Evidence map›Paper›PMID 38118365›Full record

ReviewCurrent opinion in structural biology2024

Molecular simulations integrated with experiments for probing the interaction dynamics and binding mechanisms of intrinsically disordered proteins.

Catherine Ghosh, Suhani Nagpal, Victor Muñoz

Open access · hybridAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Current opinion in structural biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

11 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
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  11. Coil-Library-Derived Amino-Acid-Specific Side-Chain χJournal of chemical theory and computation · 2025
    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 at 1 institution in 1 country.

Catherine GhoshNSF-CREST Center for Cellular and Biomolecular Machines (CCBM), University of California at Merced, Merced, 95343 CA, USA; Department of Bioengineering, University of California at Merced, Merced, 95343 CA, USA. Electronic address: https://twitter.com/cat_ghosh.
Suhani NagpalNSF-CREST Center for Cellular and Biomolecular Machines (CCBM), University of California at Merced, Merced, 95343 CA, USA; Department of Bioengineering, University of California at Merced, Merced, 95343 CA, USA; OpenEye, Cadence Molecular Sciences, Boston, 02114 MA, USA.
Victor MuñozNSF-CREST Center for Cellular and Biomolecular Machines (CCBM), University of California at Merced, Merced, 95343 CA, USA; Department of Bioengineering, University of California at Merced, Merced, 95343 CA, USA. Electronic address: vmunoz3@ucmerced.edu.
University of California, Merced · US

Funding

Mechanisms for DNA Recognition, Scanning and Nucleosome Mechanical Actions by Pioneer Transcription Factors and their Role in Cell Fate DecisionsR01GM152623 · NIGMS · UNIVERSITY OF CALIFORNIA, MERCED · PI Victor Munoz · 2024 to 2026
$1.7M
NIGMS NIH HHS R01 GM152623
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) exploit their plasticity to deploy a rich panoply of soft interactions and binding phenomena. Advances in tailoring molecular simulations for IDPs combined with experimental cross-validation offer an atomistic view of the mechanisms that control IDP binding, function, and dysfunction. The emerging theme is that unbound IDPs autonomously form transient local structures and self-interactions that determine their binding behavior. Recent results have shed light on whether and how IDPs fold, stay disordered or drive condensation upon binding; how they achieve binding specificity and select among competing partners. The disorder-binding paradigm is now being proactively used by researchers to target IDPs for rational drug design and engineer molecular responsive elements for biosensing applications.

Indexed as

Intrinsically Disordered ProteinsDrug DesignMolecular Dynamics SimulationProtein ConformationIntrinsically Disordered Proteins

Identifiers

PMID38118365
PMCPMC11242915
OpenAlexW4389939503

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.