Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Eva A. Pasyk"'
Autor:
Laura Sheu, Xiaodong Gao, Junzhi Ji, Herbert Y. Gaisano, Frederique Varoqueaux, Nils Brose, Xiaohang Huang, Eva A. Pasyk
Publikováno v:
Journal of Biological Chemistry. 278:27556-27563
The slower kinetics of insulin release from pancreatic islet beta cells, as compared with other regulated secretory processes such as chromaffin granule secretion, can in part be explained by the small number of the insulin granules that are docked t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98e3f95e121e8a3028f32f365025a469
https://doi.org/10.1074/jbc.m303203200
https://doi.org/10.1074/jbc.m303203200
Autor:
Andrea Jurisicova, David Chitayat, Robert F. Casper, J. Kevin Foskett, Monica Antenos, Eva A. Pasyk, Avraham Ben-Chetrit
Publikováno v:
Scopus-Elsevier
Formation of the blastocyst is one of the first morphological changes in early embryonic development. Ion transport has been shown to be crucial for blastocoele cavity formation and expansion, although the mechanisms that underlie this process are pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f2dd4151ef3e9aded62e1739376ae58
https://doi.org/10.1093/molehr/8.8.758
https://doi.org/10.1093/molehr/8.8.758
Autor:
J. Kevin Foskett, Eva A. Pasyk
Publikováno v:
Journal of Biological Chemistry. 270:12347-12350
Cystic fibrosis is caused by mutations in the gene encoding the cystic fibrosis transmembrane conductance regulator (CFTR), a plasma membrane-localized chloride channel. Some mutations in CFTR, including one which affects most patients (delta F508-CF
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da0b5dc823323e0f5a076d4d3ad6a4e1
https://doi.org/10.1074/jbc.270.21.12347
https://doi.org/10.1074/jbc.270.21.12347
Autor:
Ling Jun Huan, Xenia K. Morin, Yanchun Wang, Peter R. Zeman, Christine E. Bear, Eva A. Pasyk, Elizabeth Garami, Kevin Galley
Publikováno v:
The Journal of biological chemistry. 273(48)
The R domain of cystic fibrosis transmembrane conductance regulator (CFTR) connects the two halves of the protein, each of which possess a transmembrane-spanning domain and a nucleotide binding domain. Phosphorylation of serine residues, which reside
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bfb39c8264cf9cbbd58c2c39fde1c3c1
https://pubmed.ncbi.nlm.nih.gov/9822639
https://pubmed.ncbi.nlm.nih.gov/9822639
Autor:
Eva A. Pasyk, J. Kevin Foskett
Publikováno v:
The Journal of biological chemistry. 272(12)
Cystic fibrosis (CF) is characterized by abnormal regulation of epithelial ion and fluid transport due to mutations in the CF transmembrane conductance regulator (CFTR), an apical membrane-localized Cl− channel, that usually prevent it from exiting
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f32545f825837c973b551ab9eb1f1523
https://pubmed.ncbi.nlm.nih.gov/9065435
https://pubmed.ncbi.nlm.nih.gov/9065435