ReviewCritical reviews in biochemistry and molecular biology2019
The ZZ domain as a new epigenetic reader and a degradation signal sensor.
Review in Critical reviews in biochemistry and molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 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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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Integrated analysis uncoversInternational journal of medical sciences · 2026Article
- Review
- Histone Readers and Their Roles in Cancer.Cancer treatment and research · 2023Article
- Beyond the marks: reader-effectors as drivers of epigenetics and chromatin engineering.Trends in biochemical sciences · 2022Review
- The ZZ domain of HERC2 is a receptor of arginylated substrates.Scientific reports · 2022Article
- ZZ domains keep cytosol to vacuole delivery whiZZing along.The EMBO journal · 2021Article
- Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.The EMBO journal · 2021Article
- Article
- The Carcinogen Cadmium Activates Lysine 63 (K63)-Linked Ubiquitin-Dependent Signaling and Inhibits Selective Autophagy.Cancers · 2021Article
- The Ada2/Ada3/Gcn5/Sgf29 histone acetyltransferase module.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- The SAGA continues: The rise of cis- and trans-histone crosstalk pathways.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021Review
- ZZEF1 is a Histone Reader and Transcriptional Coregulator of Krüppel-Like Factors.Journal of molecular biology · 2021Article
- Natural variation in the sequestosome-related gene, sqst-5, underlies zinc homeostasis in Caenorhabditis elegans.PLoS genetics · 2020Article
- The SAGA chromatin-modifying complex: the sum of its parts is greater than the whole.Genes & development · 2020Review
- Domain cross-talk in regulation of histone modifications: Molecular mechanisms and targeting opportunities.Current opinion in chemical biology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Although relatively small in size, the ZZ-type zinc finger (ZZ) domain is a versatile signaling module that is implicated in a diverse set of cell signaling events. Here, we highlight the most recent studies focused on the ZZ domain function as a histone reader and a sensor of protein degradation signals. We review and compare the molecular and structural mechanisms underlying targeting the amino-terminal sequences of histone H3 and arginylated substrates by the ZZ domain. We also discuss the ZZ domain sensitivity to histone PTMs and summarize biological outcomes associated with the recognition of histone and non-histone ligands by the ZZ domain-containing proteins and complexes.
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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.