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Mashup Score: 1
The results of the Osaka University study might contribute to the design of novel drugs for diseases such as cancer.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 6
The APOBEC3 (A3) proteins are host antiviral cellular proteins that hypermutate the viral genome of diverse viral families. In retroviruses, this process requires A3 packaging into viral particles1-4. The lentiviruses encode a protein Vif that antagonizes A3 family members by targeting them for degradation. Diversification of A3 allows host escape from Vif whereas adaptations in Vif enable…
Source: NatureCategories: Hem/Onc News and Journals, Latest HeadlinesTweet-
Paper out today in the Accelerated Article Preview of @Nature reports the #cryoEM structure of APOBEC3G in complex with the #HIV protein Vif and co-factors. Fred Hutch's @memerman lab contributed the functional and evolutionary validation of the structure. https://t.co/10oistYEqy https://t.co/vU0wmJB1lb
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Mashup Score: 0
The results of the Osaka University study might contribute to the design of novel drugs for diseases such as cancer.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 1How the SPOP Protein Plays a Role in Cancer - 1 year(s) ago
SPOP is the most mutated protein in prostate cancer. However, it is not fully understood how SPOP mutations drive cancer. Now, scientists at St. Jude Children’s Research Hospital report they have used cryo-electron microscopy (cryo-EM) to capture the first 3D structure of the entire SPOP assembly.
Categories: Future of Medicine, Latest HeadlinesTweet-
Scientists at St. Jude Children’s Research Hospital report they have used cryo-electron microscopy (#cryoEM) to capture the first 3D structure of the entire SPOP assembly. Their findings provide insights into how SPOP mutations drive #cancer. Read more: https://t.co/NiP2KweUtt https://t.co/Yg3oEKfz1H
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Mashup Score: 4
Once derided as “blobology,” cryo-electron microscopy is being celebrated for bringing structure-based drug design into focus.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 4
Once derided as “blobology,” cryo-electron microscopy is being celebrated for bringing structure-based drug design into focus.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 2CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature - 1 year(s) ago
Cryo-EM provides a structural basis for CRISPR-Cas12a2’s mechanism of abortive infection to achieve population-level immunity.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 2CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature - 1 year(s) ago
Cryo-EM provides a structural basis for CRISPR-Cas12a2’s mechanism of abortive infection to achieve population-level immunity.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 0CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature - 1 year(s) ago
Cryo-EM provides a structural basis for CRISPR-Cas12a2’s mechanism of abortive infection to achieve population-level immunity.
Categories: Future of Medicine, Latest HeadlinesTweet
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Mashup Score: 3Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores - Nature Communications - 1 year(s) ago
Proteasomes are vital eukaryotic complexes that recycle unneeded proteins. Here, the authors present the structure of a compacted proteasome derived from the dormant stage of parasitic microsporidia and bound by an endogenous inhibitory protein.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet
Researchers at @osaka_univ_e say they clarified the structure of the centromeric region in chicken cells using #cryoEM. The results of their work could prove invaluable in advancing knowledge of cell division and growth. Learn more: https://t.co/Cx5iIloVno https://t.co/DYRww9AKsX