Article

ATP emerged to induce protein folding, inhibit aggregation and increase stability

2019-08-20

Abstract excerpt

By NMR characterization of effects of ATP and related molecules on the folding and dynamics of the ALS-causing C71G-PFN1 and nascent hSOD1, we reveal for the first time that ATP has a general capacity in inducing protein folding with the highest efficiency known so far. This capacity was further identified to result from triphosphate, a key intermediate in prebiotic chemistry, which, however, can severely trigger...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 1b3be52c-f6a8-5237-abab-660631dcf882
DOI: 10.1101/739581

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

ATP emerged to induce protein folding, inhibit aggregation and increase stabilityDOI 10.1101/739581Read

ATP enhances at low concentrations but dissolves at high concentrations liquid-liquid phase separation (LLPS) of ALS/FTD-causing FUS.Semantic proximity Read

ATP biphasically modulates LLPS of TDP-43 PLD by specifically binding arginine residues.Semantic proximity Read

Mechanism of nucleic-acid-driven LLPS of TDP-43 PLDSemantic proximity Read

Stabilization and ATP-binding for tandem RRM domains of ALS-causing TDP-43 and hnRNPA1Semantic proximity Read

Structural mechanisms for gating and ion selectivity of the human polyamine transporter ATP13A2Semantic proximity Read

Design principles to tailor Hsp104 therapeuticsSemantic proximity Read

Genetic Code Expansion and Enzymatic Modifications as Accessible Methods for Studying Site-Specific Post-Translational Modifications of Alpha-Synuclein and TauSemantic proximity Read

ATP modulates self-perpetuating conformational conversion generating structurally distinct yeast prion amyloids that limit autocatalytic amplificationSemantic proximity Read

Polyphosphate is a primordial chaperone.Semantic proximity Read

Skd3 (human <i>CLPB</i> ) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutationsSemantic proximity Read

The mitochondrial ADP/ATP carrier: functional and structural studies in the route of elucidating pathophysiological aspects.Semantic proximity Read

Structural mechanisms for gating and ion selectivity of the human polyamine transporter ATP13A2.Semantic proximity Read