Results 31 to 40 of about 343,528 (265)

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

open access: yesFEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura   +2 more
wiley   +1 more source

Epigenetic blind spots – the role of DNA methylation dynamics in stem cell‐based models of embryogenesis

open access: yesFEBS Letters, EarlyView.
Embryo‐like structures (stembryos) are an innovative tool, but they are hindered by experimental variability and limited developmental potential. DNA methylation is crucial for mammalian development, but its status in stembryo models is poorly characterized.
Sara Canil   +4 more
wiley   +1 more source

Mesoscopic numerical simulation of the dynamic mechanical behavior of concrete containing tunnel slag aggregates

open access: yesResults in Engineering
The utilization of tunnel slag as concrete aggregate is an effective means of achieving resource recycling. This study employs a mesoscopic numerical simulation method to investigate the dynamic mechanical properties of concrete incorporating tunnel slag
Taotao Feng   +3 more
doaj   +1 more source

Residual tail twisting in ascidian larvae is stabilized by asymmetric myofibrils that resist bilateral symmetry restoration

open access: yesFEBS Letters, EarlyView.
Ascidian Ciona larvae initially show strong clockwise tail twisting, which is largely corrected during development. However, a small residual twist remains. This study shows that organized helical myofibrils in tail muscles mechanically stabilize this residual asymmetry, preventing complete restoration of bilateral symmetry and revealing how embryos ...
Yuki S. Kogure   +3 more
wiley   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

The crystal structure of (E)-(2-(2-hydroxy-3-methoxybenzylidene)aminophenyl)arsonic acid, C14H14AsNO5

open access: yesZeitschrift für Kristallographie - New Crystal Structures
C14H14AsNO5, monoclinic, P21 (no. 4), a = 8.5830(5) Å, b = 7.0799(5) Å, c = 11.6011(7) Å, β = 100.059(2)∘, V = 694.13(8) Å3, Z = 2, R gt(F) = 0.0288, wR ref(F 2) = 0.0603, T = 150.0 K.
Cai Bin   +5 more
doaj   +1 more source

Theoretical model of effective elastic moduli of composites considering the inclusion features

open access: yesMaterials & Design
Quantifying the effect of composition on the two-phase composite’s mechanical properties is crucial for the life prediction and durability design of the whole structure.
Xuqian Liu, Zhangyu Wu, Shuohui Chen
doaj   +1 more source

Rab14 regulates the transport of human papillomavirus to the trans‐Golgi network for infectious cell entry

open access: yesFEBS Letters, EarlyView.
This study reveals that the small GTPase Rab14 is necessary for human papillomavirus (HPV) infection and plays an essential role in the transport of virions to the trans‐Golgi network (TGN). HPV in the early endosome (EE), which harbors GTP‐bound Rab14, is transported to the TGN through the switch of Rab14 from its GTP‐bound to GDP‐bound form.
Yoshiyuki Ishii, Iwao Kukimoto
wiley   +1 more source

The crystal structure of (E)-(2-((pyridin-2-ylmethylene)amino)phenyl)arsonic acid, C12H11AsN2O3

open access: yesZeitschrift für Kristallographie - New Crystal Structures
C12H11AsN2O3, monoclinic, P21/c (no. 14), a = 10.1258(10) Å, b = 6.3254(5) Å, c = 19.1102(16) Å, β = 97.578(3)°, V = 1213.31(18) Å3, Z = 4, Rgt(F) = 0.0409, wRref(F2) = 0.1027, T = 150.0 K.
Zhu Ji-De   +5 more
doaj   +1 more source

Degradation mechanism of the von Willebrand factor A2 domain by nattokinase

open access: yesFEBS Letters, EarlyView.
Nattokinase, a natto‐derived protease, exhibits potent antithrombotic effects. This study demonstrates that nattokinase directly cleaves the von Willebrand factor (vWF) A2 domain in vitro. Unlike the native regulator ADAMTS13, nattokinase degrades folded vWF independently of shear stress.
Ryuichi Hyakumoto   +3 more
wiley   +1 more source

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