Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Eric R Strieter"'
Autor:
Swapneeta S Date, Peng Xu, Nathaniel L Hepowit, Nicholas S Diab, Jordan Best, Boyang Xie, Jiale Du, Eric R Strieter, Lauren P Jackson, Jason A MacGurn, Todd R Graham
Publikováno v:
eLife, Vol 11 (2022)
Deciphering mechanisms controlling SNARE localization within the Golgi complex is crucial to understanding protein trafficking patterns within the secretory pathway. SNAREs are also thought to prime coatomer protein I (COPI) assembly to ensure incorp
Externí odkaz:
https://doaj.org/article/ca38160046ff46beb53e45a6f3e7c5fb
Publikováno v:
Journal of the American Society for Mass Spectrometry. 34:931-938
Publikováno v:
Frontiers in Physiology, Vol 10 (2019)
Protein ubiquitination impacts virtually every biochemical pathway in eukaryotic cells. The fate of a ubiquitinated protein is largely dictated by the type of ubiquitin modification with which it is decorated, including a large variety of polymeric c
Externí odkaz:
https://doaj.org/article/bde925a1c58443aea6ef0a67aca009ad
Autor:
Kirandeep K. Deol, Eric R. Strieter
Publikováno v:
Curr Opin Chem Biol
The diversity of ubiquitin modifications is immense. A protein can be monoubiquitylated, multi-monoubiquitylated, and polyubiquitylated with chains varying in size and shape. Ubiquitin itself can be adorned with other ubiquitin-like proteins and smal
Publikováno v:
Chembiochem
Covalently attaching ubiquitin (Ub) to cellular proteins as a post-translational modification can result in altered function of modified proteins. Enzymes regulating Ub as a post-translational modification, such as ligases and deubiquitinases, are ch
Autor:
Jiale Du, Peng Xu, Jason A. MacGurn, Boyang Xie, Lauren P. Jackson, Todd R. Graham, Swapneeta S. Date, Nathaniel L. Hepowit, Eric R. Strieter, Nicholas S. Diab, Jordan T Best
Publikováno v:
eLife. 11
Deciphering mechanisms controlling SNARE localization within the Golgi complex is crucial to understanding protein trafficking patterns within the secretory pathway. SNAREs are also thought to prime coatomer protein I (COPI) assembly to ensure incorp
Autor:
Swapneeta S Date, Peng Xu, Nathaniel L Hepowit, Nicholas S Diab, Jordan Best, Boyang Xie, Jiale Du, Eric R Strieter, Lauren P Jackson, Jason A MacGurn, Todd R Graham
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fd74c6cbc8c37ade6c199882a382527
https://doi.org/10.7554/elife.80911.sa2
https://doi.org/10.7554/elife.80911.sa2
Autor:
Eric R. Strieter, Kirandeep K. Deol, Sonja Lorenz, Bodo Sander, Marie-Annick Letzelter, Lena K. Ries
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry
Journal of Biological Chemistry
Deregulation of the HECT-type ubiquitin ligase E6AP (UBE3A) is implicated in human papilloma virus-induced cervical tumorigenesis and several neurodevelopmental disorders. Yet the structural underpinnings of activity and specificity in this crucial l
Autor:
Jiale Du, Kirandeep K. Deol, Sean O. Crowe, Heather A. Bisbee, Robert G. Guenette, Eric R. Strieter
Publikováno v:
Mol Cell
The linkage, length, and architecture of ubiquitin (Ub) chains are all important variables in providing tight control over many biological paradigms. There are clear roles for branched architectures in regulating proteasome-mediated degradation, howe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cff0c3b2f8c82bb358d678f9f9a8ef34
https://europepmc.org/articles/PMC7718437/
https://europepmc.org/articles/PMC7718437/
Publikováno v:
J Am Soc Mass Spectrom
Misregulation of the E3 ubiquitin ligase Parkin and the kinase PINK1 underlie both inherited and idiopathic Parkinson’s disease-associated neurodegeneration. Parkin and PINK1 work together to catalyze the assembly of ubiquitin chains on substrates
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9895a715260e5836997aab0fc32af9b
https://europepmc.org/articles/PMC7333183/
https://europepmc.org/articles/PMC7333183/