The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).
Open accessAbstract
We have isolated an expressible full-length cDNA clone encoding murine ERp99, an abundant, conserved transmembrane glycoprotein of the endoplasmic reticulum membrane. ERp99 is synthesized as a 92,475-kDa precursor containing 802 amino acids. It possesses a signal peptide of 21 amino acids which is cleaved cotranslationally. Analysis of the amino acid sequence deduced from the nucleotide sequence of the cDNA clone led us to propose a model for the orientation of ERp99 in the endoplasmic reticulum membrane. In this model, ERp99 possesses one membrane-spanning, stop transfer segment in the N-terminal region. The protein chain passes through the membrane only once, and approximately 75% of the protein remains on the cytoplasmic side of the ER membrane. Comparison of the ERp99 sequence to the sequence of other proteins revealed that ERp99 has extensive homology with the 90-kDa heat shock protein of Saccharomyces cerevisiae (hsp90) and the 83-kDa heat shock protein of Drosophila melanogaster. In addition, the N terminus of mature ERp99 is identical to that of the 94-kDa glucose regulated protein (GRP94) of mammalian cells.
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DNA sequencing with chain-terminating inhibitors
Sanger, F., Nicklen, S., & Coulson, A. R. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.12.5463 · Cited by 68,572
Molecular Cloning. A Laboratory Manual
Wood, E. (1983) · Biochemical Education · doi:10.1016/0307-4412(83)90068-7 · Cited by 29,533
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,843
Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288
Aviv, H., & Leder, P. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.6.1408 · Cited by 6,751
[2] New M13 vectors for cloning
Messing, J. (1983) · Methods in Enzymology · doi:10.1016/0076-6879(83)01005-8 · Cited by 5,323
Prediction of protein conformation
Chou, P. Y., & Fasman, G. D. (1974) · Biochemistry · doi:10.1021/bi00699a002 · Cited by 3,309
Atlas of Protein Sequence and Structure, 1972.
Fitch, W. M., & Dayhoff, M. O. (1973) · Systematic Zoology · doi:10.2307/2412105 · Cited by 2,436
Analysis of membrane and surface protein sequences with the hydrophobic moment plot
Eisenberg, D., Schwarz, E., Komaromy, M., & Wall, R. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90309-7 · Cited by 2,284
A C-terminal signal prevents secretion of luminal ER proteins
Munro, S., & Pelham, H. R. B. (1987) · Cell · doi:10.1016/0092-8674(87)90086-9 · Cited by 1,721
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Control of Protein Exit from the Endoplasmic Reticulum
Pelham, H. R. B. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.000245 · Cited by 787
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential
Lee, A. S. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3701 · Cited by 587
Mammalian stress response: induction of the glucose-regulated protein family
Lee, A. S. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90042-b · Cited by 442
Marzec, M., Eletto, D., & Argon, Y. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.10.013 · Cited by 390
Metadata
- Authors
- Mazzarella, R. A., & Green, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1987-06
- Volume
- 262
- Issue
- 18
- Pages
- 8875-8883
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1479809193
- Cited by
- 290
- References
- 53
- FWCI
- 6.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Mazzarella, R. A., & Green, M. (1987). ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94). Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)47496-0
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