Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Natalie J. Kolawa"'
Publikováno v:
eLife, Vol 2 (2013)
Ubiquitin-dependent proteolysis can initiate at ribosomes for myriad reasons including misfolding of a nascent chain or stalling of the ribosome during translation of mRNA. Clearance of a stalled complex is required to recycle the ribosome for future
Externí odkaz:
https://doaj.org/article/0e9700d971ba403f9a2606c83465e45d
Autor:
Natalie J. Kolawa, David C. Chan, Anna M. Salazar, Michael J. Sweredoski, Robert Graham, Nickie C. Chan, Anh H. Pham, Sonja Hess
Publikováno v:
Human Molecular Genetics
Parkin, an E3 ubiquitin ligase implicated in Parkinson's disease, promotes degradation of dysfunctional mitochondria by autophagy. Using proteomic and cellular approaches, we show that upon translocation to mitochondria, Parkin activates the ubiquiti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49b3564a1fbd87be175562091b5ccd5d
http://europepmc.org/articles/PMC3071670
http://europepmc.org/articles/PMC3071670
Autor:
Michael J. Sweredoski, Natalie J. Kolawa, Robert Graham, Robert S. Oania, Raymond J. Deshaies, Sonja Hess
Publikováno v:
Molecular & Cellular Proteomics : MCP
Yeast Cdc48 (p97/VCP in human cells) is a hexameric AAA ATPase that is thought to use ATP hydrolysis to power the segregation of ubiquitin-conjugated proteins from tightly bound partners. Current models posit that Cdc48 is linked to its substrates th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a0c4c040bf86da1b0c2da46cccc47643
https://pubmed.ncbi.nlm.nih.gov/23793018
https://pubmed.ncbi.nlm.nih.gov/23793018
Publikováno v:
eLife, Vol 2 (2013)
eLife
eLife
Ubiquitin-dependent proteolysis can initiate at ribosomes for myriad reasons including misfolding of a nascent chain or stalling of the ribosome during translation of mRNA. Clearance of a stalled complex is required to recycle the ribosome for future
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1405f3a65b5d2c767cf6b30a06aedc42
https://elifesciences.org/articles/00308
https://elifesciences.org/articles/00308
Autor:
Natalie J. Kolawa, Raymond J. Deshaies, J. Eugene Lee, Sonja Hess, Robert Graham, Geoffrey T. Smith, Michael J. Sweredoski
Publikováno v:
Molecular & Cellular Proteomics : MCP
The human genome encodes 69 different F-box proteins (FBPs), each of which can potentially assemble with Skp1-Cul1-RING to serve as the substrate specificity subunit of an SCF ubiquitin ligase complex. SCF activity is switched on by conjugation of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c897ef350cb1981448540697ea6481e
https://resolver.caltech.edu/CaltechAUTHORS:20110526-100158794
https://resolver.caltech.edu/CaltechAUTHORS:20110526-100158794
Autor:
Raymond J. Deshaies, Michael J. Sweredoski, Tara Adele Gomez, Marvin H. Gee, Natalie J. Kolawa
Publikováno v:
BMC Biology
BMC Biology, Vol 9, Iss 1, p 33 (2011)
BMC Biology, Vol 9, Iss 1, p 33 (2011)
Background The proteasome is a multi-subunit protein machine that is the final destination for cellular proteins that have been marked for degradation via an ubiquitin (Ub) chain appendage. These ubiquitylated proteins either bind directly to the int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aec572ef8dc29f5abf1ec5c337036b7b
https://pubmed.ncbi.nlm.nih.gov/21627799
https://pubmed.ncbi.nlm.nih.gov/21627799
Autor:
Raymond J. Deshaies, Geoffrey T. Smith, Ruihua Fang, Johannes Graumann, Natalie J. Kolawa, Gabriela Alexandru
Publikováno v:
Cell. (5):804-816
p97 is an ATP-dependent chaperone that plays an important role in endoplasmic reticulum-associated degradation but whose connections to turnover of soluble proteins remain sparse. Binding of p97 to substrates is mediated by cofactors that contain ubi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::133b20a26ca4ad69cf6a3593e3999fb4