cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccdc.csd.cc2ghhk1
title: CCDC 2279013: Experimental Crystal Structure Determination

description: Related Article: Richard Y. Kong, Joseph B. Parry, Guy R. Anello, Matthew E. Ong, Kyle M. Lancaster|2023|J.Am.Chem.Soc.|145|24136|doi:10.1021/jacs.3c07997
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.cc2ghwlg
title: CCDC 2279386: Experimental Crystal Structure Determination

description: Related Article: Cong-Shuai Wang, Qi Xiong, Hui Xu, Hao-Ran Yang, Yanfeng Dang, Xiu-Qin Dong, Chun-Jiang Wang|2023|Chemical Science|14|12091|doi:10.1039/D3SC03686C
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.cc2gjgq6
title: CCDC 2279948: Experimental Crystal Structure Determination

description: Related Article: Maoyi Dai, Yingying Zhang, Xiaoxiang Zhang, Ruiyi Wang, Wanxing Wei, Zhuan Zhang, Taoyuan Liang|2023|J.Org.Chem.|88|15106|doi:10.1021/acs.joc.3c01591
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.cc2gjlzl
title: CCDC 2280080: Experimental Crystal Structure Determination

description: Related Article: Abdullaev Akhrorjon Khabibjonovich, Yakubov Yuldosh Yusupboevich, Ruzmetov Abror Khamidjanovich, Normamatov Adkhamjon Sadullayevich, Ibragimov Aziz Bakhtiyarovich, Muhammad Nadeem Akhtar, Murad A. AlDamen, Ashurov Jamshid Mengnorovich|2024|J.Mol.Struct.|1295|136581|doi:10.1016/j.molstruc.2023.136581
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.cc1zrk3d
title: CCDC 1839884: Experimental Crystal Structure Determination

description: Related Article: Xuan Huang, Huichao You, Fang Fang, Fan Wang, Zhong-Quan Liu|2023|Chem.Commun.|59|13352|doi:10.1039/D3CC04275H
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.cc2gk9fs
title: CCDC 2280745: Experimental Crystal Structure Determination

description: Related Article: Kaimin Wang, Yanqiu Dong, Xiong Zhao, Xuling Bai, Lifeng Li, Jinrong Guo, Zhengliang Wang, Huaijun Tang, Yulu Ma|2024|J.Mol.Struct.|1295|136725|doi:10.1016/j.molstruc.2023.136725
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.cc2gkgq7
title: CCDC 2280909: Experimental Crystal Structure Determination

description: Related Article: Naima Munir, Navin Gürbüz, M. Naveed Zafar, Enes Evren, Betül Şen, Muhittin Aygün, İsmail Özdemir|2024|J.Mol.Struct.|1295|136679|doi:10.1016/j.molstruc.2023.136679
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.cc2gkgr8
title: CCDC 2280910: Experimental Crystal Structure Determination

description: Related Article: Naima Munir, Navin Gürbüz, M. Naveed Zafar, Enes Evren, Betül Şen, Muhittin Aygün, İsmail Özdemir|2024|J.Mol.Struct.|1295|136679|doi:10.1016/j.molstruc.2023.136679
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.cc2gkgs9
title: CCDC 2280911: Experimental Crystal Structure Determination

description: Related Article: Naima Munir, Navin Gürbüz, M. Naveed Zafar, Enes Evren, Betül Şen, Muhittin Aygün, İsmail Özdemir|2024|J.Mol.Struct.|1295|136679|doi:10.1016/j.molstruc.2023.136679
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: 10.15151/esrf-es-1317816145
title: Heidelberg BAG (HeidelBAG)

description: The HeidelBAG unites macromolecular crystallography of EMBL Heidelberg and the Heidelberg University Biochemistry Center (BZH). Central to all projects are large assemblies involved in chromosome organization and transcription control, in nuclear and cytoplasmic RNA regulation and modification, in translational control by ribosome associated factors or further in protein targeting, membrane protein insertion or post-translational modification. While O. Barabas from EMBL has left the BAG, Svetlana Dodonova and Sebastian Eustermann at EMBL will join and add projects on chromatin organization. Nearly all projects make use of integrated structural biology techniques (MX, SAXS/SANS, NMR, cryo-EM, AI approaches) that are combined with complementary methods, a strategy that warranties the continuous success of the BAG. More and more the detailed architecture and mechanistic description of entire macromolecular machines come into focus. The BAG reports on 17 publications and 30 PDB entries.
DOI: 10.15151/esrf-es-1341074648
title: Structural and dynamical studies from the Gothenburg BAG

description: The Gothenburg BAG was previously a Gothenburg/Lund BAG, but was remodelled in 2021 so as to reflect the realities that the Lund environment was more focused upon addressing their synchrotron radiation needs through MAX IV Laboratory. Moreover, serial crystallography, both at XFELs and using synchrotron radiation, has become a major of interest of several of the scientists at the University of Gothenburg, and this is not covered in the BAG but within another BAG coordinated at the ESRF. Standard MX using cryo-crystallography, as well as standard SAXS studies, are still an important aspect of our work, but now requires less beamtime than the larger BAG used in the past. Moreover, some of this work is connected to methodology developments or used as a stepping stone towards time-resolved crystallography studies. Overall, we have a diverse collection of projects from the groups in Gothenburg which continue to benefit greatly from access to the ESRF.
DOI: 10.15151/esrf-es-1365113442
title: Structural investigation of membrane and water-soluble proteins

description: The portfolio of this BAG includes structural investigation of membrane proteins as well as soluble proteins relevant to various scientific fields. These range from basic science to application-related projects with impact on biotechnology (optogenetics, biocatalysts) and medicine (understanding and combating bacterial and viral pathogens).
DOI: 10.5517/ccdc.csd.cc2gkzst
title: CCDC 2281407: Experimental Crystal Structure Determination

description: Related Article: Rong-Yao Xu, Xiu Liu, Guang Sun, Zhi-Yuan Zhang, Ming Dong, Liya Zhao, Si-Miao Zhang, Xi-Yang Wang, Hong-Xu Zhang, Shang-Jie Yang, Xiuguang Wang, Bin Li, Jian Li, Chunju Li|2023|RSC Advances|13|30269|doi:10.1039/D3RA05671F
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.cc2gl3bj
title: CCDC 2281517: Experimental Crystal Structure Determination

description: Related Article: Zhihui Zong, Fei Ya Zhou, Qinghua Chang, Fangxin Gao, Zhichen Liu, Shiling Fang, Xinyi Zheng, Junyao Tao, Lili Liang|2024|J.Mol.Struct.|1295|136617|doi:10.1016/j.molstruc.2023.136617
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.cc2glfxf
title: CCDC 2281845: Experimental Crystal Structure Determination

description: Related Article: Andrii Pyrih, Andrzej Łapiński, Sylwia Zięba, Adam Mizera, Roman Lesyk, Andrzej K. Gzella, Mariusz Jaskolski|2024|J.Mol.Struct.|1295|136748|doi:10.1016/j.molstruc.2023.136748
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.cc2glm2s
title: CCDC 2282005: Experimental Crystal Structure Determination

description: Related Article: Liam F. McGarry, Osama El-Zubir, Paul G. Waddell, Fabio Cucinotta, Andrew Houlton, Benjamin R. Horrocks|2023|Soft Matter|19|8386|doi:10.1039/D3SM01006F
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.cc2gm96m
title: CCDC 2282660: Experimental Crystal Structure Determination

description: Related Article: Diana Becerra, Jaime Portilla, Hugo Rojas, Mario A. Macías, Juan-Carlos Castillo|2024|J.Mol.Struct.|1295|136616|doi:10.1016/j.molstruc.2023.136616
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.cc2gm97n
title: CCDC 2282661: Experimental Crystal Structure Determination

description: Related Article: Diana Becerra, Jaime Portilla, Hugo Rojas, Mario A. Macías, Juan-Carlos Castillo|2024|J.Mol.Struct.|1295|136616|doi:10.1016/j.molstruc.2023.136616
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: 10.15151/esrf-es-1341069594
title: Deciphering the pyritization of organisms during diagenesis by probing experimental samples

description: Understanding the processes leading to fossilization is crucial in palaeontology and laboratory-based experiments are an effective approach to constrain their timing, controls and mechanisms. Experiments of arthropods pyritization, one of the main pathways of replication of organisms in the fossil record, were conducted. The goal of this proposal is to visualize in 3D both the organism decay and its preservation by pyrite precipitation, which has not been possible with laboratory-based X-ray Computed Tomography (CT). Data will (i) bring clues to the debate on whether tissues influence pyrite precipitation, (ii) establish a precise sequence of character decay in Crustacean, and (iii) precise the kinetics and influence of environmental factors onto ongoing destructive and preservation processes.
DOI: 10.15151/esrf-es-1340267481
title: In situ laminography investigating damage evolution and strain heterogeneity during plane strain tension loading and non-proportional loadin

description: The aim of this study is to identify the deformation and damage interactions of aluminium alloy sheets under plane strain tension conditions for different microstructures. Plane strain tension conditions are identified as critical in forming processes as early localization and the lowest deformation at fracture are found under these conditions. Using flat samples with local thickness reductions, the plane strain state can be achieved. In contrast to tomography, in situ laminography allows the evolution of the microstructure and damage as well as strain (via image correlation techniques) to be studied in the plane strain tension zone. In addition, the role of pre-strain on failure in plane strain tension will be investigated by performing a load path change on a newly designed sample. The role of crystallographic texture, obtained by complementary EBSD, on strain heterogeneity and localization followed by damage and failure will be further investigated by simulations.
DOI: 10.15151/esrf-es-1340267604
title: Assessing cellular internalisation of carbon nanodots doped with gadolinium using correlative optical microscopy and nanofocused synchrotron

description: We have developed a series of 7-9 nm Carbon nanodots (CNDs) doped with Gd (III) (Gd-CND). They present good stability, biocompatibility and r1 relaxivity values comparable with those of clinical contrast agents, making them interesting as multimodal nanomaterials for Magnetic Resonance Imaging(MRI) and theragnostic applications. ICP-MS show high Gd accumulation in cells treated with Gd CNDs, suggesting that they might penetrate inside cells (desired for new contrast agents). Unfortunately, this could not be confirmed using confocal microscopy or TEM, as those techniques cannot detect intracellular Gd-CNDs. As such, we intend to acquire correlative organelle fluorescence probe Cryo-CLEM and XRF tomograms from cells treated with our Gd-CND at ID16A. This will allow us to obtain 3D information on the localisation of the material within cells with sub-cellular resolution, helping to assess their potential as viable MRI and theragnostic agents for bioimaging and biomedical applications.
DOI: 10.6084/m9.figshare.24564421
title: <b>Ectomycorrhizal trees rely on nitrogen resorption less than arbuscular mycorrhizal trees globally</b>

description: Nitrogen (N) resorption is an important pathway of N conservation, contributing to a proportion of plant N requirement. However, whether the ratio of N resorption to N requirement would be affected by environmental factors, mycorrhizal types or atmospheric CO<sub>2</sub> concentration remains unclear. Here, we conducted a meta-analysis on the impacts of environmental factors and mycorrhizal types on this ratio. We found this ratio in ectomycorrhizal (EM) trees decreased with mean annual precipitation, mean annual temperature, soil total N content and atmospheric CO<sub>2</sub> concentration and was significantly lower than that in arbuscular mycorrhizal (AM) trees. An <i>in situ</i> <sup>15</sup>N tracing experiment further confirmed this stronger reliance on N resorption for AM trees than EM trees. Our study suggests that AM and EM trees potentially have different strategies for alleviation of progressive N limitation, highlighting the necessity of incorporating plant mycorrhizal types into Earth System Models.
DOI: 10.6084/m9.figshare.24564421.v1
title: <b>Ectomycorrhizal trees rely on nitrogen resorption less than arbuscular mycorrhizal trees globally</b>

description: Nitrogen (N) resorption is an important pathway of N conservation, contributing to a proportion of plant N requirement. However, whether the ratio of N resorption to N requirement would be affected by environmental factors, mycorrhizal types or atmospheric CO<sub>2</sub> concentration remains unclear. Here, we conducted a meta-analysis on the impacts of environmental factors and mycorrhizal types on this ratio. We found this ratio in ectomycorrhizal (EM) trees decreased with mean annual precipitation, mean annual temperature, soil total N content and atmospheric CO<sub>2</sub> concentration and was significantly lower than that in arbuscular mycorrhizal (AM) trees. An <i>in situ</i> <sup>15</sup>N tracing experiment further confirmed this stronger reliance on N resorption for AM trees than EM trees. Our study suggests that AM and EM trees potentially have different strategies for alleviation of progressive N limitation, highlighting the necessity of incorporating plant mycorrhizal types into Earth System Models.
DOI: 10.17632/6mrr5v39y8.1
title: Data for: An Experimental Study on Quartz Dissolution Kinetics in Water under Supercritical Geothermal Conditions

description: Raw data for all figures in the manuscript by Zhong et al to be published by Geochimica et Cosmochimica Acta as "An Experimental Study on Quartz Dissolution Kinetics in Water under Supercritical Geothermal Conditions"
DOI: 10.17632/ccz2d6ww94.1
title: Swimming behavior data

description: Swimming behavior data
DOI: 10.17632/y69z4cyb4p.1
title: The human disease gene ZNFX1 controls inflammation through inhibition of the NLRP3 inflammasome

description: Our data includes unprocessed and uncompressed imaging data (microscopy as well as gels and blocks) in this article
DOI: 10.17632/hr9gxsdfsf.1
title: Hydrochemical parameters of the Ob River floodplain at Kaibasovo Station, 2020-2021

description: Spatial and temporal variations of hydrochemical parameters and CO2 concentrations and emission fluxes in the floodplain
DOI: 10.17632/jw2jhn8ct9.1
title: Key galactosylated glycan receptors of SARS-CoV-2 and its inhibitor from bovine milk galactosylated glycoproteins

description: Illustrating the precise role of glycosylation in the interaction of spike (S) protein of SARS-CoV-2 and angiotensin-converting enzyme 2 (ACE2) is important for understanding molecular mechanism of SARS-COV-2 infection. In this study, we utilized the antibody-overlay lectin microarrays, molecular docking analysis and glycosidase digestion to probe roles of N-glycans on S1 subunit of SARS-CoV-2 and ACE2. Our results showed that the galactosylated glycans were dominant on both S protein and ACE2. Importantly, we proved that the β1-4 galactosylated N-glycans of ACE2 were pivotal for the bindings of SARS-CoV-2 with ACE2. Furthermore, we found that the glycoproteins isolated from bovine milk contained abundant galactosylated glycans, which were similar to the glycoforms of ACE2, and could prevent the entry of SARS-CoV-2 pseudovirus. Our study provided the evidences that the β1-4 galactosylated N-glycans on ACE2 were key glycan receptors of SARS-CoV-2, and valuable strategies for developing an inexpensive protein drug to prevent SARS-CoV-2 infection.
DOI: 10.17632/d58x978jrh.1
title: Small-molecule antivirals treatment for Covid-19: A systematic review and network meta-analysis

description: Supplemental Materials for "Small-molecule antivirals treatment for Covid-19: A systematic review and network meta-analysis". Our study was registered on PROSPERO (CRD42023396617) and followed the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) 2020 guidelines. The protocol was also showed . The study characteristics about 92 RCTs and 68 retrospective studies were shown. We utilized the revised Cochrane Risk of Bias tool for RCTs and the Newcastle Ottawa Scale (NOS) for retrospective studies. A total of 92 RCTs were included, of which 42 RCTs were comprehensively evaluated as "High risk" due to allocation concealment and blinding, 15 RCTs were evaluated as "Unclear risk" due to blinding and other biases. A total of 67 retrospective studies were included, of which 34 were mainly downgraded for the typicality of the exposed study, comparability of studies on the basis of the design or analysis, and adequacy of follow up of cohorts.