Yeast- and antibody-based tools for studying tryptophan C-mannosylation-Reference-Cited by-同舟云学术

Yeast- and antibody-based tools for studying tryptophan C-mannosylation

Published:2021-02-04 Issue:4 Volume:17 Page:428-437
ISSN:1552-4450
Container-title:Nature Chemical Biology
language:en
Short-container-title:Nat Chem Biol

Author:

John Alan^ORCID,Järvå Michael A.^ORCID,Shah Sayali,Mao Runyu^ORCID,Chappaz Stephane^ORCID,Birkinshaw Richard W.^ORCID,Czabotar Peter E.^ORCID,Lo Alvin W.,Scott Nichollas E.^ORCID,Goddard-Borger Ethan D.^ORCID

Funder

Department of Health | National Health and Medical Research Council

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/s41589-020-00727-w.pdf

Reference60 articles.

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2. de Beer, T., Vliegenthart, J. F., Löffler, A. & Hofsteenge, J. The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is α-mannopyranose. Biochemistry 34, 11785–11789 (1995).

3. Hofsteenge, J. et al. New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us. Biochemistry 33, 13524–13530 (1994).

4. Shcherbakova, A., Tiemann, B., Buettner, F. F. & Bakker, H. Distinct C-mannosylation of netrin receptor thrombospondin type 1 repeats by mammalian DPY19L1 and DPY19L3. Proc. Natl Acad. Sci. USA 114, 2574–2579 (2017).

5. Doucey, M. A., Hess, D., Cacan, R. & Hofsteenge, J. Protein C-mannosylation is enzyme-catalysed and uses dolichyl-phosphate-mannose as a precursor. Mol. Biol. Cell 9, 291–300 (1998).

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