Results 121 to 130 of about 175,539 (259)

Methodological Insights from Low-Vacuum SEM for Morphological Analysis of Schwann Cells on Electrospun Scaffolds. [PDF]

open access: yesPolymers (Basel)
Salazar-Aguilar P   +6 more
europepmc   +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

Biophysical approaches for studying viral entry

open access: yesFEBS Letters, EarlyView.
Viruses infect all living organisms and have been responsible for major epidemics and pandemics. Their ongoing evolutionary battle with host defenses creates a constant need for improved tools to study viral behavior. Advancing methods to probe viral attachment, fusion, and genome release deepen our understanding of how infections begin and support the
Inbar Yosibash, Raya Sorkin
wiley   +1 more source

The human gut microbiome across the life course

open access: yesFEBS Letters, EarlyView.
Despite significant individual variation and continuous change throughout life, the human gut microbiome follows some life stage‐specific trends. This article provides a brief overview of how gut microbiome composition shifts across different phases of life. Created in BioRender. Özkurt, E. (2026) https://BioRender.com/8q4nrnc.
Alise J. Ponsero   +4 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

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

Extensive Games

open access: yesProceedings of the National Academy of Sciences, 1950
openaire   +4 more sources

Home - About - Disclaimer - Privacy