The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant
about
Effect of chemical modification of recombinant human acetylcholinesterase by polyethylene glycol on its circulatory longevitySubstrate inhibition of acetylcholinesterase: residues affecting signal transduction from the surface to the catalytic centerEffect of human acetylcholinesterase subunit assembly on its circulatory residenceA four-to-one association between peptide motifs: four C-terminal domains from cholinesterase assemble with one proline-rich attachment domain (PRAD) in the secretory pathway.Molecular architecture of acetylcholinesterase collagen-tailed forms; construction of a glycolipid-tailed tetramerEffective protective immunity to Yersinia pestis infection conferred by DNA vaccine coding for derivatives of the F1 capsular antigen.The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathwayH and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular formsRedox regulation of mitochondrial function with emphasis on cysteine oxidation reactions.Interaction of acetylcholinesterase with neurexin-1β regulates glutamatergic synaptic stability in hippocampal neurons.Electrostatic attraction by surface charge does not contribute to the catalytic efficiency of acetylcholinesterase.Bovine acetylcholinesterase: cloning, expression and characterization.Aging of phosphylated human acetylcholinesterase: catalytic processes mediated by aromatic and polar residues of the active centrePlant-expressed cocaine hydrolase variants of butyrylcholinesterase exhibit altered allosteric effects of cholinesterase activity and increased inhibitor sensitivityInvolvement of oligomerization, N-glycosylation and sialylation in the clearance of cholinesterases from the circulation.N-glycosylation of human acetylcholinesterase: effects on activity, stability and biosynthesis.Tetramerization domain of human butyrylcholinesterase is at the C-terminus.The cholinesterase-like domain, essential in thyroglobulin trafficking for thyroid hormone synthesis, is required for protein dimerization.AcCho is hydrolyzed to Cho and acetate by ACHE
P2860
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P2860
The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. Expression of acetylcholinesterase Cys-580----Ala mutant
description
1991 nî lūn-bûn
@nan
1991 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@ast
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@en
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@nl
type
label
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@ast
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@en
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@nl
prefLabel
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@ast
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@en
The effect of elimination of i ...... esterase Cys-580----Ala mutant
@nl
P2093
P1476
The effect of elimination of i ...... sterase Cys-580----Ala mutant.
@en
P2093
A Shafferman
H Grosfeld
Y Flashner
P304
P407
P577
1991-12-15T00:00:00Z