Evidence map›Paper›PMID 34028215›Full record

ReviewAdvanced biology2021

Dual Systems for Enhancing Control of Protein Activity through Induced Dimerization Approaches.

Sarah Pearce, Chandra L Tucker

Abstract readReview
In one paragraph

Review in Advanced biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Design and engineering of light-sensitive protein switches.Current opinion in structural biology · 2022
    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.

Sarah PearceDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO, 80045, USA.
Chandra L TuckerDepartment of Pharmacology, University of Colorado School of Medicine, Aurora, CO, 80045, USA.ORCID 0000-0003-3033-1786

Funding

Control of Protein Activity Via Light Stimulated DimerizersR01GM100225 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI TUCKER, CHANDRA L · 2012 to 2019
$3.3M
Uncovering new approaches to manipulate and probe biochemical processes with spatial and temporal precision.R35GM136367 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI Chandra L Tucker · 2020 to 2026
$3.0M
Validating and extending optical tools for extended neural silencingUF1NS107710 · NINDS · UNIVERSITY OF COLORADO DENVER · PI FORD, CHRISTOPHER PETER, KENNEDY, MATTHEW J · 2018 to 2018
$2.0M
NIGMS NIH HHS R01 GM100225NIGMS NIH HHS R35 GM136367NINDS NIH HHS UF1 NS107710
6 · The paper itself

Abstract

To reveal the underpinnings of complex biological systems, a variety of approaches have been developed that allow switchable control of protein function. One powerful approach for switchable control is the use of inducible dimerization systems, which can be configured to control activity of a target protein upon induced dimerization triggered by chemicals or light. Individually, many inducible dimerization systems suffer from pre-defined dynamic ranges and overwhelming sensitivity to expression level and cellular context. Such systems often require extensive engineering efforts to overcome issues of background leakiness and restricted dynamic range. To address these limitations, recent tool development efforts have explored overlaying dimerizer systems with a second layer of regulation. Albeit more complex, the resulting layered systems have enhanced functionality, such as tighter control that can improve portability of these tools across platforms.

Indexed as

ProteinsDimerizationProteinschemical inducers of dimerizationinduced dimerizeroptogeneticprotein control

Identifiers

PMID34028215
PMCPMC8144547

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.