Výsledky vyhledávání - "Judith Murray-Rust"

Molecular Recognition of the Tes LIM2–3 Domains by the Actin-related Protein Arp7A

Autor: Phillip P. Knowles, Neil Q. McDonald, David Briggs, Erika Soriano, Judith Murray-Rust, Boyan K. Garvalov, Michael Way, Batiste Boëda

Publikováno v: The Journal of Biological Chemistry

Actin-related proteins (Arps) are a highly conserved family of proteins that have extensive sequence and structural similarity to actin. All characterized Arps are components of large multimeric complexes associated with chromatin or the cytoskeleton

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3d08505f903df59233128e1f0b96eba
https://doi.org/10.1074/jbc.m110.171264

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Endothelial, Sympathetic, and Cardiac Function in Inherited (6 R )- l -Erythro-5,6,7,8-Tetrahydro- l -Biopterin Deficiency

Autor: Simon Heales, Katherine Bleasdale-Barr, Kailash P. Bhatia, Laura Watson, Nicholas W. Wood, Mary G. Sweeney, Judith Murray-Rust, Iris Trender-Gerhard, Lydia Mason, John E. Deanfield, Lila Mayahi, Christopher J. Mathias, Ann E. Donald, Denis Pellerin, Aroon D. Hingorani, Mary B. Davis

Publikováno v: Circulation: Cardiovascular Genetics. 3:513-522

Background— (6 R )-5,6,7,8-Tetrahydro- l -biopterin (BH4) is a cofactor for enzymes involved in catecholamine and nitric oxide generation whose synthesis is initiated by GTP cyclohydrolase I (GTPCH-1), encoded by GCH1 . In the absence of a potent,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65e64a83de1d3ea62192ea1fcbbf651d
https://doi.org/10.1161/circgenetics.110.957605

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Dynamics of Lipid Transfer by Phosphatidylinositol Transfer Proteins in Cells

Autor: Shamshad Cockcroft, Patrick Ee, Sadaf Shadan, Nicolas Carvou, Roman Holic, Michelle Li, Judith Murray-Rust

Publikováno v: Traffic (Copenhagen, Denmark)

Of many lipid transfer proteins identified, all have been implicated in essential cellular processes, but the activity of none has been demonstrated in intact cells. Among these, phosphatidylinositol transfer proteins (PITP) are of particular interes

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::980afbcd7f51e30d8a445310759636fd
http://europepmc.org/articles/PMC2635478

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Phosphorylation of a Distinct Structural Form of Phosphatidylinositol Transfer Protein α at Ser166 by Protein Kinase C Disrupts Receptor-mediated Phospholipase C Signaling by Inhibiting Delivery of Phosphatidylinositol to Membranes

Autor: Bruno Ségui, Neil Q. McDonald, Judith Murray-Rust, Gopal P. Sapkota, Nick Morrice, Alison Skippen, Shamshad Cockcroft, Clive P. Morgan, Victoria Allen-Baume, Banafshé Larijani, Andrew Ball

Publikováno v: Journal of Biological Chemistry. 279:47159-47171

Phosphatidylinositol transfer protein alpha (PITPalpha) participates in the supply of phosphatidylinositol ( PI) required for many cellular events including phospholipase C (PLC) beta and gamma signaling by G-protein-coupled receptors and receptor-ty

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50791480a0756239288f458653af99b6
https://doi.org/10.1074/jbc.m405827200

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The Mycobacterium tuberculosis ino1 gene is essential for growth and virulence

Autor: Yossef Av-Gay, Neil G. Stoker, Gregory J. Bancroft, Judith Murray-Rust, Richard A. Norman, Sharon L. Kendall, Farahnaz Movahedzadeh, Debbie A. Smith, Premkumar Dinadayala, Stuart C.G. Rison, Mamadou Daffe, Mark S. B. McAlister, Neil Q. McDonald, David G. Russell

Publikováno v: Molecular Microbiology. 51:1003-1014

Inositol is utilized by Mycobacterium tuberculosis in the production of its major thiol and of essential cell wall lipoglycans. We have constructed a mutant lacking the gene encoding inositol-1-phosphate synthase (ino1), which catalyses the first com

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fb9e135f0a92a682f83b55bd23a29ef0
https://doi.org/10.1046/j.1365-2958.2003.03900.x

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S -nitrosylation of dimethylarginine dimethylaminohydrolase regulates enzyme activity: Further interactions between nitric oxide synthase and dimethylarginine dimethylaminohydrolase

Autor: Neil Q. McDonald, Judith Murray-Rust, Patrick Vallance, James Leiper

Publikováno v: Proceedings of the National Academy of Sciences. 99:13527-13532

The enzyme dimethylarginine dimethylaminohydrolase (DDAH) hydrolyses asymmetrically methylated arginine residues that are endogenously produced inhibitors of nitric oxide synthases (NOS). We and others have proposed that DDAH activity is a key determ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c7a71c66a9e13f7f04dfe2a05a58ada
https://doi.org/10.1073/pnas.212269799

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The Role of Tyrosine Residues in Fibroblast Growth Factor Receptor 1 Signaling in PC12 Cells

Autor: Simona Raffioni, Judith Murray-Rust, Erik D. Foehr, Ralph A. Bradshaw

Publikováno v: Journal of Biological Chemistry. 276:37529-37536

To assess the contribution of the intracellular domain tyrosine residues to the signaling capacity of fibroblast growth factor receptor 1 (FGFR1), stably transfected chimeras bearing the ectodomain of the platelet-derived growth factor receptor (PDGF

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::595894b06834c4aa12d81f1d3779cd5a
https://doi.org/10.1074/jbc.m103234200

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[Untitled]

Autor: Patrick Vallance, Neil Q. McDonald, Judith Murray-Rust, John P. Phelan, James Leiper, Mark Mcalister, Jo Santa Maria, Sarah J. Tilley

Publikováno v: Nature Structural Biology. 8:679-683

Nitric oxide synthase is inhibited by asymmetric NG-methylated derivatives of arginine whose cellular levels are controlled in part by dimethylarginine dimethylaminohydrolase (DDAH, EC 3.5.3.18). Levels of asymmetric NG,NG-dimethylarginine (ADMA) are

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4713b2bf87ac7773261b264485c08086
https://doi.org/10.1038/90387

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Structure-activity relationship of the p55 TNF receptor death domain and its lymphoproliferation mutants

Autor: Judith Murray-Rust, Gert De Wilde, Matthias Federwisch, Elke Boone, Carlos F. Ibáñez, Neil Q. McDonald, Axel Wollmer, Guy Haegeman, Dionne Olerenshaw

Publikováno v: European Journal of Biochemistry. 268:1382-1391

Upon stimulation with tumor necrosis factor (TNF), the TNF receptor (TNFR55) mediates a multitude of effects both in normal and in tumor cells. Clustering of the intracellular domain of the receptor, the so-called death domain (DD), is responsible fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c7c4e6770111ff05d693b6e0c516d9d5
https://doi.org/10.1046/j.1432-1327.2001.02004.x

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Distinct structural elements in GDNF mediate binding to GFRalpha 1 and activation of the GFRalpha 1-c-Ret receptor complex

Autor: Judith Murray-Rust, Susanna Eketjäll, Carlos F. Ibáñez, Mike Fainzilber

Publikováno v: The EMBO Journal. 18:5901-5910

Ligand-induced receptor oligomerization is a widely accepted mechanism for activation of cell-surface receptors. We investigated ligand-receptor interactions in the glial cell-line derived neurotrophic factor (GDNF) receptor complex, formed by the c-

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8737420933d9441481291a8b3cd82ae
https://doi.org/10.1093/emboj/18.21.5901

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