<style face="normal" font="default" size="100%">Folding and aggregation energy landscapes of tethered RRM domains of human TDP-43 are coupled via a metastable molten globule-like oligomer</style>

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<style face="normal" font="default" size="100%">Folding and aggregation energy landscapes of tethered RRM domains of human TDP-43 are coupled via a metastable molten globule-like oligomer</style>

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<style face="normal" font="default" size="100%">Early metastable assembly during the stress-induced formation of worm-like amyloid fibrils of nucleic acid binding domains of TDP-43</style>

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<style face="normal" font="default" size="100%">Electrostatic modulation of intramolecular and intermolecular interactions during the formation of an amyloid-like assembly</style>

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<style face="normal" font="default" size="100%">Multistep molecular mechanism of amyloid-like aggregation of nucleic acid-binding domain of TDP-43</style>

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<style face="normal" font="default" size="100%">Conformational enigma of TDP-43 misfolding in neurodegenerative disorders</style>

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<style face="normal" font="default" size="100%">Pathological mutations D169G and P112H electrostatically aggravate the amyloidogenicity of the functional domain of TDP-43</style>