Evidence map›Paper›PMID 31599700›Full record

ArticleMolecular biology of the cell2019

Multivalent electrostatic microtubule interactions of synthetic peptides are sufficient to mimic advanced MAP-like behavior.

Hauke Drechsler, Yong Xu, Veikko F Geyer, Yixin Zhang, Stefan Diez

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

18 citing papers in PubMed, 36 citations in OpenAlex.

  1. Capillary bundling of microtubules by condensates.bioRxiv : the preprint server for biology · 2026
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  9. Effects ofHuman reproduction open · 2024
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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

5 authors at 2 institutions in 1 country.

Hauke DrechslerB CUBE-Center for Molecular Bioengineering, Technische -Universität -Dresden, Dresden 01307, Germany.
Yong XuB CUBE-Center for Molecular Bioengineering, Technische -Universität -Dresden, Dresden 01307, Germany.
Veikko F GeyerB CUBE-Center for Molecular Bioengineering, Technische -Universität -Dresden, Dresden 01307, Germany.
Yixin ZhangB CUBE-Center for Molecular Bioengineering, Technische -Universität -Dresden, Dresden 01307, Germany.
Stefan DiezB CUBE-Center for Molecular Bioengineering, Technische -Universität -Dresden, Dresden 01307, Germany.
Technische Universität Dresden · DEMax Planck Institute of Molecular Cell Biology and Genetics · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubule-associated proteins (MAPs) are a functionally highly diverse class of proteins that help to adjust the shape and function of the microtubule cytoskeleton in space and time. For this purpose, MAPs structurally support microtubules, modulate their dynamic instability, or regulate the activity of associated molecular motors. The microtubule-binding domains of MAPs are structurally divergent, but often depend on electrostatic interactions with the negatively charged surface of the microtubule. This suggests that the surface exposure of positive charges rather than a certain structural fold is sufficient for a protein to associate with microtubules. Consistently, positively charged artificial objects have been shown to associate with microtubules and to diffuse along their lattice. Natural MAPs, however, show a more sophisticated functionality beyond lattice-diffusion. Here, we asked whether basic electrostatic interactions are sufficient to also support advanced MAP functionality. To test this hypothesis, we studied simple positively charged peptide sequences for the occurrence of typical MAP-like behavior. We found that a multivalent peptide construct featuring four lysine-alanine heptarepeats (starPEG-(KA7)

Indexed as

AlanineAnimalsChemistry Techniques, SyntheticCytoskeletonDiffusionHumansKinesinsLysineMicrotubule-Associated ProteinsMicrotubulesPeptidesPolymerizationProtein BindingStatic ElectricityTubulinAlanineKinesinsLysineMicrotubule-Associated ProteinsPeptidesTubulin

Identifiers

PMID31599700
PMCPMC6857568
OpenAlexW2979535373

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.