Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Stefanie A H de Poot"'
Autor:
Won Hoon Choi, Stefanie A. H. de Poot, Jung Hoon Lee, Ji Hyeon Kim, Dong Hoon Han, Yun Kyung Kim, Daniel Finley, Min Jae Lee
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
The proteasome plays a key role in proteostasis by mediating the degradation of ubiquitinated substrates. Here the authors show that an open-gate mutant of the proteasome is hyperactive towards a subset of substrates and can effectively delay the acc
Externí odkaz:
https://doaj.org/article/69d5789905d74b3b8111cc7dc208f815
Autor:
Marissa Ashton, Martin Weber, Mark P. Jedrychowski, Thimo Kurz, Daniel Finley, Hai Ngu, Eric J. Brown, Alexandra M. Whiteley, Stefanie A. H. de Poot, Mervyn J. Monteiro, Amy Easton, John Szpyt, Sara L. Dominguez, Steven P. Gygi, Joao A. Paulo, Miguel A. Prado
Publikováno v:
The Journal of Biological Chemistry
Familial neurodegenerative diseases commonly involve mutations that result in either aberrant proteins or dysfunctional components of the proteolytic machinery that act on aberrant proteins. UBQLN2 is a ubiquitin receptor of the UBL/UBA family that b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4817136e59d4fb8136c5a4764e71e673
https://doi.org/10.1101/2020.02.22.956524
https://doi.org/10.1101/2020.02.22.956524
Autor:
Pieter J A de Koning, J Alain Kummer, Stefanie A H de Poot, Razi Quadir, Roel Broekhuizen, Anne F McGettrick, Wayne J Higgins, Bart Devreese, D Margaret Worrall, Niels Bovenschen
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e22645 (2011)
Granzyme-mediated cell death is the major pathway for cytotoxic lymphocytes to kill virus-infected and tumor cells. In humans, five different granzymes (i.e. GrA, GrB, GrH, GrK, and GrM) are known that all induce cell death. Expression of intracellul
Externí odkaz:
https://doaj.org/article/33f3842d8dc145ba90e0a342d9af5d7d
Publikováno v:
Journal of Molecular Biology. 429:3525-3545
Three deubiquitinating enzymes-Rpn11, Usp14, and Uch37-are associated with the proteasome regulatory particle. These enzymes allow proteasomes to remove ubiquitin from substrates before they are translocated into the core particle to be degraded. Alt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::374821d18a1aef70204cebaf504a8786
https://doi.org/10.1016/j.jmb.2017.09.015
https://doi.org/10.1016/j.jmb.2017.09.015
Autor:
Roel Broekhuizen, Stefanie A. H. de Poot, Jan Meeldijk, Elisabeth M. P. Steeghs, Elisabeth A. van Erp, Roel Goldschmeding, Niels Bovenschen, Marjolein C. Olthof
Publikováno v:
Blood. 126:2893-2895
To the editor: With great interest, we read the recent Blood article by Vrazo et al,[1][1] who report on the use of luciferase-based biosensors to detect proteolytic activity of granzymes (Gr’s) A, B, and K. They show that these sensors can be used
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec213717ff6681ccb22b77d8fc68ff35
https://doi.org/10.1182/blood-2015-07-657841
https://doi.org/10.1182/blood-2015-07-657841
Autor:
Jung Hoon Lee, Won Choi, Yun Kyung Kim, Min Jae Lee, Stefanie A. H. de Poot, Dong Hoon Han, Ji Hyeon Kim, Daniel Finley
Publikováno v:
Nature Communications
NATURE COMMUNICATIONS(7)
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
NATURE COMMUNICATIONS(7)
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
When in the closed form, the substrate translocation channel of the proteasome core particle (CP) is blocked by the convergent N termini of α-subunits. To probe the role of channel gating in mammalian proteasomes, we deleted the N-terminal tail of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1419af68b4e6315e8ee5494411fb2f60
https://doi.org/10.1038/ncomms10963
https://doi.org/10.1038/ncomms10963
Autor:
Kylie J. Walters, Bradley B. Stocks, Shuangwu Sun, John R. Engen, Yuan Shi, Byung-Hoon Lee, Sergey G. Tarasov, Jacob Vannoy, Daniel Finley, Fabian Tuebing, Suzanne Elsasser, Yanhong Shi, Xiang Chen, Naixia Zhang, Stefanie A. H. de Poot, Geng Tian
Publikováno v:
Science. 351
The yin and yang of proteasomal regulation The ubiquitin-proteasome pathway regulates myriad proteins through their selective proteolysis. The small protein ubiquitin is attached, typically in many copies, to the target protein, which is then recogni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9b46dc0ac888813284c1971f4c41e8b
https://doi.org/10.1126/science.aad9421
https://doi.org/10.1126/science.aad9421
Publikováno v:
Apoptosis : an international journal on programmed cell death. 18(4)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51ba57d39b2732dc3af95f71ec91919a
https://pubmed.ncbi.nlm.nih.gov/23354943
https://pubmed.ncbi.nlm.nih.gov/23354943
Autor:
Bart Devreese, Razi Quadir, Stefanie A. H. de Poot, D. Margaret Worrall, Anne F. McGettrick, Wayne J. Higgins, Niels Bovenschen, Pieter J.A. de Koning, Roel Broekhuizen, J. Alain Kummer
Publikováno v:
PLoS ONE
PLOS ONE
PLoS ONE, Vol 6, Iss 8, p e22645 (2011)
PLOS ONE
PLoS ONE, Vol 6, Iss 8, p e22645 (2011)
Granzyme-mediated cell death is the major pathway for cytotoxic lymphocytes to kill virus-infected and tumor cells. In humans, five different granzymes (i.e. GrA, GrB, GrH, GrK, and GrM) are known that all induce cell death. Expression of intracellul
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67779b400050f253ee56c119d1f10698
http://europepmc.org/articles/PMC3152296
http://europepmc.org/articles/PMC3152296
Autor:
Roel Broekhuizen, Daniel R. Hostetter, Stefanie A. H. de Poot, Kris Gevaert, Charles S. Craik, Marijn Westgeest, Kimberly Demeyer, Kim Plasman, Niels Bovenschen, Petra Van Damme
Publikováno v:
The Biochemical journal. 437(3)
Cytotoxic lymphocyte protease GrM (granzyme M) is a potent inducer of tumour cell death and a key regulator of inflammation. Although hGrM (human GrM) and mGrM (mouse GrM) display extensive sequence homology, the substrate specificity of mGrM remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4691b7fdf937a25a95077d2e2a410e65
https://pubmed.ncbi.nlm.nih.gov/21564021
https://pubmed.ncbi.nlm.nih.gov/21564021