Evidence map›Paper›PMID 37142193›Full record

ArticleJournal of structural biology2023

NMR sample optimization and backbone assignment of a stabilized neurotensin receptor.

Mariam Mohamadi, David Goricanec, Gerhard Wagner, Franz Hagn

Open access · greenAbstract read
In one paragraph

Article in Journal of structural biology, 2023. 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
2.0field-weighted citation impact, top 14% 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, 13 citations in OpenAlex.

  1. Review
  2. 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 3 institutions in 2 countries.

Mariam MohamadiBavarian NMR Center (BNMRZ) and Structural Membrane Biochemistry, Dept. of Bioscience, TUM School of Natural Sciences, Technical University of Munich, 85748 Garching, Germany.
David GoricanecBavarian NMR Center (BNMRZ) and Structural Membrane Biochemistry, Dept. of Bioscience, TUM School of Natural Sciences, Technical University of Munich, 85748 Garching, Germany.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Franz HagnBavarian NMR Center (BNMRZ) and Structural Membrane Biochemistry, Dept. of Bioscience, TUM School of Natural Sciences, Technical University of Munich, 85748 Garching, Germany; Institute of Structural Biology, Molecular Targets and Therapeutics Center, Helmholtz Munich 85764 Neuherberg, Germany. Electronic address: franz.hagn@tum.de.
Technical University of Munich · DEHarvard University · USHelmholtz Zentrum München · DE

Funding

STRUCTURE BASIS OF IMMUNE-CELL SURFACE RECEPTOR FUNCTIONR01AI037581 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2021
$6.7M
TR&D 4 -- Advanced Magic Angle Spinning NMR methodsP41GM132079 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2021
$3.6M
Next Generation Solution NMR Techniques for GPCR Structure, Dynamics and FunctionR01GM129026 · NIGMS · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2018 to 2021
$2.0M
600 MHz NMR Spectrometer ConsoleS10OD028526 · OD · HARVARD MEDICAL SCHOOL · PI WAGNER, GERHARD · 2020 to 2020
$649k
NIAID NIH HHS R01 AI037581NIGMS NIH HHS P41 GM132079NIGMS NIH HHS R01 GM129026NIH HHS S10 OD028526
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are involved in a multitude of cellular signaling cascades and consequently are a prominent target for pharmaceutical drugs. In the past decades, a growing number of high-resolution structures of GPCRs has been solved, providing unprecedented insights into their mode of action. However, knowledge on the dynamical nature of GPCRs is equally important for a better functional understanding, which can be obtained by NMR spectroscopy. Here, we employed a combination of size exclusion chromatography, thermal stability measurements and 2D-NMR experiments for the NMR sample optimization of the stabilized neurotensin receptor type 1 (NTR1) variant HTGH4 bound to the agonist neurotensin. We identified the short-chain lipid di-heptanoyl-glycero-phosphocholine (DH

Indexed as

ProtonsReceptors, NeurotensinAmidesMagnetic Resonance SpectroscopyReceptors, G-Protein-CoupledAmidesProtonsReceptors, G-Protein-CoupledReceptors, Neurotensin

Identifiers

PMID37142193
PMCPMC10242673
OpenAlexW4367669836

What Socratic 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 Socratic graph.