Evidence map›Paper›PMID 29941666›Full record

ArticleMolecular pharmacology2018

Chaperone Activity and Dimerization Properties of Hsp90

Yoshihiro Morishima, Ranjit K Mehta, Miyako Yoshimura, Miranda Lau, Daniel R Southworth, Theodore S Lawrence, William B Pratt, Mukesh K Nyati, Yoichi Osawa

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular pharmacology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

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  12. Chemical Screening of Nuclear Receptor Modulators.International journal of molecular sciences · 2020
    Review
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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

9 authors at 1 institution in 1 country.

Yoshihiro MorishimaDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Ranjit K MehtaDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Miyako YoshimuraDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Miranda LauDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Daniel R SouthworthDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Theodore S LawrenceDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
William B PrattDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Mukesh K NyatiDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.).
Yoichi OsawaDepartments of Pharmacology (Y.M., M.Y., M.L., W.B.P., Y.O.) and Radiation Oncology (R.K.M., T.S.L., M.K.N.), University of Michigan Medical School, Ann Arbor, Michigan; and Life Sciences Institute and Departments of Biochemistry and Biophysics, University of Michigan, Ann Arbor, Michigan (D.R.S.) osawa@umich.edu.
University of Michigan–Ann Arbor · US

Funding

P450 and NO Synthase Regulation by Multiprotein ComplexesR01GM077430 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI OSAWA, YOICHI, ZHANG, HAOMING · 2006 to 2022
$6.5M
NIGMS NIH HHS R01 GM077430
6 · The paper itself

Abstract

Several hundred proteins cycle into heterocomplexes with a dimer of the chaperone heat shock protein 90 (Hsp90), regulating their activity and turnover. There are two isoforms of Hsp90, Hsp90

Indexed as

AnimalsHEK293 CellsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHumansMiceMolecular ChaperonesProtein BindingProtein MultimerizationReceptors, GlucocorticoidHSP70 Heat-Shock ProteinsHSP90AA2P protein, humanHSP90AB1 protein, humanHSP90 Heat-Shock ProteinsMolecular ChaperonesReceptors, Glucocorticoid

Identifiers

PMID29941666
PMCPMC6064783
OpenAlexW2810620131

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.