cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.5281/zenodo.4650288
title: In silico voltage-sensitive dye imaging reveals the emergent dynamics of cortical populations: figure data

description: Tabular data corresponding to figures 2 through 5 in the 2021 Nature Communcations publication entitled "In silico voltage-sensitive dye imaging reveals the emergent dynamics of cortical populations". Tabular data are provided for each figure in the form of excel spreadsheets, with individual data sheets for each figure sub-panel, where all axis and units are described in the row and column headings. Additionally, the ipython notebooks used to generate the figure data are provided (figure*.ipynb), together with the necessary raw data files (data.zip), supporting libraries (utils.zip), output folder (figures.zip), and requirements (requirements.txt). See README.rtf for detailed information and usage instructions.
DOI: 10.5255/ukda-sn-853524
title: Parent-child Conversation with Digital Personalized Books, 2017-2018

description: This study investigated parent-child reading of books with personalised and non-personalised features. Parents and children were invited to the research laboratory and asked to read a digital book that contained personalised and non-personalised features. There were new words embedded in both sections of the book. We measured whether children will learn more new words as a result of personalisation. We were also interested in potential differences in parent-child interaction around the book.
DOI: 10.5880/sfb806.63
title: CRC806_E1_AUR_Sites_Database_20210331

description: CRC 806 “Our Way to Europe” – Project E1 Population Dynamics: Demographic Changes of Hunter-Gatherer Populations during the Upper Pleistocene and Early Holocene in Europe Principal Investigator: Prof. Dr Andreas Zimmermann PostDoc: Dr Isabell Schmidt Database of georeferenced Aurignacian sites located across western and central Europe. Updated version (March 2021).
DOI: 10.5517/ccdc.csd.cc24q8kq
title: CCDC 1987613: Experimental Crystal Structure Determination

description: Related Article: Raed M. Al-Zoubi, Noor H. Al-Shatnawi, Walid K. Al-Jammal, Abdlateef Ibdah, Mazhar S. Al-Zoubi, Michael J. Ferguson, Ahmad S. Zarour, Aksam A. Yassin, Abdullah A. Ansari|2021|J.Organomet.Chem.|940|121786|doi:10.1016/j.jorganchem.2021.121786
DOI: 10.5281/zenodo.4650359
title: Dataset related to article "hATTR Pathology: Nerve Biopsy Results from Italian Referral Centers"

description: Clinical and pathological data from hATTR patients, diagnosed and followed in our center for hATTR peripheral neuropathy
description: Study supported by Telethon GUP15010F RT38 on ATTRv registry
DOI: 10.5281/zenodo.4650358
title: Dataset related to article "hATTR Pathology: Nerve Biopsy Results from Italian Referral Centers"

description: Clinical and pathological data from hATTR patients, diagnosed and followed in our center for hATTR peripheral neuropathy
description: Study supported by Telethon GUP15010F RT38 on ATTRv registry
DOI: 10.5281/zenodo.4650370
title: Appendix 2 Raw data for CD013155

description: This contains the data used for analysis for the Cochrane review: "Treatment for bleeding oesophageal varices in people with decompensated liver cirrhosis: a network meta-analysis" (DOI: 10.1002/14651858.CD013155)
DOI: 10.5281/zenodo.4288215
title: Appendix 2 Raw data for CD013155

description: This contains the data used for analysis for the Cochrane review: "Treatment for bleeding oesophageal varices in people with decompensated liver cirrhosis: a network meta-analysis" (DOI: 10.1002/14651858.CD013155)
DOI: 10.5281/zenodo.4650369
title: Dataset related to Article"Pregnancy in Charcot-Marie-Tooth disease: Data from the Italian CMT national registry"

description: Data from the Italian CMT registry and questionnaire on CMT and pregnancy.
description: Study supported by Telethon-Italy Foundation - Grant GUP13006
DOI: 10.5281/zenodo.4650368
title: Dataset related to Article"Pregnancy in Charcot-Marie-Tooth disease: Data from the Italian CMT national registry"

description: Data from the Italian CMT registry and questionnaire on CMT and pregnancy.
description: Study supported by Telethon-Italy Foundation - Grant GUP13006
DOI: 10.34808/fh3c-c731
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC3-MAG1-ROP1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens MIC3, MAG1 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 67-359 of the MIC3 antigen, 30-452 of the MAG1 antigen, 85-396 of the ROP1 antigen; B) 67-359 of the MIC3 antigen, 30-222 of the MAG1 antigen, 85-396 of the ROP1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/f9bt-cj52
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC3-MAG1-AMA1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens MIC3, MAG1 and AMA1. The produced and purified proteins are composed of amino acid residues from:  A) 67-359 of the MIC3 antigen, 30-452 of the MAG1 antigen, 67-483 of the AMA1 antigen; B) 67-359 of the MIC3 antigen, 30-222 of the MAG1 antigen, 67-483 of the AMA1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34840/4x3t-eq54
title: Morbidity and Mortality of Domestic Rabbits (Oryctolagus cuniculus) Under Primary Veterinary Care in England in 2013
DOI: 10.34808/txf2-0a91
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MAG1-AMA1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens MIC1, MAG1 and AMA1. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-483 of the AMA1 antigen; B) 25-456 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-483 of the AMA1 antigen; C) 25-456 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-483 of the AMA1 antigen; D) 25-182 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-483 of the AMA1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/p93s-ke37
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MAG1-MIC3

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens MIC1, MAG1 and MIC3. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-359 of the MIC3 antigen; B) 25-456 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-359 of the MIC3 antigen; C) 25-456 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-359 of the MIC3 antigen; D) 25-182 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-359 of the MIC3 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/7k1n-eq81
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MAG1-ROP1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens MIC1, MAG1 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 30-452 of the MAG1 antigen, 85-396 of the ROP1 antigen; B) 25-456 of the MIC1 antigen, 30-452 of the MAG1 antigen, 85-396 of the ROP1 antigen; C) 25-456 of the MIC1 antigen, 30-222 of the MAG1 antigen, 85-396 of the ROP1 antigen; D) 25-182 of the MIC1 antigen, 30-222 of the MAG1 antigen, 85-396 of the ROP1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/vf84-z096
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MIC3-ROP1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens MIC1, MIC3 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 67-359 of the MIC3 antigen, 85-396 of the ROP1 antigen; B) 25-456 of the MIC1 antigen, 67-359 of the MIC3 antigen, 85-396 of the ROP1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/3g4c-gs78
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen AMA1-MIC1-ROP1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens AMA1, MIC1 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 67-483 of the AMA1 antigen, 25-182 of the MIC1 antigen, 85-396 of the ROP1 antigen; B) 67-483 of the AMA1 antigen, 25-456 of the MIC1 antigen, 85-396 of the ROP1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/ne29-2r07
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen AMA1-MIC1-MIC3

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens AMA1, MIC1 and MIC3. The produced and purified proteins are composed of amino acid residues from:  A) 67-483 of the AMA1 antigen, 25-182 of the MIC1 antigen, 67-359 of the MIC3 antigen; B) 67-483 of the AMA1 antigen, 25-456 of the MIC1 antigen, 67-359 of the MIC3 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/jeee-vr46
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-GRA9

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and GRA9. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 21-318 of the GRA9 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/gc7v-yy93
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-GRA7

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and GRA7. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 18-236 of the GRA7 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.