Sitia R - Search Results

1

Quality control in the endoplasmic reticulum protein factory.

Sitia R, Braakman I. Sitia R, et al. Nature. 2003 Dec 18;426(6968):891-4. doi: 10.1038/nature02262. Nature. 2003. PMID: 14685249 Review.

2

Endoplasmic reticulum: a dynamic patchwork of specialized subregions.

Sitia R, Meldolesi J. Sitia R, et al. Mol Biol Cell. 1992 Oct;3(10):1067-72. doi: 10.1091/mbc.3.10.1067. Mol Biol Cell. 1992. PMID: 1421566 Free PMC article. Review. No abstract available.

3

Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum.

Valetti C, Grossi CE, Milstein C, Sitia R. Valetti C, et al. Among authors: sitia r. J Cell Biol. 1991 Nov;115(4):983-94. doi: 10.1083/jcb.115.4.983. J Cell Biol. 1991. PMID: 1955467 Free PMC article.

4

Quality control of ER synthesized proteins: an exposed thiol group as a three-way switch mediating assembly, retention and degradation.

Fra AM, Fagioli C, Finazzi D, Sitia R, Alberini CM. Fra AM, et al. Among authors: sitia r. EMBO J. 1993 Dec;12(12):4755-61. doi: 10.1002/j.1460-2075.1993.tb06164.x. EMBO J. 1993. PMID: 8223484 Free PMC article.

5

The endoplasmic reticulum as a site of protein degradation.

Fra A, Sitia R. Fra A, et al. Among authors: sitia r. Subcell Biochem. 1993;21:143-68. doi: 10.1007/978-1-4615-2912-5_7. Subcell Biochem. 1993. PMID: 8256264 Review. No abstract available.

6

Formation of reversible disulfide bonds with the protein matrix of the endoplasmic reticulum correlates with the retention of unassembled Ig light chains.

Reddy P, Sparvoli A, Fagioli C, Fassina G, Sitia R. Reddy P, et al. Among authors: sitia r. EMBO J. 1996 May 1;15(9):2077-85. EMBO J. 1996. PMID: 8641273 Free PMC article.

7

Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER.

Carelli S, Ceriotti A, Cabibbo A, Fassina G, Ruvo M, Sitia R. Carelli S, et al. Among authors: sitia r. Science. 1997 Sep 12;277(5332):1681-4. doi: 10.1126/science.277.5332.1681. Science. 1997. Retraction in: Science. 1998 Feb 27;279(5355):1288-9. doi: 10.1126/science.279.5355.1283j PMID: 9287224 Retracted.

8

ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum.

Cabibbo A, Pagani M, Fabbri M, Rocchi M, Farmery MR, Bulleid NJ, Sitia R. Cabibbo A, et al. Among authors: sitia r. J Biol Chem. 2000 Feb 18;275(7):4827-33. doi: 10.1074/jbc.275.7.4827. J Biol Chem. 2000. PMID: 10671517 Free article.

9

Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response.

Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R. Pagani M, et al. Among authors: sitia r. J Biol Chem. 2000 Aug 4;275(31):23685-92. doi: 10.1074/jbc.M003061200. J Biol Chem. 2000. PMID: 10818100 Free article.

We have previously described the human gene ERO1-L, which complements several phenotypic traits of the yeast thermo-sensitive mutant ero1-1 (Cabibbo, A., Pagani, M., Fabbri, M., Rocchi, M., Farmery, M. R., Bulleid, N. J., and Sitia, R. (2000) J. Biol. Chem. 2 …

We have previously described the human gene ERO1-L, which complements several phenotypic traits of the yeast thermo-sensitive mutant ero1-1 …

10

The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha.

Benham AM, Cabibbo A, Fassio A, Bulleid N, Sitia R, Braakman I. Benham AM, et al. Among authors: sitia r. EMBO J. 2000 Sep 1;19(17):4493-502. doi: 10.1093/emboj/19.17.4493. EMBO J. 2000. PMID: 10970843 Free PMC article.

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