cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccn5k5j
title: CCDC 601157: Experimental Crystal Structure Determination

description: Related Article: Ai-Jun Li, Min-Li Tao, Jing Ma, Xue-Qin Zhou, Dong-Zhi Liu|2006|Acta Crystallogr.,Sect.E:Struct.Rep.Online|62|o1176|doi:10.1107/S1600536806006428
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: 10.13018/bmr5540
title: 1H, 13C and 15N assignment of the hydroquinone form of flavodoxin fromDesulfovibrio vulgaris (Hildenborough)
DOI: 10.13018/bmr5541
title: 1H and 15N Chemical Shift Assignments of Lm-FABP
DOI: 10.5281/zenodo.18771645
title: Visual Acoustics Open Dataset: Cross-modal correspondence metrics with human perceptual validation

description: This repository contains the extended computational pipeline for fractal analysis and individual nevus characterization of human iris images, developed as part of the Argira Station research project. It constitutes the full methodological basis for the comparative study of two unrelated adult subjects (female, 77y and 48y) with contrasting iris phenotypes (uniform dark-brown vs sectoral heterochromia).

**This release extends the foundational pipeline** ([DOI 10.5281/zenodo.18764120](https://doi.org/10.5281/zenodo.18764120)) with three new capabilities not present in previous versions:

1. **Individual nevus detection and characterization**: each melanin deposit is segmented as an independent connected component and analyzed for area, angular/radial position, fractal dimension D (box-counting), circularity, elongation, and GLCM texture contrast.

2. **Composite pathology risk score**: combines geometric and textural features (D, circularity, elongation, contrast) into a single metric flagging nevi for longitudinal monitoring — complementing clinical assessment criteria without replacing ophthalmological diagnosis.

3. **Comparative two-subject pipeline**: full side-by-side analysis including D histograms, angular pigment distribution (polar), area vs D scatter, and a numerical metrics table — enabling inter-individual comparison across phenotypically distinct irises.

**Key findings of the included paper draft:**- Global fractal dimension of pigment: D = 1.835 (Subject A, 77y) vs D = 1.701 (Subject B/OL, 48y)- Per-nevus D clusters around 1.6 for both subjects, consistent with diffusion-limited aggregation (D_DLA ≈ 1.71), suggesting melanocyte clustering during fetal iris development follows a DLA-like process- Total pigment coverage is conserved across phenotypes: 75.2% vs 71.7%- Pupil-to-iris ratio difference (0.433 vs 0.542) is consistent with published age-related miosis data (Winn et al., 1994)

**Files included:** iris_analysis_v2.py · iris_nevi_analysis.py · iris_comparison.py · iris_comparison_AB.png · README.md

Related work: Visual Acoustics platform ([DOI 10.5281/zenodo.18760369](https://doi.org/10.5281/zenodo.18760369))
DOI: 10.13018/bmr5542
title: 1H chemical shifts for Penetratin in phospolipid bicelles
DOI: 10.13018/bmr5543
title: 1H chemical shifts for Penetratin(W48F,W56F) in phospolipid bicelles and SDS micelles
DOI: 10.13018/bmr5544
title: 1H, 13C, and 15N resonance assignments for S100B(beta beta)-Ca2+-TRTK-12 peptide complex
DOI: 10.13018/bmr5545
title: NMR assignment of the C-terminal domain of insulin-like growth factor binding protein-6 (IGFBP-6)
DOI: 10.13018/bmr5547
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Streptopain
DOI: 10.13018/bmr5548
title: Bovine Pancreatic Polypeptide (bPP) undergoes significant changes in conformation and dynamics upon binding to DPC micelles
DOI: 10.13018/bmr5549
title: Neuropeptide Y5-Receptor II: Solution Structure and Dynamics of [31Ala,32Pro]-NPY
DOI: 10.13018/bmr5550
title: Structure and Dynamics of Micelle-bound Neuropeptide Y: Comparison with unligated NPY and Implications for Receptor Selection
DOI: 10.13018/bmr5551
title: Homonuclear chemical shift assignment for LEKTI domain 6 (HF7665)
DOI: 10.13018/bmr5552
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Catalytic Domain of Pac1
DOI: 10.13018/bmr5553
title: Solution structure of influenza A virus C4 promoter
DOI: 10.13018/bmr5554
title: Structure of the N-WASP EVH1 Domain-WIP complex
DOI: 10.13018/bmr5555
title: Solution structure of the 2nd PHD domain from Mi2b
DOI: 10.13018/bmr5556
title: PHD Fingers as Protein Scaffolds
DOI: 10.13018/bmr5557
title: Solution NMR structure of the outer membrane enzyme PagP in DPC micelles
DOI: 10.13018/bmr5558
title: Sp100b SAND domain chemical shift assignments
DOI: 10.13018/bmr5559
title: Partial 1H and 13C assignments for 3'-stem-loop of human U4 small nuclear RNA
DOI: 10.5281/zenodo.18781324
title: ПРЕЖДЕВРЕМЕННЫЕ РОДЫ: ОТ ФАКТОРОВ РИСКА ДО СОВРЕМЕННЫХ МЕТОДОВ ПРОЛОНГИРОВАНИЯ
DOI: 10.5281/zenodo.18781323
title: ПРЕЖДЕВРЕМЕННЫЕ РОДЫ: ОТ ФАКТОРОВ РИСКА ДО СОВРЕМЕННЫХ МЕТОДОВ ПРОЛОНГИРОВАНИЯ
DOI: 10.13018/bmr5560
title: NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima
DOI: 10.13018/bmr5561
title: NMR solution structure of the activation domain of human procarboxipeptidase A2
DOI: 10.13018/bmr5562
title: NMR conformational study of proposed quadruplex hexanucleotide d(CCGCGG)2 in solution
DOI: 10.13018/bmr5563
title: Assignment of backbone 1H, 13C and 15N resonances of ParG, a protein required for active partition of bacterial plasmids
DOI: 10.13018/bmr5564
title: 1H, 13C and 15N resonance assignment of kinase-interacting FHA domain of Arabidopsis kinase associasted protein phosphatase
DOI: 10.13018/bmr5565
title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for porcine MSP
DOI: 10.13018/bmr5566
title: 1H, 15N and 13C Resonance Assignments for the PTB Domain of the Signaling Protein Shc
DOI: 10.13018/bmr5567
title: 1H, 15N and 13C Resonance Assignments for a Histone H3 Lysine Methyltransferase from Paramecium Bursaria Chlorella Virus 1
DOI: 10.13018/bmr5568
title: A new member of the split bab fold: Solution structure of the protein encoded by the YML108W open reading frame from Saccharomyces cerevisiae
DOI: 10.13018/bmr5569
title: 15N relaxation rates for backbone of GB1
DOI: 10.13018/bmr5570
title: 1H, 13C, and 15N NMR assignments of the hypothetical Nudix protein DR0079 from the extremely radiation-resistant bacterium Deinococcus radiodurans
DOI: 10.13018/bmr5571
title: 1H, 13C and 15N assignment of the oxidized form of flavodoxin fromDesulfovibrio vulgaris (Hildenborough)
DOI: 10.13018/bmr5572
title: Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect
DOI: 10.13018/bmr5573
title: Spruce budworm Antifreeze Protein: Changes in Structure and Dynamics at Low Temperature
DOI: 10.13018/bmr5574
title: Lipid induced conformation of the tachykinin peptide Kassinin
DOI: 10.13018/bmr5575
title: Solution Structure of the Tachykinin Peptide Eledoisin
DOI: 10.13018/bmr5576
title: Sodium/potassium-transporting ATPase alpha-1 chain in complex with ATP
DOI: 10.13018/bmr5577
title: Sodium/potassium-transporting ATPase alpha-1 chain
DOI: 10.13018/bmr5578
title: Two Homologous Rat Cellular Retinol-binding Proteins Differ in LocalConformational Flexibility
DOI: 10.13018/bmr5579
title: Two Homologous Rat Cellular Retinol-binding Proteins Differ in LocalConformational Flexibility
DOI: 10.13018/bmr5580
title: NMR solution structure of type-B lantibiotics mersacidin bound to lipid II in DPC micelles
DOI: 10.13018/bmr5581
title: NMR solution structure of type-B lantibiotics mersacidin in MeOH/H2O mixture
DOI: 10.13018/bmr5582
title: NMR solution structure of type-B lantibiotics mersacidin in DPC micelles
DOI: 10.13018/bmr5583
title: NMR structure of P41icf, a potent inhibitor of human cathepsin L
DOI: 10.13018/bmr5584
title: 13C Chemical Shift Assignments of Cu(II) plastocyanin from Synechocystis sp. PCC6803
DOI: 10.15468/dl.yh7pqj
title: Occurrence Download

description: A dataset containing 372 species occurrences available in GBIF matching the query:
{
 "and" : [
 "HasGeospatialIssue is false",
 "HasCoordinate is true",
 "OccurrenceStatus is Present",
 {
 "not" : {
 "BasisOfRecord" : [
 "is one of (Fossil, Living Specimen)"
 ]
 }
 },
 "DistanceFromCentroidInMeters is greater than or equal to 2000",
 "Geometry POLYGON ((105.610544 14.999999, 179.999961 14.999999, 179.999961 65.08290100000001, 105.610544 65.08290100000001, 105.610544 14.999999))",
 "TaxonKey is Bodianus axillaris"
 ]
}

 The dataset includes 372 records from 14 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0002891-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr5585
title: Isolation, structure and activity of GID, a novel alpha4/7-conotoxin with an extended N-terminal sequence
DOI: 10.13018/bmr5586
title: Molecular Recognition in Purine-Rich Internal Loops: Thermodynamic, Structural, and Dynamic Consequences of Purine for Adenine Substitutions in 5'(rGGCAAGCCU)2
DOI: 10.13018/bmr5587
title: Molecular Recognition in Purine-Rich Internal Loops: Thermodynamic, Structural, and Dynamic Consequences of Purine for Adenine Substitutions in 5'(rGGCAAGCCU)2
DOI: 10.13018/bmr5588
title: Molecular Recognition in Purine-Rich Internal Loops: Thermodynamic, Structural, and Dynamic Consequences of Purine for Adenine Substitutions in 5'(rGGCAAGCCU)2
DOI: 10.13018/bmr5589
title: Backbone and side chain 1H, 13C, and 15N chemical shift assignments for V. cholerae VC0424
DOI: 10.13018/bmr5590
title: 1H, 13C and 15N resonance assignments of rice telomere binding domain from Oryza sativa
DOI: 10.13018/bmr5591
title: Sequence specific assignment of part of the myosin binding site of myosin binding protein C
DOI: 10.13018/bmr5592
title: Backbone resonance assignments for the human GMEB-1 SAND domain
DOI: 10.13018/bmr5593
title: Backbone resonance assignments for the rat GMEB-2 SAND domain
DOI: 10.13018/bmr5594
title: Structural insights into the U-box, a domain associated with multi-ubiquitination
DOI: 10.13018/bmr5595
title: Letter to the Editor: 1H, 13C, 15N backbone resonance assignments of apo-NosL, a novel 18.5 kDa copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes
DOI: 10.13018/bmr5596
title: Solution Structure of the hypothetical protein yggU from E. coli. Northeast Structural Genomics Consortium Target ER14.
DOI: 10.13018/bmr5597
title: Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes
DOI: 10.13018/bmr5598
title: 1H, 13C and 15N backbone resonance assignments of domain 1 of receptor associated protein
DOI: 10.13018/bmr5599
title: The Tertiary Structure and Backbone Dynamics of Human Prolactin: Evidence for Reversible Oligomerization in Solution
DOI: 10.17632/v56gvg6jnt
title: Delphi Study for the categorisation of adaptive learning elements for digital mathematics learning environments

description: This data depicts the results of a Delphi Study aiming at developing and refining a categorisation of adaptive learning elements for digital mathematics learning environments.
DOI: 10.17632/v56gvg6jnt.1
title: Delphi Study for the categorisation of adaptive learning elements for digital mathematics learning environments

description: This data depicts the results of a Delphi Study aiming at developing and refining a categorisation of adaptive learning elements for digital mathematics learning environments.
DOI: 10.13018/bmr5600
title: Complete 1H,13C,15N assignments of zinc Clostridium pasteurianum rubredoxin
DOI: 10.13018/bmr5601
title: Complete 1H,13C,15N assignments of zinc Pyrococcus furiosus rubredoxin
DOI: 10.13018/bmr5602
title: Complete resonance assignments for the nudix hydrolase DR2356 of Deinococcus radiodurans
DOI: 10.13018/bmr5603
title: Chemical shift assignment for human proguanylin
DOI: 10.13018/bmr5604
title: Solution structure of the N-terminal domain of ZntA in the apo- and Zn(II) forms
DOI: 10.13018/bmr5605
title: Sequence-specific 1H, 13C and 15N resonance assignments of SAM22, an allergenic stress-induced protein from soy bean
DOI: 10.13018/bmr5606
title: 1H 13C and 15N chemical shift assignments for HI0719
DOI: 10.13018/bmr5607
title: NMR Structure of the Extended Second Transmembrane Domain of the Human Neuronal Glycine Receptor alpha1 Subunit in SDS Micelles
DOI: 10.13018/bmr5608
title: Solution Structure of Contryphan-Vn
DOI: 10.13018/bmr5609
title: NMR structure of [Ala1,15]kalata B1
DOI: 10.13018/bmr5610
title: The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices
DOI: 10.13018/bmr5611
title: Solution Structure of the Tachykinin Peptide Neurokinin A
DOI: 10.5281/zenodo.18781316
title: Preparing Thai Students for Global Communication: The Role of Intercultural Peer Learning
DOI: 10.13018/bmr5612
title: Structure of the Plant Defensin PhD1 from Petunia Hybrida
DOI: 10.5281/zenodo.18781315
title: Preparing Thai Students for Global Communication: The Role of Intercultural Peer Learning
DOI: 10.13018/bmr5613
title: A minimal beta-hairpin peptide scaffold for beta-turn display
DOI: 10.13018/bmr5614
title: Sheared A(anti)-A(anti) Pairs in a Destabilizing 2x2 Internal Loop: The NMR Structure of 5'(rGGCAAGCCU)2
DOI: 10.13018/bmr5615
title: 1H/13C/15N assignment of the C-terminal domain of the E. amylovora response regulator RcsB
DOI: 10.13018/bmr5616
title: Chemical Shift Assignments of the Prp40 WW Domain Pair
DOI: 10.13018/bmr5617
title: 1H chemical shift assignments for the aticarcinogenic Bowman Birk inhibitor isolated from snail medic seeds (Medicago Scutellata)
DOI: 10.13018/bmr5618
title: Backbone 1H, 13C, 15N and Side Chain 13C Chemical Shift Assignments for DFPase from Loligo vulgaris
DOI: 10.13018/bmr5619
title: Resonance assignments for the methionine sulfoxide reductase B from Bacillus subtilis, Northeast Structural Genomics Consortium target SR10
DOI: 10.13018/bmr5620
title: Assignment for ribosomal protein S28E
DOI: 10.13018/bmr5621
title: Assignment for yoag_ecoli
DOI: 10.13018/bmr5622
title: Structural and Functional Characterization of a Thioredoxin-like Protein from methanobacterium thermoautotrophicum (Delta H)
DOI: 10.13018/bmr5623
title: Assignments of 1H, 15N and 13C resonances of the proline-rich matrix protein of Moloney Murine Leukemia Virus (MA Mo-MuLV)
DOI: 10.5281/zenodo.13255584
title: Data supporting the paper "Simulating the electrostatic patch force in sphere-plate and plate-plate geometries"

description: This dataset accompanies the paper titled "Simulating the electrostatic patch force in experimental geometries" by M.H.J. de Jong and L. Mercier de Lepinay. It is a zip file that contains the figures of the publication, the raw data supporting those figures, the analysis and plotting scripts, and the toolbox to simulate the electrostatic patch force in various geometries. The structure, relation and contents of the files are detailed exhaustively in the "README.txt" file in the top level folder.

The contents of the .zip file are common image formats (.png and .pdf), readable text and data files (.txt, .csv), data files that can be opened with the python library pandas (.h5), matlab scripts (.m), python scripts (.py), and COMSOL models (.mph).
DOI: 10.5281/zenodo.18781317
title: Data supporting the paper "Simulating the electrostatic patch force in sphere-plate and plate-plate geometries"

description: This dataset accompanies the paper titled "Simulating the electrostatic patch force in experimental geometries" by M.H.J. de Jong and L. Mercier de Lepinay. It is a zip file that contains the figures of the publication, the raw data supporting those figures, the analysis and plotting scripts, and the toolbox to simulate the electrostatic patch force in various geometries. The structure, relation and contents of the files are detailed exhaustively in the "README.txt" file in the top level folder.

The contents of the .zip file are common image formats (.png and .pdf), readable text and data files (.txt, .csv), data files that can be opened with the python library pandas (.h5), matlab scripts (.m), python scripts (.py), and COMSOL models (.mph).
DOI: 10.13018/bmr5624
title: A Conserved Structural Motif at the N-terminal of Bacterial Translation Initiation Factor IF2
DOI: 10.13018/bmr5625
title: Sequential assignment of the ferricytochrome c3 from Desulfovibrio vulgaris Hildenborough
DOI: 10.13018/bmr5626
title: 1H 13C and 15N backbone resonance assignments of the N-terminal domain of Drosophila GCM protein
DOI: 10.13018/bmr5627
title: 1H, 15N, 13C Resonance Assignments of the LpxC Deacetylase from Aquifex aeolicus in Complex with the Substrate-Analog Inhibitor TU-514
DOI: 10.13018/bmr5628
title: 1H, 15N and 13C resonance assignments of the highly conserved 19kDa C-terminal domain from human Elongation Factor 1Bgamma
DOI: 10.13018/bmr5629
title: 1H, 13C, and 15N resonance assignments and topology of MTH187, a conserved protein from Methanobacterium thermoautotrophicum
DOI: 10.13018/bmr5630
title: 1H 13C and 15N Assigned Chemical Shifts for ER75, an NESG target
DOI: 10.13018/bmr5631
title: ERBIN PDZ domain bound to a phage-derived peptide
DOI: 10.13018/bmr5632
title: Solution structure of the p2b hairpin from human telomerase RNA
DOI: 10.13018/bmr5633
title: The solution structure of molt-inhibiting hormone from the kuruma prawn
DOI: 10.13018/bmr5634
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS1
DOI: 10.13018/bmr5635
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS2
DOI: 10.6084/m9.figshare.30466145
title: Data & code of "<b>Counterproductive: coinfection of a water flea by a fungus and a microsporidium reduces the reproductive outputs of all parties</b>."

description: Organisms are often coinfected by more than one parasite species. These coinfections can alter the fitness of both host and its coinfecting parasites. Changes in host fitness are usually estimated by comparing parasite virulence under coinfection to the virulence of each parasite under single infection. While many studies focus on host survival as proxies of virulence, virulence can be expressed via reduced host fecundity. Here, we studied the outcome of coinfection of water fleas (<i>Daphnia magna</i>) by two microparasitic species, the fungus <i>Metschnikowia bicuspidata </i>and the microsporidium <i>Hamiltosporidium tvaerminnensis</i>. We found that <i>Metschnikowia </i>expressed its virulence mainly via host mortality and <i>Hamiltosporidium </i>expressed it mainly via host reproduction. Despite their competitive interaction, indicated by their reduced spore production, both parasites were able to fully express their virulence during coinfection. Host survival was dominated by <i>Metschnikowia</i> while clutch-size was dominated by <i>Hamiltosporidium</i>. Furthermore, coinfected hosts experienced increased virulence that was manifested only by additional reduction in reproduction (less clutches were released). Our results demonstrate that focusing only on the survival component of host fitness can miss important outcomes of coinfections. Since reduced host fecundity is a common outcome of parasitism, the influence of coinfection on host reproduction deserves more attention.
DOI: 10.6084/m9.figshare.30466145.v2
title: Data & code of "<b>Counterproductive: coinfection of a water flea by a fungus and a microsporidium reduces the reproductive outputs of all parties</b>."

description: Organisms are often coinfected by more than one parasite species. These coinfections can alter the fitness of both host and its coinfecting parasites. Changes in host fitness are usually estimated by comparing parasite virulence under coinfection to the virulence of each parasite under single infection. While many studies focus on host survival as proxies of virulence, virulence can be expressed via reduced host fecundity. Here, we studied the outcome of coinfection of water fleas (<i>Daphnia magna</i>) by two microparasitic species, the fungus <i>Metschnikowia bicuspidata </i>and the microsporidium <i>Hamiltosporidium tvaerminnensis</i>. We found that <i>Metschnikowia </i>expressed its virulence mainly via host mortality and <i>Hamiltosporidium </i>expressed it mainly via host reproduction. Despite their competitive interaction, indicated by their reduced spore production, both parasites were able to fully express their virulence during coinfection. Host survival was dominated by <i>Metschnikowia</i> while clutch-size was dominated by <i>Hamiltosporidium</i>. Furthermore, coinfected hosts experienced increased virulence that was manifested only by additional reduction in reproduction (less clutches were released). Our results demonstrate that focusing only on the survival component of host fitness can miss important outcomes of coinfections. Since reduced host fecundity is a common outcome of parasitism, the influence of coinfection on host reproduction deserves more attention.
DOI: 10.13018/bmr5636
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS3
DOI: 10.6084/m9.figshare.30466145.v1
title: Data & code of "<b>Counterproductive: coinfection of a water flea by a fungus and a microsporidium reduces the reproductive outputs of all parties</b>."

description: Organisms are often coinfected by more than one parasite species. These coinfections can alter the fitness of both host and its coinfecting parasites. Changes in host fitness are usually estimated by comparing parasite virulence under coinfection to the virulence of each parasite under single infection. While many studies focus on host survival as proxies of virulence, virulence can be expressed via reduced host fecundity. Here, we studied the outcome of coinfection of water fleas (<i>Daphnia magna</i>) by two microparasitic species, the fungus <i>Metschnikowia bicuspidata </i>and the microsporidium <i>Hamiltosporidium tvaerminnensis</i>. We found that <i>Metschnikowia </i>expressed its virulence mainly via host mortality and <i>Hamiltosporidium </i>expressed it mainly via host reproduction. Despite their competitive interaction, indicated by their reduced spore production, both parasites were able to fully express their virulence during coinfection. Host survival was dominated by <i>Metschnikowia</i> while clutch-size was dominated by <i>Hamiltosporidium</i>. Furthermore, coinfected hosts experienced increased virulence that was manifested only by additional reduction in reproduction (less clutches were released). Our results demonstrate that focusing only on the survival component of host fitness can miss important outcomes of coinfections. Since reduced host fecundity is a common outcome of parasitism, the influence of coinfection on host reproduction deserves more attention.
DOI: 10.13018/bmr5637
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS4
DOI: 10.13018/bmr5638
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS5
DOI: 10.13018/bmr5639
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS6
DOI: 10.13018/bmr5640
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS7
DOI: 10.13018/bmr5641
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS8
DOI: 10.13018/bmr5642
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS9
DOI: 10.13018/bmr5643
title: Random Coil Proton and Carbon Chemical Shifts of Deoxyribonucleic Acids SS10
DOI: 10.17632/bw972tg3mz
title: T1D Dataset Child

description: The dataset contains anonymized medical record of pediatric patients diagnosed with Type 1 Diabetes (T1D). The dataset includes demographic information, clinical diagnoses, laboratory results, treatments, and outcomes, provided in a controlled-access format for research purposes only. Access to this dataset is restricted and granted exclusively to authorized researchers.