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Literature summary for 2.4.1.1 extracted from

  • Eronina, T.B.; Chebotareva, N.A.; Kurganov, B.I.
    Influence of osmolytes on inactivation and aggregation of muscle glycogen phosphorylase b by guanidine hydrochloride. Stimulation of protein aggregation under crowding conditions (2005), Biochemistry (Moscow), 70, 1020-1026.
    View publication on PubMed

Application

Application Comment Organism
biotechnology study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
guanidine hydrochloride study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
isoform phosphorylase b
-

Renatured (Commentary)

Renatured (Comment) Organism
study on kinetics of inactivation and aggregation at 0.7 M guanidine hydrochloride. Osmolytes trimethylamine-N-oxide and betaine exhibit the highest protective efficacy against phosphorylase b inactivation. Test system for the study of the effects of macromolecular crowding induced by osmolytes on aggregation of proteins Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle Oryctolagus cuniculus
-