Evidence map›Paper›PMID 20678074›Full record

ReviewCurrent Alzheimer research2010

Tau in Alzheimer disease and related tauopathies.

K Iqbal, F Liu, C-X Gong, I Grundke-Iqbal

Open access · greenAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current Alzheimer research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 547 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
547citing papers in PubMed, 1 pooled it
13.5field-weighted citation impact, top 1% 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

547 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,116 citations in OpenAlex.

  1. Pooled it
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  9. Patient-derived forebrain cortical organoids reveal biphasic tau-MAP6-microtubule axis dysfunction in tauopathy.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2026
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487 more citing papers are in PubMed but not listed here.

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.

K IqbalDepartment of Neurochemistry, New York State Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, New York 10314-6399, USA. khalid.iqbal.ibr@gmail.com
F Liu
C-X Gong
I Grundke-Iqbal
New York State Office for People With Developmental Disabilities · US

Funding

Abnormal Hyperphosphorylation of TauR01AG019158 · NIA · INSTITUTE FOR BASIC RES IN DEV DISABIL · PI IQBAL, KHALID · 2002 to 2011
$3.7M
Subgroups of Alzheimer DiseaseR01AG028538 · NIA · INSTITUTE FOR BASIC RES IN DEV DISABIL · PI IQBAL, KHALID · 2007 to 2011
$1.6M
O-GlcNAcylation of tau: glucose metabolism & neurodegenR01AG027429 · NIA · INSTITUTE FOR BASIC RES IN DEV DISABIL · PI GONG, CHENG-XIN · 2006 to 2010
$1.3M
NIA NIH HHS AG019158NIA NIH HHS AG028538NIA NIH HHS AG27429NIA NIH HHS R01 AG019158NIA NIH HHS R01 AG027429NIA NIH HHS R01 AG028538
6 · The paper itself

Abstract

Tau is the major microtubule associated protein (MAP) of a mature neuron. The other two neuronal MAPs are MAP1 and MAP2. An established function of MAPs is their interaction with tubulin and promotion of its assembly into microtubules and stabilization of the microtubule network. The microtubule assembly promoting activity of tau, a phosphoprotein, is regulated by its degree of phosphorylation. Normal adult human brain tau contains 2-3 moles phosphate/mole of tau protein. Hyperphosphorylation of tau depresses this biological activity of tau. In Alzheimer disease (AD) brain tau is ~three to four-fold more hyperphosphorylated than the normal adult brain tau and in this hyperphosphorylated state it is polymerized into paired helical filaments ([PHF) admixed with straight filaments (SF) forming neurofibrillary tangles. Tau is transiently hyperphosphorylated during development and during anesthesia and hypothermia but not to the same state as in AD brain. The abnormally hyperphosphorylated tau in AD brain is distinguished from transiently hyperphosphorylated tau by its ability (1) to sequester normal tau, MAP1 and MAP2 and disrupt microtubules, and (2) to self-assemble into PHF/SF. The cytosolic abnormally hyperphosphorylated tau, because of oligomerization, unlike normal tau, is sedimentable and on self-assembly into PHF/SF, loses its ability to sequester normal MAPs. Some of the tau in AD brain is truncated which also promotes its self-assembly. Tau mutations found in frontotemporal dementia apparently promote its abnormal hyperphosphorylation. Thus, the AD abnormally hyperphosphorylated tau (1) is distinguishable from both normal and transiently hyperphosphorylated taus, and (2) is inhibitory when in a cytosolic/oligomeric state but not when it is self-assembled into PHF/SF. Inhibition of abnormal hyperphosphorylation of tau offers a promising therapeutic target for AD and related tauopathies.

Indexed as

Alzheimer DiseaseAnimalsHumansPhosphorylationTauopathiestau ProteinsMAPT protein, humantau Proteins

Identifiers

PMID20678074
PMCPMC3090074
OpenAlexW2156093068

What OpenQuestion holds

Textmetadata
LicenceTDM
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.