Evidence map›Paper›PMID 20851337›Full record

ArticleChemistry & biology2010

Making it easier to regulate protein stability.

Erin K Schrader, Shameika R Wilmington, Andreas Matouschek

Abstract readComment
In one paragraph

Article in Chemistry & biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Identification of hydrophobic tags for the degradation of stabilized proteins.Chembiochem : a European journal of chemical biology · 2012
    Article
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Erin K SchraderDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Shameika R Wilmington
Andreas Matouschek
Northwestern University · US

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
TRANS-NETWORK PROJECTSU54CA143869 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI MARKO, JOHN F · 2009 to 2013
$12.8M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
NCI NIH HHS U54 CA143869NIGMS NIH HHS R01 GM063004NIGMS NIH HHS T32 GM008061
6 · The paper itself

Abstract

The ability to induce degradation of a protein of interest is a powerful experimental tool used to ascertain protein function. Iwamoto et al. (2010) describe a method that allows reversible and dose-dependent modulation of the stability of any target protein.

Identifiers

PMID20851337
PMCPMC2990474
OpenAlexW2087334382

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.