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Q37383520-1083A05C-7FDF-42D9-8F0D-8461A48807DE
Q37383520-1083A05C-7FDF-42D9-8F0D-8461A48807DE
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http://www.wikidata.org/entity/statement/Q37383520-1083A05C-7FDF-42D9-8F0D-8461A48807DE
Large-scale analysis of thermostable, mammalian proteins provides insights into the intrinsically disordered proteome
P2860
Q37383520-1083A05C-7FDF-42D9-8F0D-8461A48807DE
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Statement
http://www.wikidata.org/entity/statement/Q37383520-1083A05C-7FDF-42D9-8F0D-8461A48807DE
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wasDerivedFrom
bb2594f7e778257b7c998c3656a7375a6d631869
P2860
Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.