Evidence map›Paper›PMID 29744849›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2018

Using Molecular Tweezers to Remodel Abnormal Protein Self-Assembly and Inhibit the Toxicity of Amyloidogenic Proteins.

Ravinder Malik, Jing Di, Gayatri Nair, Aida Attar, Karen Taylor, Edmond Teng, Frank-Gerrit Klärner, Thomas Schrader, Gal Bitan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
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

12 citing papers in PubMed.

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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

9 authors.

Ravinder MalikDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Jing DiDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Gayatri NairDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Aida AttarDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Karen TaylorDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Edmond TengDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA.
Frank-Gerrit KlärnerFaculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Thomas SchraderFaculty of Chemistry, University of Duisburg-Essen, Essen, Germany.
Gal BitanDepartment of Neurology, David Geffen School of Medicine, University of California at Los Angeles, Los Angeles, CA, USA. gbitan@mednet.ucla.edu.

Funding

UCLA ALZHEIMERS DISEASE RESEARCH CENTERP50AG016570 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BREDESEN, DALE E. · 1999 to 2014
$25.9M
Misfolded protein-clearance enhancers for Alzheimer's therapyR01AG050721 · NIA · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BITAN, GAL · 2015 to 2019
$2.0M
NIA NIH HHS P50 AG016570NIA NIH HHS R01 AG050721
6 · The paper itself

Abstract

Molecular tweezers (MTs) are broad-spectrum inhibitors of abnormal protein self-assembly, which act by binding selectively to lysine and arginine residues. Through this unique mechanism of action, MTs inhibit formation of toxic oligomers and aggregates. Their efficacy and safety have been demonstrated in vitro, in cell culture, and in animal models. Here, we discuss the application of MTs in diverse in vitro and in vivo systems, the experimental details, the scope of their use, and the limitations of the approach. We also consider methods for administration of MTs in animal models to measure efficacy, pharmacokinetic, and pharmacodynamic parameters in proteinopathies.

Indexed as

Models, MolecularProtein MultimerizationAmyloidogenic ProteinsAnimalsBlood-Brain BarrierCell LineCells, CulturedHumansMiceMolecular StructureProtein AggregatesProtein Aggregation, PathologicalProteinsAmyloidogenic ProteinsProtein AggregatesProteinsAlzheimer’s diseaseAmyloidAmyloidosisBlood–brain barrierParkinson’s diseaseProtein aggregationProteinopathySynaptic toxicity

Identifiers

PMID29744849
PMCPMC6459406

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Registered trials

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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.