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Mashup Score: 0Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3 - Nature Communications - 1 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
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Mashup Score: 0Understanding VPAC receptor family peptide binding and selectivity - Nature Communications - 1 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
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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
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Mashup Score: 6Atomic model of vesicular stomatitis virus and mechanism of assembly - Nature Communications - 2 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
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Mashup Score: 2Helical ultrastructure of the metalloprotease meprin α in complex with a small molecule inhibitor - Nature Communications - 2 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
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Mashup Score: 0Structure of the membrane-bound formate hydrogenlyase complex from Escherichia coli - Nature Communications - 2 year(s) ago
New cryo-EM structures of the formate hydrogenlyase complex from the model bacterium E. coli clarify how electrons and protons move through the complex and are combined to make H2 gas. The complex shows important similarities and differences to related bioenergetic complexes across the tree of life.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Scientists from @MPIb, @RalfSteinhilper @_Murphy_Lab report cryoEM structures of the formate-hydrogen lyase complex & clarify how electrons & protons move through the complex & are combined to make H2 gas. #CryoEM #hydrogenase #bioenergetics https://t.co/PH7jLSXXHy https://t.co/M9CTcHAQCO
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Mashup Score: 4Apply - Interfolio - 2 year(s) ago
Fred Hutchinson Cancer Center invites applications for a faculty position in the Division of Basic Sciences. We seek a laboratory scientist conducting outstanding fundamental research into mechanisms that regulate the basic biology of normal or cancer cells. We welcome applications from candidates in the broad areas of molecular, cellular and/or structural biology. Of special interest are…
Source: apply.interfolio.comCategories: Hem/Onc News and Journals, Latest HeadlinesTweet-
We're #hiring for a faculty position in our Basic Sciences Division (@HutchBasicSci)! Of special interest are candidates who have expertise in #CryoEM and/or #CryoET. Learn more and apply: https://t.co/tgDBtR4FcL https://t.co/lzETOUXivS
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Mashup Score: 3Apply - Interfolio - 2 year(s) ago
Fred Hutchinson Cancer Center invites applications for a faculty position in the Division of Basic Sciences. We seek a laboratory scientist conducting outstanding fundamental research into mechanisms that regulate the basic biology of normal or cancer cells. We welcome applications from candidates in the broad areas of molecular, cellular and/or structural biology. Of special interest are…
Source: apply.interfolio.comCategories: Hem/Onc News and Journals, Latest HeadlinesTweet-
We're #hiring for a faculty position in our Basic Sciences Division (@HutchBasicSci)! Of special interest are candidates who have expertise in #CryoEM and/or #CryoET. Learn more and apply: https://t.co/tgDBtR5d2j https://t.co/cRdEppEpx3
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Mashup Score: 2Apply - Interfolio - 2 year(s) ago
Fred Hutchinson Cancer Center invites applications for a faculty position in the Division of Basic Sciences. We seek a laboratory scientist conducting outstanding fundamental research into mechanisms that regulate the basic biology of normal or cancer cells. We welcome applications from candidates in the broad areas of molecular, cellular and/or structural biology. Of special interest are…
Source: apply.interfolio.comCategories: Hem/Onc News and Journals, Latest HeadlinesTweet-
We're #hiring for a faculty position in our Basic Sciences Division (@HutchBasicSci)! Of special interest are candidates who have expertise in #CryoEM and/or #CryoET. Learn more and apply: https://t.co/tgDBtR4FcL https://t.co/EoWXXoUHIQ
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Mashup Score: 8
Researchers at the University of British Columbia have discovered a key vulnerability across all major variants of the SARS-CoV-2 virus, including the recently emerged BA.1 and BA.2 Omicron subvari…
Source: UBC NewsCategories: Infectious Disease, Latest HeadlinesTweet-
Researchers at @UBC have discovered a key 🔑 vulnerability across all major #SARSCoV2 variants. Dr. Sriram Subramaniam's team (@cryoem_UBC) used #CryoEM to reveal the atomic-level structure of the vulnerable spot on the virus’ spike protein. https://t.co/sFyT8rnd5I
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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