Evidence map›Paper›PMID 31896752›Full record

ArticleNature communications2020

Direct observation of dynamic protein interactions involving human microtubules using solid-state NMR spectroscopy.

Yanzhang Luo, ShengQi Xiang, Peter Jan Hooikaas, Laura van Bezouwen, A S Jijumon, Carsten Janke, Friedrich Förster, Anna Akhmanova, Marc Baldus

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

9 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  4. Journal of biomolecular NMR · 2023
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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 at 3 institutions in 3 countries.

Yanzhang LuoNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0001-9149-2423
ShengQi XiangNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-6874-4925
Peter Jan HooikaasCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0001-9849-9193
Laura van BezouwenCryo-Electron Microscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
A S JijumonInstitut Curie, PSL Research University, CNRS UMR3348, F-91405, Orsay, France.ORCID http://orcid.org/0000-0001-8522-3438
Carsten JankeInstitut Curie, PSL Research University, CNRS UMR3348, F-91405, Orsay, France.ORCID http://orcid.org/0000-0001-7053-2000
Friedrich FörsterCryo-Electron Microscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.ORCID http://orcid.org/0000-0002-6044-2746
Anna AkhmanovaCell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands. a.akhmanova@uu.nl.ORCID http://orcid.org/0000-0002-9048-8614
Marc BaldusNMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands. m.baldus@uu.nl.ORCID http://orcid.org/0000-0001-7068-5613
Utrecht University · NLUniversité Paris-Sud · FRUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microtubules are important components of the eukaryotic cytoskeleton. Their structural organization is regulated by nucleotide binding and many microtubule-associated proteins (MAPs). While cryo-EM and X-ray crystallography have provided detailed views of interactions between MAPs with the microtubule lattice, little is known about how MAPs and their intrinsically disordered regions interact with the dynamic microtubule surface. NMR carries the potential to directly probe such interactions but so far has been precluded by the low tubulin yield. We present a protocol to produce [

Indexed as

Magnetic Resonance SpectroscopyMicrotubule-Associated ProteinsMicrotubulesBinding SitesCarbon IsotopesHeLa CellsHumansNitrogen IsotopesProtein DomainsTubulinCarbon-13Carbon IsotopesMAP7 protein, humanMicrotubule-Associated ProteinsNitrogen-15Nitrogen IsotopesTubulin

Identifiers

PMID31896752
PMCPMC6940360
OpenAlexW2998029810

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.