An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and...
An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering
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England: eLife Sciences Publications Ltd
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English
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England: eLife Sciences Publications Ltd
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Allostery is an inherent feature of proteins, but it remains challenging to reveal the mechanisms by which allosteric signals propagate. A clearer understanding of this intrinsic circuitry would afford new opportunities to modulate protein function. Here, we have identified allosteric sites in protein tyrosine phosphatase 1B (PTP1B) by combining mu...
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An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering
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TN_cdi_doaj_primary_oai_doaj_org_article_f31e59e6c613444c8e3b921c3cf0906f
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_f31e59e6c613444c8e3b921c3cf0906f
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ISSN
2050-084X
E-ISSN
2050-084X
DOI
10.7554/eLife.36307
