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DERL1

Introduction

Der1-like domain family, member 1, also known as DERL1, is a human gene.[1]

References

References

  1. ↑ “Entrez Gene: DERL1 Der1-like domain family, member 1”.
Further reading

Further reading

  • Andersson B, Wentland MA, Ricafrente JY; et al. (1996). “A “double adaptor” method for improved shotgun library construction”. Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC; et al. (1997). “Large-scale concatenation cDNA sequencing”. Genome Res. 7 (4): 353–8. PMID 9110174.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Clark HF, Gurney AL, Abaya E; et al. (2003). “The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment”. Genome Res. 13 (10): 2265–70. doi:10.1101/gr.1293003. PMID 12975309.
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Lilley BN, Ploegh HL (2004). “A membrane protein required for dislocation of misfolded proteins from the ER”. Nature. 429 (6994): 834–40. doi:10.1038/nature02592. PMID 15215855.
  • Ye Y, Shibata Y, Yun C; et al. (2004). “A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol”. Nature. 429 (6994): 841–7. doi:10.1038/nature02656. PMID 15215856.
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
  • Katiyar S, Joshi S, Lennarz WJ (2006). “The retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulum”. Mol. Biol. Cell. 16 (10): 4584–94. doi:10.1091/mbc.E05-04-0345. PMID 16055502.
  • Lilley BN, Ploegh HL (2006). “Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane”. Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14296–301. doi:10.1073/pnas.0505014102. PMID 16186509.
  • Ye Y, Shibata Y, Kikkert M; et al. (2006). “Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane”. Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. doi:10.1073/pnas.0505006102. PMID 16186510.
  • Schulze A, Standera S, Buerger E; et al. (2006). “The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway”. J. Mol. Biol. 354 (5): 1021–7. doi:10.1016/j.jmb.2005.10.020. PMID 16289116.
  • Oda Y, Okada T, Yoshida H; et al. (2006). “Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation”. J. Cell Biol. 172 (3): 383–93. doi:10.1083/jcb.200507057. PMID 16449189.
  • Schubert V, Da Silva JS, Dotti CG (2006). “Localized recruitment and activation of RhoA underlies dendritic spine morphology in a glutamate receptor-dependent manner”. J. Cell Biol. 172 (3): 453–67. doi:10.1083/jcb.200506136. PMID 16449195.
  • Sun F, Zhang R, Gong X; et al. (2007). “Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants”. J. Biol. Chem. 281 (48): 36856–63. doi:10.1074/jbc.M607085200. PMID 16954204.
  • Crawshaw SG, Cross BC, Wilson CM, High S (2007). “The oligomeric state of Derlin-1 is modulated by endoplasmic reticulum stress”. Mol. Membr. Biol. 24 (2): 113–20. doi:10.1080/09687860600988727. PMID 17453418.

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