PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31282646-5	2019	Combining experimental and computational approaches, we demonstrated the anti-amyloidogenic effect of naphthoquinone-tryptophan-based hybrid molecules toward PHF6 (tau-derived aggregative peptide), Amyloid beta (Abeta42), and human islet amyloid polypeptide (hIAPP) implicated in AD and T2DM, respectively.	Naphthoquinones	102-116	PHD finger protein 6	Homo sapiens	158-162	
29311706-0	2018	Mechanistic insights into remodeled Tau-derived PHF6 peptide fibrils by Naphthoquinone-Tryptophan hybrids.	Naphthoquinones	72-86	PHD finger protein 6	Homo sapiens	48-52	
29311706-3	2018	In the present study, we show that Naphthoquinone-Tryptophan hybrids, i.e., NQTrp and Cl-NQTrp significantly disrupted the pre-formed fibrillar aggregates of Tau-derived PHF6 (VQIVYK) peptide and full-length tau protein in vitro, in a dose-dependent manner as evident from ThS assay, CD spectroscopy, and TEM.	Naphthoquinones	35-49	PHD finger protein 6	Homo sapiens	170-174	
29311706-4	2018	Molecular dynamics simulation of PHF6 oligomers and fibrils with the Naphthoquinone-Tryptophan hybrids provides a possible structure-function based mechanism-of-action, highlighting the role of hydrophobic interaction and hydrogen bond formation during fibril disassembly.	Naphthoquinones	69-83	PHD finger protein 6	Homo sapiens	33-37