Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.

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Evaluating the effect of mutations and ligand binding on transthyretin homotetramer dynamics.

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2017 nî lūn-bûn

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2017年の論文

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2017年論文

@yue

2017年論文

@zh-hant

2017年論文

@zh-hk

2017年論文

@zh-mo

2017年論文

@zh-tw

2017年论文

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2017年论文

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2017年论文

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Evaluating the effect of mutat ...... hyretin homotetramer dynamics.

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Evaluating the effect of mutat ...... hyretin homotetramer dynamics.

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Evaluating the effect of mutat ...... hyretin homotetramer dynamics.

@en

P1476

Evaluating the effect of mutat ...... thyretin homotetramer dynamics

@en

P2093

Giuseppe Zanotti

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P2860

Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors

The FoldX web server: an online force field

Fibril in senile systemic amyloidosis is derived from normal transthyretin

Rational design of potent human transthyretin amyloid disease inhibitors

A comparative analysis of 23 structures of the amyloidogenic protein transthyretin

Diflunisal analogues stabilize the native state of transthyretin. Potent inhibition of amyloidogenesis

Amyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSES

A Substructure Combination Strategy To Create Potent and Selective Transthyretin Kinetic Stabilizers That Prevent Amyloidogenesis and Cytotoxicity

Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding

Tafamidis, a potent and selective transthyretin kinetic stabilizer that inhibits the amyloid cascade

P304

e0181019

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P31

scholarly article

P356

10.1371/JOURNAL.PONE.0181019

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P407

English

P433

http://www.w3.org/2001/XMLSchema#string

P478

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P50

Gustavo Parisi

Tadeo E Saldaño

Sebastian Fernandez-Alberti

P577

2017-07-13T00:00:00Z

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P698

28704493

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P921

ligand binding

P932

5509292

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