ReviewACS chemical biology2012
Unraveling the complexity of ubiquitin signaling.
Review in ACS chemical biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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.
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
28 citing papers in PubMed, 71 citations in OpenAlex.
- Internal Ubiquitin Electrophiles for Covalent Trapping and Inhibition of Deubiquitinases.Chembiochem : a European journal of chemical biology · 2025Article
- CircZFR promotes colorectal cancer progression via stabilizing BCLAF1 and regulating the miR-3127-5p/RTKN2 axis.Science China. Life sciences · 2024Article
- Ubiquitin recruiting chimera: more than just a PROTAC.Biology direct · 2024Review
- Isothiouronium-Mediated Conversion of Carboxylic Acids to Cyanomethyl Thioesters.The Journal of organic chemistry · 2023Article
- Artificially Linked Ubiquitin Dimers Characterised Structurally and Dynamically by NMR Spectroscopy.Chembiochem : a European journal of chemical biology · 2019Article
- Ubiquitination and Long Non-coding RNAs Regulate Actin Cytoskeleton Regulators in Cancer Progression.International journal of molecular sciences · 2019Review
- Regulated Proteolysis in Bacteria.Annual review of biochemistry · 2018Review
- Biological and Physicochemical Functions of Ubiquitylation Revealed by Synthetic Chemistry Approaches.International journal of molecular sciences · 2017Review
- Selective adaptor dependent protein degradation in bacteria.Current opinion in microbiology · 2017Review
- Identification of a novel K311 ubiquitination site critical for androgen receptor transcriptional activity.Nucleic acids research · 2017Article
- Structure and conformational plasticity of the U6 small nuclear ribonucleoprotein core.Acta crystallographica. Section D, Structural biology · 2017Article
- Chemical Protein Ubiquitylation with Preservation of the Native Cysteine Residues.Chembiochem : a European journal of chemical biology · 2016Article
- Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities.Protein science : a publication of the Protein Society · 2016Article
- Multicolor monitoring of the proteasome's catalytic signature.ACS chemical biology · 2015Article
- Review
- Article
- Chemical strategies to understand the language of ubiquitin signaling.Biopolymers · 2014Review
- Further characterization of the target of a potential aptamer biomarker for pancreatic cancer: cyclophilin B and its posttranslational modifications.Nucleic acid therapeutics · 2013Article
- Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Modifying the vicinity of the isopeptide bond to reveal differential behavior of ubiquitin chains with interacting proteins: organic chemistry applied to synthetic proteins.Angewandte Chemie (International ed. in English) · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Protein ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as one of the most prevalent posttranslational modifications (PTMs), regulating nearly every cellular pathway. The diversity of signaling associated with this particular PTM stems from the myriad ways in which a target protein can be modified by ubiquitin, e.g., monoubiquitin, multi-monoubiquitin, and polyubiquitin linkages. In this Review, we focus on developments in both enzymatic and chemical methods that engender ubiquitin with new chemical and physical properties. Moreover, we highlight how these methods have enabled studies directed toward (i) characterizing enzymes responsible for reversing the ubiquitin modification, (ii) understanding the influence of ubiquitin on protein function and crosstalk with other PTMs, and (iii) uncovering the impact of polyubiquitin chain linkage and length on downstream signaling events.
Indexed as
Identifiers
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.