Evidence map›Paper›PMID 39340452›Full record

ArticleLangmuir : the ACS journal of surfaces and colloids2024

Mixtures of Intrinsically Disordered Neuronal Protein Tau and Anionic Liposomes Reveal Distinct Anionic Liposome-Tau Complexes Coexisting with Tau Liquid-Liquid Phase-Separated Coacervates.

Christine Tchounwou, Anjali J Jobanputra, Dylan Lasher, Bretton J Fletcher, Jorge Jacinto, Arjun Bhaduri, Rebecca L Best, William S Fisher, Kai K Ewert, Youli Li and 2 more

Abstract read
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In one paragraph

Article in Langmuir : the ACS journal of surfaces and colloids, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors.

Christine TchounwouMaterials Department, University of California, Santa Barbara, California 93106, United States.
Anjali J JobanputraMaterials Department, University of California, Santa Barbara, California 93106, United States.
Dylan LasherMaterials Department, University of California, Santa Barbara, California 93106, United States.
Bretton J FletcherMaterials Department, University of California, Santa Barbara, California 93106, United States.
Jorge JacintoMaterials Department, University of California, Santa Barbara, California 93106, United States.ORCID 0009-0005-1796-9779
Arjun BhaduriMaterials Department, University of California, Santa Barbara, California 93106, United States.
Rebecca L BestMolecular, Cellular, and Developmental Biology Department, University of California, Santa Barbara, California 93106, United States.
William S FisherMaterials Department, University of California, Santa Barbara, California 93106, United States.ORCID 0000-0002-7493-1567
Kai K EwertMaterials Department, University of California, Santa Barbara, California 93106, United States.ORCID 0000-0002-4861-8278
Youli LiMaterials Research Laboratory, University of California, Santa Barbara, California 93106, United States.ORCID 0000-0001-5117-3874
Stuart C FeinsteinMolecular, Cellular, and Developmental Biology Department, University of California, Santa Barbara, California 93106, United States.
Cyrus R SafinyaMaterials Department, University of California, Santa Barbara, California 93106, United States.ORCID 0000-0002-3295-7128

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau, an intrinsically disordered neuronal protein and polyampholyte with an overall positive charge, is a microtubule (MT) associated protein that binds to anionic domains of MTs and suppresses their dynamic instability. Aberrant tau-MT interactions are implicated in Alzheimer's and other neurodegenerative diseases. Here, we studied the interactions between full-length human protein tau and other negatively charged binding substrates, as revealed by differential interference contrast (DIC) and fluorescence microscopy. As a binding substrate, we chose anionic liposomes (ALs) containing either 1,2-dioleoyl-

Indexed as

AnionsLiposomestau ProteinsHumansIntrinsically Disordered ProteinsPhosphatidylcholinesPhosphatidylglycerolsPhosphatidylserines1,2-dioleoylphosphatidylserine1,2-dioleoyl-sn-glycero-3-phosphoglycerol1,2-oleoylphosphatidylcholineAnionsIntrinsically Disordered ProteinsLiposomesPhosphatidylcholinesPhosphatidylglycerolsPhosphatidylserinestau Proteins

Identifiers

PMID39340452

What OpenQuestion holds

Textmetadata
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.