In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.
Hendershot, L M, Wei, J Y, Gaut, J R, Lawson, B, Freiden, P J, Murti, K G
BiP possesses ATP binding/hydrolysis activities that are thought to be essential for its ability to chaperone protein folding and assembly in the endoplasmic reticulum (ER). We have produced a series...
Interconversion of three differentially modified and assembled forms of BiP.
Freiden, P J, Gaut, J R, Hendershot, L M
The immunoglobulin heavy chain binding protein BiP/GRP78 is post-translationally modified by phosphorylation and ADP ribosylation. In cells induced to synthesize higher levels of BiP, either due to...
In vivo expression of mammalian BiP ATPase mutants causes disruption of the endoplasmic reticulum.
Hendershot, L M, Wei, J Y, Gaut, J R, Lawson, B, Freiden, P J, Murti, K G
BiP possesses ATP binding/hydrolysis activities that are thought to be essential for its ability to chaperone protein folding and assembly in the endoplasmic reticulum (ER). We have produced a series...
Interconversion of three differentially modified and assembled forms of BiP.
Freiden, P J, Gaut, J R, Hendershot, L M
The immunoglobulin heavy chain binding protein BiP/GRP78 is post-translationally modified by phosphorylation and ADP ribosylation. In cells induced to synthesize higher levels of BiP, either due to...