ReviewProtein science : a publication of the Protein Society2004
The ankyrin repeat as molecular architecture for protein recognition.
Review in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 429 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.
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
429 citing papers in PubMed.
- Candidate Regulatory Relationship and Expression Correlation Between miR-33a-5p and ANK3 in Chronic Myeloid Leukemia.Current issues in molecular biology · 2026Article
- Histone modification cross talk between a host and pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Genome-Wide Identification and Expression Pattern of theInternational journal of molecular sciences · 2026Article
- ANKRD49 promotes immune evasion in lung adenocarcinoma by activating the MEF2A/PD‑L1 axis.Biology direct · 2026Article
- Histone modification crosstalk between host and pathogen.bioRxiv : the preprint server for biology · 2026Article
- Ankyrin Repeat Domain 1: A Key Regulatory Factor and Emerging Therapeutic Target in Heart Disease.Reviews in cardiovascular medicine · 2026Review
- Sequence and structural alignments reveal insights into ANKLE2 evolution and function.Protein science : a publication of the Protein Society · 2026Article
- A novel CD69 binding ankyrin repeat protein (AnkyronResearch square · 2026Article
- Identification of a putative founder effect involving the HACE1:c.1396C>T variant in two Iranian families and review of reported cases.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026Review
- Article
- The African swine fever virus MGF505-1R protein recruits the cullin-RING-ligase machinery to promote p300 degradation.Npj viruses · 2026Article
- Searching for α-solenoid proteins involved in organellar gene expression.BMC genomics · 2026Article
- Enterocytes rely on purine biosynthesis/salvage pathway to facilitate dietary fat absorption.Nature communications · 2026Article
- Ubiquitin-like SUMO protease expansion in rice (Oryza sativa L.).The plant genome · 2026Article
- ANKRD53 is downregulated in human obesity and coordinates lipolysis with mitochondrial oxidative metabolism in adipocytes.Molecular metabolism · 2026Article
- Recreating viable YYNature communications · 2026Article
- Comparative analysis of 163 ant genomes reveals recurrent horizontal gene transfer from bacteria to ants.GigaScience · 2026Article
- Identification and Classification of Fungal GPCR Gene Families.Journal of fungi (Basel, Switzerland) · 2025Article
- Article
- Regulation of Notch signaling by multiple Ankyrin repeat containing protein Mask.Cell communication and signaling : CCS · 2025Article
369 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
4 authors.
Funding
Abstract
The ankyrin repeat is one of the most frequently observed amino acid motifs in protein databases. This protein-protein interaction module is involved in a diverse set of cellular functions, and consequently, defects in ankyrin repeat proteins have been found in a number of human diseases. Recent biophysical, crystallographic, and NMR studies have been used to measure the stability and define the various topological features of this motif in an effort to understand the structural basis of ankyrin repeat-mediated protein-protein interactions. Characterization of the folding and assembly pathways suggests that ankyrin repeat domains generally undergo a two-state folding transition despite their modular structure. Also, the large number of available sequences has allowed the ankyrin repeat to be used as a template for consensus-based protein design. Such projects have been successful in revealing positions responsible for structure and function in the ankyrin repeat as well as creating a potential universal scaffold for molecular recognition.
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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.