Výsledky vyhledávání - "Kristy G Kuplast"

Abstract 2154: PARP7 inhibitor RBN-2397 increases tumoral IFN signaling leading to various tumor cell intrinsic effects and tumor regressions in mouse models

Publikováno v: Cancer Research. 82:2154-2154

Targeting cytosolic nucleic acid sensing pathways to activate the Type I interferon (IFN) response is an emerging therapeutic strategy being explored in oncology. The PARP family consists of seventeen enzymes that regulate fundamental biological proc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::138b6edb388c9ff28b5c6026a9134c0a
https://doi.org/10.1158/1538-7445.am2022-2154

Zobrazit plný text záznamu

Structure and Property Guided Design in the Identification of PRMT5 Tool Compound EPZ015666

Autor: J. Joshua Smith, Christina R. Majer, Michael John Munchhof, Roy M. Pollock, Nigel J. Waters, Kristy G Kuplast, Lei Jin, L. Danielle Johnston, Lawrence A. Reiter, Nathalie Rioux, Richard Chesworth, Margaret Porter Scott, Elayne Chan-Penebre, P. Ann Boriack-Sjodin, Robert A. Copeland, Mikel P. Moyer, Kenneth W. Duncan

Publikováno v: ACS medicinal chemistry letters. 7(2)

The recent publication of a potent and selective inhibitor of protein methyltransferase 5 (PRMT5) provides the scientific community with in vivo-active tool compound EPZ015666 (GSK3235025) to probe the underlying pharmacology of this key enzyme. Here

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45a771b83bf95b1122657893267ce967
https://pubmed.ncbi.nlm.nih.gov/26985292

Zobrazit plný text záznamu

Abstract LB-248: Protein arginine methyltransferase 5 (PRMT5) inhibition as a therapeutic strategy in B-cell lymphoma

Autor: Jesse Smith, David Soong, Kristy G Kuplast, Christine Thompson, Olena Barbash, Elayne Penebre, Rocio Montes de Oca, Christina R. Majer, Christopher L. Carpenter, Charles F. McHugh, Ryan G. Kruger, Kenneth W. Duncan, Robert A. Copeland, Richard Chesworth, Neil F. Johnson, Sarah Gerhart, Ping Zhang

Publikováno v: Cancer Research. 75:LB-248

PRMT5 is responsible for symmetric dimethylation of arginine residues in glycine and arginine rich (GAR) motifs on a variety of cytosolic and nuclear proteins including histones, spliceosome components, regulators of translation, transcription factor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::dd47649121ed3b12bab388fda4e64230
https://doi.org/10.1158/1538-7445.am2015-lb-248

Zobrazit plný text záznamu

Calsenilin interacts with transcriptional co-repressor C-terminal binding protein(s)

Autor: Wilma Wasco, Kristy G. Kuplast, Nikhat F. Zaidi, Yuji Kajiwara, Kevin J. Washicosky, Joseph D. Buxbaum

Publikováno v: Journal of neurochemistry. 98(4)

Calsenilin/potassium channel-interacting protein (KChIP)3/ downstream regulatory element sequence antagonist modulator (DREAM) is a neuronal calcium-binding protein that has been shown to have multiple functions in the cell, including the regulation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ca366a351f6e28b0b92fc7f53186284
https://pubmed.ncbi.nlm.nih.gov/16787403

Zobrazit plný text záznamu

Abstract 48: RBN-2397: A potent and selective small molecule inhibitor of PARP7 that induces tumor-derived antitumor immunity dependent on CD8 T cells

Publikováno v: Cancer Research. 81:48-48

Targeting cytosolic nucleic acid sensing pathways and the Type I interferon (IFN) response is an emerging therapeutic strategy being explored in oncology. The PARP family consists of seventeen enzymes that regulate fundamental biological processes in

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::cbbdce3f5b4baab19e0042b551ef0b95
https://doi.org/10.1158/1538-7445.am2021-48

Zobrazit plný text záznamu

Abstract 1344: Small molecule inhibitor of CD38 modulates its intra- and extracellular functions leading to antitumor activity

Autor: Kaiko Kunii, W. David Church, Danielle J. Blackwell, Kevin Wayne Kuntz, Tim J. Wigle, Kristen McEachern, Heike Keilhack, Yue Ren, Laurie B. Schenkel, Ellen Bamberg, Prashant Shambharkar, Melissa Vasbinder, Kristy Kuplast-Barr, Christina R. Majer, Joseph M. Gozgit, Jenkins L. Lemera, Luke Utley, Victoria M. Richon, Mario Niepel

Publikováno v: Cancer Research. 81:1344-1344

CD38 is an ADP-ribosyl cyclase that converts NAD+ to ADP-ribose (ADPR) or cyclic ADPR (cADPR) and nicotinamide. The enzyme can exist in either an ecto- or endo-catalytic orientation with different sub-cellular localization, and therefore can regulate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0c751ca50b9bf2528b2979338f802eef
https://doi.org/10.1158/1538-7445.am2021-1344

Zobrazit plný text záznamu

Akademický článek

Calsenilin interacts with transcriptional co-repressor C-terminal binding protein(s).

Autor: Zaidi, Nikhat F., Kuplast, Kristy G., Washicosky, Kevin J., Kajiwara, Yuji, Buxbaum, Joseph D., Wasco, Wilma

Publikováno v: Journal of Neurochemistry; Aug2006, Vol. 98 Issue 4, p1290-1301, 12p, 3 Color Photographs, 5 Black and White Photographs, 1 Chart

Zobrazit plný text záznamu

Abstract 3405: PARP7 negatively regulates the type I interferon response in cancer cells and its inhibition leads to tumor regression

Publikováno v: Cancer Research. 80:3405-3405

Targeting cytosolic nucleic acid sensing pathways and the Type I interferon (IFN) response is an emerging therapeutic strategy being explored in oncology. PARP7 is a member of the monoPARP class of enzymes, which catalyze the transfer of single units

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::112e2524350629a13849861f971ffccc
https://doi.org/10.1158/1538-7445.am2020-3405

Zobrazit plný text záznamu

Abstract DDT02-01: RBN-2397: A first-in-class PARP7 inhibitor targeting a newly discovered cancer vulnerability in stress-signaling pathways

Publikováno v: Cancer Research. 80:DDT02-01

RBN-2397: A first-in-class PARP7 inhibitor targeting a newly discovered cancer vulnerability in stress-signaling pathways PARP7 is a monoPARP that catalyzes the transfer of single units of ADP-ribose onto substrates to change their function (MARylati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::863abc28e5666d46a68f4a84fb89c594
https://doi.org/10.1158/1538-7445.am2020-ddt02-01

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání