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Ilana Shoshani
Researcher at State University of New York System
Publications - 27
Citations - 801
Ilana Shoshani is an academic researcher from State University of New York System. The author has contributed to research in topics: Adenylyl cyclase & ADCY10. The author has an hindex of 14, co-authored 27 publications receiving 786 citations. Previous affiliations of Ilana Shoshani include Stony Brook University.
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Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA
Oleg V. Tsodikov,Dmitri N. Ivanov,Barbara Orelli,Lidija Staresincic,Ilana Shoshani,Robert Oberman,Orlando D. Schärer,Gerhard Wagner,Tom Ellenberger +8 more
TL;DR: An essential protein–protein interaction of the NER pathway is investigated, the binding of the XPA protein to the ERCC1 subunit of the repair endonuclease ER CC1‐XPF, which reveals a binding interface that is amenable to the development of small molecule peptidomimetics that could be used to modulate NER repair activities in vivo.
Journal Article
Cation and structural requirements for P site-mediated inhibition of adenylate cyclase.
TL;DR: The cation and structural requirements of the intracellular inhibitory "P" site of adenylate cyclase were investigated in human platelet membranes, bovine sperm particles, and detergent-solubilized and purified preparations from rat and bovines brain, suggesting a strict requirement for an intact adenine moiety and a beta-glycosidic linkage for the ribosyl moiety.
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Isozyme-dependent Sensitivity of Adenylyl Cyclases to P-site-mediated Inhibition by Adenine Nucleosides and Nucleoside 3′-Polyphosphates
Roger A. Johnson,Laurent Désaubry,Glen Bianchi,Ilana Shoshani,Edward Lyons,Ronald Taussig,Peter A. Watson,James J. Cali,John Krupinski,Joseph P. Pieroni,Ravi Iyengar +10 more
TL;DR: The data demonstrate isozyme selectivity for some ligands, suggesting the possibility of isozyme-selective inhibitors to take advantage of differences in P-site domains among adenylyl cyclase isozymes.
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Kinetics of "P"-site-mediated inhibition of adenylyl cyclase and the requirements for substrate.
Roger A. Johnson,Ilana Shoshani +1 more
TL;DR: The data suggest a structure for activated adenylyl cyclase such that one nucleotide binding domain, selective for ATP vis-à-vis other ATP analogs, allosterically modulates a proximate P-site domain.
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2′,5′-Dideoxyadenosine 3′-Polyphosphates Are Potent Inhibitors of Adenylyl Cyclases
TL;DR: The availability of this ligand will permit the development of a variety of probes that will be extremely useful in investigating adenylyl cyclase structure and the role(s) that this class of compound may play in physiologically regulating cell function.