Saposin
From Proteopedia
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3D Structures of Saposin
Updated on 14-November-2023
References
- ↑ O'Brien JS, Kishimoto Y. Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 1991 Mar 1;5(3):301-8. PMID:2001789
- ↑ Morimoto S, Martin BM, Yamamoto Y, Kretz KA, O'Brien JS, Kishimoto Y. Saposin A: second cerebrosidase activator protein. Proc Natl Acad Sci U S A. 1989 May;86(9):3389-93. PMID:2717620
- ↑ Yuan W, Qi X, Tsang P, Kang SJ, Illarionov PA, Besra GS, Gumperz J, Cresswell P. Saposin B is the dominant saposin that facilitates lipid binding to human CD1d molecules. Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5551-6. Epub 2007 Mar 19. PMID:17372201 doi:http://dx.doi.org/10.1073/pnas.0700617104
- ↑ Azuma N, O'Brien JS, Moser HW, Kishimoto Y. Stimulation of acid ceramidase activity by saposin D. Arch Biochem Biophys. 1994 Jun;311(2):354-7. PMID:8203897
- ↑ Deconinck N, Messaaoui A, Ziereisen F, Kadhim H, Sznajer Y, Pelc K, Nassogne MC, Vanier MT, Dan B. Metachromatic leukodystrophy without arylsulfatase A deficiency: a new case of saposin-B deficiency. Eur J Paediatr Neurol. 2008 Jan;12(1):46-50. Epub 2007 Jul 5. PMID:17616409 doi:http://dx.doi.org/10.1016/j.ejpn.2007.05.004
- ↑ Matsuda J, Kido M, Tadano-Aritomi K, Ishizuka I, Tominaga K, Toida K, Takeda E, Suzuki K, Kuroda Y. Mutation in saposin D domain of sphingolipid activator protein gene causes urinary system defects and cerebellar Purkinje cell degeneration with accumulation of hydroxy fatty acid-containing ceramide in mouse. Hum Mol Genet. 2004 Nov 1;13(21):2709-23. Epub 2004 Sep 2. PMID:15345707 doi:http://dx.doi.org/10.1093/hmg/ddh281