A Facile Method for the Preparation of Gold Glyconanoparticles from Free Oligosaccharides and Their Applicability in Carbohydrate-Protein Interaction Studies

2005 ◽  
Vol 2005 (17) ◽  
pp. 3650-3659 ◽  
Author(s):  
Koen M. Halkes ◽  
Adriana Carvalho de Souza ◽  
C. Elizabeth P. Maljaars ◽  
Gerrit J. Gerwig ◽  
Johannis P. Kamerling
2007 ◽  
Vol 17 (18) ◽  
pp. 5155-5158 ◽  
Author(s):  
Carmen Jiménez-Castells ◽  
Beatriz G. de la Torre ◽  
Ricardo Gutiérrez Gallego ◽  
David Andreu

2000 ◽  
Vol 350 (3) ◽  
pp. 741-746 ◽  
Author(s):  
Julian GRUSOVIN ◽  
Violet STOICHEVSKA ◽  
Keith H. GOUGH ◽  
Katrina NUNAN ◽  
Colin W. WARD ◽  
...  

munc18c is a critical protein involved in trafficking events associated with syntaxin 4 and which also mediates inhibitory effects on vesicle docking and/or fusion. To investigate the domains of munc18c responsible for its interaction with syntaxin 4, fragments of munc18c were generated and their interaction with syntaxin 4 examined in vivo by the yeast two-hybrid assay. In vitro protein–protein interaction studies were then used to confirm that the interaction between the proteins was direct. Full-length munc18c1–592, munc18c1–139 and munc18c1–225, but not munc18c226–592, munc18c1–100, munc18c43–139 or munc18c66–139, interacted with the cytoplasmic portion of syntaxin 4, Stx42–273, as assessed by yeast two-hybrid assay of growth on nutritionally deficient media and by β-galactosidase reporter induction. The N-terminal predicted helix-a-helix-b-helix-c region of syntaxin 4, Stx429–157, failed to interact with full-length munc18c1–592, indicating that a larger portion of syntaxin 4 is necessary for the interaction. The yeast two-hybrid results were confirmed by protein–protein interaction studies between Stx42–273 and glutathione S-transferase fusion proteins of munc18c. Full-length munc18c1–592, munc18c1–139 and munc18c1–225 interacted with Stx42–273 whereas munc18c1–100 did not, consistent with the yeast two-hybrid data. These data thus identify a region of munc18c between residues 1 and 139 as a minimal domain for its interaction with syntaxin 4.


2019 ◽  
Vol 21 (16) ◽  
pp. 6393-6396
Author(s):  
Tatsuya Suzuki ◽  
Chieka Hayashi ◽  
Naoko Komura ◽  
Rie Tamai ◽  
Jun Uzawa ◽  
...  

2020 ◽  
Vol 56 (73) ◽  
pp. 10746-10749
Author(s):  
Isabelle Bertin-Jung ◽  
Anne Robert ◽  
Nick Ramalanjaona ◽  
Sandrine Gulberti ◽  
Catherine Bui ◽  
...  

Here we propose a general strategy to label carbohydrates with N-methyl-anthranilic acid to generate glycotools for fluorescence-based screening and carbohydrate–protein interaction studies.


Plant Methods ◽  
2018 ◽  
Vol 14 (1) ◽  
Author(s):  
S. V. G. N. Priyadarshani ◽  
Bingyan Hu ◽  
Weimin Li ◽  
Hina Ali ◽  
Haifeng Jia ◽  
...  

2002 ◽  
Vol 46 (2) ◽  
pp. 190-196 ◽  
Author(s):  
Lin Jiang ◽  
Ying Gao ◽  
Fenglou Mao ◽  
Zhijie Liu ◽  
Luhua Lai

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