ReviewComputational and structural biotechnology journal2014
NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
Review in Computational and structural biotechnology journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Binding of Hg(I) and Hg(II) Ions to Amyloid-Beta (Aβ) Peptide Variants Affect their Structure and Aggregation.Chembiochem : a European journal of chemical biology · 2025Article
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- Residue-specific binding of Ni(II) ions influences the structure and aggregation of amyloid beta (Aβ) peptides.Scientific reports · 2023Article
- Choosing an Optimal Solvent Is Crucial for Obtaining Cell-Penetrating Peptide Nanoparticles with Desired Properties and High Activity in Nucleic Acid Delivery.Pharmaceutics · 2023Article
- Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1.Biophysical journal · 2022Article
- Structural characterization of the self-association domain of swallow.Protein science : a publication of the Protein Society · 2021Article
- Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing ineLife · 2021Article
- Article
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
- The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex.Biochemistry · 2016Article
- Dynein Light Chain LC8 Is Required for RNA Polymerase I-Mediated Transcription in Trypanosoma brucei, Facilitating Assembly and Promoter Binding of Class I Transcription Factor A.Molecular and cellular biology · 2016Article
- Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.FEBS letters · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Most proteins in interaction networks have a small number of partners, while a few, called hubs, participate in a large number of interactions and play a central role in cell homeostasis. One highly conserved hub is a protein called LC8 that was originally identified as an essential component of the multi-subunit complex dynein but later shown to be also critical in multiple protein complexes in diverse systems. What is intriguing about this hub protein is that it does not passively bind its various partners but emerging evidence suggests that LC8 acts as a dimerization engine that promotes self-association and/or higher order organization of its primarily disordered monomeric partners. This structural organization process does not require ATP but is triggered by long-range allosteric regulation initiated by LC8 binding a pair of disordered chains forming a bivalent or polybivalent scaffold. This review focuses on the role of LC8 in promoting self-association of two of its binding partners, a dynein intermediate chain and a non dynein protein called Swallow.
Identifiers
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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.