The Experts below are selected from a list of 84 Experts worldwide ranked by ideXlab platform
David Pattersontt - One of the best experts on this subject based on the ideXlab platform.
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Multiple purine pathway enzyme activities are encoded at a single genetic locus in Drosophila (multifunctional protein/phosphoribosylamine-glycine ligase/Phosphoribosylglycinamide Formyltransferase/
2020Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
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multiple purine pathway enzyme activities are encoded at a single genetic locus in drosophila multifunctional protein phosphoribosylamine glycine ligase Phosphoribosylglycinamide Formyltransferase
2016Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
Steven Henikoff - One of the best experts on this subject based on the ideXlab platform.
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Multiple purine pathway enzyme activities are encoded at a single genetic locus in Drosophila (multifunctional protein/phosphoribosylamine-glycine ligase/Phosphoribosylglycinamide Formyltransferase/
2020Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
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multiple purine pathway enzyme activities are encoded at a single genetic locus in drosophila multifunctional protein phosphoribosylamine glycine ligase Phosphoribosylglycinamide Formyltransferase
2016Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
John Bleskant - One of the best experts on this subject based on the ideXlab platform.
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Multiple purine pathway enzyme activities are encoded at a single genetic locus in Drosophila (multifunctional protein/phosphoribosylamine-glycine ligase/Phosphoribosylglycinamide Formyltransferase/
2020Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
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multiple purine pathway enzyme activities are encoded at a single genetic locus in drosophila multifunctional protein phosphoribosylamine glycine ligase Phosphoribosylglycinamide Formyltransferase
2016Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
James S Sloan - One of the best experts on this subject based on the ideXlab platform.
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Multiple purine pathway enzyme activities are encoded at a single genetic locus in Drosophila (multifunctional protein/phosphoribosylamine-glycine ligase/Phosphoribosylglycinamide Formyltransferase/
2020Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
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multiple purine pathway enzyme activities are encoded at a single genetic locus in drosophila multifunctional protein phosphoribosylamine glycine ligase Phosphoribosylglycinamide Formyltransferase
2016Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
Michael A Keene - One of the best experts on this subject based on the ideXlab platform.
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Multiple purine pathway enzyme activities are encoded at a single genetic locus in Drosophila (multifunctional protein/phosphoribosylamine-glycine ligase/Phosphoribosylglycinamide Formyltransferase/
2020Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.
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multiple purine pathway enzyme activities are encoded at a single genetic locus in drosophila multifunctional protein phosphoribosylamine glycine ligase Phosphoribosylglycinamide Formyltransferase
2016Co-Authors: Steven Henikoff, Michael A Keene, James S Sloan, John Bleskant, David PattersonttAbstract:The Drosophila melanogaster Gart locus, known from previous work to encode the enzyme activity Phosphoribosylglycinamide Formyltransferase (GART), speci- fies two alternatively processed mRNAs and two proteins. We introduced the entire Garl locus into a Drosophila tissue culture cell line in which the locus is active. The resulting cell clones contained numerous copies of the locus and overproduced both mRNAs and both expected proteins, thus markedly facilitating analysis of these molecules. We assayed extracts of the clones for the activities of 10 enzymes important for de novo purine synthesis and found that, in addition to GART, two other purine pathway activities, phosphoribosylamine-glycine ligase (Phosphoribosylglycinamide synthetase, GARS) and phospho- ribosylformylglycinamidine cyclo-ligase (phosphoribosylami- noimidazole synthetase, AIRS), are similarly overproduced. All three activities are present together on the larger overpro- duced protein. A smaller protein appears to possess only GARS activity. Therefore, alternative mRNA processing can allow cells to produce enzyme activities in forms that are either linked or unlinked to other activities.