secreted signalling molecules. Receptor kinases are regulated by numerous post-translational modifications. Here,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c7d0d3f3a3ef8939f784f646a4ed9120
https://doi.org/10.1101/2021.08.30.457756
https://doi.org/10.1101/2021.08.30.457756
Autor:
Susan Jones, Dionne Turnbull, Kerry Leslie, Charlotte H. Hurst, Kathryn M. Wright, Piers A. Hemsley
Publikováno v:
Scientific Reports, Vol 9, Iss 1, Pp 1-9 (2019)
Scientific Reports
Scientific Reports
This work was funded by UK Biotechnology and Biological Sciences Research Council Grants BB/M024911/1 and BB/M010996/1 to P.A.H. S-acylation is a common post-translational modification of membrane protein cysteine residues with many regulatory roles.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8b8aeec6d0ed7480477251fe4c3b0c3
http://link.springer.com/article/10.1038/s41598-019-49302-x
http://link.springer.com/article/10.1038/s41598-019-49302-x
Autor:
Haixia Wang, Susan Breen, Lydia Welsh, Lina Yang, Marek Malec, Piers A. Hemsley, Eleanor M. Gilroy, Paul R. J. Birch, Tian Zhendong, Shaista Naqvi, Dionne Turnbull, Frédéric Brunner
Publikováno v:
Plant Physiology. 180:571-581
To be successful plant pathogens, microbes use “effector proteins” to manipulate host functions to their benefit. Identifying host targets of effector proteins and characterizing their role in the infection process allow us to better understand p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24ca082076e5099d33fa1b5fa2b76a0f
https://doi.org/10.1104/pp.18.01143
https://doi.org/10.1104/pp.18.01143
Autor:
Shaista Naqvi, Eleanor M. Gilroy, Carolina Aguilera-Galvez, Haixia Wang, Paul R. J. Birch, Zhendong Tian, Dionne Turnbull, Jonathan D. G. Jones, Franziska Trusch, Ingo Hein, Susan Breen, Vivianne G. A. A. Vleeshouwers
Publikováno v:
New Phytologist 232 (2021) 3
New Phytologist, 232(3), 1368-1381
New Phytologist, 232(3), 1368-1381
Knowledge of the evolutionary processes which govern pathogen recognition is critical to understanding durable disease resistance. We determined how Phytophthora infestans effector PiAVR2 is recognised by evolutionarily distinct resistance proteins R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3f4301e78ebd2f8b2b3328c2f3d0c4f
https://research.wur.nl/en/publications/evolutionarily-distinct-resistance-proteins-detect-a-pathogen-eff
https://research.wur.nl/en/publications/evolutionarily-distinct-resistance-proteins-detect-a-pathogen-eff
Publikováno v:
The New Phytologist
New Phytologist
New Phytologist
Summary An understanding of the cell biology underlying the burgeoning molecular genetic and genomic knowledge of oomycete pathogenicity is essential to gain the full context of how these pathogens cause disease on plants. An intense research focus o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31d7bbb5288d001ff638cbd5733986dd
https://pubmed.ncbi.nlm.nih.gov/32394464
https://pubmed.ncbi.nlm.nih.gov/32394464
Autor:
Dionne Turnbull, Piers A. Hemsley
Publikováno v:
Current Opinion in Plant Biology. 40:63-70
The post-translational lipid modifications N-myristoylation, prenylation and S-acylation are traditionally associated with increasing protein membrane affinity and localisation. However this is an over-simplification, with evidence now implicating th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c5d9503d2a067a4149fe9f89e35da08
https://doi.org/10.1016/j.pbi.2017.07.007
https://doi.org/10.1016/j.pbi.2017.07.007
Autor:
Susan Jones, Charlotte H. Hurst, Dionne Turnbull, Piers A. Hemsley, Kerry Leslie, Kathryn M. Wright
S-acylation is a common post-translational modification of membrane protein cysteine residues with many regulatory roles. S-acylation adjacent to transmembrane domains has been described in the literature as affecting diverse protein properties inclu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5801e1abda0cc7728aa30e881f3a8dc9
https://doi.org/10.1101/693887
https://doi.org/10.1101/693887
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2009
S-Acylation is increasingly being recognized as an important dynamic posttranslational modification of cysteine residues in proteins. Various approaches have been described for assaying protein S-acylation with acyl-switch approaches being the most c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::e1cb49b89217a6fefeaa3e00877350b4
https://pubmed.ncbi.nlm.nih.gov/31152391
https://pubmed.ncbi.nlm.nih.gov/31152391