Evidence map›Paper›PMID 9742138›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

The cellular and subcellular localization of huntingtin-associated protein 1 (HAP1): comparison with huntingtin in rat and human.

C A Gutekunst, S H Li, H Yi, R J Ferrante, X J Li, S M Hersch

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

70 citing papers in PubMed, 180 citations in OpenAlex.

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  20. Huntington's Disease and Mitochondria.Neurotoxicity research · 2017
    Review

10 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

6 authors at 2 institutions in 1 country.

C A GutekunstDepartment of Neurology, Emory University School of Medicine, Atlanta, Georgia 30329, USA.
S H Li
H Yi
R J Ferrante
X J Li
S M Hersch
Emory University · USGeriatric Research Education and Clinical Center · US

Funding

Neuronal function of huntingtin-associated proteinR01NS036232 · NINDS · EMORY UNIVERSITY · PI ESCAYG, ANDREW P · 1998 to 2021
$6.7M
HUNTINGTON PROTEIN AND THE HUNTINGTONS DISEASES MUTATIONR01NS035255 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI HERSCH, STEVEN M · 1997 to 2003
$1.6M
ANATOMIC AND MOLECULAR PATHOLOGY IN HUNTINGTON'S DISEASEK08NS001624 · NINDS · EMORY UNIVERSITY · PI HERSCH, STEVEN M · 1993 to 1997
–
NINDS NIH HHS NS01624NINDS NIH HHS NS35255NINDS NIH HHS NS36232NINDS NIH HHS R01 NS036232
6 · The paper itself

Abstract

The cellular and subcellular distribution of HAP1 was examined in rat brain by light and electron microscopic immunocytochemistry and subcellular fractionation. HAP1 localization was also determined in human postmortem tissue from control and Huntington's disease (HD) cases by light microscopic immunocytochemistry. At the cellular level, the heterogeneity of HAP1 expression was similar to that of huntingtin; however, HAP1 immunoreactivity was more widespread. The subcellular distribution of HAP1 was examined using immunogold electron microscopy. Like huntingtin, HAP1 is a cytoplasmic protein that associates with microtubules and many types of membranous organelles, including mitochondria, endoplasmic reticulum, tubulovesicles, endosomal and lysosomal organelles, and synaptic vesicles. A quantitative comparison of the organelle associations of HAP1 and huntingtin showed them to be almost identical. Within HAP1-immunoreactive neurons in rat and human brain, populations of large and small immunoreactive puncta were visible by light microscopy. The large puncta, which were especially evident in the ventral forebrain, were intensely HAP1 immunoreactive. Electron microscopic analysis revealed them to be a type of nucleolus-like body, which has been named a stigmoid body, that may play a role in protein synthesis. The small puncta, less intensely labeled, were primarily mitochondria. These results indicate that the localization of HAP1 and huntingtin is more similar than previously appreciated and provide further evidence that HAP1 and huntingtin have localizations consistent with roles in intracellular transport. Our data also suggest, however, that HAP1 is not present in the abnormal intranuclear and neuritic aggregates containing the N-terminal fragment of mutant huntingtin that are found in HD brains.

Indexed as

Carbon-Oxygen LyasesDNA-(Apurinic or Apyrimidinic Site) LyaseAnimalsBiomarkersBrain ChemistryCytoplasmEndonucleasesHumansHuntingtin ProteinHuntington DiseaseImmunoenzyme TechniquesInclusion BodiesMaleMicroscopy, ImmunoelectronMitochondriaNerve Tissue ProteinsAPEX1 protein, humanApex1 protein, ratBiomarkersCarbon-Oxygen LyasesDNA-(Apurinic or Apyrimidinic Site) LyaseEndonucleasesHTT protein, humanHtt protein, ratHuntingtin ProteinNerve Tissue ProteinsNuclear Proteins

Identifiers

PMID9742138
PMCPMC6793025
OpenAlexW2142716581

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.