ReviewPhysical biology2011
Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.
Review in Physical biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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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Who cites it
57 citing papers in PubMed.
- Protein Self-Interaction in Cellular Function and Network Evolution: Molecular Mechanisms, AI-Driven Insights, and Therapeutic Potentials.International journal of molecular sciences · 2026Review
- Homo-oligomeric forms of lectins: their structural insights for glycan binding from the genus Canavalia.Glycoconjugate journal · 2026Article
- Phosphatidylinositol 4,5-bisphosphate mediates Arl4D self-interaction to promote Pak1 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Activation of NF-κB Signaling by Optogenetic Clustering of IKKα and β.Advanced biology · 2025Article
- From Monomers to Hexamers: A Theoretical Probability of the Neighbor Density Approach to Dissect Protein Oligomerization in Cells.Analytical chemistry · 2024Article
- Functional advantages of building nanosystems using multiple molecular components.Nature chemistry · 2023Article
- Dominance analysis of competing protein assembly pathways.PloS one · 2023Article
- Oligomeric interactions maintain active-site structure in a noncooperative enzyme family.The EMBO journal · 2022Article
- Structural plasticity enables evolution and innovation of RuBisCO assemblies.Science advances · 2022Article
- Evolution of homo-oligomerization of methionine S-adenosyltransferases is replete with structure-function constrains.Protein science : a publication of the Protein Society · 2022Article
- Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad.Chemical science · 2022Article
- Designed protein multimerization and polymerization for functionalization of proteins.Biotechnology letters · 2022Review
- A novel assay that characterizes properdin function shows neutrophil-derived properdin has a distinct oligomeric distribution.Frontiers in immunology · 2022Article
- Unraveling a Ligand-Induced Twist of a Homodimeric Enzyme by Pulsed Electron-Electron Double Resonance.Angewandte Chemie (International ed. in English) · 2021Article
- Heterodimer Formation of the Homodimeric ABC Transporter OpuA.International journal of molecular sciences · 2021Article
- Molecular basis for protein-protein interactions.Beilstein journal of organic chemistry · 2021Review
- Disulfide Reduction Allosterically Destabilizes the β-Ladder Subdomain Assembly within the NS1 Dimer of ZIKV.Biophysical journal · 2020Article
- NMR pseudocontact shifts in a symmetric protein homotrimer.Journal of biomolecular NMR · 2020Article
- Establishment and characterization of silver-resistant Enterococcus faecalis.Folia microbiologica · 2020Article
- NLPEI: A Novel Self-Interacting Protein Prediction Model Based on Natural Language Processing and Evolutionary Information.Evolutionary bioinformatics online · 2020Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Many soluble and membrane proteins form homooligomeric complexes in a cell which are responsible for the diversity and specificity of many pathways, may mediate and regulate gene expression, activity of enzymes, ion channels, receptors, and cell adhesion processes. The evolutionary and physical mechanisms of oligomerization are very diverse and its general principles have not yet been formulated. Homooligomeric states may be conserved within certain protein subfamilies and might be important in providing specificity to certain substrates while minimizing interactions with other unwanted partners. Moreover, recent studies have led to a greater awareness that transitions between different oligomeric states may regulate protein activity and provide the switch between different pathways. In this paper we summarize the biological importance of homooligomeric assemblies, physico-chemical properties of their interfaces, experimental and computational methods for their identification and prediction. We particularly focus on homooligomer evolution and describe the mechanisms to develop new specificities through the formation of different homooligomeric complexes. Finally, we discuss the possible role of oligomeric transitions in the regulation of protein activity and compile a set of experimental examples with such regulatory mechanisms.
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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.