J
Jacqueline A. Dyck
Researcher at University of California, San Diego
Publications - 10
Citations - 5606
Jacqueline A. Dyck is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Retinoic acid & Retinoic acid receptor alpha. The author has an hindex of 10, co-authored 10 publications receiving 5521 citations. Previous affiliations of Jacqueline A. Dyck include Salk Institute for Biological Studies & Howard Hughes Medical Institute.
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Journal ArticleDOI
9-cis retinoic acid is a high affinity ligand for the retinoid X receptor
Richard A. Heyman,David J. Mangelsdorf,Jacqueline A. Dyck,Jacqueline A. Dyck,Robert B. Stein,Gregor Eichele,Ronald M. Evans,Ronald M. Evans,Christina Thaller +8 more
TL;DR: An experimental approach is reported that has identified 9-cis RA as an RXR ligand, up to 40-fold more potent than all-trans RA in transfection assays and binds with high affinity.
Journal ArticleDOI
Nuclear receptor that identifies a novel retinoic acid response pathway
TL;DR: By indicating the existence of an additional pathway through which retinoic acid may exert its effects, these data lead to a re-evaluation of retinoid physiology.
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A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
Jacqueline A. Dyck,Jacqueline A. Dyck,Gerd G. Maul,Wilson H. Miller,J.Don Chen,Akira Kakizuka,Ronald M. Evans +6 more
TL;DR: Not only is the POD a novel structure, but it can be ascribed an imputed function such that its disruption leads to altered myeloid maturation; this may represent a novel oncogenic target.
Journal ArticleDOI
Retinoid X receptor-COUP-TF interactions modulate retinoic acid signaling.
Steven A. Kliewer,Kazuhiko Umesono,Richard A. Heyman,David J. Mangelsdorf,Jacqueline A. Dyck,Ronald M. Evans +5 more
TL;DR: The retinoid X receptor (RXR) and COUP-TF bind preferentially to a DR-1 motif, and these results support a general proposal in which the half-site spacing preferences may be used as a means to decipher potentially complex and interactive regulatory circuits.
Journal ArticleDOI
SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells.
Huan-You Wang,Wen Lin,Jacqueline A. Dyck,Joanne M. Yeakley,Zhou Songyang,Lewis C. Cantley,Xiang-Dong Fu +6 more
TL;DR: The cloning and characterization of SRPK2 are reported, which is highly related to SRPK1 in sequence, kinase activity, and substrate specificity, and suggest that different SRPK family members may be uniquely regulated and targeted, thereby contributing to splicing regulation in different tissues, during development, or in response to signaling.