Human transthyretin binding affinity of halogenated thiophenols and halogenated phenols: An in vitro and in silico study.
Sign Up to like & getrecommendations! Published in 2021 at "Chemosphere"
DOI: 10.1016/j.chemosphere.2021.130627
Abstract: Serious harmful effects have been reported for thiophenols, which are widely used industrial materials. To date, little information is available on whether such chemicals can elicit endocrine-related detrimental effects. Herein the potential binding affinity and… read more here.
Keywords: affinity halogenated; halogenated thiophenols; human transthyretin; thiophenols halogenated ... See more keywords
Rapid Screening of Human Transthyretin Disruptors through a Tiered in Silico Approach
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DOI: 10.1021/acssuschemeng.1c00680
Abstract: In silico models have been considered as a promising tool that can be used to screen and identify potential endocrine disrupting chemicals (EDCs) effectively and assist finally realizing the sustai... read more here.
Keywords: transthyretin disruptors; human transthyretin; tiered silico; rapid screening ... See more keywords
Counter-diffusion studies of human transthyretin: the growth of high-quality crystals for X-ray and neutron crystallography
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DOI: 10.1107/s1600576724011191
Abstract: X-ray and neutron diffraction studies of human transthyretin crystallized using the non-convective counter-diffusion method provide important insights into crystallization quality relevant for the growth of high-quality large-volume crystals suitable for both X-ray and neutron structural… read more here.
Keywords: quality; human transthyretin; growth high; ray neutron ... See more keywords
Structural Analysis of the Complex of Human Transthyretin with 3′,5′-Dichlorophenylanthranilic Acid at 1.5 Å Resolution
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DOI: 10.3390/molecules27217206
Abstract: Human transthyretin (hTTR) can form amyloid deposits that accumulate in nerves and organs, disrupting cellular function. Molecules such as tafamidis that bind to and stabilize the TTR tetramer can reduce such amyloid formation. Here, we… read more here.
Keywords: human transthyretin; analysis complex; structural analysis; resolution ... See more keywords