cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5281/zenodo.4692673
title: Dataset for the ERT principles

description: The dataset is an examination of the five principles (simplicity, accessibility, affordability, flexibility, and empathy) in emergency remote teaching (ERT) among Indonesian undergraduate students. This data is an updated version of the previous data https://doi.org/10.5281/zenodo.4661610
description: The school name, email, and ID are eliminated as per ethical approval.
DOI: 10.25345/c55j77
title: MassIVE MSV000087212 - Bothrops moojeni Metalloprotease I (BmooMP-I) digested (trypsin)
title: Mass Spectrometry with theoretical database. Tryptic digests of the samples were solubilized in 0.1% (v/v) formic acid (solution A) and subjected to nano-ESI-LCMS/MS analysis, using an Ultimate 3000 HPLC (Dionex), coupled to a Q Exactive Orbitrap TM mass spectrometer (Thermo Fisher Scientific). Peptides were loaded on a Trap Column with nanoViper Fitting (P/N 164649, C18, 5 mm x 30 um, Thermo Fisher Scientific) and eluted at a flow rate of 300 nL/min using an isocratic gradient of 4% solution B (100% (v/v) acetonitrile containing 0.1% (v/v) formic acid) for 3 minutes. Thereafter, peptides were loaded on a C18 PicoChip column (Reprosil-Pur, C18-AQ, 3 um, 120 A, 105mm, New Objective, Woburn, MA, USA) using a segmented concentration gradient from 4-55% B for 30 min, 55-90% B for 1 min, 90% B over 5 min and then returning to 4% B over 20 min at a flow rate of 300 nL/min. Ion polarity was set to positive ionization mode using data-dependent acquisition (DDA) mode. Mass spectra were acquired with a scan range of m/z 200-2000, resolution of 70,000 and injection time of 100 ms. The fragmentation chamber was conditioned with collision energy between 29 to 35% with a resolution of 17,500, 50 ms of injection time, 4.0 m/z of isolation window and dynamic exclusion of 10s. The spectrometric data were acquired through the Thermo Xcalibur TM software v.4.0.27.19 (Thermo Fisher Scientific). All Raw Data were submitted to the PatternLab software v.4.0.0.84 and searched against the uniprot and SLIDER theoretical database. The following search parameters were used: semi-tryptic cleavage products (two tryptic missed cleavage allowed), carbamidomethylation of cysteine as fixed modification and oxidation of methionine as variable modification. Parent mass tolerance error was set at 40 ppm and fragment mass error at 0.02 ppm. Protein identifications were considered with a minimum of one fragment ion per peptide, five fragment ions per protein, two peptides per protein and a false discovery identification rate set to 1%, estimated by a simultaneous search against a reversed database.
DOI: 10.25345/c51v5b
title: MassIVE MSV000087213 - Lysozyme from Gallus gallus digested (trypsin)
title: Mass Spectrometry with theoretical database. Tryptic digests of the samples were solubilized in 0.1% (v/v) formic acid (solution A) and subjected to nano-ESI-LCMS/MS analysis, using an Ultimate 3000 HPLC (Dionex), coupled to a Q Exactive Orbitrap TM mass spectrometer (Thermo Fisher Scientific). Peptides were loaded on a Trap Column with nanoViper Fitting (P/N 164649, C18, 5 mm x 30 um, Thermo Fisher Scientific) and eluted at a flow rate of 300 nL/min using an isocratic gradient of 4% solution B (100% (v/v) acetonitrile containing 0.1% (v/v) formic acid) for 3 minutes. Thereafter, peptides were loaded on a C18 PicoChip column (Reprosil-Pur, C18-AQ, 3 um, 120 A, 105mm, New Objective, Woburn, MA, USA) using a segmented concentration gradient from 4-55% B for 30 min, 55-90% B for 1 min, 90% B over 5 min and then returning to 4% B over 20 min at a flow rate of 300 nL/min. Ion polarity was set to positive ionization mode using data-dependent acquisition (DDA) mode. Mass spectra were acquired with a scan range of m/z 200-2000, resolution of 70,000 and injection time of 100 ms. The fragmentation chamber was conditioned with collision energy between 29 to 35% with a resolution of 17,500, 50 ms of injection time, 4.0 m/z of isolation window and dynamic exclusion of 10s. The spectrometric data were acquired through the Thermo Xcalibur TM software v.4.0.27.19 (Thermo Fisher Scientific). All Raw Data were submitted to the PatternLab software v.4.0.0.84 and searched against the uniprot and SLIDER theoretical database. The following search parameters were used: semi-tryptic cleavage products (two tryptic missed cleavage allowed), carbamidomethylation of cysteine as fixed modification and oxidation of methionine as variable modification. Parent mass tolerance error was set at 40 ppm and fragment mass error at 0.02 ppm. Protein identifications were considered with a minimum of one fragment ion per peptide, five fragment ions per protein, two peptides per protein and a false discovery identification rate set to 1%, estimated by a simultaneous search against a reversed database.
DOI: 10.25345/c5x22b
title: MassIVE MSV000087214 - Crotoxin from Crotalus durissus collilineatus digested (trypsin)
title: Mass Spectrometry with theoretical database. Tryptic digests of the samples were solubilized in 0.1% (v/v) formic acid (solution A) and subjected to nano-ESI-LCMS/MS analysis, using an Ultimate 3000 HPLC (Dionex), coupled to a Q Exactive Orbitrap TM mass spectrometer (Thermo Fisher Scientific). Peptides were loaded on a Trap Column with nanoViper Fitting (P/N 164649, C18, 5 mm x 30 um, Thermo Fisher Scientific) and eluted at a flow rate of 300 nL/min using an isocratic gradient of 4% solution B (100% (v/v) acetonitrile containing 0.1% (v/v) formic acid) for 3 minutes. Thereafter, peptides were loaded on a C18 PicoChip column (Reprosil-Pur, C18-AQ, 3 um, 120 A, 105mm, New Objective, Woburn, MA, USA) using a segmented concentration gradient from 4-55% B for 30 min, 55-90% B for 1 min, 90% B over 5 min and then returning to 4% B over 20 min at a flow rate of 300 nL/min. Ion polarity was set to positive ionization mode using data-dependent acquisition (DDA) mode. Mass spectra were acquired with a scan range of m/z 200-2000, resolution of 70,000 and injection time of 100 ms. The fragmentation chamber was conditioned with collision energy between 29 to 35% with a resolution of 17,500, 50 ms of injection time, 4.0 m/z of isolation window and dynamic exclusion of 10s. The spectrometric data were acquired through the Thermo Xcalibur TM software v.4.0.27.19 (Thermo Fisher Scientific). All Raw Data were submitted to the PatternLab software v.4.0.0.84 and searched against the uniprot and SLIDER theoretical database. The following search parameters were used: semi-tryptic cleavage products (two tryptic missed cleavage allowed), carbamidomethylation of cysteine as fixed modification and oxidation of methionine as variable modification. Parent mass tolerance error was set at 40 ppm and fragment mass error at 0.02 ppm. Protein identifications were considered with a minimum of one fragment ion per peptide, five fragment ions per protein, two peptides per protein and a false discovery identification rate set to 1%, estimated by a simultaneous search against a reversed database.
DOI: 10.5063/sf2tkc
title: PMBA-A4-GERAL: Monitoramento de Potenciais Impactos do Rejeito de Minério de Ferro na Praia e Antepraia Adjacentes da Desembocadura do Rio Doce

description: Em 5 de novembro de 2015 o rompimento da barragem de rejeitos de minério de ferro na localidade de Mariana (MG) despejou cerca de 50x106m3 de areia e lama na zona costeira do Espírito Santo, sendo aproximadamente 16x106m3 no sistema fluvial/estuarino. O evento deslocou o volume de contaminantes ao longo de quase 700 km até à foz do Rio Doce na localidade de Regência (ES) e na plataforma continental adjacente. Em 7 de dezembro, a pluma de material em suspensão se espalhou ao longo da costa em quase 80 km, sendo 57 km para o norte e 17,5 km para o sul, além de 18 km costa-à-fora, conforme dados do IBAMA publicados no G1 na edição de dezembro de 2015. A possibilidade de contaminação das areias das praias adjacentes levou à retirada e relocação de ninhos de tartaruga para outras praias e, ainda, à proibição de banho de mar, prejudicando as atividades econômicas e recreacionais da região costeira. Neste sentido, a segurança ao banho/balneabilidade do litoral atingido e a fauna associada ao sistema praial necessitam ser avaliadas para que respostas sejam o mais prontamente dadas à sociedade. Através de estudos e monitoramento praial de curto e longo prazo, busca-se obter respostas para as seguintes questões: -Qual o alcance máximo dos contaminantes ao longo da costa? -Qual seu deslocamento ao longo do tempo? -Quais os processos morfodinâmicos envolvidos na distribuição dos contaminantes? -Existe a possibilidade de os contaminantes atingirem a berma alta da praia e a costa e, em caso afirmativo, em que condições de energia de onda? -Qual a resiliência do sistema praia-antepraia para neutralizar a ação dos contaminantes ao longo do tempo nos sedimentos e na fauna bentônica? O objetivo geral do projeto é avaliar as condições ambientais dos ecossistemas, a distribuição espacial e a magnitude dos impactos e as consequências sobre as atividades ecológicas e econômicas do litoral.
DOI: 10.6084/m9.figshare.14428952
title: Discriminating cytologically indeterminate thyroid nodules using FLIM of o-BMVC foci of fine-needle aspiration biopsies

description: Supplemental data from: Discriminating cytologically indeterminate thyroid nodules using FLIM of o-BMVC foci of fine-needle aspiration biopsies.<br>
DOI: 10.6084/m9.figshare.14428952.v2
title: Discriminating cytologically indeterminate thyroid nodules using FLIM of o-BMVC foci of fine-needle aspiration biopsies

description: Supplemental data from: Discriminating cytologically indeterminate thyroid nodules using FLIM of o-BMVC foci of fine-needle aspiration biopsies.<br>
DOI: 10.6084/m9.figshare.14428952.v1
title: Discriminating cytologically indeterminate thyroid nodules using FLIM of o-BMVC foci of fine-needle aspiration biopsies

description: Supplemental data from: Discriminating cytologically indeterminate thyroid nodules using FLIM of o-BMVC foci of fine-needle aspiration biopsies.<br>
DOI: 10.3886/e137721v1
title: Muslim conquest and institutional formation

description: Replication data and stata do file for "Muslim conquest and institutional formation"
DOI: 10.3886/e137721
title: Muslim conquest and institutional formation

description: Replication data and stata do file for "Muslim conquest and institutional formation" (published in Explorations in Economic History)
DOI: 10.3886/e137721v2
title: Muslim conquest and institutional formation

description: Replication data and stata do file for "Muslim conquest and institutional formation" (published in Explorations in Economic History)
DOI: 10.5517/ccdc.csd.cc26p031
title: CCDC 2045972: Experimental Crystal Structure Determination

description: Related Article: Toolika Agrawal, Robert T. Martin, Stephen Collins, Zachary Wilhelm, Mytia D. Edwards, Osvaldo Gutierrez, Joshua D. Sieber|2021|J.Org.Chem.|86|5026|doi:10.1021/acs.joc.0c02971
DOI: 10.5517/ccdc.csd.cc26qv71
title: CCDC 2047743: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qv82
title: CCDC 2047744: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qv93
title: CCDC 2047745: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvb4
title: CCDC 2047746: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvc5
title: CCDC 2047747: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvd6
title: CCDC 2047748: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvf7
title: CCDC 2047749: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvg8
title: CCDC 2047750: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvh9
title: CCDC 2047751: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvjb
title: CCDC 2047752: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvkc
title: CCDC 2047753: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvld
title: CCDC 2047754: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvmf
title: CCDC 2047755: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvph
title: CCDC 2047757: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvqj
title: CCDC 2047758: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.5517/ccdc.csd.cc26qvrk
title: CCDC 2047759: Experimental Crystal Structure Determination

description: Related Article: Michael S. Gruhne, Marcus Lommel, Maximilian H. H. Wurzenberger, Thomas M. Klapötke, Jörg Stierstorfer|2021|Inorg.Chem.|60|4816|doi:10.1021/acs.inorgchem.0c03752
DOI: 10.6084/m9.figshare.13670839
title: eFun Performance Data Study1 and 2

description: This dataset includes performance scores for the eFun app testing working memory, inhibition, and cognitive flexibility in primary school children. Students were tested twice (see study 1 and study 2).<br><b>Glossary:</b>ST= StudyWM = Working MemoryINHIB = InhibitionCF = Cognitive FlexibilityQ = Question
DOI: 10.6084/m9.figshare.13670839.v3
title: eFun Performance Data Study1 and 2

description: This dataset includes performance scores for the eFun app testing working memory, inhibition, and cognitive flexibility in primary school children. Students were tested twice (see study 1 and study 2).<br><b>Glossary:</b>ST= StudyWM = Working MemoryINHIB = InhibitionCF = Cognitive FlexibilityQ = Question
DOI: 10.6084/m9.figshare.13670839.v2
title: eFun Performance Data Study1 and 2

description: This dataset includes performance scores for the eFun app testing working memory, inhibition, and cognitive flexibility in primary school children. Students were tested twice (see study 1 and study 2).<br><b>Glossary:</b>ST= StudyWM = Working MemoryINHIB = InhibitionCF = Cognitive FlexibilityQ = Question
DOI: 10.6084/m9.figshare.13670842
title: Questionnaire data for eFun study 1 and 2

description: This dataset includes questionnaire data for the eFun app testing working memory, inhibition, and cognitive flexibility in primary school children. Students were tested twice (see study 1 and study 2).<br><b>Glossary:</b><br>ST= StudyWM = Working MemoryINHIB = InhibitionCF = Cognitive FlexibilityQ = Question<br>Q1= EnjoyQ2= FunQ3= ExcitingQ4= Too hardQ5= Too easyQ6= BoringQ7= Frustrating<br>
DOI: 10.6084/m9.figshare.13670842.v4
title: Questionnaire data for eFun study 1 and 2

description: This dataset includes questionnaire data for the eFun app testing working memory, inhibition, and cognitive flexibility in primary school children. Students were tested twice (see study 1 and study 2).<br><b>Glossary:</b><br>ST= StudyWM = Working MemoryINHIB = InhibitionCF = Cognitive FlexibilityQ = Question<br>Q1= EnjoyQ2= FunQ3= ExcitingQ4= Too hardQ5= Too easyQ6= BoringQ7= Frustrating<br>
DOI: 10.6084/m9.figshare.13670842.v3
title: Questionnaire data for eFun study 1 and 2

description: This dataset includes questionnaire data for the eFun app testing working memory, inhibition, and cognitive flexibility in primary school children. Students were tested twice (see study 1 and study 2).<br><b>Glossary:</b><br>ST= StudyWM = Working MemoryINHIB = InhibitionCF = Cognitive FlexibilityQ = Question<br>Q1= EnjoyQ2= FunQ3= ExcitingQ4= Too hardQ5= Too easyQ6= BoringQ7= Frustrating<br>
DOI: 10.6084/m9.figshare.14428991
title: Recipe 1

description: Selection of model inputs outputs used for running recipe 1.
DOI: 10.6084/m9.figshare.14428991.v1
title: Recipe 1

description: Selection of model inputs outputs used for running recipe 1.
DOI: 10.6084/m9.figshare.14429029
title: Additional file 1 of Correlation between the spatial distribution and colony size was common for monogenetic bacteria in laboratory conditions

description: Additional file 1: Table S1. Data used for the boxplots. Table S2. Data of temporal changes in colony size and Voronoi correlation.
DOI: 10.6084/m9.figshare.14429033
title: Additional file 2 of Construction autophagy-related prognostic risk signature combined with clinicopathological validation analysis for survival prediction of kidney renal papillary cell carcinoma patients

description: Additional file 2.
DOI: 10.6084/m9.figshare.14429033.v1
title: Additional file 2 of Construction autophagy-related prognostic risk signature combined with clinicopathological validation analysis for survival prediction of kidney renal papillary cell carcinoma patients

description: Additional file 2.
DOI: 10.6084/m9.figshare.14429036
title: Additional file 3 of Construction autophagy-related prognostic risk signature combined with clinicopathological validation analysis for survival prediction of kidney renal papillary cell carcinoma patients

description: Additional file 3.
DOI: 10.6084/m9.figshare.14429036.v1
title: Additional file 3 of Construction autophagy-related prognostic risk signature combined with clinicopathological validation analysis for survival prediction of kidney renal papillary cell carcinoma patients

description: Additional file 3.
DOI: 10.6084/m9.figshare.14429006
title: ArimaMedTempGlobal.spv

description: <b>SPSS Statistics Output Document. Introdução e processamento de dados do modelo de série temporal ARIMA (1,0,1).</b>
DOI: 10.6084/m9.figshare.14429006.v1
title: ArimaMedTempGlobal.spv

description: <b>SPSS Statistics Output Document. Introdução e processamento de dados do modelo de série temporal ARIMA (1,0,1).</b>
DOI: 10.6084/m9.figshare.14429093
title: Additional file 1 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 1: Table S1. Spreadsheet with a list of E. nipponicum transcripts with nucleotide and amino acid sequences and their lengths, sequence completeness, and information about the presence of signal peptide.
DOI: 10.6084/m9.figshare.14429093.v1
title: Additional file 1 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 1: Table S1. Spreadsheet with a list of E. nipponicum transcripts with nucleotide and amino acid sequences and their lengths, sequence completeness, and information about the presence of signal peptide.
DOI: 10.6084/m9.figshare.14429096
title: Additional file 2 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 2: Table S2. Spreadsheet representing and summarising all results from the annotation of the E. nipponicum transcriptome (outputs of BLAST analyses), including outputs of KASS and InterPro functional analyses, GO terms, and TPM values.
DOI: 10.6084/m9.figshare.14429096.v1
title: Additional file 2 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 2: Table S2. Spreadsheet representing and summarising all results from the annotation of the E. nipponicum transcriptome (outputs of BLAST analyses), including outputs of KASS and InterPro functional analyses, GO terms, and TPM values.
DOI: 10.6084/m9.figshare.14429099.v1
title: Additional file 3 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 3: Table S3. Spreadsheet presenting the most abundant E. nipponicum transcripts quantified by TPM value.
DOI: 10.6084/m9.figshare.14429102.v1
title: Additional file 4 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 4: Table S4. Spreadsheet with a list of observed E. nipponicum GO terms. Each GO term is described (annotated), sorted into one of three main categories, and quantified by the sum of TPM values and the number of included transcripts and the ratio between the TPM value and the number of transcripts.
DOI: 10.6084/m9.figshare.14429099
title: Additional file 3 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 3: Table S3. Spreadsheet presenting the most abundant E. nipponicum transcripts quantified by TPM value.
DOI: 10.6084/m9.figshare.14429102
title: Additional file 4 of Eudiplozoon nipponicum (Monogenea, Diplozoidae) and its adaptation to haematophagy as revealed by transcriptome and secretome profiling

description: Additional file 4: Table S4. Spreadsheet with a list of observed E. nipponicum GO terms. Each GO term is described (annotated), sorted into one of three main categories, and quantified by the sum of TPM values and the number of included transcripts and the ratio between the TPM value and the number of transcripts.