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6. Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism. Halaban R, Svedine S, Cheng E, Smicun Y, Aron R, Hebert DN. Proc Natl Acad Sci U S A; 2000 May 23; 97(11):5889-94. PubMed ID: 10823941 [Abstract] [Full Text] [Related]
7. Soluble tyrosinase is an endoplasmic reticulum (ER)-associated degradation substrate retained in the ER by calreticulin and BiP/GRP78 and not calnexin. Popescu CI, Paduraru C, Dwek RA, Petrescu SM. J Biol Chem; 2005 Apr 08; 280(14):13833-40. PubMed ID: 15677452 [Abstract] [Full Text] [Related]
13. Role of the endoplasmic reticulum chaperone calnexin in subunit folding and assembly of nicotinic acetylcholine receptors. Gelman MS, Chang W, Thomas DY, Bergeron JJ, Prives JM. J Biol Chem; 1995 Jun 23; 270(25):15085-92. PubMed ID: 7797492 [Abstract] [Full Text] [Related]
15. Molecular control of melanogenesis in malignant melanoma: functional assessment of tyrosinase and lamp gene families by UV exposure and gene co-transfection, and cloning of a cDNA encoding calnexin, a possible melanogenesis "chaperone". Jimbow K, Hara H, Vinayagamoorthy T, Luo D, Dakour J, Yamada K, Dixon W, Chen H. J Dermatol; 1994 Nov 23; 21(11):894-906. PubMed ID: 7531726 [Abstract] [Full Text] [Related]
16. Oculocutaneous albinism types 1 and 3 are ER retention diseases: mutation of tyrosinase or Tyrp1 can affect the processing of both mutant and wild-type proteins. Toyofuku K, Wada I, Valencia JC, Kushimoto T, Ferrans VJ, Hearing VJ. FASEB J; 2001 Oct 23; 15(12):2149-61. PubMed ID: 11641241 [Abstract] [Full Text] [Related]
17. Association of calnexin with wild type and mutant AVPR2 that causes nephrogenic diabetes insipidus. Morello JP, Salahpour A, Petäjä-Repo UE, Laperrière A, Lonergan M, Arthus MF, Nabi IR, Bichet DG, Bouvier M. Biochemistry; 2001 Jun 12; 40(23):6766-75. PubMed ID: 11389590 [Abstract] [Full Text] [Related]
18. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control. Hammond C, Braakman I, Helenius A. Proc Natl Acad Sci U S A; 1994 Feb 01; 91(3):913-7. PubMed ID: 8302866 [Abstract] [Full Text] [Related]