Evidence map›Paper›PMID 21898227›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2011

Detecting HSP90 phosphorylation.

Mehdi Mollapour, Len Neckers

Open access · greenAbstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
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

2 authors at 2 institutions in 1 country.

Mehdi MollapourUrologic Oncology Branch, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Len Neckers
National Cancer Institute · USNational Institutes of Health · US

Funding

Post-translational modifications of Hsp90 that impact drug efficacyZIABC011032 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NECKERS, LEONARD · 2009 to 2025
$11.5M
ROLE OF HSP90/GFP94 CHAPERONE PROTEINS IN CELLULAR SIGNAL TRANSDUCTIONZ01SC010074 · SC · DIVISION OF CLINICAL SCIENCES - NCI · PI NECKERS, LEONARD · 1996 to 2008
$3.7M
Post-translational modifications of Hsp90 that impact drug efficacyZ01BC011032 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NECKERS, LEONARD · 2008 to 2008
$664k
Intramural NIH HHS Z01 BC011032Intramural NIH HHS Z01 SC010074
6 · The paper itself

Abstract

Heat-shock protein 90 (HSP90) is an essential molecular chaperone in eukaryotes. It is important for chaperoning proteins that are important determinants of multistep carcinogenesis. HSP90's ATPase activity is associated with its chaperone function. Co-chaperones as well as posttranslational modifications (phosphorylation, acetylation, and S-nitrosylation) are important for regulating its ATPase activity. Yeast can be used to express and purify HSP90 and also detect its phosphorylation by pan-phosphoserine or phosphothreonine antibodies.

Indexed as

Protein Processing, Post-TranslationalAdenosine TriphosphatasesFungal ProteinsHSP90 Heat-Shock ProteinsPhosphorylationProtein BindingSaccharomyces cerevisiaeAdenosine TriphosphatasesFungal ProteinsHSP90 Heat-Shock Proteins

Identifiers

PMID21898227
PMCPMC7380563
OpenAlexW2436964155

What OpenQuestion holds

Textmetadata
LicenceTDM
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.