Zobrazeno 1 - 10
of 88
pro vyhledávání: '"MARY-JANE GETHING"'
Autor:
Mary-Jane Gething
The precise shape of a protein is a crucial factor in its function. How do proteins become folded into the right conformation? Molecular chaperones and protein folding catalysts bind to developing polypeptides in the cytoplasm and ensure correct fold
Publikováno v:
Journal of Molecular Biology. 367:770-787
The endoplasmic reticulum HSP70 chaperone BiP/Kar2p is both the sensor for the unfolded protein response (UPR) in the yeast Saccharomyces cerevisiae and a target of transcriptional up-regulation by this signaling pathway. In this study, the molecular
Publikováno v:
Journal of Biological Chemistry. 274:29850-29857
BiP, a resident endoplasmic reticulum member of the HSP70 family of molecular chaperones, associates transiently with a wide variety of newly synthesized exocytotic proteins. In addition to immunoglobulin heavy and light chains, the first natural sub
Publikováno v:
Biochemical Journal. 341:193-201
The lysosomal hydrolase N-acetylgalactosamine-4-sulphatase (4-sulphatase) is essential for the sequential degradation of the glycosaminoglycans, dermatan and chondroitin sulphate and, when deficient, causes the lysosomal storage disorder mucopolysacc
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
Autor:
Miguel S. Barbosa, Ted R. Hupp, David P. Lane, Joseph Sambrook, Fourie Anne M, Bi-Ching Sang, Mary-Jane Gething
Publikováno v:
Journal of Biological Chemistry. 272:19471-19479
Mutations within conserved regions of the tumor suppressor protein, p53, result in oncogenic forms of the protein with altered tertiary structures. In most cases, the mutant p53 proteins are selectively recognized and bound by members of the HSP70 fa
Autor:
Mary-Jane Gething
Publikováno v:
Current Biology. 6:1573-1576
The three-dimensional structure of the substrate-binding domain of DnaK, a bacterial Hsp70, shows how such molecular chaperones can be so promiscuous in recognizing different proteins, yet so accurate in discriminating between unfolded and folded for
Publikováno v:
Journal of Biological Chemistry. 270:27589-27594
During the process of folding and assembly of antibody molecules in the endoplasmic reticulum, immunoglobulin heavy and light chains associate transiently with BiP, a resident endoplasmic reticulum protein that is a member of the Hsp70 family of mole
Autor:
Sarah A. Comerford, Joseph Sambrook, Jerry Y. Niederkorn, Ding Ma, Michael B. Berman, Deborah Bellingham, Mary Jane Gething, Hassan Alizadeh
Publikováno v:
Current Eye Research. 14:449-458
The role of tissue-type plasminogen activator (tPA) in the 'spontaneous' as well as 'experimental' metastasis of ocular melanomas in mice was evaluated by transfecting the D5.1G4 murine melanoma cell line that possesses low metastatic activity and lo
Autor:
Gerhard Knarr, Joseph Sambrook, Mary Jane Gething, Johannes Buchner, Susanne Modrow, Mark S. Segal, S. Blond-Elguindi, L. Nanu, Fourie Anne M
Publikováno v:
Cold Spring Harbor Symposia on Quantitative Biology. 60:417-428