Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Eric, Okerberg"'
Autor:
Kevin B. Dagbay, Tyzoon K. Nomanbhoy, John W. Kozarich, Jennifer L. Green, Eric Okerberg, Sergey N. Savinov, Ishankumar V Soni, Arwin Aban, Jeanne A. Hardy
Publikováno v:
Biochemistry. 58(52)
Acyl phosphates of ATP (ATPAc) and related nucleotides have proven to be useful for the interrogation of known nucleotide binding sites via specific acylation of conserved lysines (K). In addition, occasional K acylations are identified in proteins w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9951abe25ba37f1bc861f527af08a296
https://pubmed.ncbi.nlm.nih.gov/31095371
https://pubmed.ncbi.nlm.nih.gov/31095371
Autor:
Jiangyue Wu, Laia Monserrat, Violeta Serra, Josilyn Sejd, Marta Palafox, Senait Alemayehu, Jennifer L. Green, Eric Okerberg, Arwin Aban, Tyzoon K. Nomanbhoy, Maria Sykes
Publikováno v:
Molecular cancer therapeutics. 18(4)
The interaction of a drug with its target is critical to achieve drug efficacy. In cases where cellular environment influences target engagement, differences between individuals and cell types present a challenge for a priori prediction of drug effic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaf0ed8e091e0546b183371c7bfcb181
https://pubmed.ncbi.nlm.nih.gov/30837298
https://pubmed.ncbi.nlm.nih.gov/30837298
Autor:
Allister Fraser, Kevin R. Shreder, Junichi Ishiyama, John W. Kozarich, Yi Hu, Yasushi Kohno, Heidi E. Brown, Lingling Du, Eric Okerberg, Christopher M. Amantea, Julia Cajica, Emme C.K. Lin, Lan M. Pham
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 23:1553-1556
AX10479, the phenyl amide of 4-hydroxy-8-methanesulfonylamino-quinoline-2-carboxylic acid, was identified as a Zn2+-dependent, 27 nM inhibitor of human plasma Lp-PLA2. Structure–activity relationship studies focused on the AX10479 2-phenylamide gro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c315b99f9891368e7cffabc5de59502a
https://doi.org/10.1016/j.bmcl.2012.11.048
https://doi.org/10.1016/j.bmcl.2012.11.048
Autor:
Gabriel M. Simon, Melissa M. Dix, Eric Okerberg, Matthew P. Patricelli, Chu Wang, Benjamin F. Cravatt
Publikováno v:
Cell. 150:426-440
Summary Caspase proteases are principal mediators of apoptosis, where they cleave hundreds of proteins. Phosphorylation also plays an important role in apoptosis, although the extent to which proteolytic and phosphorylation pathways crosstalk during
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f84703eefd9ad25cc1154240170d998a
https://doi.org/10.1016/j.cell.2012.05.040
https://doi.org/10.1016/j.cell.2012.05.040
Autor:
Eric Okerberg, Julia Cajica, Kevin R. Shreder, Yasushi Kohno, Lan M. Pham, Heidi E. Brown, Junichi Ishiyama, Yi Hu, John W. Kozarich, Allister Fraser, Lingling Du, Emme C.K. Lin, Christopher M. Amantea
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 22:868-871
AX10185, the phenyl amide of xanthurenic acid, was found to be a sub-100 nM inhibitor of Lp-PLA2. However, in the presence of EDTA the inhibitory activity of AX10185 was extinguished while the enzymatic activity of Lp-PLA2 did not change. Subsequent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de185b106366a37c0bc14bd62e17a668
https://doi.org/10.1016/j.bmcl.2011.12.045
https://doi.org/10.1016/j.bmcl.2011.12.045
Autor:
Helge Weissig, Nathanael S. Gray, Chris Herring, Arwin Aban, David Zhou, Heidi E. Brown, Eric Okerberg, Subadhra Jagannathan, John W. Kozarich, Qingkai Yang, Jianming Zhang, Jiing Dwan Lee, Tyzoon K. Nomanbhoy, Jiangyue Wu, Brian E. Nordin, Matthew P. Patricelli
Publikováno v:
Chemistry & Biology. 18:699-710
Protein kinases are intensely studied mediators of cellular signaling, yet important questions remain regarding their regulation and in vivo properties. Here we use a probe-based chemoprotemics platform to profile several well studied kinase inhibito
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2bf88204473b0d9c9c120755dfc9e3bd
https://doi.org/10.1016/j.chembiol.2011.04.011
https://doi.org/10.1016/j.chembiol.2011.04.011
Autor:
Matthew L. Plenert, Eric Okerberg, Mary Jane Gordon, Jason B. Shear, Richard Allen, Michael L. Gostkowski
Publikováno v:
Biophysical Journal. 86:3223-3229
We report photochemical and photophysical studies of a multiphoton-excited reaction of serotonin that previously has been shown to generate a photoproduct capable of emitting broadly in the visible spectral region. The current studies demonstrate tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2c6cec9a9ebb822f4b2114fa46649e1
https://doi.org/10.1016/s0006-3495(04)74370-2
https://doi.org/10.1016/s0006-3495(04)74370-2
Publikováno v:
Analytical Biochemistry. 303:199-202
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb5d429ed4406c24df1f24e36ae5c637
https://doi.org/10.1006/abio.2001.5550
https://doi.org/10.1006/abio.2001.5550
Autor:
Eric Okerberg, John W. Kozarich, Ann Shih, Tyzoon K. Nomanbhoy, Jane Wu, Arwin Aban, Heidi E. Brown, Anna Hainley, Matthew P. Patricelli, Senait Alemayehu, Jonathan S. Rosenblum
Publikováno v:
PLoS ONE, Vol 12, Iss 2, p e0172649 (2017)
PLoS ONE
PLoS ONE
We describe the identification of a novel, tumor-specific missense mutation in the active site of casein kinase 1α (CSNK1A1) using activity-based proteomics. Matched normal and tumor colon samples were analyzed using an ATP acyl phosphate probe in a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4a3499e390bc05713de49c13c8be244
https://doi.org/10.1371/journal.pone.0172649
https://doi.org/10.1371/journal.pone.0172649
Autor:
Eric Okerberg, Jonathan S. Rosenblum, Heidi E. Brown, Senait Alemayehu, Lauro Minimo, John W. Kozarich, Matthew P. Patricelli, Tyzoon K. Nomanbhoy
Publikováno v:
Journal of the American Chemical Society. 136(12)
Here we describe a chemical proteomics strategy using ATP acyl phosphates to measure the formation of a protein:protein complex between p38α and mapkap kinases 2 and/or 3. Formation of the protein:protein complex results in a new probe labeling site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0308264dfcd7129d5d21ea77b87b9f39
https://pubmed.ncbi.nlm.nih.gov/24601623
https://pubmed.ncbi.nlm.nih.gov/24601623