Evidence map›Paper›PMID 10460255›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1999

cAMP-dependent protein kinase phosphorylations on tau in Alzheimer's disease.

G A Jicha, C Weaver, E Lane, C Vianna, Y Kress, J Rockwood, P Davies

Open access · greenAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

88 citing papers in PubMed, 204 citations in OpenAlex.

  1. A complex of MAST1 and 14-3-3η regulates Tau phosphorylation in the developing cortex.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  13. Alzheimer's Disease: Significant Benefit from the Yeast-Based Models.International journal of molecular sciences · 2023
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28 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

7 authors at 1 institution in 1 country.

G A JichaDepartment of Pathology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
C Weaver
E Lane
C Vianna
Y Kress
J Rockwood
P Davies
Albert Einstein College of Medicine · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM007288 · NIGMS · YESHIVA UNIVERSITY · PI AKABAS, MYLES H. · 1985 to 2022
$35.6M
Molecular NeuropathologyT32NS007098 · NINDS · YESHIVA UNIVERSITY · PI SANTAMBROGIO, LAURA · 1985 to 2015
$5.0M
Health disparities in cognitive performance across the life spanZ01AG000194 · NIA · NATIONAL INSTITUTE ON AGING · PI ZONDERMAN, ALAN B · 2008 to 2008
$703k
TAU PROTEINS IN ALZHEIMER'S DISEASEP01AG006803 · NIA · YESHIVA UNIVERSITY · PI DICKSON, DENNIS WILLIAM · 1987 to 1998
–
AGING TRAINING GRANTT32AG000194 · NIA · YESHIVA UNIVERSITY · PI HAMERMAN, DAVID · 1989 to 1998
–
Intramural NIH HHS Z01 AG000194NIA NIH HHS AG00194NIA NIH HHS AG06803NIA NIH HHS T32 AG000194NIGMS NIH HHS T32 GM007288NIGMS NIH HHS T32GM07288NINDS NIH HHS T32 NS007098
6 · The paper itself

Abstract

To elucidate the role cAMP-dependent protein kinase (PKA) phosphorylations on tau play in Alzheimer's disease, we have generated highly specific monoclonal antibodies, CP-3 and PG-5, which recognize the PKA-dependent phosphorylations of ser214 and ser409 in tau respectively. The present study demonstrates by immunohistochemical analysis, CP-3 and PG-5 immunoreactivity with neurofibrillary pathology in both early and advanced Alzheimer's disease, but not in normal brain tissue and demonstrates that cAMP-dependent protein kinase phosphorylations on tau precede or are coincident with the initial appearance of filamentous aggregates of tau. Studies using heat-stable preparations demonstrate that neither site appears to be phosphorylated to any appreciable extent in normal rodent or human brain. Further analysis demonstrates that the beta catalytic subunit of PKA (Cbeta), the beta II regulatory subunit of PKA (RIIbeta), and the 79 kDa A-kinase-anchoring-protein (AKAP79), are tightly associated with the neurofibrillary pathology, positioning cAMP-dependent protein kinase to participate directly in the pathological hyperphosphorylation of tau seen in Alzheimer's disease.

Indexed as

Alzheimer DiseaseAmino Acid SequenceAnimalsAntibodies, MonoclonalAntibody SpecificityBrainCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesFetusGlycogen Synthase Kinase 3HippocampusHumansMiceMolecular Sequence DataNeurofibrillary TanglesOrgan SpecificityAntibodies, MonoclonalCalcium-Calmodulin-Dependent Protein KinasesCyclic AMP-Dependent Protein KinasesGlycogen Synthase Kinase 3Peptide FragmentsPhosphopeptidestau Proteins

Identifiers

PMID10460255
PMCPMC6782506
OpenAlexW2111565853

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.