Ojore Oka

901 posts

Ojore Oka

Ojore Oka

@ojoreoka

Research focuses on how proteins fold in the Endoplasmic Reticulum (ER) and mechanisms that cause cell stress and how cells adapt under stress conditions.

Katılım Eylül 2012
310 Takip Edilen245 Takipçiler
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Science Magazine
Science Magazine@ScienceMagazine·
Plant cells undergo incomplete division and remain connected. This image illustrates two daughter cells linked by strands of endoplasmic reticulum spanning plasmodesmata—tiny bridges for intercellular communication. New findings in Science reveal that the endoplasmic reticulum holds these bridges open during cell division; without it, plasmodesmata close, addressing a long-standing question about how to combine cell division and communication. bit.ly/3C5Urfe
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UK Dementia Research Institute
Image 5 of 5: AstrocytER The endoplasmic reticulum (ER), a network of membranes through which proteins and other molecules move, is stained within astrocytes, the star shaped supporting brain cells. 7/7
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UK Dementia Research Institute
Image 4 of 5: Amyloid Precursor Protein (APP) - an intracellular journey APP produces the toxic amyloid beta protein that forms amyloid plaques in Alzheimer's disease. Researchers found that APP's location in the cell is important for how much amyloid is produced. 6/7
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UK Dementia Research Institute
Image 3 of 5: Super Nova Astrocytes and Microglia eating up amyloid plaques to fight against the build up and damage caused by misfolded amyloid protein. 5/7
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UK Dementia Research Institute
Image 2 of 5: Microglia Pioneers Microglia usually help maintain brain health, but scientists believe they may contribute to the development of Alzheimer's. Here, human microglia (green) grown on a thin slice of mouse brain interact with mouse neurons (red). 4/7
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UK Dementia Research Institute
Image 1 of 5: The First Responders Microglia (red and cyan) respond to amyloid plaque (yellow), one of the hallmarks of Alzheimer’s. Microglia are specialised cells that can take on different roles depending on where and how they are needed. 3/7
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Avezov lab
Avezov lab@AvezovL·
🔔@CecileCrapart talking at #EMBOer24 about her PhD work on how ER structure dictates its function as a Ca2+ delivering device covered in pnas.org/doi/10.1073/pn… and buff.ly/45SSNs3
Avezov lab@AvezovL

Our new paper is out, buff.ly/45SSNs3📄 on how a membrane-curving protein RTN4/Nogo links neurite regeneration and the tubular ER🕸️🧠 It's all about how it narrows tubules, slows luminal transport, restricting Ca2+ supply for the outgrowth puffs ☁️🧑‍🤝‍🧑@koslovergroup 🧵

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The Nobel Prize
The Nobel Prize@NobelPrize·
BREAKING NEWS The Royal Swedish Academy of Sciences has decided to award the 2024 #NobelPrize in Chemistry with one half to David Baker “for computational protein design” and the other half jointly to Demis Hassabis and John M. Jumper “for protein structure prediction.”
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Biochemical Society
Biochemical Society@BiochemSoc·
Final call for Scientific Outreach Grant applications! With different funding levels available, don't miss out on this chance to take your molecular biosciences activities to a new and broader audience. Deadline 9 October! ow.ly/xiTy50TBpNr
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maurizio molinari
maurizio molinari@MolinariLab·
Pre-Ai, hand drawn schematics by Ari Helenius published many years ago. Up there, Ari tells us how enveloped viruses enter our cells. Down below, Ari discovers how our cells check the quality of the proteome. Seminal discoveries. Happy 80th birthday Ari.
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