Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Ebrahim C. Elguindi"'
Autor:
Mathieu Chevalier, LaShaunda King, Mary-Jane Gething, Ebrahim C. Elguindi, Chengyi Wang, Sylvie Y. Blond
Publikováno v:
Journal of Biological Chemistry. 273:26827-26835
To investigate the role of each domain in BiP/GRP78 function, we have used a full-length recombinant BiP engineered to contain two enterokinase sites; one site is located after an N-terminal FLAG epitope, and a second site has been inserted at the ju
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2ccd731b2e63201cad72428ba9c2398
https://doi.org/10.1074/jbc.273.41.26827
https://doi.org/10.1074/jbc.273.41.26827
Autor:
LaShaunda King-Simmons, Ebrahim C. Elguindi, Barbara Kroczynska, Sylvie Y. Blond, María A. Alava, Leonor Alloza
Publikováno v:
Biochemical and biophysical research communications. 338(3)
MTJ1/ERdj1 and its human homologue HTJ1 are membrane proteins that interact with the molecular chaperone BiP through their J-domain. HTJ1 also contains a C-terminal cytosolic region of unknown function that consists of two SANT domains separated by a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40713e25d0b9d96baf7e1bcec6d1b429
https://pubmed.ncbi.nlm.nih.gov/16271702
https://pubmed.ncbi.nlm.nih.gov/16271702
Autor:
Ebrahim C. Elguindi, Christina M. Evangelista, Shalaka Samant, Sylvie Y. Blond, Barbara Kroczynska
Publikováno v:
The Journal of biological chemistry. 279(12)
The murine tumor cell DnaJ-like protein 1 or MTJ1/ERdj1 is a membrane J-domain protein enriched in microsomal and nuclear fractions. We previously showed that its lumenal J-domain stimulates the ATPase activity of the molecular chaperone BiP/GRP78 (C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b544d983839785c1328c016688c1ca66
https://pubmed.ncbi.nlm.nih.gov/14668352
https://pubmed.ncbi.nlm.nih.gov/14668352
Autor:
Ebrahim C. Elguindi, Sylvie Y. Blond, Aileen Carey, Mathieu Chevalier, LaShaunda King, Michael Berg
Publikováno v:
Protein expression and purification. 22(1)
Mammalian BiP/GRP78 and Escherichia coli DnaK belong to the highly conserved hsp70 family and function as molecular chaperones in the endoplasmic reticulum or the cytosol, respectively. Induction of murine BiP/GRP78 expression in E. coli leads to gro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e63f7f024179427d3852c8bda8cf9178
https://pubmed.ncbi.nlm.nih.gov/11388813
https://pubmed.ncbi.nlm.nih.gov/11388813
The activity of Hsp70 proteins is regulated by accessory proteins, among which the most studied are the members of the DnaJ-like protein family. BiP/GRP78 chaperones the translocation and maturation of secreted and membrane proteins in the endoplasmi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a235cadf6e1ed34278021e0a6f75eacc
https://europepmc.org/articles/PMC1534116/
https://europepmc.org/articles/PMC1534116/
