Evidence map›Paper›PMID 36364032›Full record

ArticleMolecules (Basel, Switzerland)2022

Structural Analysis of the Complex of Human Transthyretin with 3',5'-Dichlorophenylanthranilic Acid at 1.5 Å Resolution.

Vivian Cody, Jia Q Truong, Bruce A Holdsworth, Jessica K Holien, Samantha J Richardson, David K Chalmers, David J Craik

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 47% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Vivian CodyHauptman-Woodward Medical Research Institute, Inc., 700 Ellicot St., Buffalo, NY 14203, USA.
Jia Q TruongSchool of Science, RMIT University, Bundoora, VIC 3083, Australia.
Bruce A HoldsworthSchool of Science, RMIT University, Bundoora, VIC 3083, Australia.
Jessica K HolienSchool of Science, RMIT University, Bundoora, VIC 3083, Australia.
Samantha J RichardsonSchool of Science, RMIT University, Bundoora, VIC 3083, Australia.ORCID 0000-0002-1708-9430
David K ChalmersMonash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia.ORCID 0000-0003-2366-569X
David J CraikInstitute for Molecular Bioscience and Australian Research Council Centre of Excellence for Innovations in Peptide and Protein Science, The University of Queensland, Brisbane, QLD 4072, Australia.ORCID 0000-0003-0007-6796
RMIT University · AUAustralian Research Council · AUHauptman-Woodward Medical Research Institute · USMonash University · AU

Funding

Australian Research Council CE200100012Cass Foundation 9840National Health and Medical Research Council 2009564
6 · The paper itself

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 studied the interaction of VCP-6 (2-((3,5-dichlorophenyl)amino)benzoic acid) with hTTR. VCP-6 binds to hTTR with 5 times the affinity of the cognate ligand, thyroxine (T

Indexed as

AmyloidosisPrealbuminAmyloidAmyloidogenic ProteinsBinding SitesCrystallography, X-RayHalogensHumansModels, MolecularProtein ConformationAmyloidAmyloidogenic ProteinsHalogensPrealbuminbinding affinityhalogen bondinghuman transthyretinmolecular structureTTR

Identifiers

PMID36364032
PMCPMC9659241
OpenAlexW4307553279

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.