Results 161 to 170 of about 26,182 (278)

Chemical Syntheses of α-Linked Disaccharides [PDF]

open access: bronze, 1973
R. U. Lemieux   +2 more
openalex   +1 more source

Comprehensive synthesis and anticoagulant evaluation of a diverse fucoidan library. [PDF]

open access: yesNat Commun
Chen SC   +10 more
europepmc   +1 more source

Involvement of GTPases and vesicle adapter proteins in Heparan sulfate biosynthesis: role of Rab1A, Rab2A and GOLPH3

open access: yesThe FEBS Journal, Volume 292, Issue 9, Page 2237-2250, May 2025.
Vesicle trafficking governs the biosynthesis of heparan sulfate (HS) by controlling the positioning of HS‐modifying enzymes within Golgi compartments. The proteins Rab1A and Rab2A play dynamic, compensatory roles that affect HS levels by influencing the transport of these enzymes.
Maria C. Z. Meneghetti   +4 more
wiley   +1 more source

Realizing the promise of ‘La Dolce Vita’ via chemical biology: glycan‐motif editing of sLeX for precision cancer therapeutics

open access: yesThe FEBS Journal, EarlyView.
Modification of the glycocalyx via ‘glycan editing’ is distinguishable from ‘glycan‐motif editing’. The former broadly remodels the glycocalyx, whereas the latter inhibits expression only of a specific oligosaccharide motif within the glycocalyx by selectively dampening the bioactivity of the key glycosyltransferase(s) programming the biosynthesis of ...
Barbara Richichi, Robert Sackstein
wiley   +1 more source

Relationship Between FODMAP Diet and Irritable Bowel Syndrome: A Mendelian Randomization Study. [PDF]

open access: yesFood Sci Nutr
Wang L   +10 more
europepmc   +1 more source

Structural and functional insights into extreme thermal stability and activity of two GH12 domains of a multidomain glycosidase from a hyperthermophilic euryarchaeon

open access: yesThe FEBS Journal, EarlyView.
The multidomain glycosidase MDG from the hyperthermophilic euryarchaeon Thermococcus sp. contains five protein domains: three catalytic domains (GH5, GH12‐1, and GH12‐2) and two cellulose‐binding modules (CBM2). In this study, the GH12‐1 and GH12‐2 domains were individually purified and biochemically characterized.
Kseniya S. Zayulina   +11 more
wiley   +1 more source

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