Zobrazeno 1 - 10
of 54
pro vyhledávání: '"Marja Makarow"'
Autor:
MARJA MAKAROW
Publikováno v:
The Engineer. 300:41-41
Despite Brexit, the coronavirus crisis should make us even more determined to ensure the UK remains at the heart of European science collaborations
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::908908599e5bdbd609c4f8f80426fa67
https://doi.org/10.12968/s0013-7758(22)90465-9
https://doi.org/10.12968/s0013-7758(22)90465-9
Publikováno v:
Yeast. 28:453-465
Proteins exit the endoplasmic reticulum (ER) in vesicles pinching off from the membrane at sites covered by the COPII coat, which consists of Sec23/24p and Sec13/31p. We have shown that the glycoprotein Hsp150 exits the ER in the absence of Sec13p or
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fc62b9f02f4b5ad0ca9f4faa64ea711
https://doi.org/10.1002/yea.1850
https://doi.org/10.1002/yea.1850
Publikováno v:
Biotechnology Progress. 19:1368-1371
Heterologous glycoproteins usually do not fold properly in yeast cells and fail to leave the endoplasmic reticulum. Here we show that the Hsp150Delta polypeptide carrier promoted proper folding and secretion of the catalytic ectodomain of rat alpha2,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27a32149c0eccec4c82b59dc9ba969e2
https://doi.org/10.1021/bp034035p
https://doi.org/10.1021/bp034035p
Publikováno v:
Journal of Biological Sciences. 6:446-456
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::283f456c408082a02bf59402ace08d11
https://doi.org/10.3923/jbs.2006.446.456
https://doi.org/10.3923/jbs.2006.446.456
Autor:
Silvia Brambillasca, Paolo Soffientini, Monica Yabal, Nica Borgese, Ramanujan S. Hegde, Sandra Stefanovic, Marja Makarow
Publikováno v:
The EMBO Journal. 24:2533-2542
A large class of proteins with cytosolic functional domains is anchored to selected intracellular membranes by a single hydrophobic segment close to the C-terminus. Although such tail-anchored (TA) proteins are numerous, diverse, and functionally imp
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c0b8f50f2d59097f51ee6aa06e5e4c6
https://doi.org/10.1038/sj.emboj.7600730
https://doi.org/10.1038/sj.emboj.7600730
Publikováno v:
Traffic. 6:562-574
Glycoproteins exit the endoplasmic reticulum (ER) of the yeast Saccharomyces cerevisiae in coat protein complex II (COPII) coated vesicles. The coat consists of the essential proteins Sec23p, Sec24p, Sec13p, Sec31p, Sar1p and Sec16p. Sec24p and its t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::86b04b908466fbd4841558810c8a54cf
https://doi.org/10.1111/j.1600-0854.2005.00297.x
https://doi.org/10.1111/j.1600-0854.2005.00297.x
Autor:
Taina Suntio, Maria Mecklin, Risto Renkonen, Eeva Sievi, Marja Makarow, Hanna Salo, Pirkko Mattila
Publikováno v:
FEMS Yeast Research. 5:341-350
Interactions between selectins and their oligosaccharide-decorated counter-receptors play an important role in the initiation of leukocyte extravasation in inflammation. L-selectin ligands are O-glycosylated with sulphated sialyl Lewis X epitopes (su
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6651e968823a738a3483ce924dbf6034
https://doi.org/10.1016/j.femsyr.2004.11.007
https://doi.org/10.1016/j.femsyr.2004.11.007
Publikováno v:
Journal of Cell Science. 117:1665-1673
Exit of proteins from the yeast endoplasmic reticulum (ER) is thought to occur in vesicles coated by four proteins, Sec13p, Sec31p, Sec23p and Sec24p, which assemble at ER exit sites to form the COPII coat. Sec13p may serve a structural function, whe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fdbd12834652213e06f332ec8d396789
https://doi.org/10.1242/jcs.01019
https://doi.org/10.1242/jcs.01019
Publikováno v:
Molecular Microbiology. 52:217-225
Thermal insult at 50 degrees C causes protein denaturation in yeast, but the cells survive if preconditioned at 37 degrees C. Survival depends on refolding of heat-denatured proteins. Refolding of cytoplasmic proteins requires Hsp104, the expression
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e36ab1490be2853d6aa8f083daea5d7e
https://doi.org/10.1111/j.1365-2958.2003.03959.x
https://doi.org/10.1111/j.1365-2958.2003.03959.x
Autor:
Marja Makarow, Leena Karhinen
Publikováno v:
Journal of Cell Science. 117:351-358
In yeast primary N- and O-glycans are attached to proteins in the endoplasmic reticulum (ER), and they are elongated in the Golgi. Thus, glycan extension by Golgi enzymes has been taken as evidence for arrival of a protein in the Golgi. Two α1,6-man
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d84744e1af26d1df40d25723f0175f0
https://doi.org/10.1242/jcs.00858
https://doi.org/10.1242/jcs.00858