Pawel Leznicki
Overview
Explore the profile of Pawel Leznicki including associated specialties, affiliations and a list of published articles.
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17
Citations
467
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Recent Articles
1.
Leznicki P, Schneider H, Harvey J, Shi W, High S
J Cell Sci
. 2021 Sep;
135(5).
PMID: 34558621
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...
2.
Nylander A, Leznicki P, Vidovic K, High S, Olsson M
Biosci Rep
. 2020 Apr;
40(5).
PMID: 32301496
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...
3.
Leznicki P, High S
EMBO Rep
. 2020 Mar;
21(5):e48835.
PMID: 32216016
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...
4.
Leznicki P, Natarajan J, Bader G, Spevak W, Schlattl A, Abdul Rehman S, et al.
J Cell Sci
. 2018 Apr;
131(10).
PMID: 29685892
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...
5.
Leznicki P, Kulathu Y
J Cell Sci
. 2017 May;
130(12):1997-2006.
PMID: 28476940
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 turnover,...
6.
Leznicki P, Korac-Prlic J, Kliza K, Husnjak K, Nyathi Y, Dikic I, et al.
J Cell Sci
. 2015 Jul;
128(17):3187-96.
PMID: 26169395
Rpn13 is an intrinsic ubiquitin receptor of the 26S proteasome regulatory subunit that facilitates substrate capture prior to degradation. Here we show that the C-terminal region of Rpn13 binds to...
7.
Darby J, Krysztofinska E, Simpson P, Simon A, Leznicki P, Sriskandarajah N, et al.
PLoS One
. 2014 Nov;
9(11):e113281.
PMID: 25415308
Background: 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...
8.
Wunderley L, Leznicki P, Payapilly A, High S
J Cell Sci
. 2014 Sep;
127(Pt 21):4728-39.
PMID: 25179605
Hydrophobic amino acids are normally shielded from the cytosol and their exposure is often used as an indicator of protein misfolding to enable the chaperone-mediated recognition and quality control of...
9.
Leznicki P, Roebuck Q, Wunderley L, Clancy A, Krysztofinska E, Isaacson R, et al.
PLoS One
. 2013 Mar;
8(3):e59590.
PMID: 23533635
Background: 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...
10.
Leznicki P, High S
Proc Natl Acad Sci U S A
. 2012 Nov;
109(47):19214-9.
PMID: 23129660
The BAG6 complex was first identified as an upstream loading factor for tail-anchored membrane proteins entering the TRC40-dependent pathway for posttranslational delivery to the endoplasmic reticulum. Subsequently, BAG6 was shown...