Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Helge Weissig"'
Autor:
Helge Weissig, Shyama Sidique, John W. Kozarich, Emme C.K. Lin, Tyzoon K. Nomanbhoy, Jonathan S. Rosenblum, Junichi Ishiyama, Yi Hu, Bei Li, Christopher M. Amantea
Unlike other members of the MAPK family, ERK5 contains a large C-terminal domain with transcriptional activation capability in addition to an N-terminal canonical kinase domain. Genetic deletion of ERK5 is embryonic lethal, and tissue-restricted dele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fa0e539b27866c3e1d8419d25b4f8e3
https://europepmc.org/articles/PMC5081620/
https://europepmc.org/articles/PMC5081620/
Autor:
Helge Weissig, Bei Li, Junichi Ishiyama, Yi Hu, Shyama Sidique, Tyzoon K. Nomanbhoy, Jonathan S. Rosenblum, Emme C.K. Lin, Christopher A. Amantea, John W. Kozarich
Unlike other members of the MAPK family, ERK5 contains a large C-terminal domain with transcriptional activation capability in addition to an N-terminal canonical kinase domain. Genetic deletion of ERK5 is embryonic lethal and tissue-restricted delet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb49cdb1aa5edb36cb53312a114b6d1f
https://doi.org/10.1101/038513
https://doi.org/10.1101/038513
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
Autor:
Helge Weissig, Doris Pik-Yiu Chun, Tyzoon K. Nomanbhoy, Min Wu, Marek Liyanage, A. Katrin Szardenings, Stephen Tanner, Arwin Aban, Matthew P. Patricelli, John W. Kozarich
Publikováno v:
Biochemistry. 46:350-358
The central role of protein kinases in signal transduction pathways has generated intense interest in targeting these enzymes for a wide range of therapeutic indications. Here we report a method for identifying and quantifying protein kinases in any
Autor:
Panagiotis A. Tsonis, Katia Del Rio-Tsonis, John R. McCarrey, Sonoko Narisawa, C. Sikström, Helge Weissig, José Luis Millán, Per G. Olsson
Publikováno v:
FEBS Letters. 547:61-68
We have cloned and characterized the expression, during spermatogenesis, of three novel zinc finger genes (Zfp94, Zfp95, Zfp96). Analysis of the deduced protein sequences reveals that all three molecules belong to the LeR family (leucine-rich zinc fi
Autor:
Wolfgang F. Bluhm, Philip E. Bourne, Talapady N. Bhat, Shri Jain, David Padilla, Narmada Thanki, Lisa Iype, Bohdan Schneider, Helen M. Berman, John D. Westbrook, Zukang Feng, Phoebe Fagan, Gary L. Gilliland, Kyle Burkhardt, Veerasamy Ravichandran, Jessica Marvin, Christine Zardecki, Tammy Battistuz, Helge Weissig
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 58:899-907
The Protein Data Bank [PDB; Berman, Westbrook et al. (2000), Nucleic Acids Res. 28, 235–242; http://www.pdb.org/] is the single worldwide archive of primary structural data of biological macromolecules. Many secondary sources of information are der
Autor:
Helen M. Berman, Z. Feng, Helge Weissig, Talapady N. Bhat, Gary L. Gilliland, John D. Westbrook
Publikováno v:
The Winnower.
Autor:
Zukang Feng, John D. Westbrook, Helge Weissig, Helen M. Berman, Philip E. Bourne, Talapady N. Bhat, Ilya N. Shindyalov, Gary L. Gilliland
Publikováno v:
Nucleic Acids Research. 28:235-242
The Protein Data Bank (PDB; http://www.rcsb.org/pdb/ ) is the single worldwide archive of structural data of biological macromolecules. This paper describes the goals of the PDB, the systems in place for data deposition and access, how to obtain furt
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:1085-1094
Databases containing macromolecular structure data provide a crystallographer with important tools for use in solving, refining and understanding the functional significance of their protein structures. Given this importance, this paper briefly summa
Autor:
Kai Nakamura, Qiang Li, Tyzoon K. Nomanbhoy, Ann Yu-Jung Shih, Helge Weissig, Oana Cociorva, Lan Pham, John W. Kozarich, Yi Hu, Melissa C. Zhang, Marek Liyanage, Julia Cajica, Kevin R. Shreder, Arwin Aban, Bei Li
Publikováno v:
Bioorganicmedicinal chemistry letters. 23(18)
As the result of a rhJNK1 HTS, the imidazo[1,2-a]quinoxaline 1 was identified as a 1.6 μM rhJNK1 inhibitor. Optimization of this compound lead to AX13587 (rhJNK1 IC50 = 160 nM) which was co-crystallized with JNK1 to identify key molecular interactio