Zobrazeno 1 - 10
of 319
pro vyhledávání: '"Jay T Groves"'
Autor:
Yujie Ye, Shumpei Morita, Justin J Chang, Patrick M Buckley, Kiera B Wilhelm, Daniel DiMaio, Jay T Groves, Francisco N Barrera
Publikováno v:
eLife, Vol 12 (2023)
The T cell receptor (TCR) is a complex molecular machine that directs the activation of T cells, allowing the immune system to fight pathogens and cancer cells. Despite decades of investigation, the molecular mechanism of TCR activation is still cont
Externí odkaz:
https://doaj.org/article/5bc68c83b835416d911a9631379addcc
Publikováno v:
eLife, Vol 12 (2023)
The Tec-family kinase Btk contains a lipid-binding Pleckstrin homology and Tec homology (PH-TH) module connected by a proline-rich linker to a ‘Src module’, an SH3-SH2-kinase unit also found in Src-family kinases and Abl. We showed previously tha
Externí odkaz:
https://doaj.org/article/c60c916d064543008f2769b180012919
Publikováno v:
eLife, Vol 11 (2022)
The phosphatidylinositol 4-phosphate 5-kinase (PIP5K) family of lipid-modifying enzymes generate the majority of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] lipids found at the plasma membrane in eukaryotic cells. PI(4,5)P2 lipids serve a criti
Externí odkaz:
https://doaj.org/article/9938dafba4bd4c5f9d778b537db3d487
Publikováno v:
eLife, Vol 10 (2021)
Clustering of ligand:receptor complexes on the cell membrane is widely presumed to have functional consequences for subsequent signal transduction. However, it is experimentally challenging to selectively manipulate receptor clustering without alteri
Externí odkaz:
https://doaj.org/article/6031d0ba643944d9a1e991839d41e8e6
Autor:
Deepti Karandur, Moitrayee Bhattacharyya, Zijie Xia, Young Kwang Lee, Serena Muratcioglu, Darren McAffee, Ethan D McSpadden, Baiyu Qiu, Jay T Groves, Evan R Williams, John Kuriyan
Publikováno v:
eLife, Vol 9 (2020)
Ca2+/calmodulin-dependent protein kinase II (CaMKII) is an oligomeric enzyme with crucial roles in neuronal signaling and cardiac function. Previously, we showed that activation of CaMKII triggers the exchange of subunits between holoenzymes, potenti
Externí odkaz:
https://doaj.org/article/811a46346e94491a8a20e6b13f51505a
Flexible linkers in CaMKII control the balance between activating and inhibitory autophosphorylation
Autor:
Moitrayee Bhattacharyya, Young Kwang Lee, Serena Muratcioglu, Baiyu Qiu, Priya Nyayapati, Howard Schulman, Jay T Groves, John Kuriyan
Publikováno v:
eLife, Vol 9 (2020)
The many variants of human Ca2+/calmodulin-dependent protein kinase II (CaMKII) differ in the lengths and sequences of disordered linkers connecting the kinase domains to the oligomeric hubs of the holoenzyme. CaMKII activity depends on the balance b
Externí odkaz:
https://doaj.org/article/e288fb9b9a424e16af273300c1822e2a
Publikováno v:
eLife, Vol 6 (2017)
The signal recognition particle (SRP) delivers ~30% of the proteome to the eukaryotic endoplasmic reticulum, or the bacterial plasma membrane. The precise mechanism by which the bacterial SRP receptor, FtsY, interacts with and is regulated at the tar
Externí odkaz:
https://doaj.org/article/3f2d251f53af40fe9473456c130d3b07
Autor:
Alan R Lowe, Jeffrey H Tang, Jaime Yassif, Michael Graf, William YC Huang, Jay T Groves, Karsten Weis, Jan T Liphardt
Publikováno v:
eLife, Vol 4 (2015)
Soluble karyopherins of the importin-β (impβ) family use RanGTP to transport cargos directionally through the nuclear pore complex (NPC). Whether impβ or RanGTP regulate the permeability of the NPC itself has been unknown. In this study, we identi
Externí odkaz:
https://doaj.org/article/2c1722a9c6944549a1041a4eceffff7c
Autor:
Margaret Stratton, Il-Hyung Lee, Moitrayee Bhattacharyya, Sune M Christensen, Luke H Chao, Howard Schulman, Jay T Groves, John Kuriyan
Publikováno v:
eLife, Vol 3 (2014)
Externí odkaz:
https://doaj.org/article/1d4c8c19cb6a4e0e93766980c0287302
Autor:
Margaret Stratton, Il-Hyung Lee, Moitrayee Bhattacharyya, Sune M Christensen, Luke H Chao, Howard Schulman, Jay T Groves, John Kuriyan
Publikováno v:
eLife, Vol 3 (2014)
The activation of the dodecameric Ca2+/calmodulin dependent kinase II (CaMKII) holoenzyme is critical for memory formation. We now report that CaMKII has a remarkable property, which is that activation of the holoenzyme triggers the exchange of subun
Externí odkaz:
https://doaj.org/article/e7ee2a33b9b94a1986048d7a6b38acc5