Výsledky vyhledávání - "Nadia P.C. Allen"

Salvador Protein Is a Tumor Suppressor Effector of RASSF1A with Hippo Pathway-independent Functions

Autor: Farida Latif, Adrianna Henson, Nadia P.C. Allen, Thomas L. Dunwell, Howard Donninger, Laura E. Gordon, Geoffrey J. Clark, Andrew Williams, Jennifer Pogue, Susannah Kassler

Publikováno v: Journal of Biological Chemistry. 286:18483-18491

The RASSF1A tumor suppressor binds and activates proapoptotic MST kinases. The Salvador adaptor protein couples MST kinases to the LATS kinases to form the hippo pathway. Upon activation by RASSF1A, LATS1 phosphorylates the transcriptional regulator

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbdc57e4dd886bf9db1ecaa889898953
https://doi.org/10.1074/jbc.m110.214874

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RASSF6 is a novel member of the RASSF family of tumor suppressors

Autor: Howard Donninger, Michele D. Vos, Luke B. Hesson, Geoffrey J. Clark, Nadia P.C. Allen, Farida Latif, Michael J. Birrer, Laura E. Gordon, Kristin Eckfeld

Publikováno v: Oncogene. 26:6203-6211

RASSF family proteins are tumor suppressors that are frequently downregulated during the development of human cancer. The best-characterized member of the family is RASSF1A, which is downregulated by promoter methylation in 40-90% of primary human tu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::569baf9a8b847fba822082b4ea593915
https://doi.org/10.1038/sj.onc.1210440

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Comprehensive Analysis of a Multidimensional Liquid Chromatography Mass Spectrometry Dataset Acquired on a Quadrupole Selecting, Quadrupole Collision Cell, Time-of-flight Mass Spectrometer

Autor: Kirk C. Hansen, Michael Rexach, Katalin F. Medzihradszky, Alma L. Burlingame, Peter R. Baker, Nadia P.C. Allen, Robert J. Chalkley

Publikováno v: Molecular & Cellular Proteomics. 4:1194-1204

A thorough analysis of the protein interaction partners of the yeast GTPase Gsp1p was carried out by a multidimensional chromatography strategy of strong cation exchange fractionation of peptides followed by reverse phase LC-ESI-MSMS using a QSTAR in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04071ac838b1bac6b16745caaaf768fe
https://doi.org/10.1074/mcp.d500002-mcp200

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Deciphering Networks of Protein Interactions at the Nuclear Pore Complex

Autor: Lan Huang, Malik Lutzmann, Eduard C. Hurt, Michael Rexach, Al Burlingame, Samir S. Patel, Nadia P.C. Allen, Robert J. Chalkley

Publikováno v: Molecular & Cellular Proteomics. 1:930-946

The nuclear pore complex (NPC) gates the only known conduit for molecular exchange between the nucleus and cytoplasm of eukaryotic cells. Macromolecular transport across the NPC is mediated by nucleocytoplasmic shuttling receptors termed karyopherins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0ebaf2fcead0ccfeb3d7de67331cdb5
https://doi.org/10.1074/mcp.t200012-mcp200

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Proteomic Analysis of Nucleoporin Interacting Proteins

Autor: Nadia P.C. Allen, Lan Huang, Al Burlingame, Michael Rexach

Publikováno v: Journal of Biological Chemistry. 276:29268-29274

The Saccharomyces cerevisiae nuclear pore complex is a supramolecular assembly of 30 nucleoporins that cooperatively facilitate nucleocytoplasmic transport. Thirteen nucleoporins that contain FG peptide repeats (FG Nups) are proposed to function as s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5eadfc7729f3b42de72b7745d8fd6745
https://doi.org/10.1074/jbc.m102629200

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The identification of protein-protein interactions of the nuclear pore complex of Saccharomyces cerevisiae using high throughput matrix-assisted laser desorption ionization time-of-flight tandem mass spectrometry

Autor: Peter R. Baker, Lan Huang, Nadia P.C. Allen, Jennifer M. Campbell, Katalin F. Medzihradszky, Michael Rexach, Ricky D. Edmondson, Peter Juhasz, Alma L. Burlingame, Steven A. Martin, David Maltby, Marvin L. Vestal, Michael A. Baldwin

Publikováno v: Molecularcellular proteomics : MCP. 1(6)

Mass spectrometry has become the technology of choice for detailed identification of proteins in complex mixtures. Although electrophoretic separation, proteolytic digestion, mass spectrometric analysis of unseparated digests, and database searching

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a075f48684a6a4b855993ad043750db
https://pubmed.ncbi.nlm.nih.gov/12169684

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The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex

Autor: Brook Mykytka, Lan Huang, Michael Rexach, Al Burlingame, Nadia P.C. Allen, Daniel P. Denning

Publikováno v: The Journal of cell biology, vol 154, iss 5
The Journal of Cell Biology
Denning, D; Mykytka, B; Allen, NPC; Huang, L; Burlingame, A; & Rexach, M. (2001). The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex. Journal of Cell Biology, 154(5), 937-950. doi: 10.1083/jcb.200101007. UC Irvine: Retrieved from: http://www.escholarship.org/uc/item/3640r8hs

The nucleoporins Nup60p, Nup2p, and Nup1p form part of the nuclear basket structure of the Saccharomyces cerevisiae nuclear pore complex (NPC). Here, we show that these necleoporins can be isolated from yeast extracts by affinity chromatography on ka

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35655b08a46f5409e5fd685924c7fb34
https://escholarship.org/uc/item/3640r8hs

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