Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Pawel Leznicki"'
Autor:
John F Darby, Ewelina M Krysztofinska, Peter J Simpson, Aline C Simon, Pawel Leznicki, Newran Sriskandarajah, David S Bishop, Lisa R Hale, Caterina Alfano, Maria R Conte, Santiago Martínez-Lumbreras, Arjun Thapaliya, Stephen High, Rivka L Isaacson
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e113281 (2014)
The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex of BAG6, T
Externí odkaz:
https://doaj.org/article/8e8a952f4dc54536822cf9d134d1aff8
Autor:
Pawel Leznicki, Quentin P Roebuck, Lydia Wunderley, Anne Clancy, Ewelina M Krysztofinska, Rivka L Isaacson, Jim Warwicker, Blanche Schwappach, Stephen High
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e59590 (2013)
The BAG6 protein is a subunit of a heterotrimeric complex that binds a range of membrane and secretory protein precursors localized to the cytosol, enforcing quality control and influencing their subsequent fate.BAG6 has an N-terminal ubiquitin-like
Externí odkaz:
https://doaj.org/article/64d12d24e67b4b8f877d17a4d74feb1f
Publikováno v:
Journal of Cell Science
article-version (VoR) Version of Record
article-version (VoR) Version of Record
Membrane proteins destined for lipid droplets (LDs), a major intracellular storage site for neutral lipids, are inserted into the endoplasmic reticulum (ER) and then trafficked to LDs where they reside in a hairpin loop conformation. Here, we show th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51a789561961420767c5b6c624165ea0
https://pubmed.ncbi.nlm.nih.gov/34558621
https://pubmed.ncbi.nlm.nih.gov/34558621
Autor:
Pawel Leznicki, Stephen High
Publikováno v:
EMBO Reports
Leznicki, P & High, S 2020, ' SGTA associates with nascent membrane protein precursors ', EMBO reports, vol. 21, no. 5 . https://doi.org/10.15252/embr.201948835
Leznicki, P & High, S 2020, ' SGTA associates with nascent membrane protein precursors ', EMBO reports, vol. 21, no. 5 . https://doi.org/10.15252/embr.201948835
The endoplasmic reticulum (ER) is a major site for membrane protein synthesis in eukaryotes. The majority of integral membrane proteins are delivered to the ER membrane via the co‐translational, signal recognition particle (SRP)‐dependent route.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31ff790aab9d274548042ec815140ae9
http://europepmc.org/articles/PMC7202230
http://europepmc.org/articles/PMC7202230
Publikováno v:
Bioscience Reports
Antibodies to the Vel blood group antigen can cause adverse hemolytic reactions unless Vel-negative blood units are transfused. Since the genetic background of Vel-negativity was discovered in 2013, DNA-based typing of the 17-bp deletion causing the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::d3a8dcac8fd8436f73d0f2cae635e08f
https://pubmed.ncbi.nlm.nih.gov/32301496
https://pubmed.ncbi.nlm.nih.gov/32301496
Autor:
Andreas Zoephel, Syed Arif Abdul Rehman, Deepika Pathak, Pawel Leznicki, Nuno L. Barbosa-Morais, Marie C. Bordone, Jayaprakash Natarajan, Simone Weidlich, Gerd Bader, Guido Boehmelt, Andreas Schlattl, Yogesh Kulathu, Walter Spevak
Publikováno v:
Journal of Cell Science.
Protein ubiquitylation is a dynamic post-translational modification that can be reversed by deubiquitylating enzymes (DUBs). It is unclear how the small number (∼100) of DUBs present in mammalian cells regulate the thousands of different ubiquityla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12c84c574a5d2f639433cf14d53e0df2
https://doi.org/10.1242/jcs.212753
https://doi.org/10.1242/jcs.212753
Autor:
Pawel Leznicki, Yogesh Kulathu
Publikováno v:
Journal of Cell Science
Deubiquitylating (or deubiquitinating) enzymes (DUBs) are proteases that reverse protein ubiquitylation and therefore modulate the outcome of this post-translational modification. DUBs regulate a variety of intracellular processes, including protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ad5762db5370d7de805b213691276a0
Publikováno v:
Journal of Cell Science
Summary Whilst the co-translational translocation of nascent proteins across the mammalian endoplasmic reticulum (ER) is well defined, the capacity of this organelle for post-translational translocation is poorly delineated. Here we identify two huma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4aaa625c232552b13337d37601242343
https://doi.org/10.1242/jcs.102608
https://doi.org/10.1242/jcs.102608
Publikováno v:
Biochemical Journal
TA (tail-anchored) proteins utilize distinct biosynthetic pathways, including TRC40 (transmembrane domain recognition complex of 40 kDa)-mediated, chaperone-dependent and/or unassisted routes to the ER (endoplasmic reticulum) membrane. We have addres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2a13e120819d923dedb252b79e680fb6
http://europepmc.org/articles/PMC3198503
http://europepmc.org/articles/PMC3198503
Publikováno v:
Journal of Cell Science. 123:2170-2178
The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during deliv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d417a4a2a3281f39ce92459773d082ab
https://doi.org/10.1242/jcs.066738
https://doi.org/10.1242/jcs.066738