Other names published for SSM4: DOA10, KIS3, E3 ubiquitin-protein ligase SSM4, YIL030C
SSM4 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
SSM4 - Primary Literature (37)
| Reference | Other Genes Addressed |
|---|---|
| Arlow T, et al. (2013) Proteasome inhibition rescues clinically significant unstable variants of the mismatch repair protein Msh2. Proc Natl Acad Sci U S A 110(1):246-51 | |
| Fredrickson EK, et al. (2013) Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility. J Biol Chem 288(9):6130-9 | |
| Guerriero CJ, et al. (2013) Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligase. J Biol Chem () | |
| Theesfeld CL and Hampton RY (2013) Insulin-induced gene protein (INSIG)-dependent sterol regulation of Hmg2 endoplasmic reticulum-associated degradation (ERAD) in yeast. J Biol Chem 288(12):8519-30 | |
| Zattas D, et al. (2013) N-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates. Mol Biol Cell 24(7):890-900 | |
| Lu S, et al. (2012) Arabidopsis ECERIFERUM9 involvement in cuticle formation and maintenance of plant water status. Plant Physiol 159(3):930-44 | |
| Mitchell DA, et al. (2012) The Erf4 subunit of the yeast Ras palmitoyl acyltransferase is required for stability of the Acyl-Erf2 intermediate and palmitoyl transfer to a Ras2 substrate. J Biol Chem 287(41):34337-48 | |
| Prasad R, et al. (2012) Biosynthetic mode can determine the mechanism of protein quality control. Biochem Biophys Res Commun 425(3):689-95 | |
| Rubenstein EM, et al. (2012) Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase. J Cell Biol 197(6):761-73 | |
| Stead BE, et al. (2012) Mcm2 phosphorylation and the response to replicative stress. BMC Genet 13(1):36 | |
| Theodoraki MA, et al. (2012) A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast. J Biol Chem 287(28):23911-22 | |
| Chantret I, et al. (2011) Endoplasmic reticulum-associated degradation (ERAD) and free oligosaccharide generation in Saccharomyces cerevisiae. J Biol Chem 286(48):41786-800 | |
| Kreft SG and Hochstrasser M (2011) An unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme. J Biol Chem 286(23):20163-74 | |
| Buck TM, et al. (2010) The Endoplasmic Reticulum-associated Degradation of the Epithelial Sodium Channel Requires a Unique Complement of Molecular Chaperones. Mol Biol Cell 21(6):1047-58 | |
| Hwang CS, et al. (2010) N-terminal acetylation of cellular proteins creates specific degradation signals. Science 327(5968):973-7 | |
| Li S, et al. (2010) Folding-competent and Folding-defective Forms of Ricin A Chain Have Different Fates after Retrotranslocation from the Endoplasmic Reticulum. Mol Biol Cell 21(15):2543-54 | |
| Liu C, et al. (2010) Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates. J Biol Chem 285(14):10265-72 | |
| Stolz A, et al. (2010) Dfm1 forms distinct complexes with Cdc48 and the ER ubiquitin ligases and is required for ERAD. Traffic 11(10):1363-9 | |
| Xie Y, et al. (2010) SUMO-independent in vivo activity of a SUMO-targeted ubiquitin ligase toward a short-lived transcription factor. Genes Dev 24(9):893-903 | |
| Adle DJ, et al. (2009) Cadmium-mediated rescue from ER-associated degradation induces expression of its exporter. Proc Natl Acad Sci U S A 106(25):10189-94 | |
| Fei W, et al. (2009) Conditions of endoplasmic reticulum stress stimulate lipid droplet formation in Saccharomyces cerevisiae. Biochem J 424(1):61-7 | |
| Metzger MB and Michaelis S (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol Biol Cell 20(3):1006-19 | |
| Xu P, et al. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137(1):133-45 | |
| Metzger MB, et al. (2008) Degradation of a Cytosolic Protein Requires Endoplasmic Reticulum-associated Degradation Machinery. J Biol Chem 283(47):32302-16 | |
| Nakatsukasa K, et al. (2008) Dissecting the ER-associated degradation of a misfolded polytopic membrane protein. Cell 132(1):101-12 | |
| Pagant S, et al. (2007) Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol Biol Cell 18(9):3398-413 | |
| Carvalho P, et al. (2006) Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins. Cell 126(2):361-73 | |
| Deng M and Hochstrasser M (2006) Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature 443(7113):827-31 | |
| Hesselberth JR, et al. (2006) Comparative analysis of Saccharomyces cerevisiae WW domains and their interacting proteins. Genome Biol 7(4):R30 | |
| Kreft SG, et al. (2006) Membrane topology of the yeast endoplasmic reticulum-localized ubiquitin ligase Doa10 and comparison with its human ortholog TEB4 (MARCH-VI). J Biol Chem 281(8):4646-53 |




