Zobrazeno 1 - 10
of 184
pro vyhledávání: '"BiP/GRP78"'
Autor:
Alena Welters, Oliver Nortmann, Laura Wörmeyer, Clemens Freiberg, Daniel Eberhard, Nadine Bachmann, Carsten Bergmann, Ertan Mayatepek, Thomas Meissner, Sebastian Kummer
Publikováno v:
International Journal of Molecular Sciences, Vol 25, Iss 2, p 1270 (2024)
The BiP co-chaperone DNAJC3 protects cells during ER stress. In mice, the deficiency of DNAJC3 leads to beta-cell apoptosis and the gradual onset of hyperglycemia. In humans, biallelic DNAJC3 variants cause a multisystem disease, including early-onse
Externí odkaz:
https://doaj.org/article/002ad8332aca42f882b49a9d746753ad
Akademický článek
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Autor:
Tsu-Jen Kuo, Yen-Hsuan Jean, Po-Chang Shih, Shu-Yu Cheng, Hsiao-Mei Kuo, Yi-Ting Lee, Yu-Cheng Lai, Chung-Chih Tseng, Wu-Fu Chen, Zhi-Hong Wen
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 15, p 8813 (2022)
Oral squamous cell carcinoma (OSCC) affects tens of thousands of people worldwide. Despite advances in cancer treatment, the 5-year survival rate of patients with late-stage OSCC is low at 50–60%. Therefore, the development of anti-OSCC therapy is
Externí odkaz:
https://doaj.org/article/b2608e51d1a24215b0619019a2e9c950
Publikováno v:
eLife, Vol 8 (2019)
Coupling of endoplasmic reticulum (ER) stress to dimerisation-dependent activation of the UPR transducer IRE1 is incompletely understood. Whilst the luminal co-chaperone ERdj4 promotes a complex between the Hsp70 BiP and IRE1’s stress-sensing lumin
Externí odkaz:
https://doaj.org/article/6243d75368fa4ac6bb92dcb63e2aed61
Publikováno v:
Data in Brief, Vol 10, Iss C, Pp 525-530 (2017)
Human BiP/GRP78 is involved in the folding and assembly of proteins in the endoplasmic reticulum. The proteins for crystallization in good amount and quality are prerequisites for obtaining ideal crystals. To meet these requirements, different BiP/GR
Externí odkaz:
https://doaj.org/article/953ac01a99a94096a9f8d5417c8b7e00
Autor:
Milena Vitale, Anush Bakunts, Andrea Orsi, Federica Lari, Laura Tadè, Alberto Danieli, Claudia Rato, Caterina Valetti, Roberto Sitia, Andrea Raimondi, John C Christianson, Eelco van Anken
Publikováno v:
eLife, Vol 8 (2019)
How endoplasmic reticulum (ER) stress leads to cytotoxicity is ill-defined. Previously we showed that HeLa cells readjust homeostasis upon proteostatically driven ER stress, triggered by inducible bulk expression of secretory immunoglobulin M heavy c
Externí odkaz:
https://doaj.org/article/1fadbf5d07454278a95cd18f5e2395cb
Publikováno v:
Toxins. 14(2)
The subtilase cytotoxin (SubAB) belongs to the family of AB5 toxins and is produced together with Shiga toxin (Stx) by certain Stx-producing E. coli strains (STEC). For most AB-type toxins, it is assumed that cytotoxic effects can only be induced by
Akademický článek
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Autor:
Steffen Preissler, Cláudia Rato, Ruming Chen, Robin Antrobus, Shujing Ding, Ian M Fearnley, David Ron
Publikováno v:
eLife, Vol 4 (2015)
The endoplasmic reticulum (ER)-localized Hsp70 chaperone BiP affects protein folding homeostasis and the response to ER stress. Reversible inactivating covalent modification of BiP is believed to contribute to the balance between chaperones and unfol
Externí odkaz:
https://doaj.org/article/6ab11f0653ec45bd9fb9b9d3b257f33e
Autor:
Steffen Preissler, Joseph E Chambers, Ana Crespillo-Casado, Edward Avezov, Elena Miranda, Juan Perez, Linda M Hendershot, Heather P Harding, David Ron
Publikováno v:
eLife, Vol 4 (2015)
DnaK/Hsp70 chaperones form oligomers of poorly understood structure and functional significance. Site-specific proteolysis and crosslinking were used to probe the architecture of oligomers formed by the endoplasmic reticulum (ER) Hsp70, BiP. These we
Externí odkaz:
https://doaj.org/article/645adf268a244bb8b406109511db4a8a