cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccdc.csd.cc26jh19
title: CCDC 2041630: Experimental Crystal Structure Determination

description: Related Article: Neel Deorukhkar, Céline Besnard, Laure Guénée, Claude Piguet|2021|Dalton Trans.|50|1206|doi:10.1039/D0DT03828H
DOI: 10.5517/ccdc.csd.cc26mv6x
title: CCDC 2044859: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.5517/ccdc.csd.cc26mv7y
title: CCDC 2044860: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.5517/ccdc.csd.cc26mv8z
title: CCDC 2044861: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.5517/ccdc.csd.cc26mv90
title: CCDC 2044862: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.5517/ccdc.csd.cc26mvb1
title: CCDC 2044863: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.5517/ccdc.csd.cc26mvc2
title: CCDC 2044864: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.5517/ccdc.csd.cc26mvd3
title: CCDC 2044865: Experimental Crystal Structure Determination

description: Related Article: Henry Shere, Michael S. Hill, Anne-Frédérique Pécharman, Mary F. Mahon|2021|Dalton Trans.|50|1283|doi:10.1039/D0DT04016A
DOI: 10.25505/fiz.icsd.cc26pcmx
title: CSD 2046329: Experimental Crystal Structure Determination

description: Related Article: Walter Jung, Bodo Böhme, Julia M. Hübner, Ulrich Burkhardt, Horst Borrmann, Matej Bobnar, Hong Duong Nguyen, Ingo Pantenburg, Martin Etter, Ulrich Schwarz, Yuri Grin, Michael Baitinger|2021|Dalton Trans.|50|1274|doi:10.1039/D0DT03339A
DOI: 10.25505/fiz.icsd.cc26pcny
title: CSD 2046330: Experimental Crystal Structure Determination

description: Related Article: Walter Jung, Bodo Böhme, Julia M. Hübner, Ulrich Burkhardt, Horst Borrmann, Matej Bobnar, Hong Duong Nguyen, Ingo Pantenburg, Martin Etter, Ulrich Schwarz, Yuri Grin, Michael Baitinger|2021|Dalton Trans.|50|1274|doi:10.1039/D0DT03339A
DOI: 10.25505/fiz.icsd.cc26pcr1
title: CSD 2046333: Experimental Crystal Structure Determination

description: Related Article: Walter Jung, Bodo Böhme, Julia M. Hübner, Ulrich Burkhardt, Horst Borrmann, Matej Bobnar, Hong Duong Nguyen, Ingo Pantenburg, Martin Etter, Ulrich Schwarz, Yuri Grin, Michael Baitinger|2021|Dalton Trans.|50|1274|doi:10.1039/D0DT03339A
DOI: 10.5517/ccdc.csd.cc26q098
title: CCDC 2046939: Experimental Crystal Structure Determination

description: Related Article: Jie Li, Peng Du, Ying-Ying Liu, Jian-Fang Ma|2021|Dalton Trans.|50|1349|doi:10.1039/D0DT04097E
DOI: 10.5517/ccdc.csd.cc26q0b9
title: CCDC 2046940: Experimental Crystal Structure Determination

description: Related Article: Jie Li, Peng Du, Ying-Ying Liu, Jian-Fang Ma|2021|Dalton Trans.|50|1349|doi:10.1039/D0DT04097E
DOI: 10.5517/ccdc.csd.cc26q0cb
title: CCDC 2046941: Experimental Crystal Structure Determination

description: Related Article: Jie Li, Peng Du, Ying-Ying Liu, Jian-Fang Ma|2021|Dalton Trans.|50|1349|doi:10.1039/D0DT04097E
DOI: 10.5517/ccdc.csd.cc26jgnw
title: CCDC 2041618: Experimental Crystal Structure Determination

description: Related Article: Neel Deorukhkar, Céline Besnard, Laure Guénée, Claude Piguet|2021|Dalton Trans.|50|1206|doi:10.1039/D0DT03828H
DOI: 10.5517/ccdc.csd.cc26jgks
title: CCDC 2041615: Experimental Crystal Structure Determination

description: Related Article: Neel Deorukhkar, Céline Besnard, Laure Guénée, Claude Piguet|2021|Dalton Trans.|50|1206|doi:10.1039/D0DT03828H
DOI: 10.5517/ccdc.csd.cc26jgrz
title: CCDC 2041621: Experimental Crystal Structure Determination

description: Related Article: Neel Deorukhkar, Céline Besnard, Laure Guénée, Claude Piguet|2021|Dalton Trans.|50|1206|doi:10.1039/D0DT03828H
DOI: 10.5517/ccdc.csd.cc26jh08
title: CCDC 2041629: Experimental Crystal Structure Determination

description: Related Article: Neel Deorukhkar, Céline Besnard, Laure Guénée, Claude Piguet|2021|Dalton Trans.|50|1206|doi:10.1039/D0DT03828H
DOI: 10.5517/ccdc.csd.cc26jgs0
title: CCDC 2041622: Experimental Crystal Structure Determination

description: Related Article: Neel Deorukhkar, Céline Besnard, Laure Guénée, Claude Piguet|2021|Dalton Trans.|50|1206|doi:10.1039/D0DT03828H
DOI: 10.5517/ccdc.csd.cc2602y8
title: CCDC 2025879: Experimental Crystal Structure Determination

description: Related Article: Wenhui Ren, Hui Liu, Fen You, Pengjuan Mao, Yat-Ming So, Xiaohui Kang, Xiaochao Shi|2021|Dalton Trans.|50|1334|doi:10.1039/D0DT04040A
DOI: 10.5517/ccdc.csd.cc2602z9
title: CCDC 2025880: Experimental Crystal Structure Determination

description: Related Article: Wenhui Ren, Hui Liu, Fen You, Pengjuan Mao, Yat-Ming So, Xiaohui Kang, Xiaochao Shi|2021|Dalton Trans.|50|1334|doi:10.1039/D0DT04040A
DOI: 10.5517/ccdc.csd.cc26sv1x
title: CCDC 2049659: Experimental Crystal Structure Determination

description: Related Article: Maotong Xu, Zheng-wang Qu, Stefan Grimme, Douglas W. Stephan|2021|J.Am.Chem.Soc.|143|634|doi:10.1021/jacs.0c11482
DOI: 10.5517/ccdc.csd.cc26sv2y
title: CCDC 2049660: Experimental Crystal Structure Determination

description: Related Article: Maotong Xu, Zheng-wang Qu, Stefan Grimme, Douglas W. Stephan|2021|J.Am.Chem.Soc.|143|634|doi:10.1021/jacs.0c11482
DOI: 10.5517/ccdc.csd.cc26t7pz
title: CCDC 2050051: Experimental Crystal Structure Determination

description: Related Article: Luong Phong Ho, Matthias Tamm|2021|Dalton Trans.|50|1202|doi:10.1039/D1DT00140J
DOI: 10.5517/ccdc.csd.cc26t7q0
title: CCDC 2050052: Experimental Crystal Structure Determination

description: Related Article: Luong Phong Ho, Matthias Tamm|2021|Dalton Trans.|50|1202|doi:10.1039/D1DT00140J
DOI: 10.6084/m9.figshare.11339807
title: Data Egyptian vultures seasonal sociality

description: data from van Overveld et al. 2020 Behavioral Ecology and Sociobiology 74:28<br>
DOI: 10.6084/m9.figshare.13691664
title: Table S1: Locations of PS data tested through parametric and non-parametric analyses and results of the statistical tests. Fault motion reversals predating the Mw 6.3 2009 Lâ€™Aquila earthquake: Insights from synthetic aperture radar data

description: Table S1: Locations of PS data tested through parametric and non-parametric analyses and results of the statistical tests.
DOI: 10.6084/m9.figshare.13691664.v1
title: Table S1: Locations of PS data tested through parametric and non-parametric analyses and results of the statistical tests. Fault motion reversals predating the Mw 6.3 2009 Lâ€™Aquila earthquake: Insights from synthetic aperture radar data

description: Table S1: Locations of PS data tested through parametric and non-parametric analyses and results of the statistical tests.
DOI: 10.6084/m9.figshare.13691239
title: Results of compression test of single corn grain

description: In this data the results of compression test for 100 grain was presented, also the summary of size and shape determination of grain was presented.
DOI: 10.6084/m9.figshare.13690795.v2
title: normalised

description: Items for UCSC browser access, Solana lab
DOI: 10.6084/m9.figshare.5772732
title: Potential roles of inorganic phosphate on the progression of initially bound glucopyranose toward the nonenzymatic glycation of human hemoglobin: Mechanistic diversity and impacts on site selectivity

description: Nonenzymatic glycation (NEG) begins with the non-covalent binding of a glucopyranose to a protein. The bound glucopyranose must then undergo structural modification to generate a bound electrophile that can reversibly form a Schiff base, which can then lead to Amadori intermediates, and ultimately to glycated proteins. Inorganic phosphate (Pi) is known to accelerate the glycation of human hemoglobin (HbA), although the specific mechanism(s) of Pi as an effector reagent have not been determined. The aim of this study was to determine whether Pi and a glucopyranose can concomitantly bind to HbA and react while bound within the early, noncovalent stages to generate electrophilic species capable of progress in NEG. <sup>31</sup>P and <sup>1</sup>HNMR of model reactions confirm that bimolecular reactions between Pi and glucopyranose occur generating modified glucose electrophiles. Computations of protein/substrate interactions predict that Pi can concomitantly bind with a glucopyranose in HbA pockets with geometries suitable for multiple acid/base mechanisms that can generate any of four transient electrophiles. Pi-facilitated mechanisms in the noncovalent stages predict that the glycation of β-Val1 of HbA to HbA1c is a “hot spot” because the β-Val1 pocket facilitates many more mechanisms than any other site. The mechanistic diversity of the Pi effect within the early noncovalent stages of NEG predicts well the overall site selectivity observed from the <i>in vivo</i> glycation of HbA in the presence of Pi. These insights extend our basic understanding of the NEG process and may have clinical implications for diabetes mellitus and even normal aging.
DOI: 10.6084/m9.figshare.5772732.v2
title: Potential roles of inorganic phosphate on the progression of initially bound glucopyranose toward the nonenzymatic glycation of human hemoglobin: Mechanistic diversity and impacts on site selectivity

description: Nonenzymatic glycation (NEG) begins with the non-covalent binding of a glucopyranose to a protein. The bound glucopyranose must then undergo structural modification to generate a bound electrophile that can reversibly form a Schiff base, which can then lead to Amadori intermediates, and ultimately to glycated proteins. Inorganic phosphate (Pi) is known to accelerate the glycation of human hemoglobin (HbA), although the specific mechanism(s) of Pi as an effector reagent have not been determined. The aim of this study was to determine whether Pi and a glucopyranose can concomitantly bind to HbA and react while bound within the early, noncovalent stages to generate electrophilic species capable of progress in NEG. <sup>31</sup>P and <sup>1</sup>HNMR of model reactions confirm that bimolecular reactions between Pi and glucopyranose occur generating modified glucose electrophiles. Computations of protein/substrate interactions predict that Pi can concomitantly bind with a glucopyranose in HbA pockets with geometries suitable for multiple acid/base mechanisms that can generate any of four transient electrophiles. Pi-facilitated mechanisms in the noncovalent stages predict that the glycation of β-Val1 of HbA to HbA1c is a “hot spot” because the β-Val1 pocket facilitates many more mechanisms than any other site. The mechanistic diversity of the Pi effect within the early noncovalent stages of NEG predicts well the overall site selectivity observed from the <i>in vivo</i> glycation of HbA in the presence of Pi. These insights extend our basic understanding of the NEG process and may have clinical implications for diabetes mellitus and even normal aging.
DOI: 10.6084/m9.figshare.6444506
title: Engineering elastic properties into an anti-TNFα monoclonal antibody

description: Injecting anti-tumor necrosis factor (TNF)α antibodies into patient joints at the site of inflammation, inter-articular (IA) delivery, has demonstrated modest success for treatment of Spondyloarthritis (SpA), Rheumatoid Arthritis (RA), and osteoarthritis. However, IA delivery is not the treatment route of choice due to rapid clearance from the site of administration. Elastin-like polypeptides (ELPs) are reported to undergo phase transition; forming reversible aggregates above their transition temperature, which when injected into IA space have a 25-fold longer half-life compared to the soluble form. Here, we fused an ELP repeat to the C-terminus of each heavy chain of an anti-TNFα monoclonal antibody (mAb) and provide detailed characterization of the fusion IgG molecule. Expression and purification yielded homogenous protein confirmed by gels, hydrophobic-interaction chromatography, Capilary Electrophoresis (CE), Mass Spectrometry (MS), and analytical ultracentrifugation. The ELPs altered hydrophobicity and pI of the parent mAb and new elastic properties were imparted to the molecule; forming large stable complexes with a hydrodynamic radius of 40 nm above 39°C that dissociated into soluble, active monomer below 37°C. The fusion mAb retained its affinity and ability to neutralize TNFα as determined by surface plasmon resonance and cell-based assay, respectively, with equal potency to unmodified anti-TNFα mAb. Differential-scanning calorimetry studies show stabilization of adjacent C<sub>H</sub>2 and C<sub>H</sub>3 domains in the fusion molecule and the aggregated molecule was found to be fully functional after 7 days at 37°C. For the first time, we reveal architecture of an ELP-fusion mAb and binding to antigen using single-particle-transmission-electron microscopy. Unstructured ELP was visualized at the C-terminus and binding to antigen was shown at the <i>N</i>-terminus. Collectively, these studies indicate that it is possible to impart elastic properties to a monoclonal antibody while retaining purity, stability, and ability to effectively bind and neutralize antigen.
DOI: 10.6084/m9.figshare.5772732.v1
title: Potential roles of inorganic phosphate on the progression of initially bound glucopyranose toward the nonenzymatic glycation of human hemoglobin: mechanistic diversity and impacts on site selectivity

description: Nonenzymatic glycation (NEG) begins with the non-covalent binding of a glucopyranose to a protein. The bound glucopyranose must then undergo structural modification to generate a bound electrophile that can reversibly form a Schiff base, which can then lead to Amadori intermediates, and ultimately to glycated proteins. Inorganic phosphate (Pi) is known to accelerate the glycation of human hemoglobin (HbA), although the specific mechanism(s) of Pi as an effector reagent have not been determined. The aim of this study was to determine whether Pi and a glucopyranose can concomitantly bind to HbA and react while bound within the early, noncovalent stages to generate electrophilic species capable of progress in NEG. <sup>31</sup>P and <sup>1</sup>HNMR of model reactions confirm that bimolecular reactions between Pi and glucopyranose occur generating modified glucose electrophiles. Computations of protein/substrate interactions predict that Pi can concomitantly bind with a glucopyranose in HbA pockets with geometries suitable for multiple acid/base mechanisms that can generate any of four transient electrophiles. Pi-facilitated mechanisms in the noncovalent stages predict that the glycation of β-Val1 of HbA to HbA1c is a “hot spot” because the β-Val1 pocket facilitates many more mechanisms than any other site. The mechanistic diversity of the Pi effect within the early noncovalent stages of NEG predicts well the overall site selectivity observed from the <i>in vivo</i> glycation of HbA in the presence of Pi. These insights extend our basic understanding of the NEG process and may have clinical implications for diabetes mellitus and even normal aging.
DOI: 10.6084/m9.figshare.6444506.v1
title: Engineering elastic properties into an anti-TNFα monoclonal antibody

description: Injecting anti-tumor necrosis factor (TNF)α antibodies into patient joints at the site of inflammation, inter-articular (IA) delivery, has demonstrated modest success for treatment of Spondyloarthritis (SpA), Rheumatoid Arthritis (RA), and osteoarthritis. However, IA delivery is not the treatment route of choice due to rapid clearance from the site of administration. Elastin-like polypeptides (ELPs) are reported to undergo phase transition; forming reversible aggregates above their transition temperature, which when injected into IA space have a 25-fold longer half-life compared to the soluble form. Here, we fused an ELP repeat to the C-terminus of each heavy chain of an anti-TNFα monoclonal antibody (mAb) and provide detailed characterization of the fusion IgG molecule. Expression and purification yielded homogenous protein confirmed by gels, hydrophobic-interaction chromatography, Capilary Electrophoresis (CE), Mass Spectrometry (MS), and analytical ultracentrifugation. The ELPs altered hydrophobicity and pI of the parent mAb and new elastic properties were imparted to the molecule; forming large stable complexes with a hydrodynamic radius of 40 nm above 39°C that dissociated into soluble, active monomer below 37°C. The fusion mAb retained its affinity and ability to neutralize TNFα as determined by surface plasmon resonance and cell-based assay, respectively, with equal potency to unmodified anti-TNFα mAb. Differential-scanning calorimetry studies show stabilization of adjacent C<sub>H</sub>2 and C<sub>H</sub>3 domains in the fusion molecule and the aggregated molecule was found to be fully functional after 7 days at 37°C. For the first time, we reveal architecture of an ELP-fusion mAb and binding to antigen using single-particle-transmission-electron microscopy. Unstructured ELP was visualized at the C-terminus and binding to antigen was shown at the <i>N</i>-terminus. Collectively, these studies indicate that it is possible to impart elastic properties to a monoclonal antibody while retaining purity, stability, and ability to effectively bind and neutralize antigen.
DOI: 10.6084/m9.figshare.13690795
title: normalised

description: Items for UCSC browser access, Solana lab
DOI: 10.6084/m9.figshare.13690795.v4
title: normalised

description: Items for UCSC browser access, Solana lab
DOI: 10.6084/m9.figshare.13690795.v3
title: normalised

description: Items for UCSC browser access, Solana lab
DOI: 10.6084/m9.figshare.13497219.v2
title: Sampling techniques for rumen microbial analysis

description: The purpose of this study was to compare the microbial composition of samples retrieved by different techniques at different timepoints post-feeding and rumen fractions (whole, liquid, and solid) to identify an appropriate non-invasive sampling method to serve as a proxy for cannula-derived rumen samples for microbial analysis. <br>
DOI: 10.6084/m9.figshare.12111375
title: figshare Files 1. Acetobacterium woodii RNA-Seq

description: RNA-Seq result of Acetobacterium woodii
DOI: 10.6084/m9.figshare.12111378
title: figshare Files 3. Clostridium drakei RNA-Seq

description: RNA-Seq result of Clostridium drakei
DOI: 10.6084/m9.figshare.12111384
title: figshare Files 7. Clostridium drakei Ribosome profiling

description: Ribosome profiling result of Clostridium drakei
DOI: 10.6084/m9.figshare.12111375.v1
title: figshare Files 1. Acetobacterium woodii RNA-Seq

description: RNA-Seq result of Acetobacterium woodii
DOI: 10.6084/m9.figshare.12111381.v1
title: figshare Files 2. Clostridium aceticum RNA-Seq

description: RNA-Seq result of Clostridium aceticum
DOI: 10.6084/m9.figshare.12111387
title: figshare Files 4. Eubacterium limosum RNA-Seq

description: RNA-Seq result of Eubacterium limosum
DOI: 10.6084/m9.figshare.12111378.v1
title: figshare Files 3. Clostridium drakei RNA-Seq

description: RNA-Seq result of Clostridium drakei
DOI: 10.6084/m9.figshare.12111381
title: figshare Files 2. Clostridium aceticum RNA-Seq

description: RNA-Seq result of Clostridium aceticum
DOI: 10.6084/m9.figshare.12111384.v1
title: figshare Files 7. Clostridium drakei Ribosome profiling

description: Ribosome profiling result of Clostridium drakei
DOI: 10.6084/m9.figshare.12111390
title: figshare Files 6. Clostridium aceticum Ribosome profiling

description: Ribosome profiling result of Clostridium aceticum
DOI: 10.6084/m9.figshare.12111393
title: figshare Files 5. Acetobacterium woodii Ribosome profiling

description: Ribosome profiling result of Acetobacterium woodii
DOI: 10.6084/m9.figshare.12111396
title: figshare Files 8. Eubacterium limosum Ribosome profiling

description: Ribosome profiling result of Eubacterium limosum
DOI: 10.6084/m9.figshare.12111387.v1
title: figshare Files 4. Eubacterium limosum RNA-Seq

description: RNA-Seq result of Eubacterium limosum
DOI: 10.6084/m9.figshare.12111390.v1
title: figshare Files 6. Clostridium aceticum Ribosome profiling

description: Ribosome profiling result of Clostridium aceticum
DOI: 10.6084/m9.figshare.12111393.v1
title: figshare Files 5. Acetobacterium woodii Ribosome profiling

description: Ribosome profiling result of Acetobacterium woodii
DOI: 10.6084/m9.figshare.12111396.v1
title: figshare Files 8. Eubacterium limosum Ribosome profiling

description: Ribosome profiling result of Eubacterium limosum
DOI: 10.6073/pasta/8a31984e539204df681dc8587fc4ea7a
title: Jornada Basin LTER: Wireless meteorological station at NPP G-IBPE site: 5-minute summary wind and air temperature data: 2013 - ongoing

description: 5-minute summary data at NPP G-IBPE met station. Average air temperature, wind speed and wind direction are measured and calculated based on 1-second scan rate of all sensors located at an automated meteorological station installed at Jornada LTER NPP G-IBPE site. Wind speed is measured at 75 cm, 150 cm, and 300 cm, wind direction at approximately 3m, and air temperature at approximate 2.5m. This climate station is operated by the Jornada LTER Program. This is an ONGOING dataset.
DOI: 10.6073/pasta/aaa047d90346994afc420b2bf42d59ac
title: Jornada Basin LTER: Wireless meteorological station at NPP G-IBPE site: 1-hour summary data: 2013 - ongoing

description: Hourly summary data at NPP G-IBPE met station. Average/maximum/minimum air temperature; average relative humidity and wind direction; average/maximum wind speed. These are measured and calculated based on 1-second scan rate of all sensors located at an automated meteorological station installed at Jornada LTER NPP G-IBPE site. Wind speed is measured at 75 cm, 150 cm, and 300 cm, wind direction at approximately 3m, and air temperature and relative humidity at approximate 2.5m. This climate station is operated by the Jornada LTER Program. This is an ONGOING dataset.
DOI: 10.34892/4q5v-gf37
title: Natural and Modified Habitat Screening Layer

description: This dataset classifies the global terrestrial land surface into one of four categories: likely Natural, potential Natural, potential Modified, and likely Modified. The dataset use freely available data layers in combination to develop a new global layer that identifies natural and modified habitat. It is aligned with the definitions of natural and modified habitat from the highly influential Performance Standard 6 (PS6) of the International Finance Corporation (IFC). However, we propose this layer as an output that can be used beyond the IFC and could be integrated into the investment decision making of global and regional banks, or the decision making of international corporations.
DOI: 10.6073/pasta/d2cbd5e8e3b16638b3a911d229ea4689
title: Jornada Basin LTER: Wireless meteorological station at NPP G-IBPE site: 30-minute summary data: 2013 - ongoing

description: 30-minute summary data at NPP G-IBPE met station. Average air temperature, relative humidity, wind speed and wind direction are measured and calculated based on 1-second scan rate of all sensors located at an automated meteorological station installed at Jornada LTER NPP G-IBPE site. Wind speed is measured at 75 cm, 150 cm, and 300 cm, wind direction at approximately 3m, and air temperature and relative humidity at approximate 2.5m. This climate station is operated by the Jornada LTER Program. This is an ONGOING dataset.