Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Mark Agacan"'
Autor:
Stephen C. Whisson, Mark Agacan, Stephan Wawra, Ian Davidson, Matteo Zanda, Pieter van West, Severine Grouffaud, Claire M. M. Gachon, Paul R. J. Birch, Justin A Boddey, Andrew J. Porter
Publikováno v:
The Journal of biological chemistry
287 (2012): 38101–38109. doi:10.1074/jbc.M112.395129
info:cnr-pdr/source/autori:Wawra, Stephan; Agacan, Mark; Boddey, Justin A.; Davidson, Ian; Gachon, Claire M. M.; Zanda, Matteo; Grouffaud, Severine; Whisson, Stephen C.; Birch, Paul R. J.; Porter, Andy J.; van West, Pieter/titolo:Avirulence Protein 3a (AVR3a) from the Potato Pathogen Phytophthora infestans Forms Homodimers through Its Predicted Translocation Region and Does Not Specifically Bind Phospholipids/doi:10.1074%2Fjbc.M112.395129/rivista:The Journal of biological chemistry (Print)/anno:2012/pagina_da:38101/pagina_a:38109/intervallo_pagine:38101–38109/volume:287
287 (2012): 38101–38109. doi:10.1074/jbc.M112.395129
info:cnr-pdr/source/autori:Wawra, Stephan; Agacan, Mark; Boddey, Justin A.; Davidson, Ian; Gachon, Claire M. M.; Zanda, Matteo; Grouffaud, Severine; Whisson, Stephen C.; Birch, Paul R. J.; Porter, Andy J.; van West, Pieter/titolo:Avirulence Protein 3a (AVR3a) from the Potato Pathogen Phytophthora infestans Forms Homodimers through Its Predicted Translocation Region and Does Not Specifically Bind Phospholipids/doi:10.1074%2Fjbc.M112.395129/rivista:The Journal of biological chemistry (Print)/anno:2012/pagina_da:38101/pagina_a:38109/intervallo_pagine:38101–38109/volume:287
The mechanism of translocation of RxLR effectors from plant pathogenic oomycetes into the cytoplasm of their host is currently the object of intense research activity and debate. Here, we report the biochemical and thermodynamic characterization of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d6c1ce10fa97b1ce0c92170e0cd40bad
https://doi.org/10.1074/jbc.m112.395129
https://doi.org/10.1074/jbc.m112.395129
Publikováno v:
FEBS Journal. 277:511-525
The bacterial twin-arginine translocation (Tat) system is a protein targeting pathway dedicated to the transport of folded proteins across the cytoplasmic membrane. Proteins transported on the Tat pathway are synthesised as precursors with N-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b0a98ee9828b66d51c8f786835dc38da
https://doi.org/10.1111/j.1742-4658.2009.07507.x
https://doi.org/10.1111/j.1742-4658.2009.07507.x
IQGAP proteins reveal an atypical phosphoinositide (aPI) binding domain with a pseudo C2 domain fold
Autor:
Martijn Schenning, Daan M. F. van Aalten, Nick R. Leslie, Ian H. Batty, Miles J. Dixon, C. Peter Downes, Lyudmila Nedyalkova, Yufeng Tong, Mark Agacan, Alexander Gray, Hee-Won Park, Wolfram Tempel
Publikováno v:
The Journal of Biological Chemistry
Background: Phosphoinositide 3-kinase lipid signals exert important biological effects through proteins with specific recognition domains. Results: We identify a novel such protein domain in IQGAP proteins and define its crystal structure and phospho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a773bdeff0d5276bbd1e4a1d325a038
https://pubmed.ncbi.nlm.nih.gov/22493426
https://pubmed.ncbi.nlm.nih.gov/22493426
Autor:
Robert Gourlay, Mark Agacan, Ian H. Batty, Nicholas A. Morrice, Alexander Gray, C. Peter Downes, Miles J. Dixon, Nick R. Leslie, François-Michel Boisvert
Publikováno v:
Molecularcellular proteomics : MCP. 10(4)
Class I phosphoinositide 3-kinases exert important cellular effects through their two primary lipid products, phosphatidylinositol 3,4,5-trisphosphate and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P(2)). As few molecular targets for PtdIns(3,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2375530e8ba5bbdc3e0ba634bbe2518e
https://pubmed.ncbi.nlm.nih.gov/21263009
https://pubmed.ncbi.nlm.nih.gov/21263009
Autor:
Lori Buetow, William N. Hunter, Lindsay B. Tulloch, Venkatasubramanian Ulaganathan, Mark Agacan
Vitamin K(2), or menaquinone, is an essential cofactor for many organisms and the enzymes involved in its biosynthesis are potential antimicrobial drug targets. One of these enzymes, 1,4-dihydroxy-2-naphthoyl-CoA synthase (MenB) from the pathogen Sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d53ec6394e573bd8473416109a61259
https://europepmc.org/articles/PMC2339762/
https://europepmc.org/articles/PMC2339762/
