ReviewCurrent opinion in structural biology2011
A new chapter in the transcription SAGA.
Review in Current opinion in structural biology, 2011. 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, 56 citations in OpenAlex.
- Histone acetyltransferase Gcn5-mediated histone H3 acetylation facilitates cryptococcal morphogenesis and sexual reproduction.mSphere · 2023Article
- Sus1 maintains a normal lifespan through regulation of TREX-2 complex-mediated mRNA export.Aging · 2022Article
- Nuclear mRNA Export and Aging.International journal of molecular sciences · 2022Review
- Molecular Mechanisms of DUBs Regulation in Signaling and Disease.International journal of molecular sciences · 2021Review
- Dissenting degradation: Deubiquitinases in cell cycle and cancer.Seminars in cancer biology · 2020Review
- SAGA-CORE subunit Spt7 is required for correct Ubp8 localization, chromatin association and deubiquitinase activity.Epigenetics & chromatin · 2020Article
- Proteomic analysis of Drosophila CLOCK complexes identifies rhythmic interactions with SAGA and Tip60 complex component NIPPED-A.Scientific reports · 2020Article
- Prp5-Spt8/Spt3 interaction mediates a reciprocal coupling between splicing and transcription.Nucleic acids research · 2020Article
- Yeast two-hybrid screening reveals a dual function for the histone acetyltransferase GcnE by controlling glutamine synthesis and development in Aspergillus fumigatus.Current genetics · 2019Article
- Functional interplay between TFIIH and KAT2A regulates higher-order chromatin structure and class II gene expression.Nature communications · 2019Article
- Structural basis for activation of SAGA histone acetyltransferase Gcn5 by partner subunit Ada2.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA.Nucleic acids research · 2017Article
- The Mediator subunit MED23 couples H2B mono-ubiquitination to transcriptional control and cell fate determination.The EMBO journal · 2015Article
- Poly(Q) Expansions in ATXN7 Affect Solubility but Not Activity of the SAGA Deubiquitinating Module.Molecular and cellular biology · 2015Article
- Myc and SAGA rewire an alternative splicing network during early somatic cell reprogramming.Genes & development · 2015Article
- Article
- The Role of Electrostatic Interactions in Binding of Histone H3K4me2/3 to the Sgf29 Tandem Tudor Domain.PloS one · 2015Article
- Architecture of the Saccharomyces cerevisiae SAGA transcription coactivator complex.The EMBO journal · 2014Article
- Histone H2B ubiquitination promotes the function of the anaphase-promoting complex/cyclosome in Schizosaccharomyces pombe.G3 (Bethesda, Md.) · 2014Article
- Functions of SAGA in development and disease.Epigenomics · 2014Review
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
Eukaryotic transcriptional coactivators are multi-subunit complexes that both modify chromatin and recognize histone modifications. Until recently, structural information on these large complexes has been limited to isolated enzymatic domains or chromatin-binding motifs. This review summarizes recent structural studies of the SAGA coactivator complex that have greatly advanced our understanding of the interplay between its different subunits. The structure of the four-protein SAGA deubiquitinating module has provided a first glimpse of the larger organization of a coactivator complex, and illustrates how interdependent subunits interact with each other to form an active and functional enzyme complex. In addition, structures of the histone binding domains of ATXN7 and Sgf29 shed light on the interactions with chromatin that help recruit the SAGA complex.
Indexed as
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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.