cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.1477820
title: NM14302-V221.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477815
title: Study of Fire Retardancy and Thermal and Mechanical Properties of HDPE-Wood Composites

description: This article reports a study of flame retardancy and thermal and mechanical properties of wood-plastic composites (WPCs) based on high-density polyethylene and pine flour. The study shows that sample composition plays an important role in WPCs' properties. The influence of additives like fillers (SiO<sub>2</sub> or CaCO<sub>3</sub>) and flame retardants ammonium polyphosphate (APP) and pentaerythritol (PER) on WPCs' properties has been considered. The best properties are shown in samples using SiO<sub>2</sub> as filler and treated with the intumescent fire retardant APP/PER. Such samples have excellent fire retardancy with V-0 rating (UL-94 test) and imply that APP/PER fire retardant ensures effective fire retardancy for WPCs.
DOI: 10.6084/m9.figshare.1477816
title: BM14149 v-230.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477818
title: NM 14185 - v.214.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477823.v1
title: NM14302-V223.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477816.v1
title: BM14149 v-230.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477818.v1
title: NM 14185 - v.214.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477820.v1
title: NM14302-V221.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477812
title: BM14119C-V206.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477811
title: BM14119C-V208.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477813
title: BM 14119B v- 238.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477811.v1
title: BM14119C-V208.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477813.v1
title: BM 14119B v- 238.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477807
title: BM14119C-V207.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477809
title: The extended AT-hook is a novel RNA binding motif

description: The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12–15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
DOI: 10.6084/m9.figshare.1477815.v2
title: Study of Fire Retardancy and Thermal and Mechanical Properties of HDPE-Wood Composites

description: This article reports a study of flame retardancy and thermal and mechanical properties of wood-plastic composites (WPCs) based on high-density polyethylene and pine flour. The study shows that sample composition plays an important role in WPCs' properties. The influence of additives like fillers (SiO<sub>2</sub> or CaCO<sub>3</sub>) and flame retardants ammonium polyphosphate (APP) and pentaerythritol (PER) on WPCs' properties has been considered. The best properties are shown in samples using SiO<sub>2</sub> as filler and treated with the intumescent fire retardant APP/PER. Such samples have excellent fire retardancy with V-0 rating (UL-94 test) and imply that APP/PER fire retardant ensures effective fire retardancy for WPCs.
DOI: 10.6084/m9.figshare.1477807.v1
title: BM14119C-V207.pdf

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477815.v1
title: Study of Fire Retardancy and Thermal and Mechanical Properties of HDPE-Wood Composites

description: This article reports a study of flame retardancy and thermal and mechanical properties of wood-plastic composites (WPCs) based on high-density polyethylene and pine flour. The study shows that sample composition plays an important role in WPCs' properties. The influence of additives like fillers (SiO<sub>2</sub> or CaCO<sub>3</sub>) and flame retardants ammonium polyphosphate (APP) and pentaerythritol (PER) on WPCs' properties has been considered. The best properties are shown in samples using SiO<sub>2</sub> as filler and treated with the intumescent fire retardant APP/PER. Such samples have excellent fire retardancy with V-0 rating (UL-94 test) and imply that APP/PER fire retardant ensures effective fire retardancy for WPCs.
DOI: 10.6084/m9.figshare.1477802
title: Overview of studies and no of pages.xls

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477809.v1
title: The extended AT-hook is a novel RNA binding motif

description: The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12–15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
DOI: 10.6084/m9.figshare.1477799
title: Inflammation factors levels before the last treatment

description: Inflammation factors levels in the aqueous humor before the last treatment/re-treatment.
DOI: 10.6084/m9.figshare.1477802.v1
title: Overview of studies and no of pages.xls

description: Clinical Study Reports on Orlistat released by EMA
DOI: 10.6084/m9.figshare.1477809.v2
title: The extended AT-hook is a novel RNA binding motif

description: The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12–15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
DOI: 10.6084/m9.figshare.1477798
title: Inflammation factors levels in pretreatment

description: Inflammation factors concentrations in the aqueous humor before the initial treatment.
DOI: 10.6084/m9.figshare.1477799.v2
title: Inflammation factors levels before the last treatment

description: Inflammation factors levels in the aqueous humor before the last treatment/re-treatment.
DOI: 10.6084/m9.figshare.1477809.v3
title: The extended AT-hook is a novel RNA binding motif

description: The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12–15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
DOI: 10.6084/m9.figshare.1477797
title: Inflammation factors levels of control group

description: Inflammation factors levels in the aqueous humor on the control group.
DOI: 10.6084/m9.figshare.1477798.v2
title: Inflammation factors levels in pretreatment

description: Inflammation factors concentrations in the aqueous humor before the initial treatment.
DOI: 10.6084/m9.figshare.1477799.v1
title: Inflammation factors levels before the last treatment

description: Inflammation factors levels in the aqueous humor before the last treatment/re-treatment.
DOI: 10.6084/m9.figshare.1477809.v5
title: The extended AT-hook is a novel RNA binding motif

description: The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12–15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
DOI: 10.6084/m9.figshare.1477798.v1
title: Inflammation factors levels in pretreatment

description: Inflammation factors concentrations in the aqueous humor before the initial treatment.
DOI: 10.6084/m9.figshare.1477809.v4
title: The extended AT-hook is a novel RNA binding motif

description: The AT-hook has been defined as a DNA binding peptide motif that contains a glycine-arginine-proline (G-R-P) tripeptide core flanked by basic amino acids. Recent reports documented variations in the sequence of AT-hooks and revealed RNA binding activity of some canonical AT-hooks, suggesting a higher structural and functional variability of this protein domain than previously anticipated. Here we describe the discovery and characterization of the extended AT-hook peptide motif (eAT-hook), in which basic amino acids appear symmetrical mainly at a distance of 12–15 amino acids from the G-R-P core. We identified 80 human and 60 mouse eAT-hook proteins and biochemically characterized the eAT-hooks of Tip5/BAZ2A, PTOV1 and GPBP1. Microscale thermophoresis and electrophoretic mobility shift assays reveal the nucleic acid binding features of this peptide motif, and show that eAT-hooks bind RNA with one order of magnitude higher affinity than DNA. In addition, cellular localization studies suggest a role for the N-terminal eAT-hook of PTOV1 in nucleocytoplasmic shuttling. In summary, our findings classify the eAT-hook as a novel nucleic acid binding motif, which potentially mediates various RNA-dependent cellular processes.
DOI: 10.6084/m9.figshare.1477780
title: Twitter Archive from Evidence Based Library and Information Practice Conference (#EBLIP8)

description: This file contains a data set of 4556 tweets (4550 unique tweets) tagged with #EBLIP8 (case not sensitive) that were published on Twitter between Sun Jun 28 05:31:01 +0000 2015 and Thu Jul 09 03:34:15 +0000 2015. This file was created and shared by Sarah Gallagher @sarahlibrarina (University of Otago, Dunedin, New Zealand) with a Creative Commons- Attribution license (CC-BY) for academic research and educational use. The Tweets contained in this file were collected using Martin Hawksey’s [@mhawksey] TAGS 6.0 http://tags.hawksey.info/ An automatic deduplication has been performed but data may require further refining. Mass tweets by trending services have been removed. Retweets have been retained. The contents of each Tweet are responsibility of the original authors. This data set has been shared “as is”, for educational and research purposes. As noted by Priego [1] “both research and experience show that the Twitter search API isn't 100% reliable. Large tweet volumes affect the search collection process. The API might "over-represent the more central users", not offering "an accurate picture of peripheral activity" (González-Bailón, Sandra, et al. 2012).” Therefore there is no guarantee that this file all Tweets tagged with (#EBLIP8) during the indicated period. This dataset is shared to encourage open research into scholarly activity on Twitter. If you use or refer to this data in any way please cite using the preferred citation above. Contact: @sarahlibrarina [1] Priego, Ernesto (2014): A #HEFCEmetrics Twitter Archive. figshare. http://dx.doi.org/10.6084/m9.figshare.1196029.
DOI: 10.6084/m9.figshare.1477779
title: Chlorophyll <i>a</i> is the crucial redox sensor and transmembrane signal transmitter in the cytochrome <i>b</i><sub>6</sub><i>f</i> complex. Components and mechanisms of state transitions from the hydrophobic mismatch viewpoint

description: The cytochrome (cyt) <i>b</i><sub>6</sub><i>f</i> complex is involved in the transmembrane redox signaling that triggers state transitions in cyanobacteria and chloroplasts. However, the components and molecular mechanisms are still unclear. In an attempt to solve this long-standing problem, we first focused on the unknown role of a single chlorophyll <i>a</i> (Chl<i>a</i>) in cyt <i>b</i><sub>6</sub><i>f</i> with a new approach based on Chl<i>a</i> structural properties. Various <i>b</i><sub>6</sub><i>f</i> X-ray crystal structures were analyzed to identify their differences, which correlate with differences in Chl<i>a</i> molecular volume. We found that the distance of the Rieske [2Fe-2S] cluster to Chl<i>a</i> correlates with the distance between a pair of residues at the <i>Q</i><sub>o</sub>-site and the distance between a pair of residues at the opposite membrane side. These correlations were accompanied by the rotation of a key peripheral residue and by changes in the hydrophobic thickness of cyt <i>b</i><sub>6</sub><i>f</i>. Parallel analysis of cyt <i>bc</i><sub>1</sub> crystal structures allowed us to conclude that Chl<i>a</i> acts as the crucial redox sensor and transmembrane signal transmitter in <i>b</i><sub>6</sub><i>f</i> for changes in the plastoquinone pool redox state. The hydrophobic mismatch induced by the changed hydrophobic thickness of cyt <i>b</i><sub>6</sub><i>f</i> is the driving force for the structural reorganizations of the photosynthetic apparatus during induction and the progression of state transitions in cyanobacteria and chloroplasts. A mechanism for LHCII kinase activation in chloroplasts is also proposed. Our understanding of the dynamic structural changes in <i>bc</i>-complexes during turnover at the <i>Q</i><sub>o</sub>-site and state transitions is augmented by the time-sequence ordering of 56 <i>bc</i> crystal structures.
DOI: 10.6084/m9.figshare.1477780.v1
title: Twitter Archive from Evidence Based Library and Information Practice Conference (#EBLIP8)

description: This file contains a data set of 4556 tweets (4550 unique tweets) tagged with #EBLIP8 (case not sensitive) that were published on Twitter between Sun Jun 28 05:31:01 +0000 2015 and Thu Jul 09 03:34:15 +0000 2015. This file was created and shared by Sarah Gallagher @sarahlibrarina (University of Otago, Dunedin, New Zealand) with a Creative Commons- Attribution license (CC-BY) for academic research and educational use. The Tweets contained in this file were collected using Martin Hawksey’s [@mhawksey] TAGS 6.0 http://tags.hawksey.info/ An automatic deduplication has been performed but data may require further refining. Mass tweets by trending services have been removed. Retweets have been retained. The contents of each Tweet are responsibility of the original authors. This data set has been shared “as is”, for educational and research purposes. As noted by Priego [1] “both research and experience show that the Twitter search API isn't 100% reliable. Large tweet volumes affect the search collection process. The API might "over-represent the more central users", not offering "an accurate picture of peripheral activity" (González-Bailón, Sandra, et al. 2012).” Therefore there is no guarantee that this file all Tweets tagged with (#EBLIP8) during the indicated period. This dataset is shared to encourage open research into scholarly activity on Twitter. If you use or refer to this data in any way please cite using the preferred citation above. Contact: @sarahlibrarina [1] Priego, Ernesto (2014): A #HEFCEmetrics Twitter Archive. figshare. http://dx.doi.org/10.6084/m9.figshare.1196029.
DOI: 10.6084/m9.figshare.1477779.v1
title: Chlorophyll <i>a</i> is the crucial redox sensor and transmembrane signal transmitter in the cytochrome <i>b</i><sub>6</sub><i>f</i> complex. Components and mechanisms of state transitions from the hydrophobic mismatch viewpoint

description: The cytochrome (cyt) <i>b</i><sub>6</sub><i>f</i> complex is involved in the transmembrane redox signaling that triggers state transitions in cyanobacteria and chloroplasts. However, the components and molecular mechanisms are still unclear. In an attempt to solve this long-standing problem, we first focused on the unknown role of a single chlorophyll <i>a</i> (Chl<i>a</i>) in cyt <i>b</i><sub>6</sub><i>f</i> with a new approach based on Chl<i>a</i> structural properties. Various <i>b</i><sub>6</sub><i>f</i> X-ray crystal structures were analyzed to identify their differences, which correlate with differences in Chl<i>a</i> molecular volume. We found that the distance of the Rieske [2Fe-2S] cluster to Chl<i>a</i> correlates with the distance between a pair of residues at the <i>Q</i><sub>o</sub>-site and the distance between a pair of residues at the opposite membrane side. These correlations were accompanied by the rotation of a key peripheral residue and by changes in the hydrophobic thickness of cyt <i>b</i><sub>6</sub><i>f</i>. Parallel analysis of cyt <i>bc</i><sub>1</sub> crystal structures allowed us to conclude that Chl<i>a</i> acts as the crucial redox sensor and transmembrane signal transmitter in <i>b</i><sub>6</sub><i>f</i> for changes in the plastoquinone pool redox state. The hydrophobic mismatch induced by the changed hydrophobic thickness of cyt <i>b</i><sub>6</sub><i>f</i> is the driving force for the structural reorganizations of the photosynthetic apparatus during induction and the progression of state transitions in cyanobacteria and chloroplasts. A mechanism for LHCII kinase activation in chloroplasts is also proposed. Our understanding of the dynamic structural changes in <i>bc</i>-complexes during turnover at the <i>Q</i><sub>o</sub>-site and state transitions is augmented by the time-sequence ordering of 56 <i>bc</i> crystal structures.
DOI: 10.6084/m9.figshare.1477010
title: Data on Baltimore restaurants

description: Read the XML data on Baltimore restaurants from here: https://d396qusza40orc.cloudfront.net/getdata%2Fdata%2Frestaurants.xml
DOI: 10.6084/m9.figshare.1477012
title: Survey about housing for the state of Idaho

description: The American Community Survey distributes downloadable data about United States communities. Download the 2006 microdata survey about housing for the state of Idaho using download.file() from here: https://d396qusza40orc.cloudfront.net/getdata%2Fdata%2Fss06pid.csv
DOI: 10.6084/m9.figshare.1477009
title: Excel spreadsheet on Natural Gas Aquisition Program

description: Download the Excel spreadsheet on Natural Gas Aquisition Program here: https://d396qusza40orc.cloudfront.net/getdata%2Fdata%2FDATA.gov_NGAP.xlsx (original data source: http://catalog.data.gov/dataset/natural-gas-acquisition-program)
DOI: 10.6084/m9.figshare.1476992
title: Input tracts (subject #05)

description: Fiber tracts of subject #05
DOI: 10.6084/m9.figshare.1476993
title: Input tracts (subject #06)

description: Fiber tracts of subject #06
DOI: 10.6084/m9.figshare.1476991
title: Input tracts (subject #04)

description: Fiber tracts of subject #04
DOI: 10.6084/m9.figshare.1476992.v1
title: Input tracts (subject #05)

description: Fiber tracts of subject #05
DOI: 10.6084/m9.figshare.1476993.v1
title: Input tracts (subject #06)

description: Fiber tracts of subject #06