cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5517/ccdc.csd.cc2j8kr4
title: CCDC 2331936: Experimental Crystal Structure Determination

description: Related Article: S. Joshi, N. Hickey, P. M. Marcos, S. Geremia|2024|Crystals|14|343|doi:10.3390/cryst14040343
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.cc2j8ks5
title: CCDC 2331937: Experimental Crystal Structure Determination

description: Related Article: S. Joshi, N. Hickey, P. M. Marcos, S. Geremia|2024|Crystals|14|343|doi:10.3390/cryst14040343
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.cc2j8kt6
title: CCDC 2331938: Experimental Crystal Structure Determination

description: Related Article: S. Joshi, N. Hickey, P. M. Marcos, S. Geremia|2024|Crystals|14|343|doi:10.3390/cryst14040343
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.cc2j8kv7
title: CCDC 2331939: Experimental Crystal Structure Determination

description: Related Article: S. Joshi, N. Hickey, P. M. Marcos, S. Geremia|2024|Crystals|14|343|doi:10.3390/cryst14040343
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: 10.5281/zenodo.18376922
title: Storm-Time GNSS Propagation at Mid-Latitude Magnetic Conjugate Points

description: This data set was used to investigate the responses of Total Electron Content (TEC) values at magnetic conjugate points during geomagnetically active conditions. It was performed for three magnetic conjugate pairs of Beijing-Learmonth, Petropavlovsk-Canberra and Bar Harbor-Palmer Station located in the mid-latitude region.
DOI: 10.5281/zenodo.8414018
title: Storm-Time GNSS Propagation at Mid-Latitude Magnetic Conjugate Points

description: This data set was used to investigate the responses of Total Electron Content (TEC) values at magnetic conjugate points during geomagnetically active conditions. It was performed for three magnetic conjugate pairs of Beijing-Learmonth, Petropavlovsk-Canberra and Bar Harbor-Palmer Station located in the mid-latitude region.
DOI: 10.5517/ccdc.csd.cc2j8qg0
title: CCDC 2332082: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8qh1
title: CCDC 2332083: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8qj2
title: CCDC 2332084: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8qk3
title: CCDC 2332085: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8ql4
title: CCDC 2332086: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8qm5
title: CCDC 2332087: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8qn6
title: CCDC 2332088: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8qp7
title: CCDC 2332089: Experimental Crystal Structure Determination

description: Related Article: Despina Dermitzaki, Angeliki Panagiotopoulou, Michael Pissas, Vassilis Psycharis, and Catherine P. Raptopoulou|2024|ChemPlusChem|89|e202400123|doi:10.1002/cplu.202400123
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.cc2j8t6v
title: CCDC 2332167: Experimental Crystal Structure Determination

description: Related Article: Ayaka Sumida, Shohei Takahashi, Sayaka Nagai, Suguru Ito|2024|Chem.Lett.|53||doi:10.1093/chemle/upae047
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.cc2j8t7w
title: CCDC 2332168: Experimental Crystal Structure Determination

description: Related Article: Ayaka Sumida, Shohei Takahashi, Sayaka Nagai, Suguru Ito|2024|Chem.Lett.|53||doi:10.1093/chemle/upae047
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.cc2j8w90
title: CCDC 2332232: Experimental Crystal Structure Determination

description: Related Article: Enrique Pérez-Gutiérrez, Youness El Bakri, Kandasamy Saravanan, Margarita Cerón, Perumal Venkatesan, Rashad Al-Salahi, S. Thamotharan, M. Judith Percino|2025|J.Mol.Struct.|1322|140559|doi:10.1016/j.molstruc.2024.140559
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.cc2j8wb1
title: CCDC 2332233: Experimental Crystal Structure Determination

description: Related Article: Enrique Pérez-Gutiérrez, Youness El Bakri, Kandasamy Saravanan, Margarita Cerón, Perumal Venkatesan, Rashad Al-Salahi, S. Thamotharan, M. Judith Percino|2025|J.Mol.Struct.|1322|140559|doi:10.1016/j.molstruc.2024.140559
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.cc2j8wc2
title: CCDC 2332234: Experimental Crystal Structure Determination

description: Related Article: Enrique Pérez-Gutiérrez, Youness El Bakri, Kandasamy Saravanan, Margarita Cerón, Perumal Venkatesan, Rashad Al-Salahi, S. Thamotharan, M. Judith Percino|2025|J.Mol.Struct.|1322|140559|doi:10.1016/j.molstruc.2024.140559
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.cc2j8ysk
title: CCDC 2332309: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j8ytl
title: CCDC 2332310: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j8yvm
title: CCDC 2332311: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j8ywn
title: CCDC 2332312: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j8yxp
title: CCDC 2332313: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j8yyq
title: CCDC 2332314: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j8yzr
title: CCDC 2332315: Experimental Crystal Structure Determination

description: Related Article: Rodrigo Plaza-Pedroche, Amparo Navarro, M. Paz Fernández-Liencres, Sonia B. Jiménez-Pulido, Nuria A. Illán-Cabeza, Sylvain Achelle, and Julián Rodríguez-López|2024|AIP J.Chem.Phys.|161|164307|doi:10.1063/5.0224650
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.cc2j921z
title: CCDC 2332410: Experimental Crystal Structure Determination

description: Related Article: R.M. Ruzibaeva, R.Ya. Okmanov, B. Tashkhodzhaev, N.I. Mukarramov, A.G. Eshimbetov A. M. Nigmatullaev|2024|Chem. Nat. Compd.|60|895|doi:10.1007/s10600-024-04472-7
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.cc2j9220
title: CCDC 2332411: Experimental Crystal Structure Determination

description: Related Article: R.M. Ruzibaeva, R.Ya. Okmanov, B. Tashkhodzhaev, N.I. Mukarramov, A.G. Eshimbetov A. M. Nigmatullaev|2024|Chem. Nat. Compd.|60|895|doi:10.1007/s10600-024-04472-7
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: 10.5518/1533
title: Ire1-LD activation by unfolded protein substrate and molecular chaperone BiP

description: Biophysical characterization of how the molecular chaperone BiP and a model Ire1 substrate interdependently control activation of the ER stress sensor Ire1
DOI: 10.5281/zenodo.18372086
title: Qualitative coding for conceptualizing asylum literacy
DOI: 10.5281/zenodo.18372087
title: Qualitative coding for conceptualizing asylum literacy
DOI: 10.5281/zenodo.17698987
title: Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress- Tabular data

description: Cells have evolved organelle-specific responses to maintain protein homeostasis (proteostasis). During proteostatic stress, mitochondria downregulate translation and enhance protein folding, yet the underlying mechanisms remain poorly defined. Here, we employed cryo-electron tomography to observe the structural consequences of mitochondrial proteostatic stress within human cells. We detected protein aggregates within the mitochondrial matrix, accompanied by a marked remodeling of cristae architecture. Concomitantly, the number of mitochondrial ribosome complexes was significantly reduced. Mitochondrial Hsp60 (mHsp60), a key protein folding machine, underwent major conformational changes to favor complexes with its co-chaperone mHsp10. We visualized the interactions of mHsp60 with native substrate proteins, and determined in vitro mHsp60 cryo- EM structures enabling nucleotide state assignment of the in situ structures. These data converge on a model of the mHsp60 functional cycle and its essential role in mitochondrial proteostasis. More broadly, our findings reveal structural mechanisms governing mitochondrial protein biosynthesis and their remodeling under proteostatic stress.
description: Numerical values in tabular format of the processed data used for plotting the respective figure panels. For orientation, see the data organization outlined below.

Organization of data:

• Fig. 1C: Membdensity_*

Each .csv file contains the mean density of membrane voxels, normalized to mitochondrial volume, per tomogram. One file is provided for each condition.

• Fig. 1D: Membdensity_distDep_*

Each .csv file contains the mean density of membrane voxels, normalized to mitochondrial volume, per tomogram. One file is provided for each distance range from the aggregate.

• Fig. 2B: PartAbundQuant_perCond_*

Each .csv file contains the mean density of particles, normalized to mitochondrial volume, per tomogram. One file is provided for each particle species and condition.

• Fig. 2E: PartAbundQuant_perCond_*

Each .csv file contains the mean density of particles, normalized to mitochondrial volume, per tomogram. One file is provided for each particle species and condition.

• Fig. 2H: PartEnrichment2Agg_*

Each .csv file contains the mean density of particles, normalized to mitochondrial volume, per tomogram. One file is provided for each particle species and distance range from the aggregate.
DOI: 10.5281/zenodo.17698986
title: Structural remodeling of the mitochondrial protein biogenesis machinery under proteostatic stress- Tabular data

description: Cells have evolved organelle-specific responses to maintain protein homeostasis (proteostasis). During proteostatic stress, mitochondria downregulate translation and enhance protein folding, yet the underlying mechanisms remain poorly defined. Here, we employed cryo-electron tomography to observe the structural consequences of mitochondrial proteostatic stress within human cells. We detected protein aggregates within the mitochondrial matrix, accompanied by a marked remodeling of cristae architecture. Concomitantly, the number of mitochondrial ribosome complexes was significantly reduced. Mitochondrial Hsp60 (mHsp60), a key protein folding machine, underwent major conformational changes to favor complexes with its co-chaperone mHsp10. We visualized the interactions of mHsp60 with native substrate proteins, and determined in vitro mHsp60 cryo- EM structures enabling nucleotide state assignment of the in situ structures. These data converge on a model of the mHsp60 functional cycle and its essential role in mitochondrial proteostasis. More broadly, our findings reveal structural mechanisms governing mitochondrial protein biosynthesis and their remodeling under proteostatic stress.
description: Numerical values in tabular format of the processed data used for plotting the respective figure panels. For orientation, see the data organization outlined below.

Organization of data:

• Fig. 1C: Membdensity_*

Each .csv file contains the mean density of membrane voxels, normalized to mitochondrial volume, per tomogram. One file is provided for each condition.

• Fig. 1D: Membdensity_distDep_*

Each .csv file contains the mean density of membrane voxels, normalized to mitochondrial volume, per tomogram. One file is provided for each distance range from the aggregate.

• Fig. 2B: PartAbundQuant_perCond_*

Each .csv file contains the mean density of particles, normalized to mitochondrial volume, per tomogram. One file is provided for each particle species and condition.

• Fig. 2E: PartAbundQuant_perCond_*

Each .csv file contains the mean density of particles, normalized to mitochondrial volume, per tomogram. One file is provided for each particle species and condition.

• Fig. 2H: PartEnrichment2Agg_*

Each .csv file contains the mean density of particles, normalized to mitochondrial volume, per tomogram. One file is provided for each particle species and distance range from the aggregate.
DOI: 10.7284/167230
title: ADCP (Acoustic Doppler Current Profiler) data collected during research cruise AR87b using a Hawaii UHDAS instrument system onboard the platform RV Neil Armstrong

description: Original (unprocessed) data collected during a Field_expedition