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Atomic structure of a nudivirus occlusion body protein determined from a 70-year-old crystal sample

Viral occlusion bodies are robust protein crystals that encapsulate virions of some insect viruses. Here, the authors determine the nudivirus occlusion body structure and describe common principles of occlusion body structure.

Jeremy R. Keown
Adam D. Crawshaw
Jonathan M. Grimes
ResearchOpen Access13 Jul 2023
Nature Communications

Volume: 14, P: 1-10
WNT10A mutation causes ectodermal dysplasia by impairing progenitor cell proliferation and KLF4-mediated differentiation

Human WNT10A mutations are associated with dental defects and adult onset ectodermal dysplasia. Xuet al. show that WNT10A-activated ß-catenin plays dual roles in adult epithelial progenitor proliferation and differentiation by complexing with KLF4 in differentiating, but not proliferating, cells.

Mingang Xu
Jeremy Horrell
Sarah E. Millar
ResearchOpen Access07 Jun 2017
Nature Communications

Volume: 8, P: 1-21
Spatial mapping of cellular senescence: emerging challenges and opportunities

SenNet Consortium members review current and emerging methodologies for spatially resolved mapping of senescent cells. They discuss their limitations and challenges involved in the aim of creating a comprehensive atlas of senescent cells during aging.

Aditi U. Gurkar
Akos A. Gerencser
João F. Passos
Reviews03 Jul 2023
Nature Aging

Volume: 3, P: 776-790
Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases

Dom Bellini
Sam Horrell
Martin A. Walsh
ResearchOpen Access10 Feb 2017
Scientific Reports

Volume: 7, P: 1-11

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Atomic structure of a nudivirus occlusion body protein determined from a 70-year-old crystal sample

WNT10A mutation causes ectodermal dysplasia by impairing progenitor cell proliferation and KLF4-mediated differentiation

Spatial mapping of cellular senescence: emerging challenges and opportunities

Dimerisation induced formation of the active site and the identification of three metal sites in EAL-phosphodiesterases

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