cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.6084/m9.figshare.13650460.v1
title: Mammalian BCAS3 and C16orf70 associate with the phagophore assembly site in response to selective and non-selective autophagy

description: Macroautophagy/autophagy is an intracellular degradation process that delivers cytosolic materials and/or damaged organelles to lysosomes. <i>De novo</i> synthesis of the autophagosome membrane occurs within a phosphatidylinositol-3-phosphate-rich region of the endoplasmic reticulum, and subsequent expansion is critical for cargo encapsulation. This process is complex, especially in mammals, with many regulatory factors. In this study, by utilizing PRKN (parkin RBR E3 ubiquitin protein ligase)-mediated mitochondria autophagy (mitophagy)-inducing conditions in conjunction with chemical crosslinking and mass spectrometry, we identified human BCAS3 (BCAS3 microtubule associated cell migration factor) and C16orf70 (chromosome 16 open reading frame 70) as novel proteins that associate with the autophagosome formation site during both non-selective and selective autophagy. We demonstrate that BCAS3 and C16orf70 form a complex and that their association with the phagophore assembly site requires both proteins. <i>In silico</i> structural modeling, mutational analyses in cells and <i>in vitro</i> phosphoinositide-binding assays indicate that the WD40 repeat domain in human BCAS3 directly binds phosphatidylinositol-3-phosphate. Furthermore, overexpression of the BCAS3-C16orf70 complex affects the recruitment of several core autophagy proteins to the phagophore assembly site. This study demonstrates regulatory roles for human BCAS3 and C16orf70 in autophagic activity. <b>Abbreviations:</b> AO: antimycin A and oligomycin; Ash: assembly helper; ATG: autophagy-related; BCAS3: BCAS3 microtubule associated cell migration factor; C16orf70: chromosome 16 open reading frame 70; DAPI: 4‘,6-diamidino-2-phenylindole; DKO: double knockout; DMSO: dimethyl sulfoxide; ER: endoplasmic reticulum; fluoppi: fluorescent-based technology detecting protein-protein interactions; FIS1: fission, mitochondrial 1; FKBP: FKBP prolyl isomerase family member 1C; FRB: FKBP-rapamycin binding; hAG: humanized azami-green; IP: immunoprecipitation; IRES: internal ribosome entry site; KO: knockout; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MFN2: mitofusin 2; MS: mass spectrometry; MT-CO2: mitochondrially encoded cytochrome c oxidase II; mtDNA: mitochondrial DNA; OPTN: optineurin; PFA: paraformaldehyde; PE: phosphatidylethanolamine; PtdIns3K: phosphatidylinositol 3-kinase; PtdIns3P: phosphatidylinositol-3-phosphate; PtdIns(3,5)P<sub>2</sub>: phosphatidylinositol-3,5-bisphosphate; PINK1: PTEN induced kinase 1; PRKN/Parkin: parkin RBR E3 ubiquitin protein ligase; PROPPIN: β-propellers that bind polyphosphoinositides; RB1CC1/FIP200: RB1 inducible coiled-coil 1; TOMM20: translocase of outer mitochondrial membrane 20; ULK1: unc-51 like autophagy activating kinase 1; WDR45B/WIPI3: WD repeat domain 45B; WDR45/WIPI4: WD repeat domain 45; WIPI: WD repeat domain, phosphoinositide interacting; WT: wild type; ZFYVE1/DFCP1: zinc finger FYVE-type containing 1
DOI: 10.6084/m9.figshare.12851423
title: SETX (senataxin), the helicase mutated in AOA2 and ALS4, functions in autophagy regulation

description: SETX (senataxin) is an RNA/DNA helicase that has been implicated in transcriptional regulation and the DNA damage response through resolution of R-loop structures. Mutations in <i>SETX</i> result in either of two distinct neurodegenerative disorders. <i>SETX</i> dominant mutations result in a juvenile form of amyotrophic lateral sclerosis (ALS) called ALS4, whereas recessive mutations are responsible for ataxia called ataxia with oculomotor apraxia type 2 (AOA2). How mutations in the same protein can lead to different phenotypes is still unclear. To elucidate AOA2 disease mechanisms, we first examined gene expression changes following SETX depletion. We observed the effects on both transcription and RNA processing, but surprisingly observed decreased R-loop accumulation in SETX-depleted cells. Importantly, we discovered a strong connection between SETX and the macroautophagy/autophagy pathway, reflecting a direct effect on transcription of autophagy genes. We show that SETX depletion inhibits the progression of autophagy, leading to an accumulation of ubiquitinated proteins, decreased ability to clear protein aggregates, as well as mitochondrial defects. Analysis of AOA2 patient fibroblasts also revealed a perturbation of the autophagy pathway. Our work has thus identified a novel function for SETX in the regulation of autophagy, whose modulation may have a therapeutic impact for AOA2. <b>Abbreviations:</b> 3ʹREADS: 3ʹ region extraction and deep sequencing; ACTB: actin beta; ALS4: amyotrophic lateral sclerosis type 4; AOA2: ataxia with oculomotor apraxia type 2; APA: alternative polyadenylation; AS: alternative splicing; ATG7: autophagy-related 7; ATP6V0D2: ATPase H+ transporting V0 subunit D2; BAF: bafilomycin A<sub>1</sub>; BECN1: beclin 1; ChIP: chromatin IP; Chloro: chloroquine; CPT: camptothecin; DDR: DNA damage response; DNMT1: DNA methyltransferase 1; DRIP: DNA/RNA IP; DSBs: double strand breaks; EBs: embryoid bodies; FTD: frontotemporal dementia; GABARAP: GABA type A receptor-associated protein; GO: gene ontology; HR: homologous recombination; HTT: huntingtin; IF: immunofluorescence; IP: immunoprecipitation; iPSCs: induced pluripotent stem cells; KD: knockdown; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MN: motor neuron; MTORC1: mechanistic target of rapamycin kinase complex 1; PASS: PolyA Site Supporting; PFA: paraformaldehyde; RNAPII: RNA polymerase II; SCA: spinocerebellar ataxia; SETX: senataxin; SMA: spinal muscular atrophy; SMN1: survival of motor neuron 1, telomeric; SQSTM1/p62: sequestosome 1; TFEB: transcription factor EB; TSS: transcription start site; TTS: transcription termination site; ULK1: unc-51 like autophagy activating kinase 1; WB: western blot; WIPI2: WD repeat domain, phosphoinositide interacting 2; XRN2: 5ʹ-3ʹ exoribonuclease 2.
DOI: 10.6084/m9.figshare.12851423.v3
title: SETX (senataxin), the helicase mutated in AOA2 and ALS4, functions in autophagy regulation

description: SETX (senataxin) is an RNA/DNA helicase that has been implicated in transcriptional regulation and the DNA damage response through resolution of R-loop structures. Mutations in <i>SETX</i> result in either of two distinct neurodegenerative disorders. <i>SETX</i> dominant mutations result in a juvenile form of amyotrophic lateral sclerosis (ALS) called ALS4, whereas recessive mutations are responsible for ataxia called ataxia with oculomotor apraxia type 2 (AOA2). How mutations in the same protein can lead to different phenotypes is still unclear. To elucidate AOA2 disease mechanisms, we first examined gene expression changes following SETX depletion. We observed the effects on both transcription and RNA processing, but surprisingly observed decreased R-loop accumulation in SETX-depleted cells. Importantly, we discovered a strong connection between SETX and the macroautophagy/autophagy pathway, reflecting a direct effect on transcription of autophagy genes. We show that SETX depletion inhibits the progression of autophagy, leading to an accumulation of ubiquitinated proteins, decreased ability to clear protein aggregates, as well as mitochondrial defects. Analysis of AOA2 patient fibroblasts also revealed a perturbation of the autophagy pathway. Our work has thus identified a novel function for SETX in the regulation of autophagy, whose modulation may have a therapeutic impact for AOA2. <b>Abbreviations:</b> 3ʹREADS: 3ʹ region extraction and deep sequencing; ACTB: actin beta; ALS4: amyotrophic lateral sclerosis type 4; AOA2: ataxia with oculomotor apraxia type 2; APA: alternative polyadenylation; AS: alternative splicing; ATG7: autophagy-related 7; ATP6V0D2: ATPase H+ transporting V0 subunit D2; BAF: bafilomycin A<sub>1</sub>; BECN1: beclin 1; ChIP: chromatin IP; Chloro: chloroquine; CPT: camptothecin; DDR: DNA damage response; DNMT1: DNA methyltransferase 1; DRIP: DNA/RNA IP; DSBs: double strand breaks; EBs: embryoid bodies; FTD: frontotemporal dementia; GABARAP: GABA type A receptor-associated protein; GO: gene ontology; HR: homologous recombination; HTT: huntingtin; IF: immunofluorescence; IP: immunoprecipitation; iPSCs: induced pluripotent stem cells; KD: knockdown; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MN: motor neuron; MTORC1: mechanistic target of rapamycin kinase complex 1; PASS: PolyA Site Supporting; PFA: paraformaldehyde; RNAPII: RNA polymerase II; SCA: spinocerebellar ataxia; SETX: senataxin; SMA: spinal muscular atrophy; SMN1: survival of motor neuron 1, telomeric; SQSTM1/p62: sequestosome 1; TFEB: transcription factor EB; TSS: transcription start site; TTS: transcription termination site; ULK1: unc-51 like autophagy activating kinase 1; WB: western blot; WIPI2: WD repeat domain, phosphoinositide interacting 2; XRN2: 5ʹ-3ʹ exoribonuclease 2.
DOI: 10.6084/m9.figshare.12851423.v2
title: SETX (senataxin), the helicase mutated in AOA2 and ALS4, functions in autophagy regulation

description: SETX (senataxin) is an RNA/DNA helicase that has been implicated in transcriptional regulation and the DNA damage response through resolution of R-loop structures. Mutations in <i>SETX</i> result in either of two distinct neurodegenerative disorders. <i>SETX</i> dominant mutations result in a juvenile form of amyotrophic lateral sclerosis (ALS) called ALS4, whereas recessive mutations are responsible for ataxia called ataxia with oculomotor apraxia type 2 (AOA2). How mutations in the same protein can lead to different phenotypes is still unclear. To elucidate AOA2 disease mechanisms, we first examined gene expression changes following SETX depletion. We observed the effects on both transcription and RNA processing, but surprisingly observed decreased R-loop accumulation in SETX-depleted cells. Importantly, we discovered a strong connection between SETX and the macroautophagy/autophagy pathway, reflecting a direct effect on transcription of autophagy genes. We show that SETX depletion inhibits the progression of autophagy, leading to an accumulation of ubiquitinated proteins, decreased ability to clear protein aggregates, as well as mitochondrial defects. Analysis of AOA2 patient fibroblasts also revealed a perturbation of the autophagy pathway. Our work has thus identified a novel function for SETX in the regulation of autophagy, whose modulation may have a therapeutic impact for AOA2.
DOI: 10.6084/m9.figshare.12851399
title: Differential activation of eMI by distinct forms of cellular stress

description: As one of the major, highly conserved catabolic pathways, autophagy delivers cytosolic components to lysosomes for degradation. It is essential for development, cellular homeostasis, and coping with stress. Reduced autophagy increases susceptibility to protein aggregation diseases and leads to phenotypes associated with aging. Of the three major forms of autophagy, macroautophagy (MA) can degrade organelles or aggregated proteins, and chaperone-mediated autophagy is specific for soluble proteins containing KFERQ-related targeting motifs. During endosomal microautophagy (eMI), cytoplasmic proteins are engulfed into late endosomes in an ESCRT machinery-dependent manner. eMI can be KFERQ-specific or occur in bulk and be induced by prolonged starvation. Its physiological regulation and function, however, are not understood. Here, we show that eMI in the <i>Drosophila</i> fat body, akin to the mammalian liver, is induced upon oxidative or genotoxic stress in an ESCRT and partially Hsc70-4-dependent manner. Interestingly, eMI activation is selective, as ER stress fails to elicit a response. Intriguingly, we find that reducing MA leads to a compensatory enhancement of eMI, suggesting a tight interplay between these degradative processes. Furthermore, we show that mutations in DNA damage response genes are sufficient to trigger eMI and that the response to oxidative stress is under the control of MAPK/JNK signaling. Our data suggest that, controlled by various signaling pathways, eMI allows an organ to react and adapt to specific types of stress and is thus likely critical to prevent disease. <b>Abbreviations:</b><i>Atg</i>: autophagy-related; CMA: chaperone-mediated autophagy; DDR: DNA damage repair; Df: deficiency (deletion); (E)GFP: (enhanced) green fluorescent protein; eMI: endosomal microautophagy; ER: endoplasmatic reticulum; ESCRT: endosomal sorting complexes required for transport; Eto: etoposide; FLP: flipase; Hsc: heat shock cognate protein; LAMP2A: lysosomal-associated membrane protein 2A; LE: late endosome; MA: macroautophagy; MI: microautophagy; MVB: multivesicular body; PA: photoactivatable; Para: paraquat; ROS: reactive oxygen species; SEM: standard error of means; Tor: target of rapamycin [serine/threonine kinase]; UPR: unfolded protein response; Vps: vacuolar protein sorting.
DOI: 10.6084/m9.figshare.12851399.v1
title: Differential activation of eMI by distinct forms of cellular stress

description: As one of the major, highly conserved catabolic pathways, autophagy delivers cytosolic components to lysosomes for degradation. It is essential for development, cellular homeostasis, and coping with stress. Reduced autophagy increases susceptibility to protein aggregation diseases and leads to phenotypes associated with aging. Of the three major forms of autophagy, macroautophagy (MA) can degrade organelles or aggregated proteins, and chaperone-mediated autophagy is specific for soluble proteins containing KFERQ-related targeting motifs. During endosomal microautophagy (eMI), cytoplasmic proteins are engulfed into late endosomes in an ESCRT machinery-dependent manner. eMI can be KFERQ-specific or occur in bulk and be induced by prolonged starvation. Its physiological regulation and function, however, are not understood. Here, we show that eMI in the <i>Drosophila</i> fat body, akin to the mammalian liver, is induced upon oxidative or genotoxic stress in an ESCRT and partially Hsc70-4-dependent manner. Interestingly, eMI activation is selective, as ER stress fails to elicit a response. Intriguingly, we find that reducing MA leads to a compensatory enhancement of eMI, suggesting a tight interplay between these degradative processes. Furthermore, we show that mutations in DNA damage response genes are sufficient to trigger eMI and that the response to oxidative stress is under the control of MAPK/JNK signaling. Our data suggest that, controlled by various signaling pathways, eMI allows an organ to react and adapt to specific types of stress and is thus likely critical to prevent disease. <b>Abbreviations:</b><i>Atg</i>: autophagy-related; CMA: chaperone-mediated autophagy; DDR: DNA damage repair; Df: deficiency (deletion); (E)GFP: (enhanced) green fluorescent protein; eMI: endosomal microautophagy; ER: endoplasmatic reticulum; ESCRT: endosomal sorting complexes required for transport; Eto: etoposide; FLP: flipase; Hsc: heat shock cognate protein; LAMP2A: lysosomal-associated membrane protein 2A; LE: late endosome; MA: macroautophagy; MI: microautophagy; MVB: multivesicular body; PA: photoactivatable; Para: paraquat; ROS: reactive oxygen species; SEM: standard error of means; Tor: target of rapamycin [serine/threonine kinase]; UPR: unfolded protein response; Vps: vacuolar protein sorting.
DOI: 10.5285/fe02d5eef9ef4ad889d1917ccad3b35f
title: ESA Sea State Climate Change Initiative (Sea_State_cci): Global remote sensing multi-mission along-track Integrated Sea State Parameters (ISSP) from SAR WV onboard Sentinel-1A & 1B, L2P product, release version 3

description: The ESA Sea State Climate Change Initiative (CCI) project has produced global multi-sensor time-series of along-track satellite synthetic aperture radar (SAR) integrated sea state parameters (ISSP) data from Sentinel-1 (referred to as SAR WV onboard Sentinel-1 Level 2P (L2P) ISSP data) with a particular focus for use in climate studies. This dataset contains the Sentinel-1 SAR Remote Sensing Integrated Sea State Parameter product (v1.0), which forms part of the ESA Sea State CCI version 3.0 release. This product provides along-track primary significant wave height measurements and secondary sea state parameters, calibrated with CMEMS model data and reference in situ measurements at 20km resolution every 100km, processed using the Pleskachevsky et. al., 2021 emprical model, separated per satellite and pass, including all measurements with flags and uncertainty estimates. These are expert products with rich content and no data loss. The SAR Wave Mode data used in the Sea State CCI SAR WV onboard Sentinel-1 Level 2P (L2P) ISSP v3 dataset come from the Sentinel-1 satellite missions spanning from 2014 to 2021 (Sentinel-1 A, Sentinel-1 B).
DOI: 10.5285/8cd1a9beabc648c8a2c91fa68791d9d7
title: ESA Sea State Climate Change Initiative (Sea_State_cci): Global remote sensing multi-mission along-track Integrated Sea State Parameters (ISSP) from SAR Wave Mode onboard ENVISAT, L2P product, release version 3

description: The ESA Sea State Climate Change Initiative (CCI) project has produced global multi-sensor time-series of along-track satellite synthetic aperture radar (SAR) integrated sea state parameters (ISSP) data from ENVISAT (referred to as SAR Wave Mode onboard ENVISAT Level 2P (L2P) ISSP data) with a particular focus for use in climate studies. This dataset contains the ENVISAT Remote Sensing Integrated Sea State Parameter product (version 1.1), which forms part of the ESA Sea State CCI version 3.0 release. This product provides along-track significant wave height (SWH) measurements at 5km resolution every 100km, processed using the Li et al., 2020 empirical model, separated per satellite and pass, including all measurements with flags and uncertainty estimates. These are expert products with rich content and no data loss. The SAR Wave Mode data used in the Sea State CCI SAR WV onboard ENVISAT Level 2P (L2P) ISSP v3 dataset come from the ENVISAT satellite mission spanning from 2002 to 2012.
DOI: 10.5285/81bab8b378db443db4482a5961a58ec1
title: ESA Sea State Climate Change Initiative (Sea_State_cci): Global remote sensing multi-mission along-track significant wave height (SWH) from SAR WV onboard Sentinel-1A & 1B, L2P product, release version 3.

description: The ESA Sea State Climate Change Initiative (CCI) project has produced global multi-sensor time-series of along-track satellite synthetic aperture radar (SAR) significant wave height (SWH) data (referred to as SAR WV onboard Sentinel-1 Level 2P (L2P) SWH data) with a particular focus for use in climate studies. This dataset contains the Sentinel-1 SAR Remote Sensing Significant Wave Height product (version 1.0), which is part of the ESA Sea State CCI Version 3.0 release. This product provides along-track SWH measurements at 20km resolution every 100km, processed using the Quach et al statistical model , separated per satellite and pass, including all measurements with flags, corrections and extra parameters from other sources. These are expert products with rich content and no data loss. The SAR Wave Mode data used in the Sea State CCI dataset v3 come from Sentinel-1 satellite missions spanning from 2015 to 2021 (Sentinel-1 A, Sentinel-1 B)
DOI: 10.6084/m9.figshare.21316554
title: In vivo SERS nanosensor for plant signaling molecules

description: 1. TEM, SEM, CLSM image files 2. raw spectrum txt files 3. extra data for supplementary notes
DOI: 10.6084/m9.figshare.21316554.v3
title: In vivo SERS nanosensor for plant signaling molecules

description: 1. TEM, SEM, CLSM image files 2. raw spectrum txt files 3. extra data for supplementary notes
DOI: 10.5281/zenodo.7193058
title: miR136 regulates proliferation and differentiation of Small Tail Han sheep preadipocytes

description: The data that support the findings of this study are available from the corresponding author upon reasonable request.
DOI: 10.5281/zenodo.7193057
title: miR136 regulates proliferation and differentiation of Small Tail Han sheep preadipocytes

description: The data that support the findings of this study are available from the corresponding author upon reasonable request.
DOI: 10.5519/qd.l9xj5a1s
title: Query on the Natural History Museum Data Portal (data.nhm.ac.uk) (7566 records)
DOI: 10.5281/zenodo.7193128
title: Supplementary material - Eggerthella lenta DSM 2243 alleviates bile acid stress response in Clostridium ramosum and Anaerostipes caccae by transformation of bile acids

description: The word document is a collection of supplementary figures and tables. <br> The excel file is a collection of raw data from experiments.
DOI: 10.5281/zenodo.6922193
title: Supplementary material - Eggerthella lenta DSM 2243 alleviates bile acid stress response in Clostridium ramosum and Anaerostipes caccae by transformation of bile acids

description: The word document is a collection of supplementary figures and tables. <br> The excel file is a collection of raw data from experiments.
DOI: 10.5281/zenodo.7193150
title: Supplementary material - Eggerthella lenta DSM 2243 alleviates bile acid stress response in Clostridium ramosum and Anaerostipes caccae by transformation of bile acids

description: The word document is a collection of supplementary figures and tables. <br> The excel file is a collection of raw data from experiments.
DOI: 10.5281/zenodo.7129499
title: Supplementary material - Eggerthella lenta DSM 2243 alleviates bile acid stress response in Clostridium ramosum and Anaerostipes caccae by transformation of bile acids

description: The word document is a collection of supplementary figures and tables. <br> The excel file is a collection of raw data from experiments.
DOI: 10.6084/m9.figshare.21324093.v1
title: diols data.xlsx

description: LCDs in SPM of the ECS
DOI: 10.48512/xcv8470845
title: Raw Data.xlsx

description: add description
DOI: 10.5517/ccdc.csd.cc2byn76
title: CCDC 2173448: Experimental Crystal Structure Determination

description: Related Article: Hyo Seon Sim, Hari Datta Khanal, Yong Rok Lee|2022|J.Org.Chem.|87|12890|doi:10.1021/acs.joc.2c01459
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.cc2byndc
title: CCDC 2173453: Experimental Crystal Structure Determination

description: Related Article: Hyo Seon Sim, Hari Datta Khanal, Yong Rok Lee|2022|J.Org.Chem.|87|12890|doi:10.1021/acs.joc.2c01459
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.cc2c08d2
title: CCDC 2175003: Experimental Crystal Structure Determination

description: Related Article: Ananya Dutta, Masilamani Jeganmohan|2022|J.Org.Chem.|87|13154|doi:10.1021/acs.joc.2c01625
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.