ArticleThe FEBS journal2012
The proline-rich tetramerization peptides in equine serum butyrylcholinesterase.
Article in The FEBS journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- Insights from analyses of low complexity regions with canonical methods for protein sequence comparison.Briefings in bioinformatics · 2022Article
- Cholinesterases in Tripartite Neuromuscular Synapse.Frontiers in molecular neuroscience · 2021Review
- Polyproline-rich peptides associated with Torpedo californica acetylcholinesterase tetramers.Chemico-biological interactions · 2020Article
- Identification of Carboxylesterase, Butyrylcholinesterase, Acetylcholinesterase, Paraoxonase, and Albumin Pseudoesterase in Guinea Pig Plasma through Nondenaturing Gel Electrophoresis.Comparative medicine · 2018Article
- Characterization of butyrylcholinesterase from porcine milk.Archives of biochemistry and biophysics · 2018Article
- Article
- Thermoresponsive and Mechanical Properties of Poly(L-proline) Gels.Biomacromolecules · 2016Article
- Transient Expression of Tetrameric Recombinant Human Butyrylcholinesterase in Nicotiana benthamiana.Frontiers in plant science · 2016Article
- Oligomerization status influences subcellular deposition and glycosylation of recombinant butyrylcholinesterase in Nicotiana benthamiana.Plant biotechnology journal · 2014Article
- Most acetylcholinesterase activity of non-nervous tissues and cells arises from the AChE-H transcript.Journal of molecular neuroscience : MN · 2014Article
- Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.Chemico-biological interactions · 2014Article
- Polyproline tetramer organizing peptides in fetal bovine serum acetylcholinesterase.Biochimica et biophysica acta · 2013Article
- Chemical polysialylation of human recombinant butyrylcholinesterase delivers a long-acting bioscavenger for nerve agents in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Soluble, tetrameric, plasma butyrylcholinesterase from horse has previously been shown to include a non-covalently attached polyproline peptide in its structure. The polyproline peptide matched the polyproline-rich region of human lamellipodin. Our goal was to examine the tetramer-organizing peptides of horse butyrylcholinesterase in more detail. Horse butyrylcholinesterase was denatured by boiling, thus releasing a set of polyproline peptides ranging in mass from 1173 to 2098 Da. The peptide sequences were determined by fragmentation in MALDI-TOF-TOF and linear ion trap quadrupole Orbitrap mass spectrometers. Twenty-seven polyproline peptides grouped into 13 families were identified. Peptides contained a minimum of 11 consecutive proline residues and as many as 21. Many of the peptides had a non-proline amino acid at the N-terminus. A search of the protein databanks matched peptides to nine proteins, although not all peptides matched a known protein. It is concluded that polyproline peptides of various lengths and sequences are included in the tetramer structure of horse butyrylcholinesterase. The function of these polyproline peptides is to serve as tetramer-organizing peptides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.