Molecular basis of UHRF1 allosteric activation for synergistic histone modification binding by PI5P
Molecular basis of UHRF1 allosteric activation for synergistic histone modification binding by PI5P
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Chromatin marks are recognized by distinct binding modules many of which are embedded in multidomain proteins or complexes. How the different protein functionalities of complex chromatin modulators are regulated is often unclear. Using a combination of biochemical, biophysical and structural approaches we delineated the regulation of the H3unmodifi...
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Full title
Molecular basis of UHRF1 allosteric activation for synergistic histone modification binding by PI5P
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TN_cdi_proquest_journals_2557923175
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2557923175
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E-ISSN
2692-8205
DOI
10.1101/2021.08.04.455045
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https://www.proquest.com/docview/2557923175?pq-origsite=primo&accountid=13902
