Yang Yang
@yyang_cella
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Assistant Professor@VAInstitute, alimni of @MRC_LMB. cryo-EM, X-ray crystallography, Neurodegenerative disorder, GPCRs, virology.
Joined November 2020
Thrilled to see our Lewy fold paper online! We found the alpha-synuclein filaments share the same structure in PD, PDD and DLB. Great thanks to @MichelGoed and @SjorsScheres support! Thanks to everyone who makes this happen!!
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RT @VAInstitute: We are thrilled to welcome Dr. Yang Yang @yyang_cella as an assistant professor in our Department of Structural Biology, w…
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Thank you @MRC_LMB! 😄It was a fantastic journey to work with many talented people at LMB. Thank you @SjorsScheres @MichelGoed and so many people helped me along my way! ! I am looking forward to the new chapter at @VAInstitute!😊
Congratulations to @yyang_cella, postdoc in @SjorsScheres group in the LMB’s Structural Studies Division, who is starting her own research group at @VAInstitute, investigating molecular mechanisms in neurodegenerative diseases! Best of luck to you Yang! #LMBAlumni
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🔬👩🔬 Exciting news! I'll soon start my lab @VAInstitute to research molecular mechanisms in Neurodegenerative diseases. 🧠💡 Now recruiting postdocs to join our dynamic research team! Email me if you're interested! #Postdoc #CryoEM #Neuroscience #ResearchOpportunity
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RT @ScienceofPD: Wow! The line up of speakers at the @VAInstitute "Grand challenges in #Parkinsons" symposium is looking really impressive…
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Our paper of Niacin receptor is out now! Thanks all for the hardworking and contributions. It’s a long journey since we got first structure on 2016, and finally we made it. See👇 Structural insights into the human niacin receptor HCA2-Gi signalling complex
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We're thrilled to have published our paper on ABeta structures with Arctic mutation from Alzheimer's disease. Many thanks to @SjorsScheres and @MichelGoed for support and guidance! Huge thanks also to all of our collaborators for their contributions! 😊🥳
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Thanks to @SjorsScheres and @MichelGoed for their support as always! And thanks to our collaborators and people who helped to this work!
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This shows the removal of the side chain by the E22G mutation increased hydrogen bonds between adjacent amyloid-beta molecules in Arctic fold.
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Tetrameric filaments consist of two pairs of non-identical protofilaments that comprise residues V12-V40 and E11-G37. A minority of Arctic Abeta42 filaments of type II was also present.
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RT @MRC_LMB: New #cryoEM structures of α-synuclein filaments from Parkinson’s disease & dementia with Lewy bodies by @MichelGoed & @SjorsSc…
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RT @ScienceofPD: New paper from @yyang_cella @MichelGoed & colleagues reports that the cryo-EM structures of α-synuclein filaments from the…
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The Lewy fold differs from MSA folds: protofilament numbers and conformations seem stark. Whereas a non-peptide factor wedges into a groove formed by four lysines, this conformation is found both in Lewy fold and MSA folds.
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The single protofilament core comprises amino acids 31-100 of the protein in a three-layer structure consisting of nine β-sheets. We found the Lewy fold protofilament does resemble recombinant α-synuclein structures.
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