Typing of <i>Yersinia pestis</i> in Challenging Forensic Samples Through Targeted Next-Generation Sequencing of Multilocus Variable Number Tandem Repeat Regions. [PDF]
Yun H, Lee SH, Gu SH, Lim SH, Song DH.
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Decoding inflammatory regulation in ovarian cancer at single-cell resolution. [PDF]
Yu J +6 more
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Synthesis, physical characteristics, and biocompatibility test of chitosan-alginate-fucoidan scaffold as an alternative material for alveolar bone substitution. [PDF]
Hamrun N +10 more
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Localized 2'-OH Acylation at Poly(A) Extends RNA Translation. [PDF]
Fang L +6 more
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Tuneable hydrogels of Caf1 protein fibers
Materials Science and Engineering: C, 2018Capsular antigen fraction 1 (Caf1) is a robust polymeric protein forming a protective layer around the bacterium Yersinia pestis. Occurring as ≈1 μm polymeric fibers, it shares its immunoglobulin-like fold with the majority of mammalian extracellular proteins such as fibronectin and this structural similarity suggests that this unusual polymer could ...
Gema Dura +4 more
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Conformational states and association mechanism of Yersinia pestis Caf1 subunits
Biochemical and Biophysical Research Communications, 2008Bacterial infectivity often relies on efficient attachment to the host cells through adhesive extensions. Unveiling the structural basis of the formation of these organelles is of paramount importance for both academic and applicative implications.
Vitagliano Luigi +3 more
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The N-terminus modulates human Caf1 activity, structural stability and aggregation
International Journal of Biological Macromolecules, 2012Caf1 is a deadenylase component of the CCR4-Not complex. Here we found that the removal of the N-terminus resulted in a 30% decrease in human Caf1 (hCaf1) activity, but had no significant influence on main domain structure. The removal of the N-terminus led to a decrease in the thermal stability, while the existence of the N-terminus promoted hCaf1 ...
Li-Kui, Feng, Yong-Bin, Yan
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Caf1 regulates Ash1 histone methyltransferase activity via sensing unmodified histone H3
2023AbstractHistone modifications are one of key mechanisms to regulate gene expression. Ash1 is a histone H3K36 methyltransferase and involved in gene activation. Ash1 forms a large complex with Mrg15 and Caf1/p55/Nurf55/RbAp48 (AMC complex). Ash1 subunit alone has very low activity due to the auto-inhibition and the binding of Mrg15 releases the auto ...
Eojin Yoon, Ji-Joon Song
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