ArticleInternational journal of molecular sciences2024
A Comprehensive Analysis of the Structural Recognition between KCTD Proteins and Cullin 3.
Article in International journal of molecular sciences, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- A Global Analysis of the Complex Structural Organization of KCTD Proteins and Their Functional Implications.International journal of molecular sciences · 2026Review
- Survey of the human proteostasis network: the ubiquitin-proteasome system.bioRxiv : the preprint server for biology · 2026Article
- Cullin-3 adaptor SHKBP1 inhibits SQSTM1/p62 oligomerization and Keap1 sequestration.The Journal of cell biology · 2026Article
- Article
- Unraveling the role of Cullin3 of E3 ubiquitin ligase in salt stress tolerance via proteomics.BMC plant biology · 2025Article
- Determinants of Chain Selection and Staggering in Heterotrimeric Collagens: A Comprehensive Review of the Structural Data.International journal of molecular sciences · 2025Review
- Report of the 5th International Symposium on Frontiers in Molecular Science (ISFMS 2025).International journal of molecular sciences · 2025Article
- Mechanistic Insights Into the Tumor-Driving and Diagnostic Roles of KCTD Family Genes in Ovarian Cancer: An Integrated In Silico and In Vitro Analysis.Cancer medicine · 2025Article
- Structural Biology in the AlphaFold Era: How Far Is Artificial Intelligence from Deciphering the Protein Folding Code?Biomolecules · 2025Review
- Analysis of cullin family genes in rectal adenocarcinoma: expression, prognostic significance, and therapeutic implications.American journal of translational research · 2025Article
- KCTD Proteins Have Redundant Functions in Controlling Cellular Growth.International journal of molecular sciences · 2024Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
KCTD ((K)potassium Channel Tetramerization Domain-containing) proteins constitute an emerging class of proteins involved in fundamental physio-pathological processes. In these proteins, the BTB domain, which represents the defining element of the family, may have the dual role of promoting oligomerization and favoring functionally important partnerships with different interactors. Here, by exploiting the potential of recently developed methodologies for protein structure prediction, we report a comprehensive analysis of the interactions of all KCTD proteins with their most common partner Cullin 3 (Cul3). The data here presented demonstrate the impressive ability of this approach to discriminate between KCTDs that interact with Cul3 and those that do not. Indeed, reliable and stable models of the complexes were only obtained for the 15 members of the family that are known to interact with Cul3. The generation of three-dimensional models for all KCTD-Cul3 complexes provides interesting clues on the determinants of the structural basis of this partnership as clear structural differences emerged between KCTDs that bind or do not bind Cul3. Finally, the availability of accurate three-dimensional models for KCTD-Cul3 interactions may be valuable for the ad hoc design and development of compounds targeting specific KCTDs that are involved in several common diseases.
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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 Socratic graph.