Results 11 to 20 of about 30,590 (168)

Structural Diversities of Lectins Binding to the Glycosphingolipid Gb3 [PDF]

open access: yesFrontiers in Molecular Biosciences, 2021
Glycolipids are present on the surfaces of all living cells and thereby represent targets for many protein receptors, such as lectins. Understanding the interactions between lectins and glycolipids is essential for investigating the functions of lectins ...
Lina Siukstaite   +5 more
doaj   +4 more sources

RIPK3 Contributes to Lyso-Gb3-Induced Podocyte Death [PDF]

open access: yesCells, 2021
Fabry disease is a lysosomal storage disease with an X-linked heritage caused by absent or decreased activity of lysosomal enzymes named alpha-galactosidase A (α-gal A).
So-Young Kim   +10 more
doaj   +3 more sources

Determination of Gb3 and Lyso-Gb3 in Fabry Disease-Affected Patients by LC-MRM/MS

open access: yesSeparations
Limited or absent activity of the enzyme α-galactosidase A (α-Gal A), due to mutation in the related gene on the X chromosome, leads to the development of a rare hereditary and genetic disease known as Fabry disease (FD).
Gennaro Battaglia   +9 more
doaj   +3 more sources

Anti-Gb3 monoclonal antibody inhibits angiogenesis and tumor development.

open access: yesPLoS ONE, 2012
Inhibiting the growth of tumor vasculature represents one of the relevant strategies against tumor progression. Between all the different pro-angiogenic molecular targets, plasma membrane glycosphingolipids have been under-investigated.
Ariane Desselle   +9 more
doaj   +5 more sources

Epithelial-Mesenchymal Transition in Kidney Tubular Epithelial Cells Induced by Globotriaosylsphingosine and Globotriaosylceramide. [PDF]

open access: yesPLoS ONE, 2015
Fabry disease is a lysosomal storage disorder caused by deficiency of alpha-galactosidase A (α-gal A), which results in the deposition of globotriaosylceramide (Gb3) in the vascular endothelium.
Yeo Jin Jeon   +4 more
doaj   +1 more source

Assessing the role of glycosphingolipids in the phenotype severity of Fabry disease mouse model

open access: yesJournal of Lipid Research, 2020
Fabry disease is caused by deficient activity of α-galactosidase A, an enzyme that hydrolyzes the terminal α-galactosyl moieties from glycolipids and glycoproteins, and subsequent accumulation of glycosphingolipids, mainly globotriaosylceramide (Gb3 ...
Siamak Jabbarzadeh-Tabrizi   +6 more
doaj   +1 more source

Nano-LC-MS/MS for Quantification of Lyso-Gb3 and Its Analogues Reveals a Useful Biomarker for Fabry Disease. [PDF]

open access: yesPLoS ONE, 2015
Biomarkers useful for diagnosis and evaluation of treatment for patients with Fabry disease are urgently needed. Recently, plasma globotriaosylsphingosine (lyso-Gb3) and lyso-Gb3-related analogues have attracted attention as promising biomarkers of Fabry
Hideaki Sueoka   +4 more
doaj   +1 more source

Shiga Toxin-Bearing Microvesicles Exert a Cytotoxic Effect on Recipient Cells Only When the Cells Express the Toxin Receptor

open access: yesFrontiers in Cellular and Infection Microbiology, 2020
Shiga toxin is the main virulence factor of non-invasive enterohemorrhagic Escherichia coli strains capable of causing hemolytic uremic syndrome. Our group has previously shown that the toxin can reach the kidney within microvesicles where it is taken up
Karl Johansson   +6 more
doaj   +1 more source

The interaction between flagellin and the glycosphingolipid Gb3 on host cells contributes to Bacillus cereus acute infection

open access: yesVirulence, 2020
Bacillus cereus is an opportunistic pathogen that can cause emetic or diarrheal foodborne illness. Previous studies have identified multiple pathogenic B. cereus strains and characterized a variety of virulence factors.
Song Gao   +9 more
doaj   +1 more source

Shiga toxin binding to glycolipids and glycans. [PDF]

open access: yesPLoS ONE, 2012
Immunologically distinct forms of Shiga toxin (Stx1 and Stx2) display different potencies and disease outcomes, likely due to differences in host cell binding.
Karen M Gallegos   +5 more
doaj   +1 more source

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