ArticleThe EMBO journal2003
Structural determinants for the binding of ubiquitin-like domains to the proteasome.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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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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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.
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Who cites it
54 citing papers in PubMed, 125 citations in OpenAlex.
- The EF-hand domain of MINDY3 is a ubiquitin and RAD23 UBL-binding domain.EMBO reports · 2026Article
- Enhanced Protein-Protein Interaction Discovery via AlphaFold-Multimer.bioRxiv : the preprint server for biology · 2024Article
- Article
- Proteasome substrate receptors and their therapeutic potential.Trends in biochemical sciences · 2022Review
- Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.The FEBS journal · 2021Review
- Structure of hRpn10 Bound to UBQLN2 UBL Illustrates Basis for Complementarity between Shuttle Factors and Substrates at the Proteasome.Journal of molecular biology · 2019Article
- Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018Review
- Article
- Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets.Nature communications · 2017Article
- Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.Cell chemical biology · 2017Article
- Investigation of the adaptor protein PLIC-2 in multiple pathways.Biochemistry and biophysics reports · 2017Article
- (1)H, (15)N, (13)C resonance assignments for Saccharomyces cerevisiae Rad23 UBL domain.Biomolecular NMR assignments · 2016Article
- Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family.Scientific reports · 2016Article
- Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome.Structure (London, England : 1993) · 2016Article
- Characterization of the 26S proteasome network in Plasmodium falciparum.Scientific reports · 2015Article
- TaUBA, a UBA domain-containing protein in wheat (Triticum aestivum L.), is a negative regulator of salt and drought stress response in transgenic Arabidopsis.Plant cell reports · 2015Article
- The F-box protein FBXO7 positively regulates bone morphogenetic protein-mediated signaling through Lys-63-specific ubiquitination of neurotrophin receptor-interacting MAGE (NRAGE).Cellular and molecular life sciences : CMLS · 2015Article
- VWA domain of S5a restricts the ability to bind ubiquitin and Ubl to the 26S proteasome.Molecular biology of the cell · 2014Article
- Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features.Antiviral research · 2014Article
- Differential expression of 26S proteasome subunits and functional activity during neonatal development.Biomolecules · 2014Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
HHR23A, a protein implicated in nucleotide excision repair, belongs to a class of proteins containing both a ubiquitin-like (Ubl) domain and one or more ubiquitin-associated (UBA) domains, suggesting a role in the ubiquitin-proteasome pathway as well. The Ubl domain binds with high affinity to the second ubiquitin-interacting motif (UIM) of the S5a subunit of the proteasome. Here we present the solution structures of the HHR23A Ubl domain, the second UIM of S5a (UIM-2), and the Ubl:S5a-UIM-2 complex. The HHR23A Ubl domain is structurally similar to ubiquitin. The S5a UIM forms an alpha-helix with an unexpected hairpin loop that contributes to the binding interface with Ubl. The molecular determinants of the Ubl-proteasome interaction are revealed by analysis of the structures, chemical shift mapping, mutant binding studies and sequence conservation.
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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.