Usdin TB

References (6)

Title : The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) - Gerhard_2004_Genome.Res_14_2121
Author(s) : Gerhard DS , Wagner L , Feingold EA , Shenmen CM , Grouse LH , Schuler G , Klein SL , Old S , Rasooly R , Good P , Guyer M , Peck AM , Derge JG , Lipman D , Collins FS , Jang W , Sherry S , Feolo M , Misquitta L , Lee E , Rotmistrovsky K , Greenhut SF , Schaefer CF , Buetow K , Bonner TI , Haussler D , Kent J , Kiekhaus M , Furey T , Brent M , Prange C , Schreiber K , Shapiro N , Bhat NK , Hopkins RF , Hsie F , Driscoll T , Soares MB , Casavant TL , Scheetz TE , Brown-stein MJ , Usdin TB , Toshiyuki S , Carninci P , Piao Y , Dudekula DB , Ko MS , Kawakami K , Suzuki Y , Sugano S , Gruber CE , Smith MR , Simmons B , Moore T , Waterman R , Johnson SL , Ruan Y , Wei CL , Mathavan S , Gunaratne PH , Wu J , Garcia AM , Hulyk SW , Fuh E , Yuan Y , Sneed A , Kowis C , Hodgson A , Muzny DM , McPherson J , Gibbs RA , Fahey J , Helton E , Ketteman M , Madan A , Rodrigues S , Sanchez A , Whiting M , Madari A , Young AC , Wetherby KD , Granite SJ , Kwong PN , Brinkley CP , Pearson RL , Bouffard GG , Blakesly RW , Green ED , Dickson MC , Rodriguez AC , Grimwood J , Schmutz J , Myers RM , Butterfield YS , Griffith M , Griffith OL , Krzywinski MI , Liao N , Morin R , Palmquist D , Petrescu AS , Skalska U , Smailus DE , Stott JM , Schnerch A , Schein JE , Jones SJ , Holt RA , Baross A , Marra MA , Clifton S , Makowski KA , Bosak S , Malek J
Ref : Genome Res , 14 :2121 , 2004
Abstract : The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline.
ESTHER : Gerhard_2004_Genome.Res_14_2121
PubMedSearch : Gerhard_2004_Genome.Res_14_2121
PubMedID: 15489334
Gene_locus related to this paper: human-AFMID , human-CES4A , human-CES5A , human-NOTUM , human-SERAC1 , human-SERHL2 , human-TMEM53 , mouse-acot1 , mouse-adcl4 , mouse-Ces2f , mouse-Ces4a , mouse-notum , mouse-q6wqj1 , mouse-Q9DAI6 , mouse-rbbp9 , mouse-SERHL , mouse-srac1 , mouse-tmm53 , rat-abhd6 , rat-abhda , rat-abhea , rat-abheb , rat-Ldah , rat-cd029 , rat-estd , rat-Kansl3 , rat-nceh1 , ratno-acph , ratno-CMBL , mouse-b2rwd2 , rat-b5den3 , rat-ab17c

Title : Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences - Strausberg_2002_Proc.Natl.Acad.Sci.U.S.A_99_16899
Author(s) : Strausberg RL , Feingold EA , Grouse LH , Derge JG , Klausner RD , Collins FS , Wagner L , Shenmen CM , Schuler GD , Altschul SF , Zeeberg B , Buetow KH , Schaefer CF , Bhat NK , Hopkins RF , Jordan H , Moore T , Max SI , Wang J , Hsieh F , Diatchenko L , Marusina K , Farmer AA , Rubin GM , Hong L , Stapleton M , Soares MB , Bonaldo MF , Casavant TL , Scheetz TE , Brownstein MJ , Usdin TB , Toshiyuki S , Carninci P , Prange C , Raha SS , Loquellano NA , Peters GJ , Abramson RD , Mullahy SJ , Bosak SA , McEwan PJ , McKernan KJ , Malek JA , Gunaratne PH , Richards S , Worley KC , Hale S , Garcia AM , Gay LJ , Hulyk SW , Villalon DK , Muzny DM , Sodergren EJ , Lu X , Gibbs RA , Fahey J , Helton E , Ketteman M , Madan A , Rodrigues S , Sanchez A , Whiting M , Young AC , Shevchenko Y , Bouffard GG , Blakesley RW , Touchman JW , Green ED , Dickson MC , Rodriguez AC , Grimwood J , Schmutz J , Myers RM , Butterfield YS , Krzywinski MI , Skalska U , Smailus DE , Schnerch A , Schein JE , Jones SJ , Marra MA
Ref : Proc Natl Acad Sci U S A , 99 :16899 , 2002
Abstract : The National Institutes of Health Mammalian Gene Collection (MGC) Program is a multiinstitutional effort to identify and sequence a cDNA clone containing a complete ORF for each human and mouse gene. ESTs were generated from libraries enriched for full-length cDNAs and analyzed to identify candidate full-ORF clones, which then were sequenced to high accuracy. The MGC has currently sequenced and verified the full ORF for a nonredundant set of >9,000 human and >6,000 mouse genes. Candidate full-ORF clones for an additional 7,800 human and 3,500 mouse genes also have been identified. All MGC sequences and clones are available without restriction through public databases and clone distribution networks (see
ESTHER : Strausberg_2002_Proc.Natl.Acad.Sci.U.S.A_99_16899
PubMedSearch : Strausberg_2002_Proc.Natl.Acad.Sci.U.S.A_99_16899
PubMedID: 12477932
Gene_locus related to this paper: bovin-q3zcj6 , danre-OVCA2 , danre-q4qrh4 , danre-q4v960 , danre-q32ls6 , danre-q503e2 , ratno-CPVL , ratno-q3mhs0 , ratno-q4qr68 , ratno-q5fvr5 , ratno-q32q55 , xenla-a2bd54 , xenla-q2tap9 , xenla-q3kq37 , xenla-q3kq76 , xenla-q4klb6 , xenla-q32n48 , xenla-q32ns5 , xenla-q52l41 , xentr-q4va73 , danre-a7mbu9

Title : Molecular biology of the vesicular ACh transporter - Usdin_1995_Trends.Neurosci_18_218
Author(s) : Usdin TB , Eiden LE , Bonner TI , Erickson JD
Ref : Trends in Neurosciences , 18 :218 , 1995
Abstract : The cholinergic synapse has long been a model for biochemical studies of neurotransmission. The molecules that are responsible for synaptic transmission are being identified rapidly. The vesicular transporter for ACh, which is responsible for the concentration of ACh within synaptic vesicles, has been characterized recently, both at the molecular and functional level. Definitive identification of the cloned gene involved genetics of Caenorhabditis elegans, the specialized Torpedo electromotor system, and expression in mammalian tissue culture. Comparison of the vesicular transporter for ACh with the vesicular transporters for monoamines demonstrates a new gene family. Gene mapping has demonstrated a unique relationship between the genes for the vesicular ACh transporter and for choline acetyltransferase.
ESTHER : Usdin_1995_Trends.Neurosci_18_218
PubMedSearch : Usdin_1995_Trends.Neurosci_18_218
PubMedID: 7610492

Title : Cloning and expression of the vesamicol binding protein from the marine ray Torpedo. Homology with the putative vesicular acetylcholine transporter UNC-17 from Caenorhabditis elegans - Varoqui_1994_FEBS.Lett_342_97
Author(s) : Varoqui H , Diebler MF , Meunier FM , Rand JB , Usdin TB , Bonner TI , Eiden LE , Erickson JD
Ref : FEBS Letters , 342 :97 , 1994
Abstract : Complementary DNA clones corresponding to a messenger RNA encoding a 56 kDa polypeptide have been obtained from Torpedo marmorata and Torpedo ocellata electric lobe libraries, by homology screening with a probe obtained from the putative acetylcholine transporter from the nematode Caenorhabditis elegans. The Torpedo proteins display approximately 50% overall identity to the C. elegans unc-17 protein and 43% identity to the two vesicle monoamine transporters (VMAT1 and VMAT2). This family of proteins is highly conserved within 12 domains which potentially span the vesicle membrane, with little similarity within the putative intraluminal glycosylated loop and at the N- and C-termini. The approximately 3.0 kb mRNA species is specifically expressed in the brain and highly enriched in the electric lobe of Torpedo. The Torpedo protein, expressed in CV-1 fibroblast cells, possesses a high-affinity binding site for vesamicol (Kd = 6 nM), a drug which blocks in vitro and in vivo acetylcholine accumulation in cholinergic vesicles.
ESTHER : Varoqui_1994_FEBS.Lett_342_97
PubMedSearch : Varoqui_1994_FEBS.Lett_342_97
PubMedID: 8143858

Title : Functional identification of a vesicular acetylcholine transporter and its expression from a cholinergic gene locus - Erickson_1994_J.Biol.Chem_269_21929
Author(s) : Erickson JD , Varoqui H , Schafer MK , Modi W , Diebler MF , Weihe E , Rand J , Eiden LE , Bonner TI , Usdin TB
Ref : Journal of Biological Chemistry , 269 :21929 , 1994
Abstract : The vesicular acetylcholine transporter (VAChT) has been identified and characterized based on the acquisition of high affinity vesamicol binding and proton-dependent, vesamicol-sensitive acetylcholine accumulation by a fibroblast cell line transfected with a clone from a rat pheochromocytoma cDNA library encoding this protein. The distribution of VAChT mRNA coincides with that reported for choline acetyltransferase (ChAT), the enzyme required for acetylcholine biosynthesis, in the peripheral and central cholinergic nervous systems. A human VAChT cDNA was used to localize the VAChT gene to chromosome 10q11.2, which is also the location of the ChAT gene. The entire sequence of the human VAChT cDNA is contained uninterrupted within the first intron of the ChAT gene locus. Transcription of VAChT and ChAT mRNA from the same or contiguous promoters within a single regulatory locus provides a previously undescribed genetic mechanism for coordinate regulation of two proteins whose expression is required to establish a mammalian neuronal phenotype.
ESTHER : Erickson_1994_J.Biol.Chem_269_21929
PubMedSearch : Erickson_1994_J.Biol.Chem_269_21929
PubMedID: 8071310

Title : Purification and characterization of a polypeptide from chick brain that promotes the accumulation of acetylcholine receptors in chick myotubes - Usdin_1986_J.Cell.Biol_103_493
Author(s) : Usdin TB , Fischbach GD
Ref : Journal of Cell Biology , 103 :493 , 1986
Abstract : Acetylcholine receptors (AChRs) are packed in the postsynaptic membrane at neuromuscular junctions at a density of approximately 20,000/micron 2, whereas the density a few micrometers away is less than 20/micron 2. To understand how this remarkable distribution comes about during nerve-muscle synapse formation, we have attempted to isolate factors from neural tissue that can promote the accumulation of AChRs and/or alter their distribution. In this paper we report the purification of a polypeptide from chick brains that can increase the rate of insertion of AChR into membranes of cultured chick myotubes at a concentration of less than 0.5 ng/ml. Based on SDS PAGE and the action of neuraminidase, the acetylcholine receptor-inducing activity (ARIA) appears to be a 42,000-D glycoprotein. ARIA was extracted in a trifluoroacetic acid-containing cocktail and purified to homogeneity by reverse-phase, ion exchange, and size exclusion high pressure liquid chromatography. Dose response curves indicate that the activity has been purified 60,000-fold compared with the starting acid extract and approximately 1,500,000-fold compared with a saline extract prepared from the same batch of brains. Although the ARIA was purified on the basis of its ability to increase receptor incorporation, we found that it increased the number and size of receptor clusters as well. It is not yet clear if the two effects are independent. The 42-kD ARIA is extremely stable: it was not destroyed by exposure to intact myotubes, low pH, organic solvents, or SDS. Its action appears to be selective in that the increase in the rate of receptor insertion was not accompanied by an increase in the rate of protein synthesis. Moreover, there was no change in cellular, surface membrane, or secreted acetylcholinesterase. The effect of ARIA is apparently independent of the state of activity of the target myotubes as its effect on receptor incorporation added to that of maximal concentrations of tetrodotoxin.
ESTHER : Usdin_1986_J.Cell.Biol_103_493
PubMedSearch : Usdin_1986_J.Cell.Biol_103_493
PubMedID: 3733876