Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Effrosyni Papanikou"'
Publikováno v:
eLife, Vol 4 (2015)
COPI coated vesicles carry material between Golgi compartments, but the role of COPI in the secretory pathway has been ambiguous. Previous studies of thermosensitive yeast COPI mutants yielded the surprising conclusion that COPI was dispensable both
Externí odkaz:
https://doaj.org/article/611501710d4b45a394e92c332b2740a1
Publikováno v:
The Journal of Cell Biology
The Golgi cisternal maturation model predicts that secretory cargo proteins should be continuously present within the cisternae while resident Golgi proteins come and go. Casler et al. verify this prediction by tracking the passage of a fluorescent s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa9aca058ff46534f9fadd6225cc8072
http://europepmc.org/articles/PMC6504904
http://europepmc.org/articles/PMC6504904
Publikováno v:
The Golgi Complex ISBN: 9781493964611
Yeast cells are well suited to visualizing organelles by 4D confocal microscopy. Typically, one or more cellular compartments are labeled with a fluorescent protein or dye, and a stack of confocal sections spanning the entire cell volume is captured
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de89c31e980eb2d54c89c700df514fdc
https://pubmed.ncbi.nlm.nih.gov/27631997
https://pubmed.ncbi.nlm.nih.gov/27631997
Publikováno v:
Cellular Logistics
FK506-binding protein (FKBP) is a monomer that binds to FK506, rapamycin, and related ligands. The F36M substitution, in which Phe36 in the ligand-binding pocket is changed to Met, leads to formation of antiparallel FKBP dimers, which can be dissocia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c30f738eed95783d1326f998fcbd4b29
http://europepmc.org/articles/PMC5058350
http://europepmc.org/articles/PMC5058350
Publikováno v:
eLife, Vol 4 (2015)
eLife
eLife
COPI coated vesicles carry material between Golgi compartments, but the role of COPI in the secretory pathway has been ambiguous. Previous studies of thermosensitive yeast COPI mutants yielded the surprising conclusion that COPI was dispensable both
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11cd03ead2643d7a663fa0015ee09191
https://doi.org/10.7554/elife.13232
https://doi.org/10.7554/elife.13232
Publikováno v:
Molecular and Cellular Biology. 28:3336-3343
In the budding yeast Saccharomyces cerevisiae, mutations in the essential gene CDC1 cause defects in Golgi inheritance and actin polarization. However, the biochemical function of Cdc1p is unknown. Previous work showed that cdc1 mutants accumulate in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::613110ff0ed1c952fc555f4f208d137f
https://doi.org/10.1128/mcb.00567-07
https://doi.org/10.1128/mcb.00567-07
Autor:
Effrosyni Papanikou, Dibyendu Bhattacharyya, Ketakee Pawar, Olivia W. Rossanese, Bhawik Kumar Jain, Prasanna Iyer, Jotham R. Austin, Koushal Pandya, Madhura Bhave, Chandrakala Sharma, Abira Ganguly, Kasey J. Day, Benjamin S. Glick
Publikováno v:
Journal of Cell Science.
Regulation of the size and abundance of membrane compartments is a fundamental cellular activity. In Saccharomyces cerevisiae, disruption of the ADP-ribosylation factor 1 (ARF1) gene yields larger and fewer Golgi cisternae by partially depleting the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::513c40c6a7c71b2da6e447ba4b4d3a4e
https://doi.org/10.1242/jcs.140996
https://doi.org/10.1242/jcs.140996
Publikováno v:
Nature reviews. Microbiology. 5(11)
All cells must traffic proteins across their membranes. This essential process is responsible for the biogenesis of membranes and cell walls, motility and nutrient scavenging and uptake, and is also involved in pathogenesis and symbiosis. The translo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01d05bc69d8d0ab79a0f2357acae20c8
https://pubmed.ncbi.nlm.nih.gov/17938627
https://pubmed.ncbi.nlm.nih.gov/17938627
Autor:
Benjamin S. Glick, Effrosyni Papanikou
Publikováno v:
FEBS Letters. (23):3746-3751
The Golgi apparatus is known to modify and sort newly synthesized secretory proteins. However, fundamental mysteries remain about the structure, operation, and dynamics of this organelle. Important insights have emerged from studying the Golgi in yea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02c35fff0b752e4a3572fcc0894558b0