Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Helena M. Schnell"'
Autor:
Shaun Rawson, Richard M. Walsh, Benjamin Velez, Helena M. Schnell, Fenglong Jiao, Marie Blickling, Jessie Ang, Meera K. Bhanu, Lan Huang, John Hanna
Publikováno v:
Nature structural & molecular biology, vol 29, iss 8
Nat Struct Mol Biol
Nat Struct Mol Biol
Proteasome inhibitors are widely used as therapeutics and research tools, and typically target one of the three active sites, each present twice in the proteasome complex. An endogeneous proteasome inhibitor, PI31, was identified 30 years ago, but it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::241ea339fbfff75f9b6d6aea39b60c5d
https://escholarship.org/uc/item/5t7677k4
https://escholarship.org/uc/item/5t7677k4
Autor:
Lucy C. Robinson, Pavel Ivanov, Marco Jochem, Rini Ravindran, Hendrik Welsch, Helena M. Schnell, Kelly Tatchell, Yagmur Micoogullari, Claire L. Riggs, Paul A. Anderson, John Hanna
Publikováno v:
FEBS J
The compartmentalization of cellular function is achieved largely through the existence of membrane-bound organelles. However, recent work suggests a novel mechanism of compartmentalization mediated by membraneless structures that have liquid droplet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7b6984aa475faae8781024eac8d3a21
https://doi.org/10.1111/febs.15802
https://doi.org/10.1111/febs.15802
Publikováno v:
J Cell Sci
Much of cellular activity is mediated by large multisubunit complexes. However, many of these complexes are too complicated to assemble spontaneously. Instead, their biogenesis is facilitated by dedicated chaperone proteins, which are themselves excl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0488d83c7c339a670019d65cffb26078
https://europepmc.org/articles/PMC9080555/
https://europepmc.org/articles/PMC9080555/
Autor:
Helena M. Schnell, Jessie Ang, Shaun Rawson, Richard M. Walsh, Yagmur Micoogullari, John Hanna
Publikováno v:
The Journal of biological chemistry. 298(5)
The active sites of the proteasome are housed within its central core particle (CP), a barrel-shaped chamber of four stacked heptameric rings, and access of substrates to the CP interior is mediated by gates at either axial end. These gates are const
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da87f38c12ca99d4b59eb0685f43c8e2
https://pubmed.ncbi.nlm.nih.gov/35398095
https://pubmed.ncbi.nlm.nih.gov/35398095
Publikováno v:
The Journal of Cell Biology
Cells are thought to adapt to proteasome inhibition by using alternative pathways for degradation such as autophagy. Sha et al. now report that cells rapidly induce GABARAPL1 and p62 upon proteasome inhibition, but this promotes cell survival by sequ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f813e8aa9944a2dd7b0ebdb11d0597c4
http://europepmc.org/articles/PMC5940303
http://europepmc.org/articles/PMC5940303
Autor:
Daniel Finley, Helena M. Schnell, Steven P. Gygi, Joao A. Paulo, Yagmur Micoogullari, Miguel A. Prado, John Hanna, Angel Guerra-Moreno, Jessie Ang
Publikováno v:
Sci Signal
The yeast stress-activated protein kinase Hog1 is best known for its role in mediating the response to osmotic stress, but it is also activated by various mechanistically distinct environmental stressors, including heat shock, endoplasmic reticulum s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70f990fa4ea31f8821cdfc9796bf9230
https://doi.org/10.1126/scisignal.aaw4956
https://doi.org/10.1126/scisignal.aaw4956
Autor:
Jessie Ang, Marta Isasa, John Hanna, Steven P. Gygi, Meera K. Bhanu, Marco Jochem, Helena M. Schnell, Lukas Ende, Yagmur Micoogullari, Angel Guerra-Moreno
Publikováno v:
Molecular and cellular biology. 39(10)
The abundance of cell surface glucose transporters must be precisely regulated to ensure optimal growth under constantly changing environmental conditions. We recently conducted a proteomic analysis of the cellular response to trivalent arsenic, a ub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbc1d21022e925d8156e954c8a11ea91
https://pubmed.ncbi.nlm.nih.gov/30886123
https://pubmed.ncbi.nlm.nih.gov/30886123