Evidence map›Paper›PMID 8114727›Full record

ArticleMolecular and cellular biology1994

Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes.

J L Johnson, T G Beito, C J Krco, D O Toft

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
4.3field-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

60 citing papers in PubMed, 192 citations in OpenAlex.

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  12. Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome.Proceedings of the National Academy of Sciences of the United States of America · 2013
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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

4 authors at 1 institution in 1 country.

J L JohnsonDepartment of Biochemistry and Molecular Biology, Mayo Graduate School, Rochester, Minnesota 55905.
T G Beito
C J Krco
D O Toft
Mayo Clinic · US

Funding

THE MOLECULAR BIOLOGY OF ANDROGEN RECEPTORP50HD009140 · NICHD · MAYO CLINIC COLL OF MEDICINE, ROCHESTER · PI SPELSBERG, THOMAS C · 1985 to 1997
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NICHD NIH HHS HD 09140
6 · The paper itself

Abstract

Immunoprecipitation of unactivated avian progesterone receptor results in the copurification of hsp90, hsp70, and three additional proteins, p54, p50, and p23. p23 is also present in immunoaffinity-purified hsp90 complexes along with hsp70 and another protein, p60. Antibody and cDNA probes for p23 were prepared in an effort to elucidate the significance and function of this protein. Antibodies to p23 detect similar levels of p23 in all tissues tested and cross-react with a protein of the same size in mice, rabbits, guinea pigs, humans, and Saccharomyces cerevisiae, indicating that p23 is a conserved protein of broad tissue distribution. These antibodies were used to screen a chicken brain cDNA library, resulting in the isolation of a 468-bp partial cDNA clone encoding a sequence containing four sequences corresponding to peptide fragments isolated from chicken p23. This partial clone was subsequently used to isolate a full-length human cDNA clone. The human cDNA encodes a protein of 160 amino acids that does not show homology to previously identified proteins. The chicken and human cDNAs are 88% identical at the DNA level and 96.3% identical at the protein level. p23 is a highly acidic phosphoprotein with an aspartic acid-rich carboxy-terminal domain. Bacterially overexpressed human p23 was used to raise several monoclonal antibodies to p23. These antibodies specifically immunoprecipitate p23 in complex with hsp90 in all tissues tested and can be used to immunoaffinity isolate progesterone receptor complexes from chicken oviduct cytosol.

Indexed as

Amino Acid SequenceAnimalsBase SequenceChickensDNA, ComplementaryGene Expression RegulationHeat-Shock ProteinsHumansMacromolecular SubstancesMolecular Sequence DataMolecular WeightNuclear ProteinsPrecipitin TestsReceptors, ProgesteroneSequence AlignmentSequence Homology, Amino AcidDNA, ComplementaryHeat-Shock ProteinsMacromolecular SubstancesNuclear ProteinsReceptors, Progesterone

Identifiers

PMID8114727
PMCPMC358554
OpenAlexW1849199569

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.