bodies raised against the turkey proteins to identify 
lamin A, lamin B, and lamin B receptor in 
Saccharomyces cerevisiae. The identification of 
these components in yeast should allow the use, in 
addition to biochemical approaches, of genetic ap- 
proaches to investigate the function of these 
proteins. 
Dr. Blobel is also Professor of Cell Biology at The 
Rockefeller University. 
PUBLICATIONS 
Articles 
Aris, J.E, and Blobel, G. 1989. Yeast nuclear envelope proteins cross react with an antibody against mam- 
malian pore complex proteins./ Cell Biol 108:2059-2067. 
Audigier, Y, Nigam, S.K., and Blobel, G. 1988. Identification of a G protein in rough endoplasmic reticulum 
of canine pancreas./ 5?o/ Chem 263:16352-16357. 
Chirico, WJ., Waters, M.G., and Blobel, G. 1988. 70K heat shock related proteins stimulate protein transloca- 
tion into microsomes. Nature 332:805-810. 
Georgatos, S.D., Maroulakou, I., and Blobel, G. 1989. Lamin A, lamin B, and lamin B receptor analogues in 
YC2iSt.J Cell Biol 108:2069-2082. 
Murakami, H., Pain, D., and Blobel, G. 1988. 70-kD heat shock-related protein is one of at least two distinct 
cytosolic factors stimulating protein import into mitochondria./ Ce//5«o/ 107:2051-2057. 
Nicchitta, C.V, and Blobel, G. 1989. Nascent secretory chain binding and translocation are distinct processes: 
differentiation by chemical alkylation./Ce//B/o/ 108:789-795. 
Pain, D., Kanwar, YS., and Blobel, G. 1988. Identification of a receptor for protein import into chloroplasts 
and its localization to envelope contact zones. Nature 331:232-237. 
Shelness, G.S., Kanwar, YS., and Blobel, G. 1988. cDNA-derived primary structure of the glycoprotein com- 
ponent of canine microsomal signal peptidase complex./fi/o/ Chem 263:17063-17070. 
Simon, S.M., Blobel, G., and Zimmerberg, J. 1989. Large aqueous channels in membrane vesicles derived 
from the rough endoplasmic reticulum of canine pancreas or the plasma membrane of Escherichia coli. 
Proc Natl Acad Sci USA 86:6176-6180. 
Watanabe, M., and Blobel, G. 1989. Binding of a soluble factor of Escherichia coli to preproteins does not re- 
quire ATP and appears to be the first step in protein export. Proc Natl Acad Sci USA 86:2248-2252. 
Watanabe, M., and Blobel, G. 1989. Cytosolic factor purified from Escherichia coli is necessary and sufficient 
for the export of a preprotein and is a homotetramer of SecB. Proc Natl Acad Sci USA 86:2728-2732. 
Watanabe, M., and Blobel, G. 1989. SecB functions as a cytosolic signal recognition factor for protein export 
inE. coli. Cell 58:695-705. 
Watanabe, M., and Blobel, G. 1989. Site-specific antibodies against the PrLA (SecY) protein of Escherichia coli 
inhibit protein export by interfering with plasma membrane binding of preproteins. Proc Natl Acad Sci 
f/SA 86: 1895-1899. 
Waters, M.G., Evans, E.A., and Blobel, G. 1988. Prepro-a-factor has a cleavable signal sequence. /Bzo/ Chem 
263:6209-6214. 
Worman, H.J., Yuan, J., Blobel, G., and Georgatos, S. 1988. A lamin B receptor in the nuclear envelope. Proc 
Natl Acad Sci USA 85:8531-8534. 
Wozniak, R.W, Bartnik, E. , and Blobel, G. 1989. Primary structure analysis of an integral membrane glycopro- 
tein of the nuclear pore. J Cell Biol 108:2083-2092. 
YaDeau, J.T, and Blobel, G. 1989. Solubilization and characterization of yeast signal peptidase./ B«o/ Chem 
264:2928-2934^ 
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