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Mashup Score: 7Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly - Nature Communications - 2 year(s) ago
In this work, the authors report a system for production of short versions of a filamentous phage enables the structure to be determined by cryo-electron microscopy. Structure combined with mutagenesis allows the identification of phage domains that are important in bacterial attack and for release of new viral progeny.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet
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Mashup Score: 2
eIF5A is the only protein known to contain hypusine. Here, the authors present the cryoEM structure of the eIF5A-DHS complex and provide mechanistic insights to understand the deoxyhypusination reaction and hypusination-related neurodegeneration.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Researchers @JagiellonskiUni present the cryoEM structure of the eIF5A-DHS complex and provide mechanistic insights on the deoxyhypusination reaction and hypusination-related neurodegeneration. #hypusination #cryoEM #crystallography https://t.co/ucyUMpb4GY https://t.co/VPNw9R7WN5
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Mashup Score: 11Disease-relevant β2-microglobulin variants share a common amyloid fold - Nature Communications - 2 year(s) ago
The authors use cryo-EM to determine amyloid fibrils structures of disease relevant variants of β2-microglobulin in vitro. Each variant is polymorphic, but all polymorphs from all samples are built from a a lego-like assembly of common building blocks, suggesting a one amyloid fold’ paradigm.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Scientists from @AstburyCentre and @radfordlab observe an #AmyloidLego like assembly in amyloid fibrils of disease relevant variants of β2-microglobulin in vitro, suggesting a one amyloid fold paradigm. @ScienceLeeds @naranson @milkowilko #CryoEM https://t.co/xHlFcEDfyS https://t.co/aiQKXZUaEL
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Mashup Score: 5rRNA methylation by Spb1 regulates the GTPase activity of Nog2 during 60S ribosomal subunit assembly - Nature Communications - 2 year(s) ago
Regulation of 60S biogenesis remains poorly understood. Using cryo-EM, the authors show that failure of Spb1 to methylate the A-loop nucleotide G2922 prematurely activates the GTPase Nog2, suggesting that Spb1 and Nog2 form a kinetic checkpoint during ribosome maturation.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Researchers from @erzbergerlab, @biophysics_utsw, @MolBiophysUTSW, including @victor_ecr and @sekulskikamil, report insights into the roles of rRNA methylation and GTPase Nog2 in 60S biogenesis. #ribosome, #RNA, #CryoEM https://t.co/9RYt6cIoyS https://t.co/rKxWbfIL1K
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Mashup Score: 0Structural basis for clearing of ribosome collisions by the RQT complex - Nature Communications - 2 year(s) ago
Ribosome collisions serve as proxy for aberrant translation to initiate rescue and quality control pathways. Here, authors elucidate the molecular mechanism of collided ribosome clearance by the ribosome quality control trigger complex.
Source: NatureCategories: General Medicine News, Latest HeadlinesTweet-
Researchers from@BeckmannLab, @GeneCenter_LMU, @inada_lab elucidate the molecular mechanism of collided ribosome clearance by the ribosome quality control trigger complex. #ribosomes, #CryoEM https://t.co/qfV2BPJ5IX https://t.co/U0bBkiEJAF
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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-
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
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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-
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/xyQ2lJ5TEB
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Mashup Score: 1How the SPOP Protein Plays a Role in Cancer - 2 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-
#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/ueyZtRcvdX
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Scientists from @the_gold_lab report the #CryoEM structure of f1 filamentous #phage & provide insights into the domains important in bacterial attack & release of new viral progeny. @conners_becky @rayenleonq @MicroMassey @LSIExeter @NatSciMassey https://t.co/bKMytlpxLH https://t.co/eJDou82ZMj