Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation-Reference-Cited by-同舟云学术

Structure of human ST8SiaIII sialyltransferase provides insight into cell-surface polysialylation

Published:2015-07-20 Issue:8 Volume:22 Page:627-635
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Volkers Gesa,Worrall Liam J,Kwan David H,Yu Ching-Ching,Baumann Lars,Lameignere Emilie,Wasney Gregory A,Scott Nichollas E,Wakarchuk Warren,Foster Leonard J,Withers Stephen G,Strynadka Natalie C J

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3060.pdf

Reference78 articles.

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2. Sato, C. & Kitajima, K. Disialic, oligosialic and polysialic acids: distribution, functions and related disease. J. Biochem. 154, 115–136 (2013).

3. Crocker, P.R., Paulson, J.C. & Varki, A. Siglecs and their roles in the immune system. Nat. Rev. Immunol. 7, 255–266 (2007).

4. Mühlenhoff, M., Rollenhagen, M., Werneburg, S., Gerardy-Schahn, R. & Hildebrandt, H. Polysialic acid: versatile modification of NCAM, SynCAM 1 and neuropilin-2. Neurochem. Res. 38, 1134–1143 (2013).

5. Acheson, A., Sunshine, J.L. & Rutishauser, U. NCAM polysialic acid can regulate both cell-cell and cell-substrate interactions. J. Cell Biol. 114, 143–153 (1991).

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