cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.1473689
title: Evaluation of measures of impairment in real and simulated driving: Results from a randomized, placebo-controlled study

description: <b>Objective</b>: Standard deviation of lateral position (SDLP) is often the primary outcome in experimental studies on impaired driving. However, other measures may be easier and more practical to obtain and reflect a broader range of driving-related behaviors. We wanted to assess the validity and sensitivity of a range of measures in a driving simulator as well as during real driving and compare these to SDLP. <b>Methods</b>: Twenty healthy male volunteers undertook 6 driving trials each, 3 in a regular car on a closed track resembling rural road conditions and 3 in a simulator with an identical driving scenario. Ethanol was used as impairing substance due to its well-characterized effects on driving. The subjects were tested sober and at blood alcohol concentrations (BAC) of approximately 0.5 and 0.9 g/L. We explored dose–response relationships between BAC and a range of driving-related measures, as well as their BAC-dependent effect sizes. <b>Results</b>: In simulator driving, ethanol intake increased steering wheel reversal frequency, steering wheel movement measures, average speed, standard deviation of speed, and pedal use frequency. At the test track, only steering wheel movement and standard deviation of speed were significantly correlated to BAC. Likewise, reaction to unexpected incidents and observance of red traffic lights were adversely affected by ethanol in the simulator but not at the test track. Whereas SDLP showed a relatively large effect size that was similar in simulated and real driving, all other measures demonstrated smaller effect sizes, with less pronounced BAC effects on the test track than in the simulator. <b>Conclusions</b>: The results suggest that the driving-related measures explored in this study are less sensitive to alcohol-mediated driving impairment than SDLP, especially during real (test track) driving. The discrepancy in effect sizes between simulated and real driving may imply low external validity of these measures in simulator studies.
DOI: 10.6084/m9.figshare.1473689.v1
title: Evaluation of measures of impairment in real and simulated driving: Results from a randomized, placebo-controlled study

description: <b>Objective</b>: Standard deviation of lateral position (SDLP) is often the primary outcome in experimental studies on impaired driving. However, other measures may be easier and more practical to obtain and reflect a broader range of driving-related behaviors. We wanted to assess the validity and sensitivity of a range of measures in a driving simulator as well as during real driving and compare these to SDLP. <b>Methods</b>: Twenty healthy male volunteers undertook 6 driving trials each, 3 in a regular car on a closed track resembling rural road conditions and 3 in a simulator with an identical driving scenario. Ethanol was used as impairing substance due to its well-characterized effects on driving. The subjects were tested sober and at blood alcohol concentrations (BAC) of approximately 0.5 and 0.9 g/L. We explored dose–response relationships between BAC and a range of driving-related measures, as well as their BAC-dependent effect sizes. <b>Results</b>: In simulator driving, ethanol intake increased steering wheel reversal frequency, steering wheel movement measures, average speed, standard deviation of speed, and pedal use frequency. At the test track, only steering wheel movement and standard deviation of speed were significantly correlated to BAC. Likewise, reaction to unexpected incidents and observance of red traffic lights were adversely affected by ethanol in the simulator but not at the test track. Whereas SDLP showed a relatively large effect size that was similar in simulated and real driving, all other measures demonstrated smaller effect sizes, with less pronounced BAC effects on the test track than in the simulator. <b>Conclusions</b>: The results suggest that the driving-related measures explored in this study are less sensitive to alcohol-mediated driving impairment than SDLP, especially during real (test track) driving. The discrepancy in effect sizes between simulated and real driving may imply low external validity of these measures in simulator studies.
DOI: 10.6084/m9.figshare.1473713.v1
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713.v2
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713.v3
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713.v4
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713.v5
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713.v7
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473713.v6
title: A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

description: The proliferating cell nuclear antigen (PCNA) is a conserved component of DNA replication factories, and interactions with PCNA mediate the recruitment of many essential DNA replication enzymes to these sites of DNA synthesis. A complete description of the structure and composition of these factories remains elusive, and a better knowledge of them will improve our understanding of how the maintenance of genome and epigenetic stability is achieved. To fully characterize the set of proteins that interact with PCNA we developed a bimolecular fluorescence complementation (BiFC) screen for PCNA-interactors in human cells. This 2-hybrid type screen for interactors from a human cDNA library is rapid and efficient. The fluorescent read-out for protein interaction enables facile selection of interacting clones, and we combined this with next generation sequencing to identify the cDNAs encoding the interacting proteins. This method was able to reproducibly identify previously characterized PCNA-interactors but importantly also identified RNF7, Maf1 and SetD3 as PCNA-interacting proteins. We validated these interactions by co-immunoprecipitation from human cell extracts and by interaction analyses using recombinant proteins. These results show that the BiFC screen is a valuable method for the identification of protein-protein interactions in living mammalian cells. This approach has potentially wide application as it is high throughput and readily automated. We suggest that, given this interaction with PCNA, Maf1, RNF7, and SetD3 are potentially involved in DNA replication, DNA repair, or associated processes.
DOI: 10.6084/m9.figshare.1473096
title: Effects of thinning paper birch on conifer productivity and understory plant diversity

description: Naturally regenerated paper birch (<i>Betula papyrifera</i> Marsh.) is commonly removed from juvenile interior Douglas-fir (<i>Pseudotsuga menziesii</i> var. <i>glauca</i> [Beissn.] Franco) plantations in southern interior British Columbia, Canada, to increase conifer productivity and create a free-growing stand; however, this practice is expensive and contentious because of possible negative ecological impacts. One solution is to retain an optimal density of birch where growth gains of understory Douglas-fir are balanced against losses to <i>Armillaria ostoyae</i> (Romagn.) Herink and understory plant species diversity. We sought to find this optimal density by comparing four evenly applied birch density reduction treatments (0, 400, 1111, and 4444 retained birch stems ha<sup>−1</sup>) and an unthinned control (&gt;7300 retained birch stems ha<sup>−1</sup>). The mortality rate of Douglas-fir due to <i>Armillaria</i> root disease increased non-significantly with thinning intensity. Mean diameter increment of surviving Douglas-fir improved the most where birch was completely removed, with little variation among intermediate thinning treatments. Height growth was unaffected by the thinning treatments. Diversity of cryptogams was significantly greater in the control than where all birch was removed. We suggest that the treatment with 4444 retained birch stems ha<sup>−1</sup> provides the best balance for improving Douglas-fir growth while minimizing risk of increased <i>Armillaria</i> root disease and reduced understory plant diversity in young mixed stands.
DOI: 10.6084/m9.figshare.1473096.v2
title: Effects of thinning paper birch on conifer productivity and understory plant diversity

description: Naturally regenerated paper birch (<i>Betula papyrifera</i> Marsh.) is commonly removed from juvenile interior Douglas-fir (<i>Pseudotsuga menziesii</i> var. <i>glauca</i> [Beissn.] Franco) plantations in southern interior British Columbia, Canada, to increase conifer productivity and create a free-growing stand; however, this practice is expensive and contentious because of possible negative ecological impacts. One solution is to retain an optimal density of birch where growth gains of understory Douglas-fir are balanced against losses to <i>Armillaria ostoyae</i> (Romagn.) Herink and understory plant species diversity. We sought to find this optimal density by comparing four evenly applied birch density reduction treatments (0, 400, 1111, and 4444 retained birch stems ha<sup>−1</sup>) and an unthinned control (&gt;7300 retained birch stems ha<sup>−1</sup>). The mortality rate of Douglas-fir due to <i>Armillaria</i> root disease increased non-significantly with thinning intensity. Mean diameter increment of surviving Douglas-fir improved the most where birch was completely removed, with little variation among intermediate thinning treatments. Height growth was unaffected by the thinning treatments. Diversity of cryptogams was significantly greater in the control than where all birch was removed. We suggest that the treatment with 4444 retained birch stems ha<sup>−1</sup> provides the best balance for improving Douglas-fir growth while minimizing risk of increased <i>Armillaria</i> root disease and reduced understory plant diversity in young mixed stands.
DOI: 10.6084/m9.figshare.1473096.v1
title: Effects of thinning paper birch on conifer productivity and understory plant diversity

description: Naturally regenerated paper birch (<i>Betula papyrifera</i> Marsh.) is commonly removed from juvenile interior Douglas-fir (<i>Pseudotsuga menziesii</i> var. <i>glauca</i> [Beissn.] Franco) plantations in southern interior British Columbia, Canada, to increase conifer productivity and create a free-growing stand; however, this practice is expensive and contentious because of possible negative ecological impacts. One solution is to retain an optimal density of birch where growth gains of understory Douglas-fir are balanced against losses to <i>Armillaria ostoyae</i> (Romagn.) Herink and understory plant species diversity. We sought to find this optimal density by comparing four evenly applied birch density reduction treatments (0, 400, 1111, and 4444 retained birch stems ha<sup>−1</sup>) and an unthinned control (&gt;7300 retained birch stems ha<sup>−1</sup>). The mortality rate of Douglas-fir due to <i>Armillaria</i> root disease increased non-significantly with thinning intensity. Mean diameter increment of surviving Douglas-fir improved the most where birch was completely removed, with little variation among intermediate thinning treatments. Height growth was unaffected by the thinning treatments. Diversity of cryptogams was significantly greater in the control than where all birch was removed. We suggest that the treatment with 4444 retained birch stems ha<sup>−1</sup> provides the best balance for improving Douglas-fir growth while minimizing risk of increased <i>Armillaria</i> root disease and reduced understory plant diversity in young mixed stands.
DOI: 10.6084/m9.figshare.1473092
title: NLR-B30.2 online supplement

description: Online supplementary material for manuscript on the evolutionary history of the NLR-B30.2 gene family in zebrafish.
DOI: 10.6084/m9.figshare.1473091
title: The Cambridge Collaboration Network

description: The Cambridge co-authorship network. Thematic research networks are highlighted in yellow on a loop.