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Graham L Hall - One of the best experts on this subject based on the ideXlab platform.
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official ers technical standards global lung function initiative reference values for the carbon monoxide Transfer Factor for caucasians
European Respiratory Journal, 2017Co-Authors: Sanja Stanojevic, Bruce Thompson, Brian L Graham, B G Cooper, Kim W Carter, Richard W Francis, Graham L HallAbstract:There are numerous reference equations available for the single-breath Transfer Factor of the lung for carbon monoxide ( T LCO ); however, it is not always clear which reference set should be used in clinical practice. The aim of the study was to develop the Global Lung Function Initiative (GLI) all-age reference values for T LCO . Data from 19 centres in 14 countries were collected to define T LCO reference values. Similar to the GLI spirometry project, reference values were derived using the LMS (lambda, mu, sigma) method and the GAMLSS (generalised additive models for location, scale and shape) programme in R. 12 660 T LCO measurements from asymptomatic, lifetime nonsmokers were submitted; 85% of the submitted data were from Caucasians. All data were uncorrected for haemoglobin concentration. Following adjustments for elevation above sea level, gas concentration and assumptions used for calculating the anatomic dead space volume, there was a high degree of overlap between the datasets. Reference values for Caucasians aged 5–85 years were derived for T LCO , Transfer coefficient of the lung for carbon monoxide and alveolar volume. This is the largest collection of normative T LCO data, and the first global reference values available for T LCO .
Elizabeth A Craig - One of the best experts on this subject based on the ideXlab platform.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A CraigAbstract:In mitochondria FeS clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14-kDa scaffold protein, and then Transferred to recipient apoproteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either Yfh1-Isu or Nfs1-Isu interactions destabilizes the complex. Cluster Transfer to recipient apoprotein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that the Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of FeS cluster proteins.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A Craig, Rafal DutkiewiczAbstract:Abstract In mitochondria Fe-S clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14 kDa scaffold protein, and then Transferred to recipient apo-proteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either the Yfh1-Isu or the Nfs1-Isu interaction destabilizes the complex. Cluster Transfer to recipient apo-protein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of Fe-S cluster proteins.
Jaroslaw Marszalek - One of the best experts on this subject based on the ideXlab platform.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A CraigAbstract:In mitochondria FeS clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14-kDa scaffold protein, and then Transferred to recipient apoproteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either Yfh1-Isu or Nfs1-Isu interactions destabilizes the complex. Cluster Transfer to recipient apoprotein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that the Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of FeS cluster proteins.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A Craig, Rafal DutkiewiczAbstract:Abstract In mitochondria Fe-S clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14 kDa scaffold protein, and then Transferred to recipient apo-proteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either the Yfh1-Isu or the Nfs1-Isu interaction destabilizes the complex. Cluster Transfer to recipient apo-protein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of Fe-S cluster proteins.
Julia Majewska - One of the best experts on this subject based on the ideXlab platform.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A CraigAbstract:In mitochondria FeS clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14-kDa scaffold protein, and then Transferred to recipient apoproteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either Yfh1-Isu or Nfs1-Isu interactions destabilizes the complex. Cluster Transfer to recipient apoprotein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that the Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of FeS cluster proteins.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A Craig, Rafal DutkiewiczAbstract:Abstract In mitochondria Fe-S clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14 kDa scaffold protein, and then Transferred to recipient apo-proteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either the Yfh1-Isu or the Nfs1-Isu interaction destabilizes the complex. Cluster Transfer to recipient apo-protein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of Fe-S cluster proteins.
Mateusz Manicki - One of the best experts on this subject based on the ideXlab platform.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A CraigAbstract:In mitochondria FeS clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14-kDa scaffold protein, and then Transferred to recipient apoproteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either Yfh1-Isu or Nfs1-Isu interactions destabilizes the complex. Cluster Transfer to recipient apoprotein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that the Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of FeS cluster proteins.
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overlapping binding sites of the frataxin homologue assembly Factor and the heat shock protein 70 Transfer Factor on the isu iron sulfur cluster scaffold protein
Journal of Biological Chemistry, 2014Co-Authors: Mateusz Manicki, Julia Majewska, Szymon J Ciesielski, Brenda Schilke, Anna Blenska, Jacek Kominek, Jaroslaw Marszalek, Elizabeth A Craig, Rafal DutkiewiczAbstract:Abstract In mitochondria Fe-S clusters, prosthetic groups critical for the activity of many proteins, are first assembled on Isu, a 14 kDa scaffold protein, and then Transferred to recipient apo-proteins. The assembly process involves interaction of Isu with both Nfs1, the cysteine desulfurase serving as a sulfur donor, and the yeast frataxin homolog (Yfh1) serving as a regulator of desulfurase activity and/or iron donor. Here, based on the results of biochemical experiments with purified wild-type and variant proteins, we report that interaction of Yfh1 with both Nfs1 and Isu are required for formation of a stable tripartite assembly complex. Disruption of either the Yfh1-Isu or the Nfs1-Isu interaction destabilizes the complex. Cluster Transfer to recipient apo-protein is known to require the interaction of Isu with the J-protein/Hsp70 molecular chaperone pair, Jac1 and Ssq1. Here we show that Yfh1 interaction with Isu involves the PVK sequence motif, which is also the site key for the interaction of Isu with Hsp70 Ssq1. Coupled with our previous observation that Nfs1 and Jac1 binding to Isu is mutually exclusive due to partially overlapping binding sites, we propose that such mutual exclusivity of cluster assembly Factor (Nfs1/Yfh1) and cluster Transfer Factor (Jac1/Ssq1) binding to Isu has functional consequences for the transition from the assembly process to the Transfer process, and thus regulation of the biogenesis of Fe-S cluster proteins.
