Zobrazeno 1 - 10
of 380
pro vyhledávání: '"endo H, endoglycosidase H"'
Publikováno v:
The Journal of Biological Chemistry
The yeast endoplasmic reticulum has three distinct protein translocation channels. The heterotrimeric Sec61 and Ssh1 complexes, which bind translating ribosomes, mediate cotranslational translocation of proteins targeted to the endoplasmic reticulum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::810aa777fb72075206ecf2186fe3f8c6
http://europepmc.org/articles/PMC8503631
http://europepmc.org/articles/PMC8503631
Autor:
Rebeca Kawahara, Fabian Soltermann, Hannes Hinneburg, Siyun Chen, Robert J. Woods, Regis Dieckmann, Morten Thaysen-Andersen, Ian Loke, Vignesh Venkatakrishnan, Weston B. Struwe, Oliver C. Grant, Alison Rodger, Julian Ugonotti, Harry C. Tjondro, Johan Bylund, Benjamin L. Parker, Anna Karlsson-Bengtsson, Sayantani Chatterjee
Publikováno v:
The Journal of Biological Chemistry
Myeloperoxidase (MPO) plays essential roles in neutrophil-mediated immunity via the generation of reactive oxidation products. Complex carbohydrates decorate MPO at discrete sites, but their functional relevance remains elusive. To this end, we have
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1fb89deed8bac3a14bb7b67d39adbec0
https://pubmed.ncbi.nlm.nih.gov/33273015
https://pubmed.ncbi.nlm.nih.gov/33273015
Autor:
Po Hao Hsu, Chih Yung Tang, Guey-Mei Jow, Yi Chih Chiu, Yi Fan Liao, Chung Jiuan Jeng, Jing Jia Huang, Ya Ching Fang, Ssu Ju Fu, Pei Tzu Chang
Publikováno v:
The Journal of Biological Chemistry
Mutations in the human gene encoding the neuron-specific Eag1 voltage-gated K+ channel are associated with neurodevelopmental diseases, indicating an important role of Eag1 during brain development. A disease-causing Eag1 mutation is linked to decrea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce43fc1dba9d6f71cdd19f2fa8947a3f
https://doi.org/10.1016/j.jbc.2021.100484
https://doi.org/10.1016/j.jbc.2021.100484
Autor:
Suresh Venkateswaran, Nicholas Siano, Jill M. Weimer, Nickita Mehta, Renee Krampetz, Nithya Selvan, Hung V. Do, Jon Brudvig, Yuliya McAnany, Finn Hung, Anuj Mehta, Matthew Graziano, Matthew Madrid, Russell Gotschall, M. Osman Sheikh, Nastry Brignol
Publikováno v:
The Journal of Biological Chemistry
Acid alpha-glucosidase (GAA) is a lysosomal glycogen-catabolizing enzyme, the deficiency of which leads to Pompe disease. Pompe disease can be treated with systemic recombinant human GAA (rhGAA) enzyme replacement therapy (ERT), but the current stand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::429632d0e97ca7f629eca76ebefcadf1
https://doi.org/10.1016/j.jbc.2021.100769
https://doi.org/10.1016/j.jbc.2021.100769
Autor:
Miyako Nakano, Eiji Miyoshi, Masato Kitano, Kazuki Nakajima, Yoichiro Harada, Saki Itoyama, Yasuhiko Kizuka, Tomoaki Sobajima, Akihiro Harada, Ryo Misaki, Naoyuki Taniguchi
Publikováno v:
The Journal of Biological Chemistry
Glycosylation, the most common posttranslational modification of proteins, is a stepwise process that relies on tight regulation of subcellular glycosyltransferase location to control the addition of each monosaccharide. Glycosyltransferases primaril
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7090ddd326a3716152f1d830ce1d43a5
https://doi.org/10.1016/j.jbc.2021.100354
https://doi.org/10.1016/j.jbc.2021.100354
Autor:
Luca Jovine, Elisa Dioguardi, Isha Raj, Marcel Bokhove, Katharina Gegenschatz-Schmid, K. Nishimura, Hamed Sadat Al Hosseini, Takako Saito, Daniele de Sanctis, Ling Han
Publikováno v:
Journal of Structural Biology
We present a strategy to obtain milligrams of highly post-translationally modified eukaryotic proteins, transiently expressed in mammalian cells as rigid or cleavable fusions with a mammalianized version of bacterial maltose-binding protein (mMBP). T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a4c8bcbb1b36465f3ae53db997e15f1
https://doi.org/10.1016/j.jsb.2016.01.016
https://doi.org/10.1016/j.jsb.2016.01.016
Autor:
Hüttner, Silvia, Veit, Christiane, Vavra, Ulrike, Schoberer, Jennifer, Dicker, Martina, Maresch, Daniel, Altmann, Friedrich, Strasser, Richard
Publikováno v:
Biochemical Journal
N-glycosylation of proteins plays an important role in the determination of the fate of newly synthesized glycoproteins in the endoplasmic reticulum (ER). Specific oligosaccharide structures recruit molecular chaperones that promote folding or mannos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9dd38cd0497bff9ab4a6e40fcbe4d833
http://europepmc.org/articles/PMC4255730
http://europepmc.org/articles/PMC4255730
Publikováno v:
FEBS Open Bio, Vol 4, Iss C, Pp 229-239 (2014)
FEBS Open Bio
FEBS Open Bio
Graphical abstract
Highlights • Ursolic acid inhibits cell-surface expression of ICAM-1. • Ursolic acid induces accumulation of high-mannose-type ICAM-1 in ER. • Ursolic acid induces morphological changes of Golgi apparatus. • Ursolic ac
Highlights • Ursolic acid inhibits cell-surface expression of ICAM-1. • Ursolic acid induces accumulation of high-mannose-type ICAM-1 in ER. • Ursolic acid induces morphological changes of Golgi apparatus. • Ursolic ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::354b094db571c8e4429ea425fce4d6d4
http://www.sciencedirect.com/science/article/pii/S2211546314000205
http://www.sciencedirect.com/science/article/pii/S2211546314000205
Publikováno v:
Biochemical Journal
N-linked glycosylation is a critical determinant of protein structure and function, regulating processes such as protein folding, stability and localization, ligand–receptor binding and intracellular signalling. TβRII [type II TGF-β (transforming
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9eefad18816770a2287ef96b70c9280
https://doi.org/10.1042/bj20111923
https://doi.org/10.1042/bj20111923
Doppel and PrPC co-immunoprecipitate in detergent-resistant membrane domains of epithelial FRT cells
Autor:
Chiara Zurzolo, Maddalena Costanzo, Alessandro Negro, Vincenza Campana, Daniela Sarnataro, M. Catia Sorgato, Anna Caputo
Publikováno v:
Biochemical Journal
Biochemical Journal, 2010, 425 (2), pp.341-51. ⟨10.1042/BJ20091050⟩
Biochemical Journal, Portland Press, 2010, 425 (2), pp.341-51. ⟨10.1042/BJ20091050⟩
Biochemical Journal, 2010, 425 (2), pp.341-51. ⟨10.1042/BJ20091050⟩
Biochemical Journal, Portland Press, 2010, 425 (2), pp.341-51. ⟨10.1042/BJ20091050⟩
International audience; Dpl (doppel) is a paralogue of the PrPC (cellular prion protein), whose misfolded conformer (the scrapie prion protein, PrPSc) is responsible for the onset of TSEs (transmissible spongiform encephalopathies) or prion diseases.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b535cf11e1441f046e7235fd030d365
https://doi.org/10.1042/bj20091050
https://doi.org/10.1042/bj20091050