ArticleChemistry (Weinheim an der Bergstrasse, Germany)2015
Conformational Flexibility in the Transmembrane Protein TSPO.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
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Who cites it
17 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.
- Association between FDG- and TSPO-PET signals across human and animal studies investigating neurodegenerative conditions: a systematic review.Molecular psychiatry · 2026Pooled it
- TSPO Radioligands for Neuroinflammation: An Overview.Molecules (Basel, Switzerland) · 2024Review
- New TSPO Crystal Structures of Mutant and Heme-Bound Forms with Altered Flexibility, Ligand Binding, and Porphyrin Degradation Activity.Biochemistry · 2023Article
- Essential Principles and Recent Progress in the Development of TSPO PET Ligands for Neuroinflammation Imaging.Current medicinal chemistry · 2022Review
- TSPO protein binding partners in bacteria, animals, and plants.Journal of bioenergetics and biomembranes · 2021Review
- Interactions of SARS-CoV-2 envelope protein with amilorides correlate with antiviral activity.PLoS pathogens · 2021Article
- Molecular Characterization and Functional Analysis of Two Steroidogenic Genes TSPO and SMAD4 in Yellow Catfish.International journal of molecular sciences · 2021Article
- Membrane-embedded TSPO: an NMR view.European biophysics journal : EBJ · 2021Article
- The Interplay of Cholesterol and Ligand Binding inMolecules (Basel, Switzerland) · 2021Article
- Insight into the Structural Features of TSPO: Implications for Drug Development.Trends in pharmacological sciences · 2020Review
- A unified structural model of the mammalian translocator protein (TSPO).Journal of biomolecular NMR · 2019Article
- Characterization of the High-Affinity Drug Ligand Binding Site of Mouse Recombinant TSPO.International journal of molecular sciences · 2019Article
- Challenges and approaches to understand cholesterol-binding impact on membrane protein function: an NMR view.Cellular and molecular life sciences : CMLS · 2018Review
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- Cholesterol-mediated allosteric regulation of the mitochondrial translocator protein structure.Nature communications · 2017Article
- Tetrapyrroles as Endogenous TSPO Ligands in Eukaryotes and Prokaryotes: Comparisons with Synthetic Ligands.International journal of molecular sciences · 2016Review
- Translocator Protein 18 kDa (TSPO): An Old Protein with New Functions?Biochemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The translocator protein (TSPO) is an integral membrane protein that interacts with a wide variety of endogenous ligands, such as cholesterol and porphyrins, and is also the target for several small molecules with substantial in vivo efficacy. When complexed with the TSPO-specific radioligand (R)-PK11195, TSPO folds into a rigid five-helix bundle. However, little is known about the structure and dynamics of TSPO in the absence of high-affinity ligands. By means of NMR spectroscopy, we show that TSPO exchanges between multiple conformations in the absence of (R)-PK11195. Extensive motions on time scales from pico- to microseconds occur all along the primary sequence of the protein, leading to a loss of stable tertiary interactions and local unfolding of the helical structure in the vicinity of the ligand-binding site. The flexible nature of TSPO highlights the importance of conformational plasticity in integral membrane proteins.
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Registered trials
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.