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pro vyhledávání: '"N. Erwin Ivessa"'
Autor:
Marioara Chiritoiu, Gabriela N. Chiritoiu, Cristian V. A. Munteanu, Florin Pastrama, N. Erwin Ivessa, Stefana M. Petrescu
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 10, p 3468 (2020)
Endoplasmic reticulum (ER)-associated degradation (ERAD) is the main mechanism of targeting ER proteins for degradation to maintain homeostasis, and perturbations of ERAD lead to pathological conditions. ER-degradation enhancing α-mannosidase-like (
Externí odkaz:
https://doaj.org/article/03d05dfb8a4c4e2d9f6e19e1f4c46de9
Autor:
Gabriela Chiritoiu, N. Erwin Ivessa, Cristian V.A. Munteanu, Marioara Chiritoiu, Stefana M. Petrescu, Florin Pastrama
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 10
International Journal of Molecular Sciences, Vol 21, Iss 3468, p 3468 (2020)
Volume 21
Issue 10
International Journal of Molecular Sciences, Vol 21, Iss 3468, p 3468 (2020)
Endoplasmic reticulum (ER)-associated degradation (ERAD) is the main mechanism of targeting ER proteins for degradation to maintain homeostasis, and perturbations of ERAD lead to pathological conditions. ER-degradation enhancing &alpha
mannosida
mannosida
Autor:
Marcela Hermann, Bernadette Kienzle, Edward F. Rehberg, Robert Hermann, Wolfgang J. Schneider, Fridolin Seif, David A. Gordon, N. Erwin Ivessa
Publikováno v:
Gene. 523:1-9
During an egg-laying cycle, oviparous animals transfer massive amounts of triglycerides, the major lipid component of very low density lipoprotein (VLDL), from the liver to the developing oocytes. A major stimulus for this process is the rise in estr
Autor:
Clara C. Manns, Marcela Hermann, Wolfgang J. Schneider, N. Erwin Ivessa, Julia A. Plieschnig, Miriam Kamper
Publikováno v:
Biochimie. 112
Although the early human embryo is capable of covering its cholesterol demand by endogenous synthesis, during later stages of development the fetus may become dependent on transplacental cholesterol transport. On one hand, this conclusion is based on
Endoplasmic-reticulum-associated protein degradation inside and outside of the endoplasmic reticulum
Publikováno v:
Scopus-Elsevier
Newly synthesized polypeptides that enter the endomembrane system encounter a folding environment in the lumen of the endoplasmic reticulum (ER) constituted by enzymes, lectinlike proteins, and molecular chaperones. The folding process is under scrut
Publikováno v:
Journal of Biological Chemistry. 272:20828-20834
In cells exposed to brefeldin A (BFA), enzymes of the Golgi apparatus are redistributed to the endoplasmic reticulum (ER) by retrograde membrane flow, where they may cause modifications on resident ER proteins. We have used a truncated form of the ro
Publikováno v:
XXIst International Carbohydrate Symposium 2002.
Publikováno v:
The Journal of biological chemistry. 273(16)
In the endoplasmic reticulum (ER), an efficient "quality control system" operates to ensure that mutated and incorrectly folded proteins are selectively degraded. We are studying ER-associated degradation using a truncated variant of the rough ER-spe
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Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. (1):25-33
The synthesis and secretion of apolipoprotein A-I (apoA-I) in response to the treatment with estrogen were investigated in the chicken hepatoma cell line, LMH-2A. Exposure of these cells to exogenous estrogen for up to 48 h results in a decrease of a