-
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
-
Mashup Score: 2CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature - 2 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-
In the #CRISPR toolkit, Cas12a2 is like a Swiss Army Knife—Now, researchers shed light on its nuclease activity by solving its structure. Using #cryoEM, the team reports structures of Cas12a2 in binary, ternary, and quaternary complexes... Learn more: https://t.co/JYOQlDSigy https://t.co/5julWeLHLB
-
-
Mashup Score: 2CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature - 2 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-
CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature #CryoEM provides a structural basis for CRISPR-Cas12a2's mechanism of abortive infection to achieve population-level immunity. Learn more: https://t.co/ict80fgSUu https://t.co/j9dsPV9WCH
-
-
Mashup Score: 0CRISPR-Cas12a2's Structure Reveals Its Indiscriminate Nature - 2 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-
In the #CRISPR toolkit, Cas12a2 is like a Swiss Army Knife—Now, researchers shed light on its nuclease activity by solving its structure. Using #cryoEM, the team reports structures of Cas12a2 in binary, ternary, and quaternary complexes... Learn more: https://t.co/JYOQlDSigy https://t.co/SmlHf6436m
-
-
Mashup Score: 3Structure of the reduced microsporidian proteasome bound by PI31-like peptides in dormant spores - Nature Communications - 2 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 from @Barandunlab report the structure of a compacted microsporidian proteasome bound by an endogenous inhibitory protein. @kai_ehrenbolger #microsporidia #cryoEM https://t.co/jqwAgCfePU https://t.co/GdxBRZANSa
-
-
Mashup Score: 0Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3 - Nature Communications - 2 year(s) ago
The deamination of all adenosines in the wobble base position is essential to empower the individual tRNA to decode several codons. Here, the authors present the cryo-EM structure of the tRNA-bound ADAT2/3 deaminase, revealing how the geometry-specific enzyme acquiesces sequence-divergent tRNAs to its active site.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Researchers @lgdolce and @emblgrenoble from @emblgrenoble present the cryo-EM structure of the tRNA-bound ADAT2/3 deaminase. #cryoEM https://t.co/pitcc0orVH https://t.co/wGrQ8KsdpN
-
-
Mashup Score: 0Understanding VPAC receptor family peptide binding and selectivity - Nature Communications - 2 year(s) ago
Previously, peptide selectivity in the VPAC receptor family of GPCRs was poorly understood. Here, authors combine cryo-EM and MD data to understand binding and selectivity of VPAC1R and PAC1R peptide agonists that can guide future drug development.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
"The authors @SarahJ_Piper, @PatrickMSexton1, @denise_wootten and others from @CCeMMP, @MIPS_DDB report insights into the binding and selectivity of VPAC1R and PAC1R peptide agonists #GPCR #CryoEM https://t.co/B4Za1mpGY3 https://t.co/Q3GLWA5GDy
-
-
Mashup Score: 1
Chronic pain is an extremely common disease that affects about 20% people of general population. Given the shortage of effective and non-addictive
Source: Mirage NewsCategories: Healthcare Professionals, Latest HeadlinesTweet-
Researchers Provide Structural Insights into NaV1.7 Modulation by Inhibitors https://t.co/jPHggDiiMm #VoltageGated #channels #Pain #ChronicPain #analgesics Structural basis for #NaV1_7 inhibition by #poreblockers https://t.co/yf9FZdbpe9 #cryoEM
-
-
Mashup Score: 6Atomic model of vesicular stomatitis virus and mechanism of assembly - Nature Communications - 3 year(s) ago
Zhou and Si et al. used cryogenic electron microscopy and tomography to delineate the molecular interactions among genomic RNA, nucleocapsid protein, matrix protein and glycoprotein in vesicular stomatitis virus and suggest a model of assembly.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Atomic model of vesicular stomatitis virus and mechanism of assembly @zhou_lab #virology #CryoEM #structures https://t.co/jjWNxBuiYM https://t.co/dR7LfJM8U4
-
-
Mashup Score: 2Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor - Nature Communications - 3 year(s) ago
Meprin α is a proteolytic regulator of the extracellular matrix that forms enormous oligomeric filaments of unknown purpose. Here, the authors determine by cryo-EM the structural basis of the meprin supercoiled filament and further characterise a small molecule inhibitor bound to its active site.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Here, the authors @bj_charles, @LuptonCJ, @ClaudiaSpahn3 determine by cryo-EM the structural basis of the meprin supercoiled filament & characterise a small molecule inhibitor bound to its active site. #proteases, #ECM, #cryoEM, #cryoET, #filamentous https://t.co/E0wYZwqQ9k https://t.co/MbxV1jFLwP
-
#CryoEM Incites a “Resolution Revolution,” Rousing #DrugDiscovery Once derided as “blobology,” cryo-electron microscopy is being celebrated for bringing structure-based drug design into focus. Read more: https://t.co/yvHi53SSh8 https://t.co/A4gBGE3CuB