Raw gel images and datasets related to the SAXS studies accompanying publication: Ciechanowska et al. The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding. bioRxiv 2023.06.28.546842; doi: https://doi.o

A set of raw gel images and datasets related to SAXS studies used in the article: Ciechanowska et al. The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding. bioRxiv 2023.06.28.546842; doi: https://doi.org/10.1101/2023.06.28.546842

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Publication Details

Journal
Zenodo (CERN European Organization for Nuclear Research)
Published
2024-11-19
DOI
https://doi.org/10.5281/zenodo.10953316
Primary Topic
Environmental DNA in Biodiversity Studies
Type
article
Field-Weighted Citation Impact
0.00
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article

Raw gel images and datasets related to the SAXS studies accompanying publication: Ciechanowska et al. The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding. bioRxiv 2023.06.28.546842; doi: https://doi.o

Zenodo (CERN European Organization for Nuclear Research)
Environmental DNA in Biodiversity Studies
article

Raw gel images and datasets related to the SAXS studies accompanying publication: Ciechanowska et al. The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding. bioRxiv 2023.06.28.546842; doi: https://doi.o

article en

Abstract

A set of raw gel images and datasets related to SAXS studies used in the article: Ciechanowska et al. The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding. bioRxiv 2023.06.28.546842; doi: https://doi.org/10.1101/2023.06.28.546842

Zenodo (CERN European Organization for Nuclear Research)
Institute of Bioorganic Chemistry, Polish Academy of Sciences (PL)
Openalex Percentile: Top 57%
Environmental DNA in Biodiversity Studies
DOIOpen Access PDFOpenAlex
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Raw gel images and datasets related to the SAXS studies accompanying publication: Ciechanowska et al. The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding. bioRxiv 2023.06.28.546842; doi: https://doi.o · Zenodo (CERN European Organization for Nuclear Research) (2024) | TGRS Research Map | TGRS