cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.21476642.v1
title: <i>IRF1</i> expression might be a biomarker of CD8+ T cell infiltration in cutaneous melanoma

description: This study aimed to explore the expression profile of interferon regulatory factor (IRF) genes in skin cutaneous melanoma (SKCM), their association with CD8 + T cell infiltration, and the potential regulatory network in melanoma and non-melanoma cells. Bioinformatic analysis was conducted using the SKCM subset of The Cancer Genome Atlas (TCGA) Pan-Cancer, Genotype-Tissue Expression Project (GTEx), and single-cell RNA-seq data from the Human Protein Atlas and Jerby-Arnon et al. 2018ʹs dataset. <i>IRF1</i> expression is robustly associated with moderate to strong CD8 + T cell infiltration in the tumor microenvironment. It is ubiquitously expressed in tumor and non-tumor cells in melanoma. Melanoma tumor cells and macrophages had 16/36 and 9/27 cell-specific <i>IRF1</i>-correlated genes, respectively. The methylation of four CpG sites (cg00255919, cg21138405, cg15375424, and cg27587780) within the <i>IRF1</i> gene locus showed moderate to strong negative correlations with <i>IRF1</i> expression. <i>IRF1</i> expression might serve as a biomarker indicating CD8 + T cell infiltration in skin melanoma. It might exert different regulatory effects in melanoma and non-melanoma cells in the tumor microenvironment. Cg00255919, cg21138405, cg15375424, and cg27587780 are four critical CpG sites that might modulate the transcription of <i>IRF1</i>.
DOI: 10.5281/zenodo.5786091
title: Numerical methodology for design and evaluation of natural circulation systems for MSR applications - Dataset

description: Dataset associated to the 2022 ANS Annual meeting conference paper "Numerical methodology for design and evaluation of natural circulation systems for MSR applications".
DOI: 10.5281/zenodo.5786092
title: Numerical methodology for design and evaluation of natural circulation systems for MSR applications - Dataset

description: Dataset associated to the 2022 ANS Annual meeting conference paper "Numerical methodology for design and evaluation of natural circulation systems for MSR applications".
DOI: 10.17864/1947.000394
title: Unique thermal expansion properties of water key to the formation of sea ice on Earth: model outputs

description: Description: Outputs from the MIT General Circulation Model (MITgcm) run in an idealized coupled ocean-atmopshere-sea ice configuration. This dataset contains all data necessary to reproduce figures and analysis published in Roquet et al. (2022). It includes outputs from the ocean, atmosphere, sea ice, and land surface components of the MITgcm simulations of the Control simulation and sensitivity experiments. Outputs cover the last 50 years of all simulations after spin-up. Roquet, F., D. Ferreira, R. Caneill, D. Schlesinger, and G. Madec, 2022: Unique thermal expansion properties of water key to the formation of sea ice on Earth. Science Advances. DOI:10.1126/sciadv.abq0793
DOI: 10.6084/m9.figshare.20509272
title: CPGView

description: CPGview-RSG: A Package for Visualizing the Repeats and Spliced Genes of Chloroplast genomes
DOI: 10.6084/m9.figshare.20509272.v1
title: CPGView

description: CPGview-RSG: A Package for Visualizing the Repeats and Spliced Genes of Chloroplast genomes
DOI: 10.5281/zenodo.7317896
title: Minimizer collision statistics (BLEND: A Fast, Memory-Efficient, and Accurate Mechanism to Find Fuzzy Seed Matches in Genome Analysis)

description: This dataset includes the statistics for the minimizers that generate the same hash value (i.e., collisions). The hash values are generated using a low-collision hash function and the SimHash technique in BLEND. *collision_stats.txt files include the overall collision statistics for a tool and configuration of the tool (i.e., the number of colliding minimizer pairs with a certain edit distance and their ratio to all number of collisions). For example blend_n3_collision_stats.txt shows the statistics for BLEND where the number of neighbors is set to 3 when running BLEND. _sim.csv files include all minimizer pairs with the same hash value and the edit distance between them.
DOI: 10.5281/zenodo.7317895
title: Minimizer collision statistics (BLEND: A Fast, Memory-Efficient, and Accurate Mechanism to Find Fuzzy Seed Matches in Genome Analysis)

description: This dataset includes the statistics for the minimizers that generate the same hash value (i.e., collisions). The hash values are generated using a low-collision hash function and the SimHash technique in BLEND. *collision_stats.txt files include the overall collision statistics for a tool and configuration of the tool (i.e., the number of colliding minimizer pairs with a certain edit distance and their ratio to all number of collisions). For example blend_n3_collision_stats.txt shows the statistics for BLEND where the number of neighbors is set to 3 when running BLEND. _sim.csv files include all minimizer pairs with the same hash value and the edit distance between them.
DOI: 10.5281/zenodo.6644086
title: Numerical model setup for studying the energetics of the ocean current under sea ice

description: This dataset contains model code and input files for studying the energetics of the ocean current under sea ice. The model used in this study is the Massachusetts Institute of Technology general circulation model (MITgcm). Original source code is the MITgcm_c66m. code: contains code configuration. input_PD: contains parameter settings and input files for the base experiment Exp-PD (initial perturbation + ice-ocean drag). input_D: contains parameter settings and input files for the sensitivity experiment Exp-D (no initial perturbation). input_P: contains parameter settings and input files for the sensitivity experiment Exp-P (no ice-ocean drag). input_PD100: contains parameter settings and input files for the sensitivity experiment Exp-PD100 (a restart of Exp-P from day 100 and is run for 100 days with the ice-ocean drag).
DOI: 10.5281/zenodo.7317884
title: Numerical model setup for studying the energetics of the ocean current under sea ice

description: This dataset contains model code and input files for studying the energetics of the ocean current under sea ice. The model used in this study is the Massachusetts Institute of Technology general circulation model (MITgcm). Original source code is the MITgcm_c66m. code: contains code configuration for Exp-PD, Exp-D, Exp-P, and Exp-PD100. code_F: contains code configuration for Exp-PF. input_PD: contains parameter settings and input files for the base experiment Exp-PD (initial perturbation + ice-ocean drag). input_D: contains parameter settings and input files for the sensitivity experiment Exp-D (no initial perturbation). input_P: contains parameter settings and input files for the sensitivity experiment Exp-P (no ice-ocean drag). input_PD100: contains parameter settings and input files for the sensitivity experiment Exp-PD100 (a restart of Exp-P from day 100 and is run for 100 days with the ice-ocean drag). input_F: contains parameter settings and input files for the sensitivity experiment Exp-PF (no sea ice model; Forcings include surface stress, shortwave radiation, and heat and freshwater fluxes diagnosed from Exp-PD).
DOI: 10.5281/zenodo.6644085
title: Numerical model setup for studying the energetics of the ocean current under sea ice

description: This dataset contains model code and input files for studying the energetics of the ocean current under sea ice. The model used in this study is the Massachusetts Institute of Technology general circulation model (MITgcm). Original source code is the MITgcm_c66m. code: contains code configuration for Exp-PD, Exp-D, Exp-P, and Exp-PD100. code_F: contains code configuration for Exp-PF. input_PD: contains parameter settings and input files for the base experiment Exp-PD (initial perturbation + ice-ocean drag). input_D: contains parameter settings and input files for the sensitivity experiment Exp-D (no initial perturbation). input_P: contains parameter settings and input files for the sensitivity experiment Exp-P (no ice-ocean drag). input_PD100: contains parameter settings and input files for the sensitivity experiment Exp-PD100 (a restart of Exp-P from day 100 and is run for 100 days with the ice-ocean drag). input_F: contains parameter settings and input files for the sensitivity experiment Exp-PF (no sea ice model; Forcings include surface stress, shortwave radiation, and heat and freshwater fluxes diagnosed from Exp-PD).
DOI: 10.5281/zenodo.6862458
title: Datasets for ``Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo''

description: <pre>This directory contains Supplemental Material and an index.html file with links to the run directories and idl plotting routines with secondary data for the other figures for the paper "Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo" by A. Brandenburg, H. Zhou and R. Sharma. If anything turns out to be incomplete, please email brandenb@nordita.org. </pre>
DOI: 10.5281/zenodo.6862459
title: Datasets for ``Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo''

description: <pre>This directory contains an index.html file with links to the run directories and idl plotting routines with secondary data for the other figures for the paper "Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo" by A. Brandenburg, H. Zhou and R. Sharma. If anything turns out to be incomplete, please email brandenb@nordita.org. </pre>
DOI: 10.5281/zenodo.7281479
title: Datasets for ``Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo''

description: <pre>This directory contains an index.html file with links to the run directories and idl plotting routines with secondary data for the other figures for the paper "Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo" by A. Brandenburg, H. Zhou and R. Sharma. If anything turns out to be incomplete, please email brandenb@nordita.org. </pre>
DOI: 10.5281/zenodo.7317954
title: Datasets for ``Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo''

description: <pre>This directory contains Supplemental Material and an index.html file with links to the run directories and idl plotting routines with secondary data for the other figures for the paper "Batchelor, Saffman, and Kazantsev spectra in the small-scale dynamo" by A. Brandenburg, H. Zhou and R. Sharma. If anything turns out to be incomplete, please email brandenb@nordita.org. </pre>
DOI: 10.5281/zenodo.7317956
title: Results of first survey

description: This file contains the raw results of our first survey.
DOI: 10.5281/zenodo.7317955
title: Results of first survey

description: This file contains the raw results of our first survey.
DOI: 10.5281/zenodo.7316370
title: GRIST simulations

description: GRIST simulations
DOI: 10.5281/zenodo.7316369
title: GRIST simulations

description: GRIST simulations
DOI: 10.5281/zenodo.7317318
title: patch description generation

description: patch description generation
DOI: 10.5281/zenodo.7317317
title: patch description generation

description: patch description generation
DOI: 10.6084/m9.figshare.21550527
title: Final data.xlsx

description: COVID-19 vaccine breakthrough infections among healthcare workers in atertiary care hospital
DOI: 10.6084/m9.figshare.21550527.v2
title: Final data.xlsx

description: COVID-19 vaccine breakthrough infections among healthcare workers in atertiary care hospital
DOI: 10.6084/m9.figshare.21550527.v1
title: Final data.xlsx

description: COVID-19 vaccine breakthrough infections among healthcare workers in atertiary care hospital
DOI: 10.34740/kaggle/dsv/4508645
title: AutoXGB
DOI: 10.5519/qd.se6c2hfn
title: Query on the Natural History Museum Data Portal (data.nhm.ac.uk) (5327959 records)
DOI: 10.5519/qd.iqjbc4n9
title: Query on the Natural History Museum Data Portal (data.nhm.ac.uk) (1948458 records)
DOI: 10.6084/m9.figshare.21550595
title: Structural basis of the key residue W320 responsible for Hsp90 conformational change

description: The 90-kDa heat shock protein (Hsp90) is a homodimeric molecular chaperone with ATPase activity, which has become an intensely studied target for the development of drugs for the treatment of cancer, neurodegenerative and infectious diseases. The equilibrium between Hsp90 dimers and oligomers is important for modulating its function. In the absence of ATP, the passive chaperone activity of Hsp90 dimers and oligomers has been shown to stabilize client proteins as a holdase, which enhances substrate binding and prevents irreversible aggregation and precipitation of the substrate proteins. In the presence of ATP and its associated cochaperones, Hsp90 homodimers act as foldases with the binding and hydrolysis of ATP driving conformational changes that mediate client folding. Crystal structures of both wild type and W320A mutant Hsp90αMC (middle/C-terminal domain) have been determined, which displayed a preference for hexameric and dimeric states, respectively. Structural analysis showed that W320 is a key residue for Hsp90 oligomerization by forming intermolecular interactions at the Hsp90 hexameric interface through cation-π interactions with R367. W320A substitution results in the formation of a more open conformation of Hsp90, which has not previously been reported, and the induction of a conformational change in the catalytic loop. The structures provide new insights into the mechanism by which W320 functions as a key switch for conformational changes in Hsp90 self-oligomerization, and binding cochaperones and client proteins. Communicated by Ramaswamy H. Sarma
DOI: 10.6084/m9.figshare.21550595.v1
title: Structural basis of the key residue W320 responsible for Hsp90 conformational change

description: The 90-kDa heat shock protein (Hsp90) is a homodimeric molecular chaperone with ATPase activity, which has become an intensely studied target for the development of drugs for the treatment of cancer, neurodegenerative and infectious diseases. The equilibrium between Hsp90 dimers and oligomers is important for modulating its function. In the absence of ATP, the passive chaperone activity of Hsp90 dimers and oligomers has been shown to stabilize client proteins as a holdase, which enhances substrate binding and prevents irreversible aggregation and precipitation of the substrate proteins. In the presence of ATP and its associated cochaperones, Hsp90 homodimers act as foldases with the binding and hydrolysis of ATP driving conformational changes that mediate client folding. Crystal structures of both wild type and W320A mutant Hsp90αMC (middle/C-terminal domain) have been determined, which displayed a preference for hexameric and dimeric states, respectively. Structural analysis showed that W320 is a key residue for Hsp90 oligomerization by forming intermolecular interactions at the Hsp90 hexameric interface through cation-π interactions with R367. W320A substitution results in the formation of a more open conformation of Hsp90, which has not previously been reported, and the induction of a conformational change in the catalytic loop. The structures provide new insights into the mechanism by which W320 functions as a key switch for conformational changes in Hsp90 self-oligomerization, and binding cochaperones and client proteins. Communicated by Ramaswamy H. Sarma
DOI: 10.5281/zenodo.7317978
title: GEDI and ALS LiDAR data for the Upper Austrian national park "Kalkalpen"

description: This dataset contains GEDI L1B,L2B,L2A data for the Upper Austrian national park "Kalkalpen".<br> Also included are the obtained ALS return pulses for the Kalkalpen. The GEDI waveforms are averaged to 1m vertical height layers. Afterwards, the mean noise level stored in GEDI L1B dataset is subtracted from each waveform The ALS pulses are collocated to the GEDI waveforms (x/y-shift = +- 10m).
DOI: 10.5281/zenodo.7317977
title: GEDI and ALS LiDAR data for the Upper Austrian national park "Kalkalpen"

description: This dataset contains GEDI L1B,L2B,L2A data for the Upper Austrian national park "Kalkalpen".<br> Also included are the obtained ALS return pulses for the Kalkalpen. The GEDI waveforms are averaged to 1m vertical height layers. Afterwards, the mean noise level stored in GEDI L1B dataset is subtracted from each waveform The ALS pulses are collocated to the GEDI waveforms (x/y-shift = +- 10m).
DOI: 10.6084/m9.figshare.21550599
title: Evaluating the effect of digital technology on the learning of orthodontic cephalometric measurement

description: This study investigated the effect of applying the digital technology (the Dolphin software®) in cephalometric learning, demonstrating better effect and acceptance of this technology.
DOI: 10.5517/ccdc.csd.cc269hjk
title: CCDC 2034918: Experimental Crystal Structure Determination

description: Related Article: Bin Huang, Wenbing Yu, Li Yang, Yan Li, Ning Gu|2022|Heliyon|8|e11221|doi:10.1016/j.heliyon.2022.e11221
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc269hkl
title: CCDC 2034919: Experimental Crystal Structure Determination

description: Related Article: Bin Huang, Wenbing Yu, Li Yang, Yan Li, Ning Gu|2022|Heliyon|8|e11221|doi:10.1016/j.heliyon.2022.e11221
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2blrb1
title: CCDC 2162973: Experimental Crystal Structure Determination

description: Related Article: Wen Lu, Jiongya Tang, Zhenzhen Gu, Lu Sun, Haimeng Wei, Yanqin Wang, Shilong Yang, Xingwei Chi, Li Xu|2022|J.Inorg.Biochem.|238|112030|doi:10.1016/j.jinorgbio.2022.112030
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2blrc2
title: CCDC 2162974: Experimental Crystal Structure Determination

description: Related Article: Wen Lu, Jiongya Tang, Zhenzhen Gu, Lu Sun, Haimeng Wei, Yanqin Wang, Shilong Yang, Xingwei Chi, Li Xu|2022|J.Inorg.Biochem.|238|112030|doi:10.1016/j.jinorgbio.2022.112030
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7bq
title: CCDC 2168243: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7cr
title: CCDC 2168244: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7ds
title: CCDC 2168245: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7ft
title: CCDC 2168246: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7gv
title: CCDC 2168247: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7hw
title: CCDC 2168248: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
DOI: 10.5517/ccdc.csd.cc2bs7jx
title: CCDC 2168249: Experimental Crystal Structure Determination

description: Related Article: Michael L. Tarlton, Suntharalingam Skanthakumar, Danielle Hutchison, Alexander J. Gremillion, Allen G. Oliver, Richard E. Wilson|2022|Inorg.Chem.|61|17101|doi:10.1021/acs.inorgchem.2c02546
description: An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.