cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.15468/dl.xgmzb2
title: Occurrence Download

description: A dataset containing 0 species occurrences available in GBIF matching the query:
{
 "and" : [
 "TaxonKey is Heptacodium miconioides Rehder",
 "HasCoordinate is true",
 "Country is Japan",
 "HasGeospatialIssue is false"
 ]
}

 The dataset includes 0 records from 0 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0205555-220831081235567/datasets/export for details.
DOI: 10.15468/dl.jzf5yb
title: Occurrence Download

description: A dataset containing 10655 species occurrences available in GBIF matching the query:
{
 "TaxonKey" : [
 "is Crotalus horridus Linnaeus, 1758"
 ]
}

 The dataset includes 10655 records from 104 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0261346-230224095556074/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.15468/dl.78vc7e
title: Occurrence Download

description: A dataset containing 5 species occurrences available in GBIF matching the query:
{
 "and" : [
 "TaxonKey is Centaurea nigra L.",
 "HasCoordinate is true",
 "Country is Japan",
 "HasGeospatialIssue is false"
 ]
}

 The dataset includes 5 records from 3 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0201008-220831081235567/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.15468/dl.aer68c
title: Occurrence Download

description: A dataset containing 0 species occurrences available in GBIF matching the query:
{
 "and" : [
 "TaxonKey is Solanum laciniatum Aiton",
 "HasCoordinate is true",
 "Country is Japan",
 "HasGeospatialIssue is false"
 ]
}

 The dataset includes 0 records from 0 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0205550-220831081235567/datasets/export for details.
DOI: 10.15468/dl.5hgtgn
title: Occurrence Download

description: A dataset containing 15206 species occurrences available in GBIF matching the query:
{
 "TaxonKey" : [
 "is Ambystoma opacum (Gravenhorst, 1807)"
 ]
}

 The dataset includes 15206 records from 86 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0261372-230224095556074/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.15468/dl.a38q6f
title: Occurrence Download

description: A dataset containing 0 species occurrences available in GBIF matching the query:
{
 "and" : [
 "TaxonKey is Saposhnikovia divaricata (Turcz.) Schischk.",
 "HasCoordinate is true",
 "Country is Japan",
 "HasGeospatialIssue is false"
 ]
}

 The dataset includes 0 records from 0 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0208169-220831081235567/datasets/export for details.
DOI: 10.5281/zenodo.10416608
title: Critical Domains for NACC2-NTRK2 Fusion Protein Activation

description: Critical Domains for NACC2-NTRK2 Fusion Protein Activation.  Authors: Wei Yang, April N. Meyer, Zian Jiang, Xuan Jiang, and Daniel J. Donoghue. This dataset contains annotated raw images of immunoblots to accompany article. Abstract: Neurotrophic receptor tyrosine kinases (NTRKs) belong to the receptor tyrosine kinase (RTK) family. NTRKs are responsible for the activation of multiple downstream signaling pathways that regulate cell growth, proliferation, differentiation, and apoptosis. NTRK-associated mutations often result in oncogenesis and lead to aberrant activation of downstream signaling pathways including MAPK, JAK/STAT, and PLCγ. This study characterizes the NACC2-NTRK2 oncogenic fusion protein that leads to pilocytic astrocytoma and pediatric glioblastoma. This fusion joins the BTB domain (Broad-complex, Tramtrack, and Bric-a-brac) domain of NACC2 (Nucleus Accumbens-associated protein 2) with the transmembrane helix and tyrosine kinase domain of NTRK2. We focus on identifying critical domains for the biological activity of the fusion protein. Mutations were introduced in the charged pocket of the BTB domain or in the monomer core, based on a structural comparison of the NACC2 BTB domain with that of PLZF, another BTB-containing protein. Mutations were also introduced into the NTRK2-derived portion to allow comparison of two different breakpoints that have been clinically reported. We show that activation of the NTRK2 kinase domain relies on multimerization of the BTB domain in NACC2-NTRK2. Mutations which disrupt BTB-mediated multimerization significantly reduce kinase activity and downstream signaling. The ability of these mutations to abrogate biological activity suggests that BTB domain inhibition could be a potential treatment for NACC2-NTRK2-induced cancers. Removal of the transmembrane helix leads to enhanced stability of the fusion protein and increased activity of the NACC2-NTRK2 fusion, suggesting a mechanism for the oncogenicity of a distinct NACC2-NTRK2 isoform observed in pediatric glioblastoma.
DOI: 10.5281/zenodo.10884619
title: Critical Domains for NACC2-NTRK2 Fusion Protein Activation

description: Critical Domains for NACC2-NTRK2 Fusion Protein Activation.  Authors: Wei Yang, April N. Meyer, Zian Jiang, Xuan Jiang, and Daniel J. Donoghue. This dataset contains annotated raw images of immunoblots to accompany article, as well as files showing quantitation presented in various figures. Abstract: Neurotrophic receptor tyrosine kinases (NTRKs) belong to the receptor tyrosine kinase (RTK) family. NTRKs are responsible for the activation of multiple downstream signaling pathways that regulate cell growth, proliferation, differentiation, and apoptosis. NTRK-associated mutations often result in oncogenesis and lead to aberrant activation of downstream signaling pathways including MAPK, JAK/STAT, and PLCγ. This study characterizes the NACC2-NTRK2 oncogenic fusion protein that leads to pilocytic astrocytoma and pediatric glioblastoma. This fusion joins the BTB domain (Broad-complex, Tramtrack, and Bric-a-brac) domain of NACC2 (Nucleus Accumbens-associated protein 2) with the transmembrane helix and tyrosine kinase domain of NTRK2. We focus on identifying critical domains for the biological activity of the fusion protein. Mutations were introduced in the charged pocket of the BTB domain or in the monomer core, based on a structural comparison of the NACC2 BTB domain with that of PLZF, another BTB-containing protein. Mutations were also introduced into the NTRK2-derived portion to allow comparison of two different breakpoints that have been clinically reported. We show that activation of the NTRK2 kinase domain relies on multimerization of the BTB domain in NACC2-NTRK2. Mutations which disrupt BTB-mediated multimerization significantly reduce kinase activity and downstream signaling. The ability of these mutations to abrogate biological activity suggests that BTB domain inhibition could be a potential treatment for NACC2-NTRK2-induced cancers. Removal of the transmembrane helix leads to enhanced stability of the fusion protein and increased activity of the NACC2-NTRK2 fusion, suggesting a mechanism for the oncogenicity of a distinct NACC2-NTRK2 isoform observed in pediatric glioblastoma.
DOI: 10.15468/dl.wbakck
title: Occurrence Download

description: A dataset containing 12410057 species occurrences available in GBIF matching the query:
{
 "and" : [
 "Continent is South America",
 "HasCoordinate is true",
 "HasGeospatialIssue is false",
 "Year 2004-2013"
 ]
}

 The dataset includes 12410057 records from 3302 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0006929-240425142415019/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.15468/dl.tkhbbq
title: Occurrence Download

description: A dataset containing 307 species occurrences available in GBIF matching the query:
{
 "and" : [
 "Country is United States of America",
 "DatasetKey is one of (iNaturalist Research-grade Observations, University of Florida Herpetology)",
 "Geometry POLYGON((-82.77185 29.2644,-81.85759 29.23423,-81.80231 30.17926,-82.86028 30.26486,-82.77185 29.2644))",
 "HasCoordinate is true",
 "HasGeospatialIssue is false",
 "PublishingOrg is one of (8483a1f0-1032-11db-ae00-b8a03c50a862, 28eb1a3f-1c15-4a95-931a-4af90ecb574d)",
 "TaxonKey is Lithobates sphenocephalus (Cope, 1886)",
 "Year 1990-2024"
 ]
}

 The dataset includes 307 records from 2 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0044341-240626123714530/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.5281/zenodo.13151784
title: Binary black-hole simulation SXS:BBH:1895

description: Simulation of a black-hole binary system evolved by the SpEC code.
DOI: 10.5281/zenodo.13151785
title: Binary black-hole simulation SXS:BBH:1895

description: Simulation of a black-hole binary system evolved by the SpEC code.
DOI: 10.5281/zenodo.13151812
title: Binary black-hole simulation SXS:BBH:2044

description: Simulation of a black-hole binary system evolved by the SpEC code.
DOI: 10.5281/zenodo.13151813
title: Binary black-hole simulation SXS:BBH:2044

description: Simulation of a black-hole binary system evolved by the SpEC code.
DOI: 10.15468/dl.88cxz6
title: Occurrence Download

description: A dataset containing 8 species occurrences available in GBIF matching the query:
{
 "and" : [
 {
 "and" : [
 "HasGeospatialIssue is false",
 "HasCoordinate is true",
 "OccurrenceStatus is Present",
 {
 "not" : {
 "BasisOfRecord" : [
 "is one of (Fossil, Living Specimen)"
 ]
 }
 }
 ]
 },
 "TaxonKey is Croton pyrifolius Müll.Arg."
 ]
}

 The dataset includes 8 records from 6 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0044342-240626123714530/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.15468/dl.sbsfpp
title: Occurrence Download

description: A dataset containing 302 species occurrences available in GBIF matching the query:
{
 "and" : [
 "CoordinateUncertaintyInMeters 0.0-200.0",
 "HasCoordinate is true",
 "HasGeospatialIssue is false",
 "IsInCluster is false",
 "LifeStage is one of (Nestling, Chick)",
 "TaxonKey is Buteo buteo (Linnaeus, 1758)"
 ]
}

 The dataset includes 302 records from 4 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0044343-240626123714530/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.5281/zenodo.13151818
title: Binary black-hole simulation SXS:BBH:1980

description: Simulation of a black-hole binary system evolved by the SpEC code.
DOI: 10.5281/zenodo.13151819
title: Binary black-hole simulation SXS:BBH:1980

description: Simulation of a black-hole binary system evolved by the SpEC code.
DOI: 10.6084/m9.figshare.26142382
title: Data for "Machine Learning Metallic Glass Critical Cooling Rates Through Elemental and Molecular Simulation Based Featurization"

description: The machine learning data and results from the work titled "Machine Learning Metallic Glass Critical Cooling Rates Through Elemental and Molecular Simulation Based Featurization."
DOI: 10.6084/m9.figshare.26142382.v1
title: Data for "Machine Learning Metallic Glass Critical Cooling Rates Through Elemental and Molecular Simulation Based Featurization"

description: The machine learning data and results from the work titled "Machine Learning Metallic Glass Critical Cooling Rates Through Elemental and Molecular Simulation Based Featurization."
DOI: 10.35003/nskggk/khkvz3
title: Figures_1-6 and captions.docx

description: :unav
DOI: 10.35003/nskggk
title: Replication Data for: Evaporation of Boron from Aluminoborosilicate Melt

description: Key Points: - Experiments on B2O3 evaporation from Ca- and Mg-bearing aluminoborosilicate melts were conducted at 1250 and 1350 °C for 60-1020 hours, under varying oxygen fugacities (FMQ-6 to FMQ+1.5) and in air. - Results indicate that B evaporation increases by an order of magnitude under higher oxygen fugacities compared to reducing conditions, with two possible gas-phase speciation reactions for B2O3 suggested by Gibbs free energy minimization. - B2O3 evaporation rate constants were calculated from the final glass compositions, showing slower evaporation rates than diffusion rates, indicating that evaporation is the rate-limiting process.
DOI: 10.35003/nskggk/iqqg7q
title: Tables_1-4.tab

description: :unav
DOI: 10.6084/m9.figshare.26426959
title: BiSim Tool: a binding simulation tool to aid and simplify ligand-binding assay design and development

description: Ligand-binding assays (LBAs) rely on the reversible, noncovalent binding between the analyte of interest and the assay reagents, and understanding their dynamic equilibrium is key to building robust LBA methods. Although the dynamic interplay of free and bound fractions can be calculated using mathematical models, these are not routinely applied. This approach is costly in terms of both assay development time and reagents, and can result in an under-exploration of the possible parameter combinations. Therefore, we have created a user-friendly simulation tool to facilitate LBA development (the BiSim Tool). We describe the models driving the mathematical simulations and the main features of our software solution by means of case studies, illustrating the tool's value in drug development. To support drug development for all patients worldwide, the BiSim Tool is now available as an open-source code project and as a free web-based tool at https://proteinbindingsimulation.shinyapps.io/BiSim-ProteinBindingSimulation [1]. Ligand-binding assays (LBAs) are essential for analyzing the interaction between an analyte and assay reagents through reversible, noncovalent binding. Understanding the dynamic equilibrium between free and bound fractions in LBAs is crucial for developing effective assay methods. Despite the importance, mathematical models to calculate this dynamic interplay are not commonly used in practice. We developed a new user-friendly simulation tool, BiSim, to make the application of mathematical models in LBA development more accessible. The tool and its underlying mathematical models are explained through case studies, such as determining assay performance requirements, predicting expected complex formation, time-to-equilibrium and assay optimization. BiSim is available as an open-source code project, allowing for wide accessibility and the possibility of community improvements. Additionally, a free web-based service hosts the BiSim Tool, ensuring easy access for users without the need for software installation: https://proteinbindingsimulation.shinyapps.io/BiSim-ProteinBindingSimulation. The combination of detailed use cases and the freely available tool provide a valuable resource for researchers and developers in drug development, saving both time and development costs.
DOI: 10.6084/m9.figshare.26426959.v1
title: BiSim Tool: a binding simulation tool to aid and simplify ligand-binding assay design and development

description: Ligand-binding assays (LBAs) rely on the reversible, noncovalent binding between the analyte of interest and the assay reagents, and understanding their dynamic equilibrium is key to building robust LBA methods. Although the dynamic interplay of free and bound fractions can be calculated using mathematical models, these are not routinely applied. This approach is costly in terms of both assay development time and reagents, and can result in an under-exploration of the possible parameter combinations. Therefore, we have created a user-friendly simulation tool to facilitate LBA development (the BiSim Tool). We describe the models driving the mathematical simulations and the main features of our software solution by means of case studies, illustrating the tool's value in drug development. To support drug development for all patients worldwide, the BiSim Tool is now available as an open-source code project and as a free web-based tool at https://proteinbindingsimulation.shinyapps.io/BiSim-ProteinBindingSimulation [1]. Ligand-binding assays (LBAs) are essential for analyzing the interaction between an analyte and assay reagents through reversible, noncovalent binding. Understanding the dynamic equilibrium between free and bound fractions in LBAs is crucial for developing effective assay methods. Despite the importance, mathematical models to calculate this dynamic interplay are not commonly used in practice. We developed a new user-friendly simulation tool, BiSim, to make the application of mathematical models in LBA development more accessible. The tool and its underlying mathematical models are explained through case studies, such as determining assay performance requirements, predicting expected complex formation, time-to-equilibrium and assay optimization. BiSim is available as an open-source code project, allowing for wide accessibility and the possibility of community improvements. Additionally, a free web-based service hosts the BiSim Tool, ensuring easy access for users without the need for software installation: https://proteinbindingsimulation.shinyapps.io/BiSim-ProteinBindingSimulation. The combination of detailed use cases and the freely available tool provide a valuable resource for researchers and developers in drug development, saving both time and development costs.
DOI: 10.5517/ccdc.csd.cc2fr74l
title: CCDC 2256649: Experimental Crystal Structure Determination

description: Related Article: Iuliia V. Strelnikova, Ilya D. Shutilov, Alexander S. Ovsyannikov, Daut R. Islamov, Andrew V. Pyataev, Tatiana P. Gerasimova, Ayrat R. Khamatgalimov, Mikhail N. Khrizanforov, Aidar T. Gubaidullin, Vladimir A. Burilov, Svetlana E. Solovieva, Igor S. Antipin|2024|CrystEngComm|26|3973|doi:10.1039/D4CE00347K
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.cc2h4z1p
title: CCDC 2298682: Experimental Crystal Structure Determination

description: Related Article: Janusz Szklarzewicz, Maciej Hodorowicz, Anna Jurowska|2024|New J.Chem.|48|13196|doi:10.1039/D4NJ02448F
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.cc2jfldz
title: CCDC 2336761: Experimental Crystal Structure Determination

description: Related Article: Mariana Rakhmanova, Taisiya Sukhikh, Ekaterina Kovalenko|2024|CrystEngComm|26|3954|doi:10.1039/D4CE00375F
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.cc2jflg1
title: CCDC 2336763: Experimental Crystal Structure Determination

description: Related Article: Mariana Rakhmanova, Taisiya Sukhikh, Ekaterina Kovalenko|2024|CrystEngComm|26|3954|doi:10.1039/D4CE00375F
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.cc2jflh2
title: CCDC 2336764: Experimental Crystal Structure Determination

description: Related Article: Mariana Rakhmanova, Taisiya Sukhikh, Ekaterina Kovalenko|2024|CrystEngComm|26|3954|doi:10.1039/D4CE00375F
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.cc2jflj3
title: CCDC 2336765: Experimental Crystal Structure Determination

description: Related Article: Mariana Rakhmanova, Taisiya Sukhikh, Ekaterina Kovalenko|2024|CrystEngComm|26|3954|doi:10.1039/D4CE00375F
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.cc2jflk4
title: CCDC 2336766: Experimental Crystal Structure Determination

description: Related Article: Mariana Rakhmanova, Taisiya Sukhikh, Ekaterina Kovalenko|2024|CrystEngComm|26|3954|doi:10.1039/D4CE00375F
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.cc2jgxtr
title: CCDC 2338045: Experimental Crystal Structure Determination

description: Related Article: Firudin I. Guseinov, Viacheslav O. Ovsyannikov, Elena V. Shuvalova, Leonid M. Kustov, Konstantin I. Kobrakov, Aida I. Samigullina, Kamran T. Mahmudov|2024|New J.Chem.|48|12869|doi:10.1039/D4NJ01789G
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.cc2jgxvs
title: CCDC 2338046: Experimental Crystal Structure Determination

description: Related Article: Firudin I. Guseinov, Viacheslav O. Ovsyannikov, Elena V. Shuvalova, Leonid M. Kustov, Konstantin I. Kobrakov, Aida I. Samigullina, Kamran T. Mahmudov|2024|New J.Chem.|48|12869|doi:10.1039/D4NJ01789G
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.cc2jgxwt
title: CCDC 2338047: Experimental Crystal Structure Determination

description: Related Article: Firudin I. Guseinov, Viacheslav O. Ovsyannikov, Elena V. Shuvalova, Leonid M. Kustov, Konstantin I. Kobrakov, Aida I. Samigullina, Kamran T. Mahmudov|2024|New J.Chem.|48|12869|doi:10.1039/D4NJ01789G
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.