ArticleProteins2007
High incidence of ubiquitin-like domains in human ubiquitin-specific proteases.
Article in Proteins, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
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.
Who cites it
25 citing papers in PubMed, 64 citations in OpenAlex.
- Ubiquitin-specific peptidase-19 links TDP-43 aggregation to ER stress.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Caspase 3-specific cleavage of ubiquitin-specific peptidase 48 enhances drug-induced apoptosis in AML.Cancer biology & therapy · 2025Article
- AKT and DUBs: a bidirectional relationship.Cellular & molecular biology letters · 2025Review
- Integrative and comprehensive pan-cancer analysis of ubiquitin specific peptidase 11 (Heliyon · 2024Article
- Genome-wide screening for deubiquitinase subfamily identifies ubiquitin-specific protease 49 as a novel regulator of odontogenesis.Cell death and differentiation · 2022Article
- The Dual Role of USP11 in Cancer.Journal of oncology · 2022Review
- Regulation of Wnt Signaling through Ubiquitination and Deubiquitination in Cancers.International journal of molecular sciences · 2020Review
- Discovery of peptide ligands targeting a specific ubiquitin-like domain-binding site in the deubiquitinase USP11.The Journal of biological chemistry · 2019Article
- USP7: Novel Drug Target in Cancer Therapy.Frontiers in pharmacology · 2019Article
- The Regulations of Deubiquitinase USP15 and Its Pathophysiological Mechanisms in Diseases.International journal of molecular sciences · 2017Review
- X-ray Structure and Enzymatic Activity Profile of a Core Papain-like Protease of MERS Coronavirus with utility for structure-based drug design.Scientific reports · 2017Article
- PCNA-Dependent Cleavage and Degradation of SDE2 Regulates Response to Replication Stress.PLoS genetics · 2016Article
- Recent Advances in the Discovery of Deubiquitinating Enzyme Inhibitors.Progress in medicinal chemistry · 2016Review
- Structural Characterization of Interaction between Human Ubiquitin-specific Protease 7 and Immediate-Early Protein ICP0 of Herpes Simplex Virus-1.The Journal of biological chemistry · 2015Article
- Murine coronavirus ubiquitin-like domain is important for papain-like protease stability and viral pathogenesis.Journal of virology · 2015Article
- The DUSP-Ubl domain of USP4 enhances its catalytic efficiency by promoting ubiquitin exchange.Nature communications · 2014Article
- Structure and catalytic regulatory function of ubiquitin specific protease 11 N-terminal and ubiquitin-like domains.Biochemistry · 2014Article
- Ubiquitin-specific protease 9x deubiquitinates and stabilizes the spinal muscular atrophy protein-survival motor neuron.The Journal of biological chemistry · 2012Article
- Review
- Autoregulation of Parkin activity through its ubiquitin-like domain.The EMBO journal · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitin-specific proteases (USPs) emerge as key regulators of numerous cellular processes and account for the bulk of human deubiquitinating enzymes (DUBs). Their modular structure, mostly annotated by sequence homology, is believed to determine substrate recognition and subcellular localization. Currently, a large proportion of known human USP sequences are not annotated either structurally or functionally, including regions both within and flanking their catalytic cores. To extend the current understanding of human USPs, we applied consensus fold recognition to the unannotated content of the human USP family. The most interesting discovery was the marked presence of reliably predicted ubiquitin-like (UBL) domains in this family of enzymes. The UBL domain thus appears to be the most frequently occurring domain in the human USP family, after the characteristic catalytic domain. The presence of multiple UBL domains per USP protein, as well as of UBL domains embedded in the USP catalytic core, add to the structural complexity currently recognized for many DUBs. Possible functional roles of the newly uncovered UBL domains of human USPs, including proteasome binding, and substrate and protein target specificities, are discussed.
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What OpenQuestion holds
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.