Evidence map›Paper›PMID 10449722›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Phosphorylated tau can promote tubulin assembly.

H C Tseng, Q Lu, E Henderson, D J Graves

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

17 citing papers in PubMed, 48 citations in OpenAlex.

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  15. FEZ1/LZTS1 gene at 8p22 suppresses cancer cell growth and regulates mitosis.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  16. Article
  17. Pregnenolone binds to microtubule-associated protein 2 and stimulates microtubule assembly.Proceedings of the National Academy of Sciences of the United States of America · 2000
    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

4 authors at 1 institution in 1 country.

H C TsengNeuroscience Program, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011, USA.
Q Lu
E Henderson
D J Graves
Iowa State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation can affect the function of microtubule-associated protein tau. Here, the human brain tau with 441 amino acids was phosphorylated by cyclic-AMP-dependent protein kinase (PKA) or glycogen synthase kinase-3beta. PKA-phosphorylated tau (2.7 mol phosphates/mol) does not promote tubulin assembly as judged by spectrophotometric and atomic force microscopy measurements, unless trimethylamine N-oxide (TMAO), a natural occurring osmolyte, is included in these assays. TMAO is also found to promote tubulin assembly of glycogen synthase kinase-3beta-phosphorylated tau (1.6 mol phosphates/mol). TMAO does not act by causing a chemical dephosphorylation of phosphorylated tau, but it acts to overcome the functional deficit caused by phosphorylation. PKA-phosphorylated tau binds to tubulin in the presence of TMAO and lowers the critical concentration of tubulin needed for assembly. From these data, we conclude that PKA-phosphorylated tau retains the ability to bind tubulin and promote tubulin assembly. TMAO is required, however, to sensitize the reaction. Possible uses of TMAO in relation to studies of tubulin assembly in vitro, in intact cells, and in relation to Alzheimer's disease are presented in this report.

Indexed as

Brain ChemistryCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesGlycogen Synthase Kinase 3Glycogen Synthase KinasesHumansMethylaminesMicroscopy, Atomic ForceMicrotubule-Associated ProteinsPhosphorylationtau ProteinsTubulinCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesGlycogen Synthase Kinase 3Glycogen Synthase KinasesMethylaminesMicrotubule-Associated Proteinstau ProteinstrimethyloxamineTubulin

Identifiers

PMID10449722
PMCPMC22238
OpenAlexW2134291063

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.