Evidence map›Paper›PMID 38339159›Full record

ArticleInternational journal of molecular sciences2024

A Comprehensive Analysis of the Structural Recognition between KCTD Proteins and Cullin 3.

Nicole Balasco, Luciana Esposito, Giovanni Smaldone, Marco Salvatore, Luigi Vitagliano

Open access · goldAbstract read
In one paragraph

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.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
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  9. Review
  10. Article
  11. KCTD Proteins Have Redundant Functions in Controlling Cellular Growth.International journal of molecular sciences · 2024
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Nicole BalascoInstitute of Molecular Biology and Pathology, CNR c/o Department Chemistry, Sapienza University of Rome, 00185 Rome, Italy.
Luciana EspositoInstitute of Biostructures and Bioimaging, CNR, 80131 Naples, Italy.ORCID 0000-0001-6431-2677
Giovanni SmaldoneIRCCS SYNLAB SDN, 80143 Naples, Italy.ORCID 0000-0002-1989-4740
Marco SalvatoreIRCCS SYNLAB SDN, 80143 Naples, Italy.ORCID 0000-0001-9734-7702
Luigi VitaglianoInstitute of Biostructures and Bioimaging, CNR, 80131 Naples, Italy.ORCID 0000-0002-3032-3375
Institute of Biostructure and Bioimaging · ITInstitute of Molecular Biology and Pathology · IT

Funding

Governo Italiano CN1 PNRR
6 · The paper itself

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.

Indexed as

Cullin ProteinsPotassium ChannelsAmino Acid SequenceHumansProtein BindingProtein MultimerizationCUL3 protein, humanCullin ProteinsPotassium ChannelsCul3 recognitionKCTD proteinsoligomeric stateprotein structure-functionprotein structure prediction

Identifiers

PMID38339159
PMCPMC10856315
OpenAlexW4391533494

What Socratic holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.