Výsledky vyhledávání - "Stephen Rush Fuhs"

Structural basis for differential recognition of phosphohistidine-containing peptides by 1-pHis and 3-pHis monoclonal antibodies

Autor: Rajasree Kalagiri, James J. La Clair, Stephen Rush Fuhs, Tony Hunter, Robyn L. Stanfield, Ian A. Wilson, Jill Meisenhelder

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America

Significance Phosphohistidine (pHis) is a labile posttranslational modification with two isoforms, 1-pHis and 3-pHis, involved in many cellular processes across the kingdoms of life. Due to its lability, it is difficult to study the pHis modification

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84b506bbbc6ddc23fe71c2db0489b229
https://doi.org/10.1073/pnas.2010644118

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pHisphorylation: the emergence of histidine phosphorylation as a reversible regulatory modification

Autor: Stephen Rush Fuhs, Tony Hunter

Publikováno v: Current Opinion in Cell Biology. 45:8-16

Histidine phosphorylation is crucial for prokaryotic signal transduction and as an intermediate for several metabolic enzymes, yet its role in mammalian cells remains largely uncharted. This is primarily caused by difficulties in studying histidine p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d908be01f67b39a704f863b43453e43c
https://doi.org/10.1016/j.ceb.2016.12.010

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A non-acidic method using hydroxyapatite and phosphohistidine monoclonal antibodies allows enrichment of phosphopeptides containing non-conventional phosphorylations for mass spectrometry analysis

Autor: J. La Clair, James J. Moresco, A. Aslanian, Kevin Adam, J. Diedrich, Stephen Rush Fuhs, Tony Hunter, John R. Yates, Jill Meisenhelder

Four types of phosphate-protein linkage generate nine different phosphoresidues in living organisms. Histidine phosphorylation is a long-time established but largely unexplored post-translational modification, mainly because of the acid-lability of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cc68ba78f3add55bb7c6b6593d66350

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Identification of PGAM5 as a Mammalian Protein Histidine Phosphatase that Plays a Central Role to Negatively Regulate CD4 + T Cells

Autor: Edward Y. Skolnik, Tony Hunter, Shekhar Srivastava, Stephen Rush Fuhs, Zhai Li, Saswati Panda, Martin Vaeth

Publikováno v: Molecular Cell. 63:457-469

Whereas phosphorylation of serine, threonine, and tyrosine is exceedingly well characterized, the role of histidine phosphorylation in mammalian signaling is largely unexplored. Here we show that phosphoglycerate mutase family 5 (PGAM5) functions as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::482f3284592a4c177673adbf2e805690
https://doi.org/10.1016/j.molcel.2016.06.021

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The protein histidine phosphatase LHPP is a tumour suppressor

Autor: Charlotte K.Y. Ng, Dritan Liko, Paul Jenoe, Michael N. Hall, Charles Betz, Tony Hunter, Yakir Guri, Markus H. Heim, Luigi Terracciano, Sravanth K. Hindupur, Marco Colombi, Matthias S. Matter, Salvatore Piscuoglio, Stephen Rush Fuhs, Luca Quagliata, Suzette Moes, Marion Cornu, Kevin Adam

Histidine phosphorylation, the so-called hidden phosphoproteome, is a poorly characterized post-translational modification of proteins1,2. Here we describe a role of histidine phosphorylation in tumorigenesis. Proteomic analysis of 12 tumours from an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9f6092cd0a2c4742a98882b4d878852
https://edoc.unibas.ch/62663/

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Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation

Autor: John R. Yates, Magda Stankova, Aaron Aslanian, Li Ma, Jacques Mauger, Stephen Rush Fuhs, Alan Binnie, Tony Hunter, Fahad Al-Obeidi, Anna Zagórska, Greg Lemke, Jill Meisenhelder

Publikováno v: Cell. 162(1):198-210

SummaryHistidine phosphorylation (pHis) is well studied in bacteria; however, its role in mammalian signaling remains largely unexplored due to the lack of pHis-specific antibodies and the lability of the phosphoramidate (P-N) bond. Both imidazole ni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df0f23eac62ae949ac6d6d1b88cfe2cc

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Histidine phosphorylation relieves copper inhibition in the mammalian potassium channel KCa3.1

Autor: Tony Hunter, Zhai Li, Stevan R. Hubbard, Stephen Rush Fuhs, Edward Y. Skolnik, Dennis J. Thiele, Shekhar Srivastava, Saswati Panda

Publikováno v: eLife, Vol 5 (2016)
eLife

KCa2.1, KCa2.2, KCa2.3 and KCa3.1 constitute a family of mammalian small- to intermediate-conductance potassium channels that are activated by calcium-calmodulin. KCa3.1 is unique among these four channels in that activation requires, in addition to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35220343d4bd67140912e6d11b2779f4
https://elifesciences.org/articles/16093

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Pharmacology and Signaling Properties of Epidermal Growth Factor Receptor Isoforms Studied by Bioluminescence Resonance Energy Transfer

Autor: Steven Wong, Esther C. Reding, Fabrice Piu, Hans H. Schiffer, Qing Lu, Roger Olsson, Anne E. Knapp, Pey Lih H. Littler, Phil K. Tan, William Keefe, D. M. Weiner, Mark R. Brann, Stephen Rush Fuhs, Norman Nash

Publikováno v: Molecular Pharmacology. 71:508-518

We have developed a new assay for measuring epidermal growth factor receptor (EGFR) activation using the bioluminescence resonance energy transfer (BRET) technology, which directly measures the recruitment of signaling proteins to activated EGFR. Our

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c38e28c3b1e9f960d9c3ad4f02675a03
https://doi.org/10.1124/mol.106.027656

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