Human Polyhomeotic Homolog 3 (PHC3) Sterile Alpha Motif (SAM) Linker Allows Open-Ended Polymerization of PHC3 SAM
Author:
Affiliation:
1. Department of Biochemistry and CTRC, University of Texas Health Science Center at San Antonio, MSC 7760, 7703 Floyd Curl Drive, San Antonio, Texas 78229-3990, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi3004318
Reference27 articles.
1. SAM domains: uniform structure, diversity of function
2. The Many Faces of SAM
3. Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression
4. Structural Organization of a Sex-comb-on-midleg/Polyhomeotic Copolymer
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1. Structural analysis of the SAM domain of the Arabidopsis mitochondrial tRNA import receptor;Journal of Biological Chemistry;2024-05
2. CBX7C⋅PHC2 interaction facilitates PRC1 assembly and modulates its phase separation properties;iScience;2024-04
3. Structural analysis of the Sterile alpha motif (SAM) domain of the Arabidopsis mitochondrial tRNA import receptor;2023-11-20
4. How a disordered linker in the Polycomb protein Polyhomeotic tunes phase separation and oligomerization;2023-10-27
5. Polycomb condensates can promote epigenetic marks but are not required for sustained chromatin compaction;Nature Communications;2021-10-07
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