cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.25378/janelia.24502861.v1
title: Compiled sptPALM data and trajectories for <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>

description: Compiled trajectories and all associated analysis organized by molecule and by ERMCS.Contact Chris with organization or structuring questions: cjobara@gmail.com or obarac@janelia.hhmi.orgObara + Nixon-Abell et al. 2023, https://www.biorxiv.org/content/10.1101/2022.09.03.505525v1<b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle-organelle contact sites. Endoplasmic reticulum-mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signaling molecules, lipids, and metabolites. ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle. However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation, a clear understanding of their nanoscale organization and regulation is still lacking. Here, we combine 3D electron microscopy with high-speed molecular tracking of a model organelle tether, VAPB, to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodeling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis (ALS)-associated mutation in VAPB perturbs these subdomains, likely impairing their remodeling capacity and resulting in impaired inter-organelle communication. These results establish high speed single molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis.
DOI: 10.25378/janelia.24502861
title: Compiled sptPALM data and trajectories for <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>

description: Compiled trajectories and all associated analysis organized by molecule and by ERMCS.Contact Chris with organization or structuring questions: cjobara@gmail.com or obarac@janelia.hhmi.orgObara + Nixon-Abell et al. 2023, https://www.biorxiv.org/content/10.1101/2022.09.03.505525v1<b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle-organelle contact sites. Endoplasmic reticulum-mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signaling molecules, lipids, and metabolites. ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle. However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation, a clear understanding of their nanoscale organization and regulation is still lacking. Here, we combine 3D electron microscopy with high-speed molecular tracking of a model organelle tether, VAPB, to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodeling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis (ALS)-associated mutation in VAPB perturbs these subdomains, likely impairing their remodeling capacity and resulting in impaired inter-organelle communication. These results establish high speed single molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis.
DOI: 10.26183/z1zj-8487
title: Pasifika Communities in Australia: 2021 Census dataset

description: This report provides a comprehensive analysis of Pasifika communities in Australia based on the 2021 Australian Bureau of Statistics (ABS) Census. The Australian Pasifika Educators Network (APEN) define 'Pasifika' as peoples and communities, who are genealogically, spiritually, and culturally connected to the lands, the skies and seas of the Pasifika region (including Aotearoa, New Zealand), and who have chosen to settle in and call Australia home. This analysis seeks to track key trends that have emerged since the 2015 Pacific Communities report published by Professor Jioji Ravulo based on the 2011 Census. In accordance with the intent of the original report, this current version seeks to provide an understanding of the current demographic, and socioeconomic experiences of Pasifika communities with a particular focus on education. This analysis covers population, education levels, employment patterns, as well as family and household characteristics to not only shed light on the unique circumstances faced by Pasifika communities, but also track key trends over the last decade. In addition, an examination of the Western Sydney region has been included, highlighting the significance of place-based insights on Pasifika communities towards informing policy responses and initiatives.
Dataset: 
OVERVIEW
This report compiles data from the 2021 Census of Population and Housing conducted by the Australian Bureau of Statistics (ABS). This document provides the second iteration on the human geography of Pasifika peoples within an Australian context,10 aimed at gathering greater insight into Pasifika communities, as well as comparing and tracing key trends through various datapoints. In addition, this report provides a spotlight on Pasifika communities in Western Sydney, where nearly 20% of the nation’s Pasifika population currently resides.
DOI: 10.25378/janelia.24502954
title: Raw FIB-SEM Volume (COS7 cells) for <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>

description: Raw FIB-SEM volume for paper (8nm voxels).For the paper:Obara + Nixon-Abell et al. 2023, https://www.biorxiv.org/content/10.1101/2022.09.03.505525v1<b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle-organelle contact sites. Endoplasmic reticulum-mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signaling molecules, lipids, and metabolites. ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle. However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation, a clear understanding of their nanoscale organization and regulation is still lacking. Here, we combine 3D electron microscopy with high-speed molecular tracking of a model organelle tether, VAPB, to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodeling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis (ALS)-associated mutation in VAPB perturbs these subdomains, likely impairing their remodeling capacity and resulting in impaired inter-organelle communication. These results establish high speed single molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis.
DOI: 10.25378/janelia.24502954.v1
title: Raw FIB-SEM Volume (COS7 cells) for <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>

description: Raw FIB-SEM volume for paper (8nm voxels).For the paper:Obara + Nixon-Abell et al. 2023, https://www.biorxiv.org/content/10.1101/2022.09.03.505525v1<b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle-organelle contact sites. Endoplasmic reticulum-mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signaling molecules, lipids, and metabolites. ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle. However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation, a clear understanding of their nanoscale organization and regulation is still lacking. Here, we combine 3D electron microscopy with high-speed molecular tracking of a model organelle tether, VAPB, to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodeling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis (ALS)-associated mutation in VAPB perturbs these subdomains, likely impairing their remodeling capacity and resulting in impaired inter-organelle communication. These results establish high speed single molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis.
DOI: 10.25378/janelia.24514249
title: Plasmid Maps and sequence information for <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>

description: Plasmid maps and sequencing information for Obara + Nixon-Abell et al. 2023. https://www.biorxiv.org/content/10.1101/2022.09.03.505525v1Plasmid maps in macvector format, generic .gb format, and images of the maps. All constructs are also deposited at Addgene or available upon request from the authors. <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle-organelle contact sites. Endoplasmic reticulum-mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signaling molecules, lipids, and metabolites. ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle. However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation, a clear understanding of their nanoscale organization and regulation is still lacking. Here, we combine 3D electron microscopy with high-speed molecular tracking of a model organelle tether, VAPB, to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodeling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis (ALS)-associated mutation in VAPB perturbs these subdomains, likely impairing their remodeling capacity and resulting in impaired inter-organelle communication. These results establish high speed single molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis.
DOI: 10.25378/janelia.24514249.v1
title: Plasmid Maps and sequence information for <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>

description: Plasmid maps and sequencing information for Obara + Nixon-Abell et al. 2023. https://www.biorxiv.org/content/10.1101/2022.09.03.505525v1Plasmid maps in macvector format, generic .gb format, and images of the maps. All constructs are also deposited at Addgene or available upon request from the authors. <b>Motion of VAPB molecules reveals ER-mitochondria contact site subdomains</b>To coordinate cellular physiology, eukaryotic cells rely on the rapid exchange of molecules at specialized organelle-organelle contact sites. Endoplasmic reticulum-mitochondrial contact sites (ERMCSs) are particularly vital communication hubs, playing key roles in the exchange of signaling molecules, lipids, and metabolites. ERMCSs are maintained by interactions between complementary tethering molecules on the surface of each organelle. However, due to the extreme sensitivity of these membrane interfaces to experimental perturbation, a clear understanding of their nanoscale organization and regulation is still lacking. Here, we combine 3D electron microscopy with high-speed molecular tracking of a model organelle tether, VAPB, to map the structure and diffusion landscape of ERMCSs. We uncovered dynamic subdomains within VAPB contact sites that correlate with ER membrane curvature and undergo rapid remodeling. We show that VAPB molecules enter and leave ERMCSs within seconds, despite the contact site itself remaining stable over much longer time scales. This metastability allows ERMCSs to remodel with changes in the physiological environment to accommodate metabolic needs of the cell. An amyotrophic lateral sclerosis (ALS)-associated mutation in VAPB perturbs these subdomains, likely impairing their remodeling capacity and resulting in impaired inter-organelle communication. These results establish high speed single molecule imaging as a new tool for mapping the structure of contact site interfaces and reveal that the diffusion landscape of VAPB at contact sites is a crucial component of ERMCS homeostasis.
DOI: 10.5519/qd.2p4vzcbi
title: Query on the Natural History Museum Data Portal (data.nhm.ac.uk) (1 records)
DOI: 10.17894/ucph.50635abe-4993-4ce5-af21-d76f2083ca1e
title: GCB_Hermesdorf_et_al_tundra_CO2
DOI: 10.6084/m9.figshare.24514711
title: Small test data for TKSM

description: Small test data for TKSM simulator (https://github.com/vpc-ccg/tksm)
DOI: 10.6084/m9.figshare.24514711.v1
title: Small test data for TKSM

description: Small test data for TKSM simulator (https://github.com/vpc-ccg/tksm)
DOI: 10.26183/t29f-sy52
title: State of the arts and culture in Western Sydney dataset

description: This report explores various trends in the arts in Western Sydney, utilising publicly accessible data, as well as data provided by Create NSW under a Freedom of Information request on 10 February, 2023. The report draws on data provided by Create NSW at the broad level at which it was supplied. Data requested of Create NSW for this report included: 1. NSW Cultural Arts Funding awarded, 2. grant applications, 3. grant recipients/awarded (including COVID-19 relief) and 4. Creative Kids providers and use of Creative Kids vouchers by LGA (2015 to 2021–22). The first three data points were supplied at a broad, top-level of detail, whereas the creative kids voucher data was excluded from the data pack provided to the team as this was not geographically classified for the spatial analysis required.
The stakeholder consultations for this project were limited in scope due to the complexities of the sector and the availability of participants within the time parameters of this project. A series of one-on-one interviews were held by an invitation only process. Two workshops were facilitated with the Western Sydney Arts Alliance and included members of the Alliance as well as external arts and culture stakeholders. Furthermore, while the study sample of participants from the small to medium arts sector was broad, this project did not specifically target underrepresented groups for participation. 
This dataset is privately archived with Western Sydney University. To discuss the data, please contact the author Rhonda Itaoui r.itaoui@westernsydney.edu.au 0000-0002-1647-0109.
DOI: 10.5517/ccdc.csd.cc2grj0s
title: CCDC 2286715: Experimental Crystal Structure Determination

description: Related Article: Zhen Yuan, Liangji Chen, Xin Zhou, Lu Li, Yunbin Li, Yisi Yang, Zhiqi Zhou, Yanting Chen, Shengchang Xiang, Banglin Chen, Zhangjing Zhang|2023|J.Mater.Chem.A|11|21857|doi:10.1039/D3TA04738E
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.cc2grj1t
title: CCDC 2286716: Experimental Crystal Structure Determination

description: Related Article: Zhen Yuan, Liangji Chen, Xin Zhou, Lu Li, Yunbin Li, Yisi Yang, Zhiqi Zhou, Yanting Chen, Shengchang Xiang, Banglin Chen, Zhangjing Zhang|2023|J.Mater.Chem.A|11|21857|doi:10.1039/D3TA04738E
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.cc2grj2v
title: CCDC 2286717: Experimental Crystal Structure Determination

description: Related Article: Zhen Yuan, Liangji Chen, Xin Zhou, Lu Li, Yunbin Li, Yisi Yang, Zhiqi Zhou, Yanting Chen, Shengchang Xiang, Banglin Chen, Zhangjing Zhang|2023|J.Mater.Chem.A|11|21857|doi:10.1039/D3TA04738E
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.cc2gtt04
title: CCDC 2288916: Experimental Crystal Structure Determination

description: Related Article: I. V. Bakaev, N. F. Romashev, V. I. Komlyagina, D. G. Samsonenko, A. L. Gushchin|2023|New J.Chem.|47|18825|doi:10.1039/D3NJ03832G
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.cc2gtt15
title: CCDC 2288917: Experimental Crystal Structure Determination

description: Related Article: I. V. Bakaev, N. F. Romashev, V. I. Komlyagina, D. G. Samsonenko, A. L. Gushchin|2023|New J.Chem.|47|18825|doi:10.1039/D3NJ03832G
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.cc2gtt26
title: CCDC 2288918: Experimental Crystal Structure Determination

description: Related Article: I. V. Bakaev, N. F. Romashev, V. I. Komlyagina, D. G. Samsonenko, A. L. Gushchin|2023|New J.Chem.|47|18825|doi:10.1039/D3NJ03832G
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.cc2gtt37
title: CCDC 2288919: Experimental Crystal Structure Determination

description: Related Article: I. V. Bakaev, N. F. Romashev, V. I. Komlyagina, D. G. Samsonenko, A. L. Gushchin|2023|New J.Chem.|47|18825|doi:10.1039/D3NJ03832G
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.cc2gvdnd
title: CCDC 2289494: Experimental Crystal Structure Determination

description: Related Article: Yijue Xu, Miriam Calabrese, Nicola Demitri, Andrea Pizzi, Tamali Nag, Ivan Hung, Zhehong Gan, Giuseppe Resnati, David L. Bryce|2023|Chem.Commun.|59|12609|doi:10.1039/D3CC04090A
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.cc2gvsrw
title: CCDC 2289869: Experimental Crystal Structure Determination

description: Related Article: Marcel E. Baumert, Victoria Le, Po-Hua Su, Yosuke Akae, Dominic Bresser, Patrick Théato, Max M. Hansmann|2023|J.Am.Chem.Soc.|145|23334|doi:10.1021/jacs.3c09153
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.cc2gvssx
title: CCDC 2289870: Experimental Crystal Structure Determination

description: Related Article: Marcel E. Baumert, Victoria Le, Po-Hua Su, Yosuke Akae, Dominic Bresser, Patrick Théato, Max M. Hansmann|2023|J.Am.Chem.Soc.|145|23334|doi:10.1021/jacs.3c09153
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.cc2gvsty
title: CCDC 2289871: Experimental Crystal Structure Determination

description: Related Article: Marcel E. Baumert, Victoria Le, Po-Hua Su, Yosuke Akae, Dominic Bresser, Patrick Théato, Max M. Hansmann|2023|J.Am.Chem.Soc.|145|23334|doi:10.1021/jacs.3c09153
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.