ArticleNature structural & molecular biology2012
Newly folded substrates inside the molecular cage of the HtrA chaperone DegQ.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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.
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.
Who cites it
33 citing papers in PubMed, 59 citations in OpenAlex.
- Review
- Streptococcus pneumoniae HtrA is a dynamic and monomeric virulence factor capable of forming larger oligomeric complexes.Protein science : a publication of the Protein Society · 2026Article
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Molecular mechanism of proteolytic cleavage-dependent activation of CadC-mediated response to acid in E. coli.Communications biology · 2024Article
- Identification of heptapeptides targeting a lethal bacterial strain in septic mice through an integrative approach.Signal transduction and targeted therapy · 2022Article
- Structural basis of DegP protease temperature-dependent activation.Science advances · 2021Article
- The Tail-Specific Protease Is Important for Legionella pneumophila To Survive Thermal Stress in Water and inside Amoebae.Applied and environmental microbiology · 2021Article
- Oligomeric assembly regulating mitochondrial HtrA2 function as examined by methyl-TROSY NMR.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Article
- Pneumococcal Extracellular Serine Proteases: Molecular Analysis and Impact on Colonization and Disease.Frontiers in cellular and infection microbiology · 2021Review
- How do Chaperones Bind (Partly) Unfolded Client Proteins?Frontiers in molecular biosciences · 2021Review
- The role of the bacterial protease Prc in the uropathogenesis of extraintestinal pathogenic Escherichia coli.Journal of biomedical science · 2020Article
- Exploring the Potential Role of Moonlighting Function of the Surface-Associated Proteins FromFrontiers in immunology · 2019Article
- The crystal structure of Mycobacterium tuberculosis high-temperature requirement A protein reveals an autoregulatory mechanism.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Periplasmic Chaperones and Prolyl Isomerases.EcoSal Plus · 2018Review
- Amino-Terminal Processing ofFrontiers in microbiology · 2018Article
- ER stress-induced aggresome trafficking of HtrA1 protects against proteotoxicity.Journal of molecular cell biology · 2017Article
- Structure and assembly of scalable porous protein cages.Nature communications · 2017Article
- Emodin Alleviates Sodium Taurocholate-Induced Pancreatic Acinar Cell InjuryFrontiers in immunology · 2017Article
- HtrA Is Important for Stress Resistance and Virulence in Haemophilus parasuis.Infection and immunity · 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
8 authors at 4 institutions in 4 countries.
Funding
Abstract
The HtrA protein family combines chaperone and protease activities and is essential for protein quality control in many organisms. Whereas the mechanisms underlying the proteolytic function of HtrA proteins are well characterized, their chaperone activity remains poorly understood. Here we describe cryo-EM structures of Escherichia coli DegQ in its 12- and 24-mer states in complex with model substrates, providing a structural model of HtrA chaperone action. Up to six lysozyme substrates bind inside the DegQ 12-mer cage and are visualized in a close-to-native state. An asymmetric reconstruction reveals the binding of a well-ordered lysozyme to four DegQ protomers. DegQ PDZ domains are located adjacent to substrate density and their presence is required for chaperone activity. The substrate-interacting regions appear conserved in 12- and 24-mer cages, suggesting a common mechanism of chaperone function.
Indexed as
Identifiers
What OpenQuestion holds
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.