Un Seng Chio
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Explore the profile of Un Seng Chio including associated specialties, affiliations and a list of published articles.
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23
Citations
841
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Recent Articles
1.
Moore C, Wong E, Kaur U, Chio U, Zhou Z, Ostrowski M, et al.
bioRxiv
. 2024 Sep;
PMID: 39314305
ATP-dependent chromatin remodeling enzymes mobilize nucleosomes, but how such mobilization affects chromatin condensation is unclear. Here, we investigate effects of two major remodelers, ACF and RSC using chromatin condensates and...
2.
Saunders H, Chio U, Moore C, Ramani V, Cheng Y, Narlikar G
bioRxiv
. 2024 Sep;
PMID: 39229246
The essential architectural protein HMGB1 increases accessibility of nucleosomal DNA and counteracts the effects of linker histone H1. However, HMGB1 is less abundant than H1 and binds nucleosomes more weakly...
3.
Chio U, Palovcak E, Smith A, Autzen H, Munoz E, Yu Z, et al.
Nat Commun
. 2024 Mar;
15(1):2225.
PMID: 38472177
Single-particle cryo-EM is widely used to determine enzyme-nucleosome complex structures. However, cryo-EM sample preparation remains challenging and inconsistent due to complex denaturation at the air-water interface (AWI). Here, to address...
4.
Abdulhay N, Hsieh L, McNally C, Ostrowski M, Moore C, Ketavarapu M, et al.
Nat Struct Mol Biol
. 2023 Sep;
30(10):1571-1581.
PMID: 37696956
Nearly all essential nuclear processes act on DNA packaged into arrays of nucleosomes. However, our understanding of how these processes (for example, DNA replication, RNA transcription, chromatin extrusion and nucleosome...
5.
Chio U, Palovcak E, Autzen A, Autzen H, Munoz E, Yu Z, et al.
bioRxiv
. 2023 Aug;
PMID: 37546986
Single-particle cryo-EM is widely used to determine enzyme-nucleosome complex structures. However, cryo-EM sample preparation remains challenging and inconsistent due to complex denaturation at the air-water interface (AWI). To address this...
6.
Wu H, Munoz E, Hsieh L, Chio U, Gourdet M, Narlikar G, et al.
Science
. 2023 Jun;
381(6655):319-324.
PMID: 37384669
Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of INO80 bound to a...
7.
Gupta A, Lentzsch A, Siegel A, Yu Z, Chio U, Cheng Y, et al.
Sci Adv
. 2023 May;
9(19):eadf5336.
PMID: 37163603
Ring-forming AAA chaperones solubilize protein aggregates and protect organisms from proteostatic stress. In metazoans, the AAA chaperone Skd3 in the mitochondrial intermembrane space (IMS) is critical for human health and...
8.
Chio U, Rechiche O, Bryll A, Zhu J, Leith E, Feldman J, et al.
Sci Adv
. 2023 Apr;
9(15):eadf7586.
PMID: 37058572
Sirtuin 6 (SIRT6) is a multifaceted protein deacetylase/deacylase and a major target for small-molecule modulators of longevity and cancer. In the context of chromatin, SIRT6 removes acetyl groups from histone...
9.
Chio U, Rechiche O, Bryll A, Zhu J, Feldman J, Peterson C, et al.
bioRxiv
. 2023 Mar;
PMID: 36993468
Teaser: The structure of the SIRT6 deacetylase/nucleosome complex suggests how the enzyme acts on both histone H3 K9 and K56 residues.
10.
Remesh S, Merz G, Brilot A, Chio U, Rizo A, Pospiech Jr T, et al.
Structure
. 2023 Feb;
31(3):253-264.e6.
PMID: 36805129
The SARS-CoV-2 Omicron variant, with 15 mutations in Spike receptor-binding domain (Spike-RBD), renders virtually all clinical monoclonal antibodies against WT SARS-CoV-2 ineffective. We recently engineered the SARS-CoV-2 host entry receptor,...