Sialidase NEU3 and its pathological significance
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
https://link.springer.com/content/pdf/10.1007/s10719-022-10067-7.pdf
Reference58 articles.
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2. Milner, C.M., Smith, S.V., Carrillo, M.B., Taylor, G.L., Hollinshead, M., Campbell, R.D.: Identification of a sialidase encoded in the human major histocompatibility complex. J. Biol. Chem. 272, 4549–4558 (1997)
3. Pshezhetsky, A.V., Richard, C., Michaud, L., Igdoura, S., Wang, S., Elsliger, M.A., Qu, J., Leclerc, D., Gravel, R., Dallaire, L., Potier, M.: Cloning, expression and chromosomal mapping of human lysosomal sialidase and characterization of mutations in sialidosis. Nat. Genet. 15, 316–320 (1997)
4. Carrillo, M.B., Milner, C.M., Ball, S.T., Snoek, M., Campbell, R.D.: Cloning and characterization of a sialidase from the murine histocompatibility-2 complex: low levels of mRNA and a single amino acid mutation are responsible for reduced sialidase activity in mice carrying the Neu1a allele. Glycobiology. 7, 975–986 (1997)
5. Miyagi, T., Konno, K., Emori, Y., Kawasaki, H., Suzuki, K., Yasui, A., Tsuik, S.: Molecular cloning and expression of cDNA encoding rat skeletal muscle cytosolic sialidase. J. Biol. Chem. 268, 26435–26440 (1993)
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