Results 91 to 100 of about 17,651 (213)

Sulfonylurea Bioisosteres of Sulfonic Acid in JFD 00458‐Based ST6GAL1 Inhibitors Enhance Membrane Permeability

open access: yesChemMedChem, Volume 21, Issue 16, 27 August 2026.
ST6GAL1 sialylates glycoconjugates in the Golgi, modulating immune recognition and enabling tumor immune evasion. To effectively reach ST6GAL1, inhibitors should demonstrate good membrane permeability. Based on nonpermeable hit JFD 00458, we developed sulfonylurea analogs achieving increased membrane permeability and potency.
Natan Koraj   +9 more
wiley   +1 more source

Identification of aberrant α-2,3 sialylation of cartilage associated with osteonecrosis of the femoral head based on integrated multi-omics analyses

open access: yesBBA Advances
Purpose: Osteonecrosis of the femoral head (ONFH) is one of the most common and devastating articular cartilage diseases worldwide. The role of glycosylation in cartilage degeneration of ONFH is not yet fully understood.
Xueliang Lu   +8 more
doaj   +1 more source

Sialylation-immune-related lncRNA LINC01605 promotes tumor-infiltrating CD8+ T cell exhaustion and malignancy of clear cell renal cell carcinoma

open access: yesFrontiers in Immunology
BackgroundDysregulated expression of long non-coding RNAs (lncRNAs) has been shown to play a critical role in the tumorigenicity of clear cell renal cell carcinoma (ccRCC).
Ziran Dai   +11 more
doaj   +1 more source

Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1.

open access: yesPLoS ONE, 2015
The central molecular event underlying prion diseases involves conformational change of the cellular form of the prion protein (PrPC), which is a sialoglycoprotein, into the disease-associated, transmissible form denoted PrPSc.
Elizaveta Katorcha   +10 more
doaj   +1 more source

Targeted Approaches to Inhibit Sialylation of Multiple Myeloma in the Bone Marrow Microenvironment

open access: yesFrontiers in Bioengineering and Biotechnology, 2019
Aberrant glycosylation modulates different aspects of tumor biology, and it has long been recognized as a hallmark of cancer. Among the different forms of glycosylation, sialylation, the addition of sialic acid to underlying oligosaccharides, is often ...
Alessandro Natoni   +3 more
doaj   +1 more source

Regulation of Sialylation in the Drosophila Nervous System

open access: yes, 2018
Sialylation is a common post-translational modification in animal cells, yet its molecular and cellular regulation is poorly understood. It is involved in many vital functions in vertebrates, while perturbations in sialylation have been implicated in ...
Scott, Hilary Anne
core   +1 more source

Triple-negative and HER2-overexpressing breast cancer cell sialylation impacts tumor microenvironment T-lymphocyte subset recruitment: a possible mechanism of tumor escape

open access: yes, 2018
Christian Garbar,1,2 Corinne Mascaux,1,2 Yacine Merrouche,1,2 Armand Bensussan3 1Biopathology Department, Institut Jean Godinot – Unicancer, Reims, France; 2DERM-I-C EA7319, Université de Reims Champagne – Ardenne, Reims, France ...
Mascaux C   +3 more
core  

Systemic blockade of sialylation in mice with a global inhibitor of sialyltransferases

open access: yes, 2014
Sialic acid terminates glycans of glycoproteins and glycolipids that play numerous biological roles in health and disease. Although genetic tools are available for interrogating the effects of decreased or abolished sialoside expression in mice ...
Rillahan, Cory D.   +8 more
core   +1 more source

Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis

open access: yesNature Communications, 2016
Post-translational modifications, such as glycosylation and sialylation, are thought to confer disease modifying effects on autoimmune-associated antibodies, including anti-citrullinated protein antibodies in rheumatoid arthritis.
Yuhsuke Ohmi   +18 more
doaj   +1 more source

Ablation of ST6Gal-I Downregulates BACE1 Expression and Suppresses Production of Aβ42 Plaques in Alzheimer’s Disease

open access: yesEngineering
Recent studies indicate the involvement of glycosylation in the pathogenesis of Alzheimer’s disease (AD). α2,6-Sialylation, catalyzed by α2,6-sialyltransferase-I (ST6Gal-I), corresponds to the development of the infant brain and nervous system, however ...
Kangkang Yang   +6 more
doaj   +1 more source

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