Evidence map›Paper›PMID 7519974›Full record

ArticleChromosoma1994

Generation and characterization of novel antibodies highly selective for phosphorylated linker histone H1 in Tetrahymena and HeLa cells.

M J Lu, C A Dadd, C A Mizzen, C A Perry, D R McLachlan, A T Annunziato, C D Allis

Abstract read
PubMed Publisher
In one paragraph

Article in Chromosoma, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 61 citations in OpenAlex.

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  11. Regulation of hypermutation by activation-induced cytidine deaminase phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2006
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  19. An HP1-like protein is missing from transcriptionally silent micronuclei of Tetrahymena.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
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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

7 authors at 3 institutions in 2 countries.

M J LuDepartment of Biology, Syracuse University, NY 13244.
C A Dadd
C A Mizzen
C A Perry
D R McLachlan
A T Annunziato
C D Allis
Syracuse University · USBoston College · USUniversity of Toronto · CA

Funding

INFLUENCE OF HISTONE H1 AND HMGS ON GENE EXPRESSIONR01GM040922 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ALLIS, CHARLES DAVID · 1989 to 2022
$10.0M
HISTONE/DNA INTERACTIONS DURING CHROMATIN BIOSYNTHESISR01GM035837 · NIGMS · BOSTON COLLEGE · PI ANNUNZIATO, ANTHONY · 1986 to 2005
$1.2M
NIGMS NIH HHS GM 35837NIGMS NIH HHS GM 40922
6 · The paper itself

Abstract

Phosphorylated forms of Tetrahymena macronuclear histone H1 were separated from each other and from dephosphorylated H1 by cation-exchange HPLC. A homogeneous fraction of hyperphosphorylated macronuclear H1 was then used to generate novel polyclonal antibodies highly selective for phosphorylated H1 in Tetrahymena and in human cells. These antibodies fail to recognize dephosphorylated forms of H1 in both organisms and are not reactive with most other nuclear or cytoplasmic phosphoproteins including those induced during mitosis. The selectivity of these antibodies for phosphorylated forms of H1 in Tetrahymena and in HeLa argues strongly that these antibodies recognize highly conserved phosphorylated epitopes found in most H1s and from this standpoint Tetrahymena H1 is not atypical. Using these antibodies in indirect immunofluorescence analyses, we find that a significant fraction of interphase mammalian cells display a strikingly punctate pattern of nuclear fluorescence. As cells enter S-phase, nuclear staining becomes more diffuse, increases significantly, and continues to increase as cells enter mitosis. As cells exit from mitosis, staining with the anti-phosphorylated H1 antibodies is rapidly lost presumably owing to the dephosphorylation of H1. These immunofluorescent data document precisely the cell cycle changes in the level of H1 phosphorylation determined by earlier biochemical studies and suggest that these antibodies represent a powerful new tool to probe the function(s) of H1 phosphorylation in a wide variety of eukaryotic systems.

Indexed as

AnimalsAntibodies, ProtozoanAntibody SpecificityCell CycleChromatography, High Pressure LiquidEpitopesHeLa CellsHistonesHumansImmunizationPhosphorylationRabbitsTetrahymenaAntibodies, ProtozoanEpitopesHistones

Identifiers

PMID7519974
OpenAlexW1987067190

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.