Zobrazeno 1 - 10
of 11
pro vyhledávání: '"David E. Puleo"'
Autor:
Kanak Raina, Chris D. Forbes, Rebecca Stronk, Jonathan P. Rappi, Kyle J. Eastman, Samuel W. Gerritz, Xinheng Yu, Hao Li, Amit Bhardwaj, Mia Forgione, Abigail Hundt, Madeline P. King, Zoe M. Posner, Allison Denny, Andrew McGovern, David E. Puleo, Ethan Garvin, Rebekka Chenard, Nilesh Zaware, James J. Mousseau, Jennifer Macaluso, Michael Martin, Kyle Bassoli, Kelli Jones, Marco Garcia, Katia Howard, Levi M. Smith, Jinshan M. Chen, Cesar A. De Leon, John Hines, Katherine J. Kayser-Bricker, Craig M. Crews
While specific cell signaling pathway inhibitors have yielded great success in oncology, directly triggering cancer cell death is one of the great drug discovery challenges facing biomedical research in the era of precision oncology. Attempts to erad
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::23ae61c78302824016b90ccec8643f82
https://doi.org/10.1101/2023.01.01.522436
https://doi.org/10.1101/2023.01.01.522436
Autor:
Thomas K. Dawson, S.G. Krimmer, Maria-Elena Liosi, Kara J. Cutrona, Ana S. Newton, David E. Puleo, Joseph Schlessinger, Yoshihisa Suzuki, William L. Jorgensen
Publikováno v:
J Med Chem
Janus kinases (JAKs) are non-receptor tyrosine kinases that are essential components of the JAK-STAT signaling pathway. Associated aberrant signaling is responsible for many forms of cancer and disorders of the immune system. The present focus is on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4147c54acb04879d3ac21b985bb19a75
https://europepmc.org/articles/PMC7949251/
https://europepmc.org/articles/PMC7949251/
Autor:
Sean P. Henry, Joseph Schlessinger, Ana S. Newton, Maria-Elena Liosi, John C. Faver, William L. Jorgensen, S.G. Krimmer, Luca Deiana, David E. Puleo
Publikováno v:
Tetrahedron Lett
Small molecules that selectively bind to the pseudokinase JH2 domain over the JH1 kinase domain of JAK2 kinase are sought. Virtual screening led to the purchase of 17 compounds among which 9 were found to bind to V617F JAK2 JH2 with affinities of 40
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e209b41f18875b8e5be9d836830e8c7b
https://doi.org/10.1016/j.tetlet.2021.153248
https://doi.org/10.1016/j.tetlet.2021.153248
Publikováno v:
Pharmaceutical Patent Analyst. 6:273-282
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae63491fd386f14c96b3c885f9429c20
https://doi.org/10.4155/ppa-2017-0028
https://doi.org/10.4155/ppa-2017-0028
Autor:
Henrik Hammaren, William L. Jorgensen, David E. Puleo, Daniela Ungureanu, Joseph Schlessinger, Olli Silvennoinen, Kaury Kucera, Ana S. Newton
Publikováno v:
ACS Medicinal Chemistry Letters. 8:618-621
Janus kinases (JAKs) regulate hematopoiesis via the cytokine-mediated JAK-STAT signaling pathway. JAKs contain tandem C-terminal pseudokinase (JH2) and tyrosine kinase (JH1) domains. The JAK2 pseudokinase domain adopts a protein kinase fold and, desp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::928a2aa7e8b23aa679b5c49cb5f38e32
https://doi.org/10.1021/acsmedchemlett.7b00153
https://doi.org/10.1021/acsmedchemlett.7b00153
Autor:
José A. Cisneros, Joseph Schlessinger, Kara J. Cutrona, Luca Deiana, William L. Jorgensen, David E. Puleo, Ana S. Newton
Publikováno v:
ACS Medicinal Chemistry Letters. 8:614-617
A competitive fluorescence polarization (FP) assay is reported for determining binding affinities of probe molecules with the pseudokinase JAK2 JH2 allosteric site. The syntheses of the fluorescent 5 and 6 used in the assay are reported as well as Kd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90d96713a7e4bb7cc07181bcbe4e03b1
https://doi.org/10.1021/acsmedchemlett.7b00154
https://doi.org/10.1021/acsmedchemlett.7b00154
Autor:
Yaping Wang, Xin Chen, Zhuoliang Chen, John William Giraldes, Kirk Wright, Sean Kim, José S. Duca, Eric J. Martin, J. Tres Brazell, Kristen Hurov, Elizabeth R. Sprague, Yun Feng, David E. Puleo, Subarna Shakya, Yanqiu Yuan, David Sage, Matthew J. Meyer, Yuji Mishina, Yan Yan-Neale, Christopher Sean Straub, Li Tian, Simon Mathieu, Dongshu Chen, Wenlin Shao, B. Barry Touré, Troy Smith
Publikováno v:
Journal of Medicinal Chemistry. 59:4711-4723
MELK kinase has been implicated in playing an important role in tumorigenesis. Our previous studies suggested that MELK is involved in the regulation of cell cycle and its genetic depletion leads to growth inhibition in a subset of high MELK-expressi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eef8110b976db9c7b26d95564840f324
https://doi.org/10.1021/acs.jmedchem.6b00052
https://doi.org/10.1021/acs.jmedchem.6b00052
Autor:
Andrey V. Reshetnyak, Navjot Kaur, David E. Puleo, Mansoor Ahmed, Anton Poliakov, Alexander N. Plotnikov, Francisco Tome, Joseph Schlessinger, Jyotidarsini Mohanty, Irit Lax, Arul M. Cinnaiyan
Elucidating the physiological roles and modes of action of the recently discovered ligands (designated ALKAL1,2 or AUG-α,β) of the receptor tyrosine kinases Anaplastic Lymphoma Kinase (ALK) and Leukocyte Tyrosine Kinase (LTK) has been limited by di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7afaee2d35c44ce508c4d87139b69053
https://europepmc.org/articles/PMC6099872/
https://europepmc.org/articles/PMC6099872/
Autor:
Karen S. Anderson, Kathleen M. Frey, Krasimir A. Spasov, William L. Jorgensen, David E. Puleo, Mariella Bollini
Publikováno v:
Journal of Medicinal Chemistry
The development of novel non-nucleoside inhibitors (NNRTIs) with activity against variants of HIV reverse transcriptase (RT) is crucial for overcoming treatment failure. The NNRTIs bind in an allosteric pocket in RT ∼10 Å away from the active site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::120073538f08972fcd09487cb6b691fa
https://doi.org/10.1021/jm501908a
https://doi.org/10.1021/jm501908a
Publikováno v:
Journal of Molecular Biology. 411:190-200
Here, we report high-resolution X-ray structures of Bacillus subtilis aspartate transcarbamoylase (ATCase), an enzyme that catalyzes one of the first reactions in pyrimidine nucleotide biosynthesis. Structures of the enzyme have been determined in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bd7ca1dcc9a153fa749d9262fbb6271
https://doi.org/10.1016/j.jmb.2011.05.036
https://doi.org/10.1016/j.jmb.2011.05.036