sialyl lex
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Fucosyltransferase 7. GDP-Fucose Lactosamine α1,3-Fucosyltransferase. Sialyl-Lex Specific (FUT7)

2014 ◽  
pp. 573-580
Author(s):  
Takashi Kudo ◽  
Hisashi Narimatsu
Keyword(s):  
Sialyl Lex

scholarly journals A novel sialyl LeX expression score as a potential prognostic tool in colorectal cancer

2012 ◽  
Vol 10 (1) ◽  
Author(s):  
Leif Schiffmann ◽  
Fabian Schwarz ◽  
Michael Linnebacher ◽  
Friedrich Prall ◽  
Jens Pahnke ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Prognostic Tool ◽  
Sialyl Lex ◽  
Expression Score

Ganglioside Biosynthesis in Developing Brains and Apoptotic Cancer Cells: X. Regulation of Glyco-genes Involved in GD3 and Sialyl-Lex/a Syntheses

2012 ◽  
Vol 37 (6) ◽  
pp. 1245-1255 ◽  
Author(s):  
Subhash Basu ◽  
Rui Ma ◽  
Joseph R. Moskal ◽  
Manju Basu
Keyword(s):  
Cancer Cells ◽  
Sialyl Lex ◽  
Ganglioside Biosynthesis

ChemInform Abstract: Synthesis of a Versatile Tetrasaccharide of Sialyl Lex and Lex Antigens.

ChemInform ◽  
2010 ◽  
Vol 28 (4) ◽  
pp. no-no
Author(s):  
U. S. CHOWDHURY
Keyword(s):  
Sialyl Lex

ChemInform Abstract: Exploration of β-Turn Scaffolding Motifs as Components of Sialyl Lex Mimetics and Their Relevance to P-Selectin.

ChemInform ◽  
2010 ◽  
Vol 30 (6) ◽  
pp. no-no
Author(s):  
S. HANESSIAN ◽  
H. K. HUYNH ◽  
G. V. REDDY ◽  
G. MCNAUGHTON-SMITH ◽  
B. ERNST ◽  
...  
Keyword(s):  
Sialyl Lex

scholarly journals Induction of sialyl-Lex expression by herpes simplex virus type 1 is dependent on viral immediate early RNA-activated transcription of host fucosyltransferase genes

Glycobiology ◽  
2009 ◽  
Vol 19 (8) ◽  
pp. 847-859 ◽  
Author(s):  
K. Nystrom ◽  
R. Norden ◽  
I. Muylaert ◽  
P. Elias ◽  
G. Larson ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Immediate Early ◽  
Sialyl Lex ◽  
Simplex Virus

Expression of sialyl Lex, sialyl Lea, Lex and Ley glycotopes in secreted human ovarian cyst glycoproteins

Biochimie ◽  
2009 ◽  
Vol 91 (3) ◽  
pp. 423-433 ◽  
Author(s):  
Zhangung Yang ◽  
June H. Wu ◽  
Hsiang-Wei Kuo ◽  
Reiji Kannagi ◽  
Albert M. Wu
Keyword(s):  
Ovarian Cyst ◽  
Sialyl Lex ◽  
Sialyl Lea

scholarly journals Normal cellular prion protein is a ligand of selectins: binding requires LeX but is inhibited by sLeX

2007 ◽  
Vol 406 (2) ◽  
pp. 333-341 ◽  
Author(s):  
Chaoyang Li ◽  
Poki Wong ◽  
Tao Pan ◽  
Fan Xiao ◽  
Shaoman Yin ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Fusion Protein ◽  
Human Brain ◽  
Prion Protein ◽  
Fusion Proteins ◽  
Cellular Prion Protein ◽  
The Other ◽  
Dependent Manner ◽  
Peripheral Tissues ◽  
Sialyl Lex

The normal PrPC (cellular prion protein) contains sLeX [sialyl-LeX (Lewis X)] and LeX. sLeX is a ligand of selectins. To examine whether PrPC is a ligand of selectins, we generated three human PrPC–Ig fusion proteins: one with LeX, one with sLeX, and the other with neither LeX nor sLeX. Only LeX-PrPC–Ig binds E-, L- and P-selectins. Binding is Ca2+-dependent and occurs with nanomolar affinity. Removal of sialic acid on sLeX-PrPC–Ig enables the fusion protein to bind all selectins. These findings were confirmed with brain-derived PrPC. The selectins precipitated PrPC in human brain in a Ca2+-dependent manner. Treatment of brain homogenates with neuraminidase increased the amounts of PrPC precipitated. Therefore the presence of sialic acid prevents the binding of PrPC in human brain to selectins. Hence, human brain PrPC interacts with selectins in a manner that is distinct from interactions in peripheral tissues. Alternations in these interactions may have pathological consequences.

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