Kerr, W. G., Cooper, M. D., Feng, L., Burrows, P. D., Hendershot, L. M., Watanabe, Takeshi
In pre-B cells, the earliest identiflable stage of B cell differentiation, there is an asynchrony of Immunoglobulin chain expression in that μ heavy chains are synthesized in the absence of light...
Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153).
Wang, X Z, Lawson, B, Brewer, J W, Zinszner, H, Sanjay, A, Mi, L J, ...
The gene encoding C/EBP-homologous protein (CHOP), also known as growth arrest and DNA-damage-inducible gene 153 (GADD153), is activated by agents that adversely affect the function of the...
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...
Hendershot, L M, Ting, J, Lee, A S
The 78,000-dalton glucose-regulated protein (GRP78) and the immunoglobulin heavy-chain-binding protein (BiP) were shown to be the same protein by NH2-terminal sequence comparison. Immunoprecipitation...
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...
Brewer, J W, Cleveland, J L, Hendershot, L M
The stress-induced unfolded protein response (UPR) is the only signaling pathway known to regulate expression of genes encoding the resident endoplasmic reticulum (ER) molecular chaperones and...
Signals from the stressed endoplasmic reticulum induce C/EBP-homologous protein (CHOP/GADD153).
Wang, X Z, Lawson, B, Brewer, J W, Zinszner, H, Sanjay, A, Mi, L J, ...
The gene encoding C/EBP-homologous protein (CHOP), also known as growth arrest and DNA-damage-inducible gene 153 (GADD153), is activated by agents that adversely affect the function of the...
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...
Hendershot, L M, Ting, J, Lee, A S
The 78,000-dalton glucose-regulated protein (GRP78) and the immunoglobulin heavy-chain-binding protein (BiP) were shown to be the same protein by NH2-terminal sequence comparison. Immunoprecipitation...
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...
Brewer, J W, Cleveland, J L, Hendershot, L M
The stress-induced unfolded protein response (UPR) is the only signaling pathway known to regulate expression of genes encoding the resident endoplasmic reticulum (ER) molecular chaperones and...