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Michael L van de Weijer

Explore the profile of Michael L van de Weijer including associated specialties, affiliations and a list of published articles. Areas
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Articles 11
Citations 293
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Recent Articles
1.
Sergejevs N, Avci D, van de Weijer M, Corey R, Lemberg M, Carvalho P
J Cell Sci . 2024 Nov; 137(23). PMID: 39513424
Cleavage of transmembrane segments on target proteins by the aspartyl intramembrane protease signal peptide peptidase (SPP, encoded by HM13) has been linked to immunity, viral infection and protein quality control....
2.
van de Weijer M, Samanta K, Sergejevs N, Jiang L, Duenas M, Heunis T, et al.
Nat Commun . 2024 Oct; 15(1):8508. PMID: 39353943
Immune surveillance by cytotoxic T cells eliminates tumor cells and cells infected by intracellular pathogens. This process relies on the presentation of antigenic peptides by Major Histocompatibility Complex class I...
3.
Cremer T, Hoelen H, van de Weijer M, Janssen G, Costa A, Van Veelen P, et al.
PLoS One . 2024 May; 19(5):e0287877. PMID: 38787820
Type 1 diabetes (T1D) is characterized by HLA class I-mediated presentation of autoantigens on the surface of pancreatic β-cells. Recognition of these autoantigens by CD8+ T cells results in the...
4.
Krshnan L, van de Weijer M, Carvalho P
Cold Spring Harb Perspect Biol . 2022 Aug; 14(12). PMID: 35940909
Misfolded, potentially toxic proteins in the lumen and membrane of the endoplasmic reticulum (ER) are eliminated by proteasomes in the cytosol through ER-associated degradation (ERAD). The ERAD process involves the...
5.
van de Weijer M, Krshnan L, Liberatori S, Guerrero E, Robson-Tull J, Hahn L, et al.
Mol Cell . 2020 Oct; 80(2):374-375. PMID: 33065021
No abstract available.
6.
van de Weijer M, Krshnan L, Liberatori S, Guerrero E, Robson-Tull J, Hahn L, et al.
Mol Cell . 2020 Aug; 79(5):768-781.e7. PMID: 32738194
Misfolded proteins in the endoplasmic reticulum (ER) are degraded by ER-associated degradation (ERAD). Although ERAD components involved in degradation of luminal substrates are well characterized, much less is known about...
7.
van de Weijer M, Schuren A, Van den Boomen D, Mulder A, Claas F, Lehner P, et al.
J Cell Sci . 2017 Jul; 130(17):2883-2892. PMID: 28743740
Misfolded endoplasmic reticulum (ER) proteins are dislocated towards the cytosol and degraded by the ubiquitin-proteasome system in a process called ER-associated protein degradation (ERAD). During infection with human cytomegalovirus (HCMV),...
8.
van de Weijer M, van Muijlwijk G, Visser L, Costa A, Wiertz E, Lebbink R
Viruses . 2016 Nov; 8(11). PMID: 27854284
Misfolded proteins from the endoplasmic reticulum (ER) are transported back into the cytosol for degradation via the ubiquitin-proteasome system. The human cytomegalovirus protein US11 hijacks this ER-associated protein degradation (ERAD)...
9.
van de Weijer M, Luteijn R, Wiertz E
Semin Immunol . 2015 Apr; 27(2):125-37. PMID: 25887630
The MHC class I antigen presentation pathway enables cells infected with intracellular pathogens to signal the presence of the invader to the immune system. Cytotoxic T lymphocytes are able to...
10.
van de Weijer M, Bassik M, Luteijn R, Voorburg C, Lohuis M, Kremmer E, et al.
Nat Commun . 2014 May; 5:3832. PMID: 24807418
Misfolded ER proteins are retrotranslocated into the cytosol for degradation via the ubiquitin-proteasome system. The human cytomegalovirus protein US11 exploits this ER-associated protein degradation (ERAD) pathway to downregulate HLA class...