J
Jay C. Strum
Researcher at Research Triangle Park
Publications - 72
Citations - 6575
Jay C. Strum is an academic researcher from Research Triangle Park. The author has contributed to research in topics: Cancer & Cyclin-dependent kinase. The author has an hindex of 22, co-authored 71 publications receiving 5778 citations. Previous affiliations of Jay C. Strum include University of Illinois at Urbana–Champaign.
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Journal ArticleDOI
The Orphan G Protein-coupled Receptors GPR41 and GPR43 Are Activated by Propionate and Other Short Chain Carboxylic Acids
Andrew J. Brown,Susan M. Goldsworthy,Ashley A. Barnes,Michelle M. Eilert,Lili Tcheang,Dion A. Daniels,Alison I. Muir,Mark J. Wigglesworth,Ian Kinghorn,Neil J. Fraser,Nicholas B. Pike,Jay C. Strum,Klaudia Steplewski,Paul R. Murdock,Julie C. Holder,Fiona H. Marshall,Philip G. Szekeres,Shelagh Wilson,Diane M. Ignar,Steve M. Foord,Alan Wise,Simon J. Dowell +21 more
TL;DR: GPR41 was expressed primarily in adipose tissue, whereas the highest levels of GPR43 were found in immune cells, and was activated by similar ligands but with differing specificity for carbon chain length, with pentanoate being the most potent agonist.
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The Orphan G Protein-coupled Receptor GPR40 Is Activated by Medium and Long Chain Fatty Acids
Celia P. Briscoe,Mohammad Tadayyon,E. John L. Andrews,William G. Benson,Jon K. Chambers,Michelle M. Eilert,Catherine E. Ellis,Nabil Elshourbagy,Aaron S. Goetz,Dana T. Minnick,Paul R. Murdock,Howard Ray Sauls,Usman Shabon,Lisa D. Spinage,Jay C. Strum,Philip G. Szekeres,Kong B. Tan,James M. Way,Diane M. Ignar,Shelagh Wilson,Alison I. Muir +20 more
TL;DR: expression analysis by quantitative reverse transcription-PCR showed that GPR40 was specifically expressed in brain and Pancreas, with expression in rodent pancreas being localized to insulin-producing β-cells.
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CDK4/6 Inhibition Augments Antitumor Immunity by Enhancing T-cell Activation
Jiehui Deng,Jiehui Deng,Eric S. Wang,Russell W. Jenkins,Shuai Li,Ruben Dries,Kathleen B. Yates,Sandeep Chhabra,Wei Huang,Hongye Liu,Amir Reza Aref,Elena Ivanova,Cloud P. Paweletz,Michaela Bowden,Chensheng W. Zhou,Grit S. Herter-Sprie,Jessica A. Sorrentino,John E. Bisi,Patrick H. Lizotte,Ashley A. Merlino,Max M. Quinn,Lauren E. Bufe,Annan Yang,Yanxi Zhang,Hua Zhang,Peng Gao,Ting Chen,Megan E. Cavanaugh,Amanda J. Rode,Eric Haines,Patrick J. Roberts,Jay C. Strum,William G. Richards,Jochen H. Lorch,Sareh Parangi,Viswanath Gunda,Genevieve M. Boland,Raphael Bueno,Sangeetha Palakurthi,Gordon J. Freeman,Gordon J. Freeman,Jerome Ritz,W. Nicholas Haining,Norman E. Sharpless,Haribabu Arthanari,Geoffrey I. Shapiro,Geoffrey I. Shapiro,David A. Barbie,David A. Barbie,Nathanael S. Gray,Kwok-Kin Wong +50 more
TL;DR: It is shown that short-term exposure to small-molecule inhibitors of cyclin-dependent kinases 4 and 6 significantly enhances T- cell activation, contributing to antitumor effects in vivo, due in part to the derepression of NFAT family proteins and their target genes, critical regulators of T-cell function.
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Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells.
TL;DR: Ghosh et al. as mentioned in this paper showed that the carboxyl-terminal domain of Raf-1 kinase (RafC) interacted strongly with phosphatidic acid (PA), and the binding of RafC to PA displayed positive cooperativity with Hill numbers between 3.3 and 6.2.
Journal ArticleDOI
A model of acquired autoresistance to a potent ErbB2 tyrosine kinase inhibitor and a therapeutic strategy to prevent its onset in breast cancer
Wenle Xia,Sarah S. Bacus,Priti S. Hegde,Intisar Husain,Jay C. Strum,Leihua Liu,Georgina Paulazzo,Ljuba Lyass,Patricia Trusk,Jason Hill,Jennifer L. Harris,Neil L. Spector +11 more
TL;DR: It is confirmed that lapatinib induces ER signaling in tumor biopsies from patients with ErbB2-overexpressing breast cancers receiving Lapatinib therapy, providing the rationale for preventing the development of acquired resistance by simultaneously inhibiting both ER and ErBB2 signaling pathways.