cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.13018/bmr20014
title: STRUCTURE OF ANTIBACTERIAL PEPTIDE CAPISTRUIN: A 19-RESIDUE LARIAT PROTOKNOT WITH A THREADED 9-MEMBER SIDECHAIN TO-BACKBONE RING
DOI: 10.13018/bmr20015
title: NMR structure of a V3 (SF2 isolate) peptide
DOI: 10.13018/bmr20016
title: NMR structure of Temporin-SHa in micellar SDS
DOI: 10.13018/bmr20017
title: NMR structure of Temporin-SHb in micellar SDS
DOI: 10.13018/bmr20018
title: NMR structure of Temporin-SHc in micellar SDS
DOI: 10.13018/bmr20019
title: NMR structure of a V3 (MN isolate) peptide
DOI: 10.13018/bmr20020
title: NMR structure of a V3 (LAI isolate) peptide
DOI: 10.13018/bmr20022
title: 1H Chemical Shift Assignments for metastin analog, s5a
DOI: 10.13018/bmr20023
title: Structure, dynamics and selectivity of the sodium channel blocker mu-conotoxin SIIIA
DOI: 10.13018/bmr20024
title: NMR solution structure of mu-conotoxin TIIIA
DOI: 10.13018/bmr20025
title: NMR solution structure of mu-conotoxin SIIIA
DOI: 10.13018/bmr20026
title: Mutagenesis and nuclear magnetic resonance analyses of the fusion peptide of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus F protein
DOI: 10.13018/bmr20027
title: Brome Mosaic Virus protein 1a Helix A bound to SDS micelle
DOI: 10.13018/bmr20028
title: Structures of 1-15 peptide fragment of Statherin
DOI: 10.6084/m9.figshare.31422338
title: The mean free path for isotope-enriched graphite samples and HOPG at 300 K

description: Comparison of mean free path for isotope-enriched graphite samples and HOPG at 300 K, I-scattering and N-scattering.
DOI: 10.6084/m9.figshare.31422338.v1
title: The mean free path for isotope-enriched graphite samples and HOPG at 300 K

description: Comparison of mean free path for isotope-enriched graphite samples and HOPG at 300 K, I-scattering and N-scattering.
DOI: 10.13018/bmr20029
title: 13C and 1H atom assignments and structure for Apelin 17 (Human form) at 35C
DOI: 10.13018/bmr20030
title: 13C, 1H chemical shifts and structure of apelin 17(human form, major conformation) at 5C
DOI: 10.13018/bmr20031
title: 13C, 1H chemical shifts and structure of Apelin 17 (Human form, minor conformation at 5C)
DOI: 10.13018/bmr20032
title: Solution structure of Gelatinase Biosynthesis-Activating Pheromone (GBAP), a 11-residue peptide lactone, from the Gram-positive bacterium Enterococcus faecalis
DOI: 10.13018/bmr20033
title: Solution structure of dicarba-ImI: an alpha-conotoxin with a non-reducible cystine analogue
DOI: 10.13018/bmr20034
title: Solution NMR Structure of 4F Associated With DMPC Disc
DOI: 10.13018/bmr20036
title: Cyclic Pseudotetrapeptide L-Phe-L-Trp-L-Lys-L-Thr
DOI: 10.13018/bmr20037
title: Cyclic Pseudotetrapeptide D-Phe-L-Trp-L-Lys-L-Thr
DOI: 10.13018/bmr20038
title: Cyclic Pseudotetrapeptide L-Phe-D-Trp-L-Lys-L-Thr
DOI: 10.13018/bmr20039
title: Cyclic Pseudotetrapeptide L-Phe-L-Trp-D-Lys-L-Thr
DOI: 10.13018/bmr20040
title: Cyclic Pseudotetrapeptide D-Phe-D-Trp-D-Lys-L-Thr
DOI: 10.13018/bmr20041
title: Cyclic Pseudotetrapeptide L-Phe-D-Trp-D-Lys-L-Thr
DOI: 10.13018/bmr20042
title: Cyclic Pseudotetrapeptide L-Phe-L-Trp-D-Lys-D-Thr
DOI: 10.13018/bmr20043
title: Cyclic Pseudotetrapeptide L-Phe-D-Trp-L-Lys-D-Thr
DOI: 10.13018/bmr20044
title: NMR structure of the Interleukin-8 C-terminal domain in solution with SDS micelles
DOI: 10.13018/bmr20045
title: SOLUTION NMR STRUCTURE OF HUMAN IAPP-1-19
DOI: 10.13018/bmr20046
title: SOLUTION NMR STRUCTURE OF RAT IAPP-1-19
DOI: 10.13018/bmr20047
title: INTERACTION OF THE DENGUE VIRUS FUSION PEPTIDE WITH MEMBRANES ASSESSED BY NMR: THE ESSENTIAL ROLE OF THE ENVELOPE PROTEIN TRP101 FOR MEMBRANE FUSION
DOI: 10.13018/bmr20048
title: NMR solution structure of an analgesic Mu-contoxin KIIIA
DOI: 10.13018/bmr20049
title: NMR solution structure of Mu-KIIIA[C1A,C9A]
DOI: 10.13018/bmr20050
title: NMR STRUCTURE OF DPAKKR, A CYCLIC PENTAPEPTIDE MIMIC OF BDNF
DOI: 10.13018/bmr20051
title: Biological and structural study of Obestatin and its analogues Structural importance of Obestatin and its biology
DOI: 10.13018/bmr20052
title: Solution NMR Structure of Insulin A-chain peptide
DOI: 10.13018/bmr20053
title: Solution NMR structure of Insulin A-chain variant peptide
DOI: 10.13018/bmr20054
title: Tetramer of KIA7W peptide
DOI: 10.13018/bmr20055
title: Tetramer of KIA7H peptide
DOI: 10.13018/bmr20056
title: LSEAL penta-peptide Calpain inhibitor
DOI: 10.13018/bmr20057
title: NMR structure of designed peptide, YI12WF in the presence of Lipopolysaccharide
DOI: 10.13018/bmr20058
title: Solution structure of designed peptide, YI12WW in the presence of Lipopolysaccharide
DOI: 10.5281/zenodo.18785404
title: Dataset
DOI: 10.5281/zenodo.18785403
title: Dataset
DOI: 10.13018/bmr20059
title: Solution structure of designed peptide, YI12WY in the presence of LPS bilayer
DOI: 10.13018/bmr20060
title: Solution structure of designed peptide, YI12FF in the presence of LPS bilayer
DOI: 10.13018/bmr20061
title: Solution structure of designed peptide GG8WF in the presence of LPS bilayer
DOI: 10.13018/bmr20062
title: 3D NMR models of MBP83-99 peptide in DMSO
DOI: 10.13018/bmr20063
title: NMR STRUCTURE OF A MODEL PEPTIDE BOUND TO GROEL
DOI: 10.13018/bmr20064
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.18710/jm6u7b
title: Supplementary dataset and reproducible codes for LLM-assisted mapping feedstocks of eight conversion technologies from over 121,000 studies

description: This dataset was developed to systematically characterise feedstock–technology relationships across eight major biomass conversion technologies by mining a large Scopus-derived bibliographic corpus (1887–2025; partial coverage for 2025). The workflow is LLM-assisted and fully reproducible, combining automated extraction of feedstock and technology phrases from bibliographic text fields (titles, abstracts, and keywords) with rule-based cleaning and a subsequent LLM-based validation step, followed by targeted manual curation for final release. The dataset is intended for use in technology landscape analyses, evidence synthesis, and comparative assessments of biomass conversion pathways, where consistent and traceable feedstock descriptors are required across a very large volume of studies.

A data descriptor titled "A large-scale, LLM-assisted and validated dataset of biomass and waste conversion technologies and feedstocks" with the following abstract will published based on this dataset:

Biomass, organic wastes and biogenic by-products are increasingly targeted for low-carbon fuels and value-added chemicals. However, strategic decision-making from a circular economy perspective requires a big-picture view of the relative significance of different conversion technologies in handling diverse feedstock portfolios, and no large-scale, cross-technology mapping of these portfolios is currently available. Thus, a literature-derived dataset was assembled, that links eight major waste-to-x valorisation technologies (gasification, pyrolysis, hydrothermal liquefaction, torrefaction, anaerobic digestion, aerobic digestion, fermentation and transesterification) to their reported feedstocks. Using the Scopus database, 121,365 records were retrieved with harmonised search strings, spanning publications from 1887 to 2025. This constrained yet scalable search strategy both facilitates automated extraction and validation and yields a rich dataset. Further, a large language model assisted workflow was implemented to extract candidate technology and feedstock phrases, followed by a two-level validation that combines rule-based cleaning with targeted LLM re-evaluation to minimise manual curation. The resulting dataset provides technology-specific, validated feedstock descriptors that supports comparative analyses and decision-support applications in a circular bioeconomy context.
description: Python, 3.11
description: Microsoft Excel, 365
DOI: 10.13018/bmr20065
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.13018/bmr20066
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.13018/bmr20067
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.13018/bmr20068
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.13018/bmr20069
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.15468/dl.tw6n2h
title: Occurrence Download

description: A dataset containing 362 species occurrences available in GBIF matching the query:
{
 "TaxonKey" : [
 "is Psoralea corylifolia"
 ]
}

 The dataset includes 362 records from 50 constituent datasets; see https://api.gbif.org/v1/occurrence/download/0003260-260225131425191/datasets/export for details.
 
Data from some individual datasets included in this download may be licensed under less restrictive terms.
DOI: 10.13018/bmr20070
title: Design, Synthesis, Biological Evaluation, and Structural Characterization of Potent Histone Deacetylase Inhibitors Based on Cyclic alpha/beta-tetrapeptide architectures
DOI: 10.13018/bmr20071
title: Probing the Bioactive Conformation of an Archetypal Natural Product HDAC Inhibitor Using Conformationally Homogeneous Triazole-Modified Cyclic Tetrapeptides
DOI: 10.13018/bmr20072
title: Probing the Bioactive Conformation of an Archetypal Natural Product HDAC Inhibitor Using Conformationally Homogeneous Triazole-Modified Cyclic Tetrapeptides
DOI: 10.13018/bmr20073
title: Probing the Bioactive Conformation of an Archetypal Natural Product HDAC Inhibitor Using Conformationally Homogeneous Triazole-Modified Cyclic Tetrapeptides
DOI: 10.13018/bmr20074
title: Protein Fibril
DOI: 10.13018/bmr20075
title: Solution structure of the N(1-21)MeuTXK-beta in presence of TFE
DOI: 10.13018/bmr20076
title: NMR Solution Structure of a TC5b_D9E miniprotein
DOI: 10.13018/bmr20078
title: Solution Structure of Antimicrobial Peptide Hedistin
DOI: 10.13018/bmr20079
title: NMR solution structure of the loopregion Tyr67 - Leu77 of visual arrestin in complex with lightactivated rhodopsin
DOI: 10.6084/m9.figshare.31422278.v1
title: <b>Laminar patterning transcription factors orchestrate spatial metabolite partitioning in </b><b><i>Capsicum</i></b><b> fruit</b>

description: Chili pepper (<i>Capsicum annuum </i>L<i>.</i>) produces specialized metabolites, notably the pungent capsaicin and the red capsanthin. Although their biosynthetic pathways are well characterized, the cellular architecture that underpins spatial regulation remains unclear. Here, we present a spatiotemporal single-nucleus atlas of pepper development, integrating single-nucleus RNA sequencing and spatial transcriptomics, profiling 263,076 high-quality cells from 56 samples spanning seedlings to mature fruits. This resource reveals a multilayered organization and precisely maps metabolic genes to defined cell types and spatial regions. We further identify laminar patterning transcription factors (LPTFs), including <i>WRKY6</i>, <i>ZAT10</i>, and <i>BTF3</i>, whose layer-specific expression correlates with localized capsanthin accumulation. Our work establishes a framework for dissecting laminar control of specialized metabolism and provides a valuable reference for comparative studies across species. The atlas is openly accessible at http://Pepper-Cell-Atlas.com.
DOI: 10.13018/bmr20080
title: Structure and interactions in membranes of human and bovine Catestatin by solution and solid-state NMR spectroscopy
DOI: 10.13018/bmr20081
title: solution structures of bradykinin - penta-O-galloyl-D-glucopyranose complexe
DOI: 10.13018/bmr20082
title: Apelin17 bound to SDS micelles
DOI: 10.13018/bmr20084
title: DIRHODIUM PEPTIDE COMPLEX
DOI: 10.13018/bmr20085
title: Solution structure of SFT-L1
DOI: 10.13018/bmr20086
title: Helical Agonist of Nociceptin (NOP) Receptor
DOI: 10.13018/bmr20087
title: Novel Helix-Constrained Nociceptin Derivatives Are Potent Agonists and Antagonists of ERK Phosphorylation and Thermal Analgesia in Mice
DOI: 10.13018/bmr20088
title: Novel Helix-Constrained Nociceptin Derivatives Are Potent Agonists and Antagonists of ERK Phosphorylation and Thermal Analgesia in Mice
DOI: 10.13018/bmr20089
title: Novel Helix-Constrained Nociceptin Derivatives Are Potent Agonists and Antagonists of ERK Phosphorylation and Thermal Analgesia in Mice
DOI: 10.13018/bmr20090
title: KAAAD, single alpha helix turn
DOI: 10.13018/bmr20091
title: RSV_1nal
DOI: 10.13018/bmr20092
title: To be advised
DOI: 10.13018/bmr20093
title: REV_HIV peptides
DOI: 10.13018/bmr20094
title: Effects of Peptoid Residue Substitutions on Structural Flexibility and Bacterial-Cell Selectivity of Piscidin 1
DOI: 10.13018/bmr20095
title: Effects of Peptoid Residue Substitutions on Structural Flexibility and Bacterial-Cell Selectivity of Piscidin 1
DOI: 10.13018/bmr20098
title: Effects of Peptoid Residue Substitutions on Structural Flexibility and Bacterial-Cell Selectivity of Piscidin 1
DOI: 10.13018/bmr20101
title: Lipid-induced Conformation of Substance P
DOI: 10.13018/bmr20102
title: C-Terminal helix of the SERCA2b Ca2+ pump (ATP2A2B)
DOI: 10.13018/bmr20103
title: Structural studies of antimicrobial peptide XT-7 and its Lysine4 analogue
DOI: 10.13018/bmr20104
title: structural studies of antimicrobial peptide XT-7 and its Lysine mutated peptide
DOI: 10.13018/bmr20105
title: BI-32169
DOI: 10.13018/bmr20107
title: NMR structure of conotoxin ImI analogue
DOI: 10.13018/bmr20108
title: Conformational Flexibility of SecA IRA1 Loop Region
DOI: 10.13018/bmr20109
title: CHARACTERIZATION OF THE LIGAND-FREE CONSTITUTIVE ACTIVITY OF THE THROMBOXANE A2 RECEPTOR BY THE INTEGRATED APPROACHES OF NMR SPECTROSCOPY AND A RECOMBINANT RECEPTOR
DOI: 10.13018/bmr20110
title: Solution structure of PV1-VPgpU
DOI: 10.13018/bmr20111
title: Conformational Flexibility of SecA IRA1 Loop Region
DOI: 10.13018/bmr20112
title: CHARACTERIZATION OF THE LIGAND-FREE CONSTITUTIVE ACTIVITY OF THE THROMBOXANE A2 RECEPTOR BY THE INTEGRATED APPROACHES OF NMR SPECTROSCOPY AND A RECOMBINANT RECEPTOR
DOI: 10.13018/bmr20113
title: 1H, 13C assignments and NMR structure of temporin-SHf
DOI: 10.13018/bmr20114
title: alpha-conotoxin FI
DOI: 10.13018/bmr20115
title: Substance P 40 structures in water pH 5.5 298 K NMR DATA & STRUCTURES
DOI: 10.13018/bmr20116
title: Substance P in DMPC:CHAPS q=0.25 bicelles
DOI: 10.13018/bmr20117
title: Substance P 40 structures in water pH 5.5 298 K NMR DATA & STRUCTURES
DOI: 10.13018/bmr20118
title: A 15-residue peptide corresponding to the C-terminal domain of the Gq protein alpha subunit (Gaq-Ct peptide) was synthesized and characterized using NMR spectroscopic studies.
DOI: 10.13018/bmr20119
title: Assembling NMR structures for the intracellular loops of the human thromboxane A2 receptor: Implication of the G protein-coupling pocket
DOI: 10.13018/bmr20121
title: Tubulysin conformation bound to tubulin
DOI: 10.13018/bmr20122
title: Solution structure of CCAP-vil with one disulfide bond from Conus villepinii
DOI: 10.13018/bmr20123
title: NS4A(1-22)
DOI: 10.13018/bmr20124
title: Structure and lipid interactions of an anti-atherogenic Apolipoprotein J peptide using solution NMR
DOI: 10.13018/bmr20125
title: DPC micelle bound VK22
DOI: 10.13018/bmr20126
title: Alpha-conotoxin Vc1.2
DOI: 10.13018/bmr20127
title: Nociceptin Agonist
DOI: 10.13018/bmr20128
title: solution structure of conotoxin qc16a
DOI: 10.25420/britishmuseum.31411047
title: 2023SG09 Project Metadata

description: Metadata spreadsheet with all the metadata information for the assets uploaded in project 2023SG09 following the Material Culture Ethnography Metadata Schema (MCEMS), which was developed for the Endangered Material Knowledge Programme (EMKP). MCEMS is intended to record the metadata for digital objects that were created as part of ethnographic research recording material culture, living heritage, cultural practices, and different forms of knowledge. Its aim is to aid the preservation of ethnography-specific information, facilitate archiving for future re-use and accessibility, and increase the online findability and presence of ethnographic data and research.
DOI: 10.25420/britishmuseum.31411047.v1
title: 2023SG09 Project Metadata

description: Metadata spreadsheet with all the metadata information for the assets uploaded in project 2023SG09 following the Material Culture Ethnography Metadata Schema (MCEMS), which was developed for the Endangered Material Knowledge Programme (EMKP). MCEMS is intended to record the metadata for digital objects that were created as part of ethnographic research recording material culture, living heritage, cultural practices, and different forms of knowledge. Its aim is to aid the preservation of ethnography-specific information, facilitate archiving for future re-use and accessibility, and increase the online findability and presence of ethnographic data and research.
DOI: 10.13018/bmr21000
title: Lasso peptide based integrin inhibitor: Microcin J25 variant with RGD substitution of Gly12-Ile13-Gly14
DOI: 10.13018/bmr21001
title: NMR solution of a tridimensional peptidic structure in bilayer lipids: Examplewith neurotensin in Small Unilamellar Vesicle environment
DOI: 10.6084/m9.figshare.31422341
title: The propagation length and the second sound velocity of second sound

description: The propagation length and the second sound velocity from the measured and the simulated TTG signals.
DOI: 10.13018/bmr21002
title: Solution NMR structure of TZ2C-BG
DOI: 10.6084/m9.figshare.31422341.v1
title: The propagation length and the second sound velocity of second sound

description: The propagation length and the second sound velocity from the measured and the simulated TTG signals.
DOI: 10.13018/bmr21006
title: alpha-conotoxin ImI cystathionine 2-4
DOI: 10.13018/bmr21007
title: alpha-conotoxin ImI cystathionine 1-3
DOI: 10.13018/bmr21008
title: LPS bound structure of Temporin-1Tl
DOI: 10.13018/bmr21009
title: The Binding Mechanism of a Peptidylic Cyclic Serine Protease Inhibitor - upain-1
DOI: 10.13018/bmr21010
title: The Binding Mechanism of a Peptidylic Cyclic Serine Protease Inhibitor - extended upain
DOI: 10.13018/bmr21011
title: LPS bound structure of Cysteine deleted TachyplesinI
DOI: 10.13018/bmr21013
title: DPC micelle bound RI23
DOI: 10.13018/bmr21014
title: solution structure of conotoxin lt14a
DOI: 10.13018/bmr21015
title: solution structure of conotoxin pu14a
DOI: 10.13018/bmr21018
title: Compstatin 10
DOI: 10.6084/m9.figshare.30293189
title: Concept, Challenges, and Requirements of Hybrid Collaboration Spaces: A Systematic Literature Review

description: In recent years, hybrid work has surged globally, making <i>Hybrid Collaboration Spaces</i>—the physical and virtual environments facilitating hybrid collaboration—increasingly relevant. However, this aspect is often not addressed in research and its scientific discourse is not always obviously apparent. In the existing body of literature, there are terminological ambiguities as well as temporal trends which make it hard to quickly identify relevant research. We thus present a systematic literature review on <i>Hybrid Collaboration Spaces</i> based on seven academic data sources (90 publications included, 996 screened). Our review encompasses several scientific fields and domains, contributing a detailed bibliometric report and a thorough thematic analysis highlighting challenges in hybrid collaboration and requirements for related spaces. We aim to 1) provide a concise overview of the research landscape, 2) advance the cross-domain dialog on hybrid collaboration, and 3) contribute to the disambiguation of terminology and establishment of a shared vocabulary.
DOI: 10.6084/m9.figshare.30293189.v2
title: Concept, Challenges, and Requirements of Hybrid Collaboration Spaces: A Systematic Literature Review

description: In recent years, hybrid work has surged globally, making <i>Hybrid Collaboration Spaces</i>—the physical and virtual environments facilitating hybrid collaboration—increasingly relevant. However, this aspect is often not addressed in research and its scientific discourse is not always obviously apparent. In the existing body of literature, there are terminological ambiguities as well as temporal trends which make it hard to quickly identify relevant research. We thus present a systematic literature review on <i>Hybrid Collaboration Spaces</i> based on seven academic data sources (90 publications included, 996 screened). Our review encompasses several scientific fields and domains, contributing a detailed bibliometric report and a thorough thematic analysis highlighting challenges in hybrid collaboration and requirements for related spaces. We aim to 1) provide a concise overview of the research landscape, 2) advance the cross-domain dialog on hybrid collaboration, and 3) contribute to the disambiguation of terminology and establishment of a shared vocabulary.
DOI: 10.13018/bmr21019
title: NMR structure, localization and vesicle fusion of Chikungunya Virus Fusion Peptide
DOI: 10.6084/m9.figshare.30293189.v1
title: Concept, Challenges, and Requirements of Hybrid Collaboration Spaces: A Systematic Literature Review

description: In recent years, hybrid work has surged globally, making <i>Hybrid Collaboration Spaces</i>—the physical and virtual environments facilitating hybrid collaboration—increasingly relevant. However, this aspect is often not addressed in research and its scientific discourse is not always obviously apparent. In the existing body of literature, there are terminological ambiguities as well as temporal trends which make it hard to quickly identify relevant research. We thus present a systematic literature review on <i>Hybrid Collaboration Spaces</i> based on seven academic data sources (90 publications included, 996 screened). Our review encompasses several scientific fields and domains, contributing a detailed bibliometric report and a thorough thematic analysis highlighting challenges in hybrid collaboration and requirements for related spaces. We aim to 1) provide a concise overview of the research landscape, 2) advance the cross-domain dialog on hybrid collaboration, and 3) contribute to the disambiguation of terminology and establishment of a shared vocabulary.
DOI: 10.13018/bmr21022
title: MDCSGCSRPG cyclic + copper(I) from acidic