ReviewCell stress & chaperones2011
Versatile TPR domains accommodate different modes of target protein recognition and function.
Review in Cell stress & chaperones, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 127 papers.
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.
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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
127 citing papers in PubMed, 248 citations in OpenAlex.
- TurboID proximity labeling reveals protein interaction networks for germline Argonautes.bioRxiv : the preprint server for biology · 2026Article
- Genome-wide association analysis and candidate gene identification for plant height in Shanxi local foxtail millet varieties.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2026Article
- RPAP3: Structural evolution, chaperone networks, and disease implications of a transcriptional Co-chaperone.The Journal of biological chemistry · 2026Review
- Transcriptome sequencing (RNA-Seq) reveals non-coding pseudogene CDC27P9 role in cervical cancer.Apoptosis : an international journal on programmed cell death · 2026Article
- FKBP9 enhances IGF2BP1-mediated mJHEP reports : innovation in hepatology · 2025Article
- Cell splitting in Staphylococcus aureus is controlled by an adaptor protein facilitating degradation of a peptidoglycan hydrolase.PLoS genetics · 2025Article
- Tandem-repeat proteins introduce tuneable properties to engineered biomolecular condensates.Chemical science · 2025Article
- A human gut bacterium antagonizes neighboring bacteria by altering their protein-folding ability.Cell host & microbe · 2025Article
- Chaperone-dependent and chaperone-independent functions of carboxylate clamp tetratricopeptide repeat (CC-TPR) proteins.Trends in biochemical sciences · 2025Review
- Hsf1 is essential for proteotoxic stress response in smyd1b-deficient embryos and fish survival under heat shock.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- Case Report: Prenatal diagnosis of gastrointestinal defects and immunodeficiency syndrome caused by compound heterozygous mutations in TTC7A gene.Frontiers in immunology · 2025Article
- Multiomics Identifies Potential Biomarkers in Ankylosing Spondylitis Bone Formation.Human mutation · 2025Article
- Genetic gradual reduction of OGT activity unveils the essential role of O-GlcNAc in the mouse embryo.PLoS genetics · 2025Article
- The roles of OGT and its mechanisms in cancer.Cell & bioscience · 2024Review
- IFIT1 modulates the proliferation, migration and invasion of pancreatic cancer cells via Wnt/β-catenin signaling.Cellular oncology (Dordrecht, Netherlands) · 2024Article
- Genome-Wide Identification and Interaction Analysis of Turbot Heat Shock Protein 40 and 70 Families Suggest the Mechanism of Chaperone Proteins Involved in Immune Response after Bacterial Infection.International journal of molecular sciences · 2024Article
- The Thioredoxin Fold Protein (TFP2) from Extreme AcidophilicInternational journal of molecular sciences · 2024Article
- Article
- IFT88 maintains sensory function by localising signalling proteins alongLife science alliance · 2024Article
- The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024Review
67 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tetratricopeptide repeat (TPR) motif is one of many repeat motifs that form structural domains in proteins that can act as interaction scaffolds in the formation of multi-protein complexes involved in numerous cellular processes such as transcription, the cell cycle, protein translocation, protein degradation and host defence against invading pathogens. The crystal structures of many TPR domain-containing proteins have been determined, showing TPR motifs as two anti-parallel α-helices packed in tandem arrays to form a structure with an amphipathic groove which can bind a target peptide. This is however not the only mode of target recognition by TPR domains, with short amino acid insertions and alternative TPR motif conformations also shown to contribute to protein interactions, highlighting diversity in TPR domains and the versatility of this structure in mediating biological events.
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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.