Results 81 to 90 of about 11,605 (209)

Rare‐Variant Burden across Lysosomal Genes Implicates Sialylation and Ganglioside Metabolism in Parkinson's Disease

open access: yesMovement Disorders, Volume 41, Issue 9, Page 2349-2356, September 2026.
Abstract Background Lysosomal dysfunction is central to Parkinson's disease (PD) pathogenesis, with GBA1 representing the strongest established genetic risk factor. Numerous other genes involved in lysosomal sphingolipid, glycosphingolipid, and ceramide metabolism have been proposed as contributors to PD, highlighting the need for genetic analyses ...
Konstantin Senkevich   +21 more
wiley   +1 more source

Lactosylceramide molecular species specificity of rat liver CMP-N-acetylneuraminate:lactosylceramide sialyltransferase.

open access: yesJournal of Lipid Research, 1989
Six naturally occurring and three synthetic molecular species of lactosylceramide (LacCer) were used to examine the molecular species specificity of CMP-N-acetylneuraminate:lactosylceramide alpha 2,3-sialyltransferase in a Golgi-rich fraction of rat ...
H Kadowaki   +3 more
doaj   +1 more source

Biosynthesis and intracellular transport of alpha-2,6-sialyltransferase in rat hepatoma cells.

open access: yes, 1992
We investigated biosynthesis, intracellular transport and release of beta-galactoside alpha-2,6-sialyltransferase in a dexamethasone-inducible rat hepatoma cell line.
Bosshart H, Berger EG
core   +1 more source

Sialylmotifs of sialyltransferases.

open access: yesIndian journal of biochemistry & biophysics, 1997
The sialyl moiety of sialylated glycoconjugates expressed on the cell surface are increasingly recognized as the key determinants of various biological recognition events. The transfer of sialic acid to these glycoconjugates are catalyzed by sialyltransferases, a group of 15 or more Golgi enzymes.
A K, Datta, J C, Paulson
openaire   +1 more source

A Multifunctional Pasteurella multocida Sialyltransferase:  A Powerful Tool for the Synthesis of Sialoside Libraries

open access: yes, 2016
A multifunctional sialyltransferase has been cloned from Pasteurella multocida strain P-1059 and expressed in E. coli as a truncated C-terminal His6-tagged recombinant protein (tPm0188Ph).
Harshal Chokhawala (2050390)   +8 more
core   +1 more source

Human liver and human placenta both contain CMP-NeuAc:Galβ1→4GlcNAc-R α2→3- as well as α2→6-sialyltransferase activity [PDF]

open access: yes, 1992
A high pH anion exchange chromatographic (HPAEC) system for the separation of isomeric sialo-oligosaccharide products was developed. Employing this system, using Galβ1→4GlcNAcβ1→2Manα1→6Manβ1→4GlcNAc as a substrate, a Galβ1→4GlcNAc-R α2→3 ...
Nemansky, Martin   +7 more
core   +1 more source

Cleavage of ST6Gal I by Radiation-Induced BACE1 Inhibits Golgi-Anchored ST6Gal I-Mediated Sialylation of Integrin β1 and Migration in Colon Cancer Cells

open access: yesRadiation Oncology, 2012
Background Previously, we found that β-galactoside α2,6-sialyltransferase (ST6Gal I), an enzyme that adds sialic acids to N-linked oligosaccharides of glycoproteins and is frequently overexpressed in cancer cells, is up-regulated by ionizing radiation ...
Lee Minyoung   +3 more
doaj   +1 more source

PmST2: A novel Pasteurella multocida glycolipid α2-3-sialyltransferase

open access: yes, 2011
Pasteurella multocida (Pm) is a multi-species pathogen that causes diseases in animals and humans. Sialyltransferase activity has been detected in multiple Pm strains and sialylation has been shown to be important for the pathogenesis of Pm.
Lau, Kam   +9 more
core   +1 more source

Increased CMP-NeuAc:Gal beta 1,4GlcNAc-R alpha 2,6 sialyltransferase activity in human colorectal cancer tissues

open access: yes, 1989
The sialyltransferase activities of 10 human colorectal specimens were compared with those of the corresponding adjacent normal mucosa. Using asialofetuin as an acceptor we found, in tumor tissues of 9 out of 10 patients, an increased sialyltransferase ...
Serafini, F   +5 more
core   +1 more source

Development of a novel method to evaluate sialylation of glycoproteins and analysis of gp96 sialylation in Hela, SW1990 and A549 cell lines

open access: yesBiological Research, 2015
BACKGROUND: Glycoproteins play a critical role in the cellular activities of eukaryotes. Sialic acid is typically the outermost monosaccharide of glycolipids and glycoproteins, and is necessary for normal development.
Yangui Liang   +4 more
doaj   +1 more source

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