Structural and biochemical characterization of theN‐terminal domain of flocculinLg‐Flo1p fromSaccharomyces pastorianusreveals a unique specificity for phosphorylated mannose-Reference-Cited by-同舟云学术

Structural and biochemical characterization of theN‐terminal domain of flocculinLg‐Flo1p fromSaccharomyces pastorianusreveals a unique specificity for phosphorylated mannose

Published:2013-01-24 Issue:4 Volume:280 Page:1073-1083
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Sim Lyann¹,Groes Magnus²,Olesen Kjeld²,Henriksen Anette¹

Affiliation:

1. The Protein Chemistry Group Carlsberg Laboratory Copenhagen Denmark

2. Carlsberg Research Center Copenhagen Denmark

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.12102

Reference45 articles.

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2. Repression and induction of flocculation interactions in Saccharomyces cerevisiae;Miki BL;J Bacteriol,1982

3. Localization and cell surface anchoring of the Saccharomyces cerevisiae flocculation protein Flo1p

4. A mannose-binding protein from the cell surface of flocculentSaccharomyces cerevisiae (NCIM 3528): its role in flocculation

5. Late fermentation expression of FLO1 in Saccharomyces cerevisiae;Verstrepen KJ;J Am Soc Brew Chem,2001

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