Results 41 to 50 of about 7,639 (223)

Structural and functional characterisation of human sulfotransferases [PDF]

open access: yes, 1998
The human aryl sulfotransferases HAST4 and HAST4v vary by only two amino acids but exhibit markedly different affinity towards the sulfonate acceptor p-nitrophenol and the sulfonate donor 3'-phosphoadenosine-5'-phosphosulfate (PAPS).
McManus, M. E.   +3 more
core   +1 more source

Chondroitin / dermatan sulfate modification enzymes in zebrafish development.

open access: yesPLoS ONE, 2015
Chondroitin/dermatan sulfate (CS/DS) proteoglycans consist of unbranched sulfated polysaccharide chains of repeating GalNAc-GlcA/IdoA disaccharide units, attached to serine residues on specific proteins.
Judith Habicher   +6 more
doaj   +1 more source

Identification of Human Sulfotransferases Active towards Silymarin Flavonolignans and Taxifolin

open access: yesMetabolites, 2020
Natural phenolic compounds are known to be metabolized by phase II metabolic reactions. In this study, we examined the in vitro sulfation of the main constituents of silymarin, an herbal remedy produced from the fruits of the milk thistle.
Jiří Vrba   +5 more
doaj   +1 more source

Carrageenan biosynthesis in red algae: A review

open access: yesThe Cell Surface, 2023
In this review, we summarize the current state of knowledge on the biosynthesis of carrageenan by exploring both the enzyme activities and their localizations.
Antonin Chevenier   +2 more
doaj   +1 more source

Computational Analysis of Chemical Space of Natural Compounds Interacting with Sulfotransferases

open access: yesMolecules, 2021
The aim of this study was to investigate the chemical space and interactions of natural compounds with sulfotransferases (SULTs) using ligand- and structure-based in silico methods.
Iglika Lessigiarska   +10 more
doaj   +1 more source

Photoaffinity labeling of human recombinant sulfotransferases with 2-azidoadenosine 3′,5′-[5′-32P]bisphosphate

open access: yes, 1996
Photoaffinity labeling with 2-azidoadenosine 3′,5′-[5′-P]bisphosphate was used to identify and characterize adenosine 3′,5′-bisphosphate-binding proteins in human liver cytosol and recombinant sulfotransferase proteins. The sulfotransferases investigated
Veronese, Maurice E.   +17 more
core   +1 more source

Understanding the substrate specificity of the heparan sulfate sulfotransferases by an integrated biosynthetic and crystallographic approach [PDF]

open access: yes, 2012
Heparan sulfates (HSs) have potential therapeutic value as anti-inflammatory and antimetastasis drugs, in addition to their current use as anticoagulants.
Moon, Andrea   +3 more
core   +1 more source

Carbohydrate sulfotransferases: mediators of extracellular communication

open access: yes, 1999
Sulfated carbohydrates mediate diverse extracellular recognition events in both normal and pathological processes. The sulfotransferases that generate specific carbohydrate ‘sulfoforms’ have recently been recognized as key modulators of these processes ...
Bowman, Kendra G, Bertozzi, Carolyn R
core   +1 more source

The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties

open access: yesFrontiers in Cell and Developmental Biology, 2020
Heparan sulfate (HS) is a glycosaminoglycan found mainly in its protein-conjugated form at the cell surface and the extracellular matrix. Its high sulfation degree mediates functional interactions with positively charged amino acids in proteins.
Felipe C. O. B. Teixeira   +11 more
doaj   +1 more source

CHST1 Drives Immunotherapy Resistance in Triple‐Negative Breast Cancer by Orchestrating an Immunosuppressive Microenvironment via the NKRF–CCL20–Macrophage Axis

open access: yesAdvanced Science, EarlyView.
Proposed model of CHST1‐associated immune remodeling in triple‐negative breast cancer. In CHST1‐low tumors, greater nuclear accumulation of NKRF is associated with repression of an NF‐κB‐related CCL20 transcriptional program and an immune‐inflamed microenvironment.
Shu‐Hao Jiang   +6 more
wiley   +1 more source

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