Results 171 to 180 of about 10,478,036 (300)

Congenital disorders of glycosylation. Part II. Defects of protein O-glycosylation

open access: yes, 2013
Glycosylation is a form of post-translational modification of proteins and occurs in every living cell. The carbohydrate chains attached to the proteins serve various functions.
Chrostek, Lech   +3 more
core  

Plant secondary metabolites: flavonoids and their glycosylation modification

open access: yes
Flavonoids are a class of phenolic compounds that are widely distributed in nature. They have a variety of physiological and pharmacological activities. They exist in free form or in the form of glycosides.
K. Lei   +5 more
core   +1 more source

Glycoproteomics and Its Role in Understanding Bacterial O-Linked Glycosylation

open access: yes
Protein glycosylation is now recognized as a ubiquitous process observed in all domains of life. Within bacterial species, carbohydrates can be attached to multiple residues with glycosylation of serine, threonine, or tyrosine residues via their hydroxyl
Karlic, KI, Tahir, H, Scott, NE
core   +1 more source

Protein O-Glycosylation in Yeast [PDF]

open access: yesJournal of Biological Chemistry, 1995
Marc Lussier   +4 more
openaire   +1 more source

SlSEC1- and SlSPY-mediated O-glycosylation stabilizes the transcription factor SlNOR to promote tomato fruit ripening. [PDF]

open access: yesPlant Cell
Wu YD   +18 more
europepmc   +1 more source

Erratum to Loss of GalNAc-T14 links O-glycosylation defects to alterations in B cell homing in IgA nephropathy. [PDF]

open access: yesJ Clin Invest
Prakash S   +34 more
europepmc   +1 more source

Late‐Stage Functionalization of Peptides on the Solid Phase

open access: yesAngewandte Chemie International Edition, EarlyView.
Peptide modifications are essential to control pharmacodynamic and pharmacokinetic properties of peptide drugs. Consequently, strategies that allow for efficient and rapid incorporation of non‐canonical modifications into peptides in parallel formats are highly sought after.
Marius Werner   +2 more
wiley   +1 more source

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