Other names published for PMR1: BSD1, LDB1, SSC1, Ca(2+)/Mn(2+)-transporting P-type ATPase PMR1, YGL167C
PMR1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PMR1 - Alias (9)
| Reference | Other Genes Addressed |
|---|---|
| Olivero I, et al. (2003) The ldb1 mutant of Saccharomyces cerevisiae is defective in Pmr1p, the yeast secretory pathway/Golgi Ca(2+)/Mn(2+)-ATPase. FEMS Microbiol Lett 219(1):137-42 | |
| Manas P, et al. (1998) Proteolytic processing of a secreted glycoprotein and O-glycosylation of mannoproteins are affected in the N-glycosylation mutant Saccharomyces cerevisiae ldb1. Biochim Biophys Acta 1380(3):320-8 | |
| Manas P, et al. (1997) Isolation of new nonconditional Saccharomyces cerevisiae mutants defective in asparagine-linked glycosylation. Glycobiology 7(4):487-97 | |
| Klima R, et al. (1996) A putative helicase, the SUA5, PMR1, tRNALys1 genes and four open reading frames have been detected in the DNA sequence of an 8.8 kb fragment of the left arm of chromosome VII of Saccharomyces cerevisiae. Yeast 12(10B Suppl):1033-40 | |
| Ramjee MK, et al. (1996) A novel yeast expression/secretion system for the recombinant plant thiol endoprotease propapain. Protein Eng 9(11):1055-61 | |
| James CM, et al. (1995) DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43. Yeast 11(14):1413-9 | |
| Lapinskas PJ, et al. (1995) Mutations in PMR1 suppress oxidative damage in yeast cells lacking superoxide dismutase. Mol Cell Biol 15(3):1382-8 | |
| Liu XF and Culotta VC (1994) The requirement for yeast superoxide dismutase is bypassed through mutations in BSD2, a novel metal homeostasis gene. Mol Cell Biol 14(11):7037-45 | |
| Rudolph HK, et al. (1989) The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. Cell 58(1):133-45 |



