Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
about
The synaptic acetylcholinesterase tetramer assembles around a polyproline II helixHuman butyrylcholinesterase produced in insect cells: huprine-based affinity purification and crystal structureConformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallographyCrystallization and X-ray structure of full-length recombinant human butyrylcholinesteraseCocrystallization studies of full-length recombinant butyrylcholinesterase (BChE) with cocaineA mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha,beta-hydrolase fold protein familyTargeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunitEffect of human acetylcholinesterase subunit assembly on its circulatory residenceEvolution of acetylcholinesterase and butyrylcholinesterase in the vertebrates: an atypical butyrylcholinesterase from the Medaka Oryzias latipes.Use of a novel radiometric method to assess the inhibitory effect of donepezil on acetylcholinesterase activity in minimally diluted tissue samplesThe PRiMA-linked cholinesterase tetramers are assembled from homodimers: hybrid molecules composed of acetylcholinesterase and butyrylcholinesterase dimers are up-regulated during development of chicken brainTetrameric mouse acetylcholinesterase: continuum diffusion rate calculations by solving the steady-state Smoluchowski equation using finite element methods.The proline-rich tetramerization peptides in equine serum butyrylcholinesteraseThe C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathwayHis-tag truncated butyrylcholinesterase as a useful construct for in vitro characterization of wild-type and variant butyrylcholinesterases.Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana.A plaidoyer for cutaneous enzymology: our view of some important unanswered questions on the contributions of selected key enzymes to epidermal homeostasis.The butyrylcholinesterase K variant confers structurally derived risks for Alzheimer pathology.Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.Molecular Assembly and Biosynthesis of Acetylcholinesterase in Brain and Muscle: the Roles of t-peptide, FHB Domain, and N-linked Glycosylation.Neuronal AChE splice variants and their non-hydrolytic functions: redefining a target of AChE inhibitors?Reassessment of the role of the central cholinergic system.Bovine acetylcholinesterase: cloning, expression and characterization.Plant-expressed cocaine hydrolase variants of butyrylcholinesterase exhibit altered allosteric effects of cholinesterase activity and increased inhibitor sensitivityRadiometric assay of ghrelin hydrolase activity and 3H-ghrelin distribution into mouse tissuesModel of human butyrylcholinesterase tetramer by homology modeling and dynamics simulation.Elements of the C-terminal t peptide of acetylcholinesterase that determine amphiphilicity, homomeric and heteromeric associations, secretion and degradation.Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase: expression, purification, characterization and crystallization.Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase.Proline-Rich Chaperones Are Compared Computationally and Experimentally for Their Abilities to Facilitate Recombinant Butyrylcholinesterase Tetramerization in CHO Cells.Breast cancer metastasis alters acetylcholinesterase activity and the composition of enzyme forms in axillary lymph nodes.Polyclonal Antibodies in Microplates to Predict the Maximum Adsorption Activities of Enzyme/Mutants from Cell Lysates.Polyproline promotes tetramerization of recombinant human butyrylcholinesterase.
P2860
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P2860
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@en
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@nl
type
label
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@en
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@nl
prefLabel
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@en
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@nl
P2093
P2860
P356
P1433
P1476
Tetramerization domain of human butyrylcholinesterase is at the C-terminus.
@en
P2093
P2860
P304
P356
10.1042/BJ3270747
P407
P478
327 ( Pt 3)
P577
1997-11-01T00:00:00Z