Commit 9e297c11 authored by mk11g11's avatar mk11g11
Browse files

update

parent f973b6ce
......@@ -1739,7 +1739,7 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf},
}
 
@Article{hilf2009,
author = {Hilf, R. J. and Dutzler, R.},
author = {Hilf, R. J. C. and Dutzler, R.},
title = {Structure of a potentially open state of a proton-activated pentameric ligand-gated ion channel},
journal = {Nature},
year = {2009},
......@@ -1749,8 +1749,8 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf},
issn = {1476-4687 (Electronic)
0028-0836 (Linking)},
doi = {10.1038/nature07461},
type = {Journal Article},
url = {http://www.ncbi.nlm.nih.gov/pubmed/18987630},
type = {Journal Article},
}
 
@Article{hille1978,
......@@ -1818,7 +1818,7 @@ http://www.sciencemag.org/content/336/6079/348.full.pdf},
}
 
@Article{huang1999,
author = {Huang, Y. and Williamson, M. S. and Devonshire, A. L. and Windass, J. D. and Lansdell, S. J. and Millar, N. S.},
author = {Huang, Y. and Williamson, M. and Devonshire, A. L. and Windass, J. D. and Lansdell, S. J. and Millar, N. S.},
title = {Molecular characterization and imidacloprid selectivity of nicotinic acetylcholine receptor subunits from the peach-potato aphid Myzus persicae},
journal = {Journal of Neurochemistry},
year = {1999},
......@@ -4014,9 +4014,8 @@ http://www.nature.com/nature/journal/v423/n6943/pdf/nature01748.pdf},
pages = {2017--23},
issn = {0261-4189 (Print)
0261-4189 (Linking)},
url = {http://www.ncbi.nlm.nih.gov/pmc/articles/PMC556666/pdf/emboj00091-0029.pdf},
type = {Journal Article},
url = {http://www.ncbi.nlm.nih.gov/pubmed/1376242
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC556666/pdf/emboj00091-0029.pdf},
}
 
@Article{sims1994,
......@@ -4674,9 +4673,8 @@ http://jcb.rupress.org/content/111/6/2623.full.pdf},
pages = {1101--24},
issn = {0022-2836 (Print)
0022-2836 (Linking)},
url = {http://www.sciencedirect.com/science/article/pii/S0022283683711071},
type = {Journal Article},
url = {http://www.ncbi.nlm.nih.gov/pubmed/8445638
http://www.sciencedirect.com/science/article/pii/S0022283683711071},
}
 
@Article{unwin1995,
......@@ -8002,17 +8000,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
publisher = {Elsevier},
}
 
@Article{jones2007b,
author = {Jones, A. K. and Davis, P. and Hodgkin, J. and Sattelle, D. B.},
title = {The nicotinic acetylcholine receptor gene family of the nematode Caenorhabditis elegans: an update on nomenclature},
journal = {Invertebrate Neuroscience},
year = {2007},
volume = {7},
number = {2},
pages = {129--131},
publisher = {Springer},
}
@Article{taylor1978,
author = {Taylor, A. L. and Sasser, J. N.},
title = {Biology, identification and control of root-knot nematodes},
......@@ -11049,17 +11036,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
publisher = {Rockefeller University Press},
}
 
@Article{hilf2008a,
author = {Hilf, Ricarda JC and Dutzler, Raimund},
title = {X-ray structure of a prokaryotic pentameric ligand-gated ion channel},
journal = {Nature},
year = {2008},
volume = {452},
number = {7185},
pages = {375},
publisher = {Nature Publishing Group},
}
@Article{tamkun1986,
author = {Tamkun, John W and DeSimone, Douglas W and Fonda, Deborah and Patel, Ramila S and Buck, Clayton and Horwitz, Alan F and Hynes, Richard O},
title = {Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin},
......@@ -12620,7 +12596,7 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
}
 
@Article{alkondon2000,
author = {Alkondon, M and Pereira, E F and Eisenberg, H M and Albuquerque, E X},
author = {Alkondon, M. and Pereira, E. F. and Eisenberg, H. M. and Albuquerque, E. X.},
title = {Nicotinic receptor activation in human cerebral cortical interneurons: a mechanism for inhibition and disinhibition of neuronal networks.},
journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience},
year = {2000},
......@@ -14835,7 +14811,7 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
}
 
@Online{eu2019a,
author = {The European Commission},
author = {The European Commission.},
title = {EU Pesticides database. Entry for Sulfoxaflor.},
year = {Accessed 01 Sep 2019},
date = {2019},
......@@ -16488,7 +16464,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
pages = {173--179},
issn = {0006-8993},
doi = {10.1016/0006-8993(87)91234-0},
__markedentry = {[monik:]},
abstract = {Immunohistochemistry of the locust central nervous system with antibody to choline acetyltransferase (ChAT) purified from the same species shows: first, there are relatively few immunoreactive cell bodies in the CNS; and second, sensory neuropiles, such as the ventral association centre and the ventral VAC (vVAC), the anterior ring tract, the tritocerebrum and the antennal lobe, are immunoreactive. That ChAT is contained in sensory neurones is suggested by immunoreactivity found in peripheral neurone cell bodies. These results indicate that acetylcholine serves primarily as a sensory transmitter in the locust.},
chemicals = {Choline O-Acetyltransferase},
citation-subset = {IM},
......@@ -16526,7 +16501,6 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
pages = {533--543},
issn = {0021-9967},
doi = {10.1002/cne.902800404},
__markedentry = {[monik:6]},
abstract = {In situ hybridization with radiolabeled complementary RNA (cRNA) probes was used to determine the location of the messenger RNA (mRNA) encoding choline acetyltransferase (ChAT) in Drosophila nervous system. Areas in the cell-rich cortical regions of the cerebrum and optic lobes hybridized with substantial concentrations of the probe. This contrasted with the cell-sparse neuropil areas where no significant concentrations of probe were observed. Although most of the cortical regions were substantially labeled, there were regions within all of the areas where labeling was sparse or nonexistent. For example in the lamina, even though the monopolar cell layer appeared to be heavily labeled, there were some neuronal profiles that were not associated with the probe. Moreover, the epithelial glia that form an arch of cell profiles subjacent to the monopolar cells were not labeled, nor were amacrine neurons in the apex of the lamina near the external optic chiasma. The highest concentration of probe (approximately 140 grains/400 microns2) was observed in the laminar monopolar cell region and the cerebral cortical rind. The next most heavily labeled region (approximately 90 grains/400 microns2) occurred over cortical cells of the medulla-lobula. In the peripheral nervous system, label over the antennal sensory neurons amounted to about 75 grains/400 microns2, and the retinular cell layer of the compound eye exhibited about 60 grains/400 microns2. The control probe did not hybridize in significant quantities in either cellular or noncellular regions. This study presents evidence that large numbers of Drosophila cortical and primary sensory neurons contain the messenger RNA necessary for the production of ChAT, the acetylcholine-synthesizing enzyme. Further, our findings provide baseline information for use in ontogenetic studies of cholinergic neurons in Drosophila, and they also provide normative data for studying the effects of mutant alleles at the Cha or Ace loci upon the transcription of ChAT messenger RNA.},
chemicals = {RNA, Messenger, Choline O-Acetyltransferase},
citation-subset = {IM},
......@@ -16542,8 +16516,8 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
revised = {2007-11-14},
}
 
@Article{yasuyama 1999,
author = {Yasuyama K,. Salvaterra P. M.},
@Article{yasuyama1999,
author = {Yasuyama, K. Salvaterra, P. M.},
title = {Localization of choline acetyltransferase-expressing neurons in Drosophila nervous system.},
journal = {Microsc Res Tech},
date = {1999},
......@@ -16553,4 +16527,838 @@ http://www.sciencemag.org/content/336/6079/351.full.pdf},
pages = {65-79},
}
 
@Article{hill1910,
author = {Hill, A. V.},
title = {The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves},
journal = {Journal of Physiology},
date = {1910},
volume = {40},
pages = {4-7},
}
@Article{hall1976,
author = {Hall, J. C. and Kankel, D. R.},
title = {Genetics of acetylcholinesterase in Drosophila melanogaster.},
journal = {Genetics},
year = {1976},
volume = {83},
issue = {3 PT.2},
month = jul,
pages = {517--535},
issn = {0016-6731},
abstract = {Genes in Drosophila melanogaster that control acetylcholinesterase (AChE) were searched for by segmental aneuploidy techniques. Homogenates of flies containing duplications or deletions for different segments were assayed for enzyme activity. A region on the third chromosome was found for which flies having one dose consistently gave lower AChE activity than euploid flies, which in turn had lower activity than flies with three doses. The activity differences were in the approximate ratio 1:2:3. Fine structure deletion mapping within this region revealed a very small segment for which one-dose flies have approximately half-normal activity. To obtain putative AchE-null mutations, lethal mutations within this region were assayed. Four allelic lethals have approximately half-normal activity in heterozygous condition. These lethals probably define the structural locus (symbol: Ace) for AchE.},
chemicals = {Acetylcholinesterase},
citation-subset = {IM},
completed = {1976-10-20},
country = {United States},
issn-linking = {0016-6731},
keywords = {Acetylcholinesterase, metabolism; Aneuploidy; Animals; Chromosome Aberrations; Drosophila melanogaster, enzymology; Genes; Genes, Lethal; Genes, Recessive; Genotype; Phenotype},
nlm-id = {0374636},
owner = {NLM},
pmc = {PMC1213530},
pmid = {821817},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2018-11-13},
}
@Article{greenspan1980,
author = {Greenspan, R. J. and Finn, J. A. and Hall, J. C.},
title = {Acetylcholinesterase mutants in Drosophila and their effects on the structure and function of the central nervous system.},
journal = {The Journal of comparative neurology},
year = {1980},
volume = {189},
issue = {4},
month = feb,
pages = {741--774},
issn = {0021-9967},
doi = {10.1002/cne.901890409},
abstract = {Mutations that eliminate acetylcholinesterase (AChE) activity were used to study the effects of disrupted acetylcholine metabolism on the form and function of the central nervous system in Drosophila melanogaster. Mutants in the Ace gene, which have no AChE activity, usually die in early development, but the postembryonic effects of this lesion can be studied in genetic mosaics, or with conditional mutants. Adult mosaics, which expressed Ace mutations in part of their CNS, exhibited morphological defects in any ganglionic neuropile whose cells were mutant. The defects included reduction in ganglionic volume, a condensed appearance, and for a very large clone, degeneration. Examination of many such mosaics indicated that small clones restricted to one side of the CNS were not usually lethal. However, mosaics with large clones, with clones on either side of the posterior slope of the protocerebrum, or with clones encompassing symmetrical structures on both sides of the CNS rarely survived to adulthood. Mosaics with AChE-null tissue on either side of the optic lobes or the posterior-inferior protocerebrum had marked deficits in optomotor behavior, although they were outwardly normal in their movement and posture. Mosaics with Ace mutant tissue in the first-order optic lobe, the lamina, lacked a synaptic component of the electroretinogram, the "off" transient. Tests of courtship behavior revealed that AChE mosaics with mutant clones in the superior protocerebrum were often capable of demonstrating male courtship. However, their behavior was quantitatively and perhaps qualitatively deficient. In order to study critical periods for the effects of mutant AChE, temperature-sensitive mutations of the Ace gene were isolated. Flies bearing certain of these new mutations produced AchE activity that was thermolabile in vivo and in vitro. The critical period during which the mutants were most susceptible to conditional lethality was late in embryogenesis.},
chemicals = {Acetylcholinesterase},
citation-subset = {IM},
completed = {1980-08-15},
country = {United States},
issn-linking = {0021-9967},
keywords = {Acetylcholinesterase, deficiency, genetics, physiology; Animals; Drosophila melanogaster, physiology; Electroretinography; Female; Genes, Lethal; Male; Mosaicism; Movement; Mutation; Nervous System, enzymology; Retina, physiology; Sexual Behavior, Animal, physiology; Temperature},
nlm-id = {0406041},
owner = {NLM},
pmid = {6769980},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2006-11-15},
}
@Article{slemmon1982,
author = {Slemmon, J. R. and Salvaterra, P. M. and Crawford, G. D. and Roberts, E.},
title = {Purification of choline acetyltransferase from Drosophila melanogaster.},
journal = {The Journal of biological chemistry},
year = {1982},
volume = {257},
issue = {7},
month = apr,
pages = {3847--3852},
issn = {0021-9258},
abstract = {Choline acetyltransferase (EC 2.3.1.6) from Drosophila melanogaster (Canton S, wild type) was purified 12,500-fold to a final specific activity of 500 mumol min-1 mg protein-1. The purification used homogenized fly heads and consisted of polyethylene glycol precipitation, DEAE-Bio-Gel A chromatography, Octyl-Sepharose chromatography, and affinity chromatography using solid phase Green A-agarose. The molecular weight of the native enzyme, as determined by molecular exclusion chromatography, was approximately 67,000 daltons. The final enzyme preparation showed two major protein bands at 67,000 and 54,000 daltons on polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS). After molecular exclusion chromatography, both SDS gel bands were present in the single symmetrical peak that contained the enzyme activity. Two-dimensional tryptic peptide maps prepared from the individual SDS gel bands indicated that they have very similar primary structures. Both SDS gel bands were precipitated by two different monoclonal antibodies derived against Drosophila choline acetyltransferase activity. The structural and immunological relatedness of the two SDS gel bands indicates that the enzyme is essentially homogeneous and that, in the native state, it may consist of more than one polypeptide chain.},
chemicals = {Antigen-Antibody Complex, Immune Sera, Peptide Fragments, Choline O-Acetyltransferase, Trypsin},
citation-subset = {IM},
completed = {1982-05-27},
country = {United States},
issn-linking = {0021-9258},
keywords = {Amino Acid Sequence; Animals; Antigen-Antibody Complex; Choline O-Acetyltransferase, isolation & purification, metabolism; Drosophila melanogaster, enzymology; Immune Sera; Kinetics; Molecular Weight; Peptide Fragments, analysis; Trypsin},
nlm-id = {2985121R},
owner = {NLM},
pmid = {6801053},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2007-11-14},
}
@Article{Driskell1978,
author = {Driskell, W J and Weber, B H and Roberts, E},
title = {Purification of choline acetyltransferase from Drosophila melanogaster.},
journal = {Journal of neurochemistry},
year = {1978},
volume = {30},
issue = {5},
month = may,
pages = {1135--1141},
issn = {0022-3042},
doi = {10.1111/j.1471-4159.1978.tb12408.x},
chemicals = {Choline O-Acetyltransferase},
citation-subset = {IM},
completed = {1978-08-28},
country = {England},
issn-linking = {0022-3042},
keywords = {Animals; Choline O-Acetyltransferase, isolation & purification; Drosophila melanogaster, enzymology; Drug Stability; Kinetics},
nlm-id = {2985190R},
owner = {NLM},
pmid = {96214},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2019-06-30},
}
@Article{chao1980,
author = {Chao, L P},
title = {Choline acetyltransferase: purification and characterization.},
journal = {Journal of neuroscience research},
year = {1980},
volume = {5},
issue = {2},
pages = {85--115},
issn = {0360-4012},
doi = {10.1002/jnr.490050202},
chemicals = {Isoenzymes, Choline O-Acetyltransferase},
citation-subset = {IM},
completed = {1980-10-24},
country = {United States},
issn-linking = {0360-4012},
keywords = {Animals; Brain, enzymology; Cattle; Chemical Phenomena; Chemistry; Choline O-Acetyltransferase, antagonists & inhibitors, immunology, isolation & purification; Cockroaches, enzymology; Decapodiformes, enzymology; Drosophila melanogaster, enzymology; Enzyme Activation; Female; Fishes, metabolism; Horseshoe Crabs, enzymology; Humans; Isoenzymes, isolation & purification; Kinetics; Methods; Mice; Placenta, enzymology; Pregnancy; Rats; Snails, enzymology},
nlm-id = {7600111},
owner = {NLM},
pmid = {6772798},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2008-11-21},
}
@Article{Tellam2003,
author = {Tellam, R L and Vuocolo, T and Eisemann, C and Briscoe, S and Riding, G and Elvin, C and Pearson, R},
title = {Identification of an immuno-protective mucin-like protein, peritrophin-55, from the peritrophic matrix of Lucilia cuprina larvae.},
journal = {Insect biochemistry and molecular biology},
year = {2003},
volume = {33},
issue = {2},
month = feb,
pages = {239--252},
issn = {0965-1748},
abstract = {A mucin-like glycoprotein, peritrophin-55 was isolated and purified from the peritrophic matrix of Lucilia cuprina larvae. When injected into sheep, peritrophin-55 induced an immune response that inhibited larval growth by 51-66% when larvae subsequently fed on sera from the vaccinated sheep. The protein may have potential use as an immunogen probably accompanying other antigens to protect sheep from the cutaneous myiasis caused by these larvae. Peritrophin-55 was uniformly distributed throughout the peritrophic matrix where it probably lubricates the surface of the peritrophic matrix and protects the midgut from invasion by bacteria. The protein consists of an 8-cysteine amino-terminal domain (peritrophin-B domain) and a carboxy-terminal proline and threonine-rich domain with high probability for extensive O-linked glycosylation. The gene consists of two exons separated by a small intron. Peritrophin-55 mRNA was only detected in the larval cardia and midgut and to a minor extent in the hindgut. Sequence upstream of the transcriptional start site contained a putative promoter region, sequence similar to an ecdysone response element, sequence related to the Drosophila transposon S element and a tetranucleotide repeat region. A putative Drosophila melanogaster ortholog or paralog of peritrophin-55 (CG7714) was located within a 3458 bp intron of the Cha gene (choline-O-acetyltransferase), but on the opposite strand. Comparison of the putative promoter regions of the peritrophin-55 and CG7714 genes revealed little similarity except for a small semi-conserved sequence that is suggestive of a common transcription factor-binding site possibly contributing to the highly restricted developmental and tissue-specific expression patterns of these genes.},
chemicals = {Insect Proteins, Membrane Glycoproteins, Mucins, Peptide Fragments, peritrophin-55 protein, Lucilia cuprina},
citation-subset = {IM},
completed = {2003-04-17},
country = {England},
issn-linking = {0965-1748},
keywords = {Amino Acid Sequence; Animals; Base Sequence; Diptera, immunology; Insect Proteins, chemistry, genetics, isolation & purification; Larva; Membrane Glycoproteins, chemistry, genetics, isolation & purification; Molecular Sequence Data; Mucins, isolation & purification; Peptide Fragments, chemistry; Reverse Transcriptase Polymerase Chain Reaction},
nlm-id = {9207282},
owner = {NLM},
pii = {S0965174802002084},
pmid = {12535682},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2006-11-15},
}
@Article{hsiao2004,
author = {Hsiao, Y. and Lai, J. and Liao, Hsiu-Y. and Feng, Hai-T.},
title = {Purification and characterization of acetylcholinesterase from oriental fruit fly [Bactrocera dorsalis (Hendel)](Diptera: Tephritidae)},
journal = {Journal of agricultural and food chemistry},
year = {2004},
volume = {52},
number = {17},
pages = {5340--5346},
publisher = {ACS Publications},
}
@Article{harel2000,
author = {Harel, M. and Kryger, G. and Rosenberry, T. L. and Mallender, W. D. and Lewis, T. and Fletcher, R. J. and Guss, J. M. and Silman, I. and Sussman, J. L.},
title = {Three-dimensional structures of Drosophila melanogaster acetylcholinesterase and of its complexes with two potent inhibitors},
journal = {Protein Science},
year = {2000},
volume = {9},
number = {6},
pages = {1063--1072},
publisher = {Cambridge University Press},
}
@Article{kerkut1970,
author = {Kerkut, G. A. and Oliver, G. W. O. and Rick, J. T. and Walker, R. J.},
title = {The effects of drugs on learning in a simple preparation},
journal = {Comparative and general pharmacology},
year = {1970},
volume = {1},
number = {4},
pages = {437--484},
publisher = {Elsevier},
}
@Article{carlyle1963,
author = {Carlyle, R. F.},
title = {The mode of action of neostigmine and physostigmine on the guinea-pig trachealis muscle},
journal = {British journal of pharmacology and chemotherapy},
year = {1963},
volume = {21},
number = {1},
pages = {137--149},
publisher = {Wiley Online Library},
}
@Article{greenspan1980b,
author = {Greenspan, R. J.},
title = {Mutations of choline acetyltransferase and associated neural defects},
journal = {Journal of comparative physiology},
year = {1980},
volume = {137},
number = {1},
pages = {83--92},
publisher = {Springer},
}
@Article{pahud1998,
author = {Pahud, G. and Salem, N. and Van De Goor, J. and Medilanski, J. and Pellegrinelli, N. and Eder-Colli, L.},
title = {Study of subcellular localization of membrane-bound choline acetyltransferase in Drosophila central nervous system and its association with membranes},
journal = {European Journal of Neuroscience},
year = {1998},
volume = {10},
number = {5},
pages = {1644--1653},
publisher = {Wiley Online Library},
}
@Article{lutz1988,
author = {Lutz, E. M. and Lloyd, S. J. and Tyrer, N. M.},
title = {Purification of choline acetyltransferase from the locust Schistocerca gregaria and production of serum antibodies to this enzyme},
journal = {Journal of neurochemistry},
year = {1988},
volume = {50},
number = {1},
pages = {82--89},
publisher = {Wiley Online Library},
}
@Article{fabian1997,
author = {Fabian, R. and Seyfarth, Ernst-A.},
title = {Acetylcholine and histamine are transmitter candidates in identifiable mechanosensitive neurons of the spider Cupiennius salei: an immunocytochemical study},
journal = {Cell and tissue research},
year = {1997},
volume = {287},
number = {2},
pages = {413--423},
publisher = {Springer},
}
@Article{kitamoto1998,
author = {Kitamoto, T. and Wang, W. and Salvaterra, P. M.},
title = {Structure and organization of the Drosophila cholinergic locus.},
journal = {The Journal of biological chemistry},
year = {1998},
volume = {273},
issue = {5},
month = jan,
pages = {2706--2713},
issn = {0021-9258},
doi = {10.1074/jbc.273.5.2706},
abstract = {The Drosophila cholinergic locus is composed of two distinct genetic functions: choline acetyltransferase (ChAT; EC 2.3.1.6), the enzyme catalyzing biosynthesis of neurotransmitter acetylcholine (ACh), and the vesicular ACh transporter (VAChT), the synaptic vesicle membrane protein which pumps transmitter into vesicles. Both genes share a common first exon and the remainder of the VAChT gene contains a single coding exon residing entirely within the first intron of ChAT. RNase protection analysis indicates that all Drosophila VAChT specific transcripts contain the shared first exon and suggests common transcriptional control for ChAT and VAChT. Similar types of genomic organization have been evolutionarily conserved for cholinergic loci in nematodes and vertebrates, and may operate to ensure coordinate expression of these functionally related genes in the same cells. The relative levels of Drosophila ChAT and VAChT mRNA differ, however, in different tissues or in Cha mutants, indicating that independent regulation of ChAT and VAChT transcripts may occur post-transcriptionally. The predicted Drosophila VAChT protein is composed of 578 amino acids and contains 12 conserved putative transmembrane domains. Full-length VAChT cDNA is 7.2 kilobase long and has unusually long 5'- and 3'-untranslated regions (UTR). The 5'-UTR contains a GTG ChAT translational initiation codon along with three other potential ATG initiation codons. These features of the VAChT 5'-UTR region suggest that a ribosome scanning model may not be used for VAChT translation initiation.},
chemicals = {Carrier Proteins, DNA, Complementary, Drosophila Proteins, Membrane Transport Proteins, Nerve Tissue Proteins, RNA Precursors, VAChT protein, Drosophila, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Choline O-Acetyltransferase},
citation-subset = {IM},
completed = {1998-02-23},
country = {United States},
issn-linking = {0021-9258},
keywords = {Amino Acid Sequence; Animals; Base Sequence; Carrier Proteins, biosynthesis, genetics; Choline O-Acetyltransferase, biosynthesis, genetics; Cholinergic Fibers; DNA, Complementary, genetics; Drosophila Proteins; Drosophila melanogaster, genetics; Exons; Genomic Library; Introns; Membrane Transport Proteins; Molecular Sequence Data; Nerve Tissue Proteins, biosynthesis, genetics; Nucleic Acid Conformation; Protein Conformation; RNA Precursors, chemistry, genetics; RNA Processing, Post-Transcriptional; Sequence Homology, Amino Acid; Species Specificity; Transcription, Genetic; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins},
nlm-id = {2985121R},
owner = {NLM},
pmid = {9446576},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2019-05-08},
}
@Article{song1997,
author = {Song, H. and Ming, G. and Fon, E. and Bellocchio, E. and Edwards, R. H. and Poo, M.},
title = {Expression of a putative vesicular acetylcholine transporter facilitates quantal transmitter packaging.},
journal = {Neuron},
year = {1997},
volume = {18},
issue = {5},
month = may,
pages = {815--826},
issn = {0896-6273},
doi = {10.1016/s0896-6273(00)80320-7},
abstract = {A putative vesicular acetylcholine transporter (VAChT) was overexpressed in developing Xenopus spinal neurons by injection of rat VAChT cDNA or synthetic mRNA into Xenopus embryos. This resulted in a marked increase in the amplitude and frequency of miniature excitatory postsynaptic currents at neuromuscular synapses, reflecting an over 10-fold increase in the vesicular packaging of acetylcholine (ACh). The effect appeared in developing neurons even before synaptogenesis and was blocked by L-vesamicol, a specific blocker of ACh uptake into synaptic vesicles. Mutational studies showed that two highly conserved aspartate residues within putative transmembrane domains 4 and 10 are essential for the transport activity. These results provide direct evidence for the physiological function of a putative VAChT and demonstrate that quantal size can be regulated by changes in vesicular transporter activity.},
chemicals = {Carrier Proteins, Membrane Transport Proteins, Neuromuscular Depolarizing Agents, Piperidines, Slc18a3 protein, rat, Synaptophysin, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Aspartic Acid, vesamicol, Acetylcholine},
citation-subset = {IM},
completed = {1997-06-30},
country = {United States},
issn-linking = {0896-6273},
keywords = {Acetylcholine, metabolism; Animals; Aspartic Acid, genetics; Blastomeres; Carrier Proteins, analysis, genetics, metabolism; Cells, Cultured; Embryo, Nonmammalian, chemistry, physiology; Female; Gene Expression Regulation, Developmental, physiology; Membrane Transport Proteins; Microinjections; Muscles, cytology; Mutagenesis, physiology; Nervous System, cytology; Neuromuscular Depolarizing Agents, pharmacology; Neurons, chemistry, physiology, ultrastructure; Patch-Clamp Techniques; Piperidines, pharmacology; Rats; Synapses, chemistry, physiology; Synaptic Transmission, drug effects, physiology; Synaptophysin, analysis; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins; Xenopus laevis},
nlm-id = {8809320},
owner = {NLM},
pii = {S0896-6273(00)80320-7},
pmid = {9182805},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2019-08-22},
}
@Article{varoqui1996,
author = {Varoqui, H. and Erickson, J. D.},
title = {Active transport of acetylcholine by the human vesicular acetylcholine transporter.},
journal = {The Journal of biological chemistry},
year = {1996},
volume = {271},
issue = {44},
month = nov,
pages = {27229--27232},
issn = {0021-9258},
doi = {10.1074/jbc.271.44.27229},
abstract = {The characteristics of ATP-dependent transport of acetylcholine (ACh) in homogenates of pheochromocytoma (PC-12) cells stably transfected with the human vesicular acetylcholine transporter (VAChT) cDNA are described. The human VAChT protein was abundantly expressed in this line and appeared as a diffuse band with a molecular mass of approximately 75 kDa on Western blots. Vesicular [3H]ACh accumulation increased approximately 20 times over levels attained by the endogenous rat VAChT, expressed at low levels in control PC-12 cells. The transport of [3H]ACh by human VAChT was dependent upon the addition of exogenous ATP at 37 degrees C. Uptake was abolished by low temperature (4 degrees C), the proton ionophore carbonyl cyanide p-trifluoromethoxyphenylhydrazone (2.5 microM) and bafilomycin A1 (1 microM), a specific inhibitor of the vesicular H+-ATPase. The kinetics of [3H]ACh uptake by human VAChT were saturable, exhibiting an apparent Km of 0.97 +/- 0.1 mM and Vmax of 0.58 +/- 0.04 nmol/min/mg. Maximal steady-state levels of vesicular [3H]ACh accumulation were directly proportional to the concentration of substrate present in the medium with saturation occurring at approximately 4 mM. Uptake was stereospecifically inhibited by L-vesamicol with an IC50 of 14.7 +/- 1.5 nM. The apparent affinity (Kd) of [3H]vesamicol for human VAChT was 4.1 +/- 0.5 nM, and the Bmax was 8.9 +/- 0.6 pmol/mg. The turnover (Vmax/Bmax) of the human VAChT was approximately 65/min. This expression system should prove useful for the structure/function analysis of VAChT.},
chemicals = {Carrier Proteins, Membrane Transport Proteins, Neuromuscular Depolarizing Agents, Piperidines, Recombinant Proteins, SLC18A3 protein, human, Slc18a3 protein, rat, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, vesamicol, Acetylcholine, Tetrabenazine},
citation-subset = {IM},
completed = {1996-12-26},
country = {United States},
issn-linking = {0021-9258},
keywords = {Acetylcholine, metabolism; Adrenal Gland Neoplasms; Animals; Biological Transport, Active, drug effects; Carrier Proteins, biosynthesis, metabolism; Cytosol, metabolism; Humans; Kinetics; Membrane Transport Proteins; Neuromuscular Depolarizing Agents, metabolism, pharmacology; PC12 Cells; Pheochromocytoma; Piperidines, metabolism, pharmacology; Rats; Recombinant Proteins, biosynthesis, metabolism; Substrate Specificity; Tetrabenazine, metabolism, pharmacology; Transfection; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins},
nlm-id = {2985121R},
owner = {NLM},
pmid = {8910293},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2019-05-08},
}
@Article{kitamoto2000,
author = {Kitamoto, T and Xie, X and Wu, C F and Salvaterra, P M},
title = {Isolation and characterization of mutants for the vesicular acetylcholine transporter gene in Drosophila melanogaster.},
journal = {Journal of neurobiology},
year = {2000},
volume = {42},
issue = {2},
month = feb,
pages = {161--171},
issn = {0022-3034},
abstract = {The Drosophila vesicular acetylcholine transporter gene (Vacht) is nested within the first intron of the choline acetyltransferase gene (Cha). To isolate Vacht mutants, we performed an F(2) genetic screen and identified mutations that failed to complement Df(3R)Cha(5), a deletion lacking Cha and the surrounding genes. Of these mutations, three mapped to a small genomic region where Cha resides. Complementation tests with a Cha mutant allele and rescue experiments using a transgenic Vacht minigene have revealed that two of these three mutations are nonconditional lethal alleles of Vacht (Vacht(1) and Vacht(2) ). The other is a new temperature-sensitive allele of Cha (Cha(ts3) ). Newly isolated Vacht mutants were used to reexamine the existing Cha mutations. We found that all deficiencies uncovering Cha also lack Vacht function, reflecting the nested organization of the two genes. The effective lethal phase for Vacht(1) is the embryonic stage, whereas that for Vacht(2) is the larval stage. Viable first-instar larvae homozygous for Vacht(2) showed reduced motility. Adult flies heterozygous for Vacht mutations were found to have defective responses in the dorsal longitudinal muscles following high-frequency brain stimulation. Since cholinergic synapses have been shown to be involved in the giant fiber pathway that mediates this response, the result suggested that reduction in the Vacht activity to 50% causes an abnormality in cholinergic transmission when stressed by a high-frequency stimulus.},
chemicals = {Carrier Proteins, Drosophila Proteins, Membrane Transport Proteins, VAChT protein, Drosophila, Vesicular Acetylcholine Transport Proteins, Vesicular Transport Proteins, Choline O-Acetyltransferase},
citation-subset = {IM},
completed = {2000-02-08},
country = {United States},
issn-linking = {0022-3034},
keywords = {Alleles; Animals; Blotting, Western; Brain, enzymology; Carrier Proteins, genetics, physiology; Choline O-Acetyltransferase, metabolism; Drosophila Proteins; Drosophila melanogaster, genetics, physiology; Electrophysiology; Female; Genes, Lethal; Heterozygote; Larva, genetics, physiology; Male; Membrane Transport Proteins; Motor Activity, genetics; Muscles, enzymology; Mutagenesis; Nerve Fibers, enzymology, physiology; Synapses, genetics, physiology; Temperature; Vesicular Acetylcholine Transport Proteins; Vesicular Transport Proteins},
nlm-id = {0213640},
owner = {NLM},
pii = {10.1002/(SICI)1097-4695(20000205)42:2<161::AID-NEU1>3.0.CO;2-P},
pmid = {10640324},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2007-11-14},
}
@Article{karnovsky1964,
author = {Karnovsky, M. J. and Roots, L.},
title = {A "direct-coloring thiocholine method for cholinesterase".},
journal = {The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society},
year = {1964},
volume = {12},
month = mar,
pages = {219--221},
issn = {0022-1554},
doi = {10.1177/12.3.219},
chemicals = {Coloring Agents, Thiocholine, Copper, Cholinesterases, Choline},
citation-subset = {OM},
completed = {1996-12-01},
country = {United States},
issn-linking = {0022-1554},
keywords = {Choline; Cholinesterases; Color; Coloring Agents; Copper; Histocytochemistry; Research; Staining and Labeling; Thiocholine; CHOLINE; CHOLINESTERASE; COPPER; EXPERIMENTAL LAB STUDY; HISTOCYTOCHEMISTRY; STAINS AND STAINING},
nlm-id = {9815334},
owner = {NLM},
pmid = {14187330},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2018-12-01},
}
@Article{gorczyca1987,
author = {Gorczyca, M. G. and Hall, J. C.},
title = {Immunohistochemical localization of choline acetyltransferase during development and in Chats mutants of Drosophila melanogaster.},
journal = {The Journal of neuroscience : the official journal of the Society for Neuroscience},
year = {1987},
volume = {7},
issue = {5},
month = may,
pages = {1361--1369},
issn = {0270-6474},
abstract = {The distribution of choline acetyltransferase (CAT) in the nervous system of Drosophila melanogaster was determined by indirect immunohistochemical procedures using a monoclonal antibody specific to the enzyme. Immunoreactivity was first detected in the nervous system of 16 hr embryos, and increased considerably by the end of embryogenesis. Neuropil was preferentially stained, though cell bodies could also be observed. Staining was prominent in the CNS of all 3 larval instars but decreased substantially during the mid-pupal stage. Prior to eclosion, the level of immunoreactivity increased and the adult staining pattern became discernible. In the adult brain, staining was extensive, with numerous structures, such as the optic lobes and mushroom bodies, staining strongly. The adult thoracic ganglia were also moderately immunoreactive. These results imply a wide distribution of cholinergic neurons in the CNS of Drosophila. Immunoreactivity was also determined for 2 temperature-sensitive CAT mutants, Chats1 and Chats2. These files exhibit reduced CAT activity at permissive temperature, 18 degrees C, which eventually falls to undetectable levels after incubation at nonpermissive temperature, 30 degrees C. Chats2 mutants, after incubation at either 18 or 30 degrees C displayed virtually no staining. This result indicated that the immunoreactivity observed in wild-type flies was specifically associated with the enzyme encoded by the Cha gene. The intensity of staining in Chats1 mutants incubated at 18 degrees C appeared greater than in control flies, even though CAT enzyme activity in Chats1 is lower. This suggests that the enzyme molecule itself is structurally altered in Chats1 mutants. After incubation at 30 degrees C, staining in Chats1 flies decreased but did not disappear.},
chemicals = {Horseradish Peroxidase, Choline O-Acetyltransferase},
citation-subset = {IM},
completed = {1987-06-25},
country = {United States},
issn-linking = {0270-6474},
keywords = {Animals; Central Nervous System, enzymology; Choline O-Acetyltransferase, analysis; Drosophila melanogaster, enzymology, genetics; Embryo, Nonmammalian; Histocytochemistry; Horseradish Peroxidase; Immunologic Techniques; Larva; Mutation; Neurons, enzymology; Pupa; Temperature},
nlm-id = {8102140},
owner = {NLM},
pmid = {3106590},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2007-11-14},
}
@Article{sattelle1983,
author = {Sattelle, D. B. and Harrow, I. D. and Hue, B. and Pelhate, M. and Gepner, J. I. and Hall, L. M.},
title = {$\alpha$-Bungarotoxin Blocks excitatory synaptic transmission between cercal sensory neurones and Giant Interneurone 2 of the cockroach, Peripianeta americana},
journal = {Journal of experimental biology},
year = {1983},
volume = {107},
number = {1},
pages = {473--489},
publisher = {The Company of Biologists Ltd},
}
@Article{daley1988,
author = {Daley, D. L. and Camhi, J. M.},
title = {Connectivity pattern of the cercal-to-giant interneuron system of the American cockroach},
journal = {Journal of neurophysiology},
year = {1988},
volume = {60},
number = {4},
pages = {1350--1368},
publisher = {American Physiological Society Bethesda, MD},
}
@Article{scheidler1990,
author = {Scheidler, A. and Kaulen, P. and Briining, G. and Erber, J.},
title = {Quantitative autoradiographic localization of [125I]α-bungarotoxin binding sites in the honeybee brain.},
journal = {Brain Research},
date = {1990},
volume = {534},
pages = {332-335},
}
@Article{schmidt-nielsen1977,
author = {Schmidt-Nielsen, B. K. and Gepner, J. I. and Teng, N. N. and Hall, L. M.},
title = {Characterization of an alpha-bungarotoxin binding component from Drosophila melanogaster.},
journal = {Journal of neurochemistry},
year = {1977},
volume = {29},
issue = {6},
month = dec,
pages = {1013--1029},
issn = {0022-3042},
doi = {10.1111/j.1471-4159.1977.tb06505.x},
chemicals = {Bungarotoxins, Receptors, Cholinergic, Acetylcholine},
citation-subset = {IM},
completed = {1978-03-21},
country = {England},
issn-linking = {0022-3042},
keywords = {Acetylcholine, pharmacology; Animals; Binding Sites; Brain Chemistry; Bungarotoxins, antagonists & inhibitors, metabolism; Dose-Response Relationship, Drug; Drosophila melanogaster; Kinetics; Methods; Receptors, Cholinergic, analysis; Synapses, analysis; Time Factors},
nlm-id = {2985190R},
owner = {NLM},
pmid = {413880},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2019-06-30},
}
@Article{hildebrand1979,
author = {Hildebrand, J. G. and Hall, L. M. and Osmond, B. C.},
title = {Distribution of binding sites for 125I-labeled alpha-bungarotoxin in normal and deafferented antennal lobes of Manduca sexta.},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
year = {1979},
volume = {76},
issue = {1},
month = jan,
pages = {499--503},
issn = {0027-8424},
doi = {10.1073/pnas.76.1.499},
abstract = {125I-Labeled alpha-bungarotoxin has been used to determine the distribution of putative acetylcholine receptors in normal and chronically deafferented antennal lobes in the brain of the moth Manduca sexta. Toxin-binding sites are confined to synaptic regions in deafferented lobes. These findings suggest that receptors can develop in the insect central nervous system independently of normal synaptic influences.},
chemicals = {Bungarotoxins, Receptors, Cholinergic},
citation-subset = {IM},
completed = {1979-05-26},
country = {United States},
issn-linking = {0027-8424},
keywords = {Afferent Pathways; Animals; Brain, cytology, metabolism; Bungarotoxins, metabolism; Denervation; Lepidoptera, metabolism; Moths, metabolism; Receptors, Cholinergic, metabolism; Synapses, metabolism},
nlm-id = {7505876},
owner = {NLM},
pmc = {PMC382969},
pmid = {284367},
pubmodel = {Print},
pubstatus = {ppublish},
revised = {2019-05-01},
}