Evidence map›Paper›PMID 38109992›Full record

ReviewJournal of molecular biology2024

Dimerization Rules of Mammalian PAS Proteins.

Brenda L Rojas, Emmanuel Vazquez-Rivera, Carrie L Partch, Christopher A Bradfield

Open access · hybridAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2024. 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
1.1field-weighted citation impact, top 22% 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, 7 citations in OpenAlex.

  1. Juvenile hormone receptor relies on conserved domain interfaces for dimerization-dependent activity.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. The Period (Animals : an open access journal from MDPI · 2026
    Article
  3. Article
  4. 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

4 authors at 2 institutions in 1 country.

Brenda L RojasMolecular and Environmental Toxicology Center, University of Wisconsin at Madison, USA.
Emmanuel Vazquez-RiveraMolecular and Environmental Toxicology Center, University of Wisconsin at Madison, USA.
Carrie L PartchDepartment of Chemistry and Biochemistry, University of California at Santa Cruz, USA.
Christopher A BradfieldMolecular and Environmental Toxicology Center, University of Wisconsin at Madison, USA; McArdle Laboratory for Cancer Research. University of Wisconsin, School of Medicine and Public Health, Madison, WI, USA. Electronic address: bradfield@oncology.wisc.edu.
University of Wisconsin–Madison · USUniversity of California, Santa Cruz · US

Funding

UW COMPREHENSIVE CANCER CENTER SUPPORTP30CA014520 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI Justine Yang Bruce · 1985 to 2026
$142.6M
Molecular & Environmental Toxicology Pre-& Postdoctoral Training ProgramT32ES007015 · NIEHS · UNIVERSITY OF WISCONSIN-MADISON · PI CHRISTOPHER A BRADFIELD · 1985 to 2026
$11.5M
The PAS Sensor Family and Human HealthR35ES028377 · NIEHS · UNIVERSITY OF WISCONSIN-MADISON · PI BRADFIELD, CHRISTOPHER A · 2017 to 2024
$6.7M
Structures and mechanisms of circadian rhythms from cyanobacteria to humansR35GM141849 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA CRUZ · PI PARTCH, CARRIE L · 2021 to 2025
$4.6M
Summer Research Experience for Minority UndergraduatesR25ES020720 · NIEHS · UNIVERSITY OF WISCONSIN-MADISON · PI CHRISTOPHER A BRADFIELD, Sean M. Ronnekleiv-Kelly · 2011 to 2026
$1.3M
NCI NIH HHS P30 CA014520NIEHS NIH HHS R25 ES020720NIEHS NIH HHS R35 ES028377NIEHS NIH HHS T32 ES007015NIGMS NIH HHS R35 GM141849
6 · The paper itself

Abstract

The PAS (PER, ARNT, SIM) protein family plays a vital role in mammalian biology and human disease. This analysis arose from an interest in the signaling mechanics by the Ah receptor (AHR) and the Ah receptor nuclear translocator (ARNT). After more than fifty years by studying this and related mammalian sensor systems, describing the role of PAS domains in signal transduction is still challenging. In this perspective, we attempt to interpret recent studies of mammalian PAS protein structure and consider how this new insight might explain how these domains are employed in human signal transduction with an eye towards developing strategies to target and engineer these molecules for a new generation of therapeutics. Our approach is to integrate our understanding of PAS protein history, cell biology, and molecular biology with recent structural discoveries to help explain the mechanics of mammalian PAS protein signaling. As a learning set, we focus on sequences and crystal structures of mammalian PAS protein dimers that can be visualized using readily available software.

Indexed as

Aryl Hydrocarbon Receptor Nuclear TranslocatorReceptors, Aryl HydrocarbonAnimalsHumansProtein MultimerizationAryl Hydrocarbon Receptor Nuclear TranslocatorReceptors, Aryl Hydrocarbon

Identifiers

PMID38109992
PMCPMC10922841
OpenAlexW4389828481

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.