Evidence map›Paper›PMID 19309730›Full record

ArticleProtein science : a publication of the Protein Society2009

Opposite allosteric mechanisms in TetR and CAP.

Jennifer E Seedorff, Michael E Rodgers, Robert Schleif

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2009. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Article
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

3 authors.

Jennifer E SeedorffDepartment of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Michael E Rodgers
Robert Schleif

Funding

REGULATORY MECHANISMS OF THE E COLI ARABINOSE OPERONR37GM018277 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHLEIF, ROBERT F. · 1994 to 2004
$2.3M
REGULATORY MECHANISMS OF THE E COLI ARABINOSE OPERONR01GM018277 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHLEIF, ROBERT F. · 1985 to 2009
$2.2M
NIGMS NIH HHS GM018277
6 · The paper itself

Abstract

Regulation of the DNA binding affinity of an oligomeric protein can be considered to consist of an intrinsic component, in which the affinity of an individual DNA-binding domain is modulated in response to effector binding, and an extrinsic component, in which the relative position of the protein's two DNA-binding domains are altered so that they can or cannot contact both half-site operators simultaneously. We demonstrated directly that the TetR repressor utilizes an extrinsic mechanism and CAP, the catabolite activator protein, utilizes an intrinsic mechanism.

Indexed as

Allosteric RegulationCyclic AMPCyclic AMP Receptor ProteinDNADNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsProtein BindingRepressor ProteinsTetracyclineCyclic AMPCyclic AMP Receptor ProteinDNADNA-Binding ProteinsEscherichia coli ProteinsRepressor ProteinsTetracyclinetetracycline resistance-encoding transposon repressor protein

Identifiers

PMID19309730
PMCPMC2762589

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.