Evidence map›Paper›PMID 41040204›Full record

ArticlebioRxiv : the preprint server for biology2025

Stabilization versus flexibility: detergent-dependent trade-offs in neurotensin receptor 1 GPCR ensembles.

James B Bower, Wijnand J C van der Velden, Karen P Gomez, Mingzhe Pan, Fabian Bumbak, Nagarajan Vaidehi, Joshua J Ziarek

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

James B BowerMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana USA.
Wijnand J C van der VeldenDepartment of Computational and Quantitative Medicine, Beckman Research Institute of City of Hope, Duarte, California.
Karen P GomezPharmacology Department, Northwestern University Feinberg School of Medicine, Chicago, Illinois USA.
Mingzhe PanMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana USA.
Fabian BumbakARC Centre for Cryo-electron Microscopy of Membrane Proteins and Drug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, VIC 3052, Australia.
Nagarajan VaidehiDepartment of Computational and Quantitative Medicine, Beckman Research Institute of City of Hope, Duarte, California.
Joshua J ZiarekPharmacology Department, Northwestern University Feinberg School of Medicine, Chicago, Illinois USA.ORCID 0000-0002-3740-9999

Funding

The role of dynamics in GPCR and arrestin allosteryR35GM143054 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI ZIAREK, JOSHUA JAMES · 2021 to 2025
$2.1M
Deciphering GPCR signal transduction through NMR structure and dynamics studiesR00GM115814 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI ZIAREK, JOSHUA JAMES · 2017 to 2019
$747k
NIGMS NIH HHS R00 GM115814NIGMS NIH HHS R35 GM143054
6 · The paper itself

Abstract

Detergents provide essential membrane-mimetic environments for studying G protein-coupled receptors (GPCRs), but their molecular impact on receptor energetics remains incompletely understood. We combined ligand binding, thermostability measurements and atomistic molecular dynamics to dissect detergent- versus ligand-driven stabilization in a thermostabilized neurotensin receptor 1 (enNTS1). Circular dichroism and ligand binding assays revealed that apo enNTS1 becomes progressively more stable in decyl maltoside (DM), dodecyl maltoside (DDM), and lauryl maltose neopentyl glycol (LMNG). Yet this gain in baseline stability was accompanied by a paradox: LMNG, the most stabilizing detergent, supported the weakest neurotensin agonist binding affinity. Thermodynamic analysis resolved this contradiction by partitioning stability into detergent-driven conformational rigidity (ΔG

Indexed as

Class A GPCRconformational energeticshydrophobic mismatchmembrane protein stabilitymolecular dynamics (MD)Protein-detergent interactionsstructural rigiditythermodynamic partitioning

Identifiers

PMID41040204
PMCPMC12485910

What OpenQuestion holds

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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.