Synaptic and epidermal accumulations of human acetylcholinesterase are encoded by alternative 3'-terminal exons. - Wikidata - awgldk - TriplyDB

Synaptic and epidermal accumulations of human acetylcholinesterase are encoded by alternative 3'-terminal exons.

Synaptic and epidermal accumulations of human acetylcholinesterase are encoded by alternative 3'-terminal exons.

http://www.wikidata.org/entity/Q40016340

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Acetylcholinesterase-R increases germ cell apoptosis but enhances sperm motility Alzheimer's disease: Targeting the Cholinergic System Human osteogenesis involves differentiation-dependent increases in the morphogenically active 3' alternative splicing variant of acetylcholinesterase.Genetic predisposition to adverse consequences of anti-cholinesterases in 'atypical' BCHE carriers.From brain to blood: alternative splicing evidence for the cholinergic basis of Mammalian stress responses.Functional redundancy of acetylcholinesterase and neuroligin in mammalian neuritogenesis Excess "read-through" acetylcholinesterase attenuates but the "synaptic" variant intensifies neurodeterioration correlates.Plant-derived human acetylcholinesterase-R provides protection from lethal organophosphate poisoning and its chronic aftermath.New treatments for myasthenia: a focus on antisense oligonucleotides.Localization of mRNAs encoding acetylcholinesterase and butyrylcholinesterase in the rat spinal cord by nonradioactive in situ hybridization.Developmental regulation of acetylcholinesterase transcripts in the mouse diaphragm: alternative splicing and focalization.A paradigm for single nucleotide polymorphism analysis: the case of the acetylcholinesterase gene.Expression of recombinant human acetylcholinesterase in transgenic tomato plants.Rat serum carboxylesterase partly hydrolyses gamma-butyrobetaine esters.Antisense treatment for myasthenia gravis: experience with monarsen.Molecular isoform distribution and glycosylation of acetylcholinesterase are altered in brain and cerebrospinal fluid of patients with Alzheimer's disease.

P2860

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P2860

Synaptic and epidermal accumulations of human acetylcholinesterase are encoded by alternative 3'-terminal exons.

http://www.wikidata.org/entity/Q40016340

description

1995 nî lūn-bûn

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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1995年论文

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1995年论文

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name

Synaptic and epidermal accumul ...... alternative 3'-terminal exons.

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Synaptic and epidermal accumul ...... alternative 3'-terminal exons.

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Synaptic and epidermal accumul ...... alternative 3'-terminal exons.

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Molecular and Cellular Biology

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Synaptic and epidermal accumul ...... alternative 3'-terminal exons.

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P2093

Ben Aziz-Aloya R

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Kaufer-Nachum D

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Seidman S

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Soreq H

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Sternfeld M

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Timberg R

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P2860

Expression of a human acetylcholinesterase promoter-reporter construct in developing neuromuscular junctions of Xenopus embryos

Molecular cloning and construction of the coding region for human acetylcholinesterase reveals a G + C-rich attenuating structure

Molecular and cellular biology of cholinesterases

Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression

Cloning and expression of a rat acetylcholinesterase subunit: generation of multiple molecular forms and complementarity with a Torpedo collagenic subunit

Electron microscope radioautography as a quantitative tool in enzyme cytochemistry. I. The distribution of acetylcholinesterase at motor end plates of a vertebrate twitch muscle.

Intramolecular relationships in cholinesterases revealed by oocyte expression of site-directed and natural variants of human BCHE.

Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells.

Complex alternative splicing of acetylcholinesterase transcripts in Torpedo electric organ; primary structure of the precursor of the glycolipid-anchored dimeric form.

H and T subunits of acetylcholinesterase from Torpedo, expressed in COS cells, generate all types of globular forms

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2993-3002

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10.1128/MCB.15.6.2993

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6

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15

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7760797

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230530

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