Yang Yang (@yyang_cella) profile picture

Yang Yang

@yyang_cella

Assistant Professor@VAInstitute, alimni of @MRC_LMB. cryo-EM, X-ray crystallography, Neurodegenerative disorder, GPCRs, virology.

Joined November 2020
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Photo by Yang Yang (@yyang_cella)Photo by Yang Yang (@yyang_cella)Photo by Yang Yang (@yyang_cella)Photo by Yang Yang (@yyang_cella)Photo by Yang Yang (@yyang_cella)Photo by Yang Yang (@yyang_cella)Photo by Yang Yang (@yyang_cella)
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!! nature.com/articles/s41586-0…
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We are thrilled to welcome Dr. Yang Yang @yyang_cella as an assistant professor in our Department of Structural Biology, where she will investigate the factors that give rise to disorders such as #Parkinsons and #Alzheimers: vai.org/article/van-andel-in…
Van Andel Institute welcomes structural biologist and neuroscientist Dr. Yang Yang – Van Andel...

Van Andel Institute welcomes structural biologist and neuroscientist Dr. Yang Yang – Van Andel...

Read about Van Andel Institute welcomes structural biologist and neuroscientist Dr. Yang Yang on Van Andel Institute – Stay updated on the latest research and groundbreaking discoveries in science...

vai.org
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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!😊
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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
Image from Yang Yang (@yyang_cella)
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Wow! The line up of speakers at the @VAInstitute "Grand challenges in #Parkinsons" symposium is looking really impressive this year - including @MarkRCookson1 @MaluTansey @Hlashuel @lvolpic @ChuHongyuan @yyang_cella @LabGandhi vai.org/event/grand-challeng…
Image from The Science of Parkinson's (@ScienceofPD)
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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 nature.com/articles/s41467-0…
Structural insights into the human niacin receptor HCA2-Gi signalling complex

Structural insights into the human niacin receptor HCA2-Gi signalling complex

Nature Communications - Hydroxyl-carboxylic acid receptor 2 (HCA2) functions as a high-affinity receptor for nicotinic acid (vitamin B3). Here, authors report the cryo-EM structure of the HCA2-Gi...

nature.com
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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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🥳 Check out our paper of cryo-EM structures of #amyloid -beta filaments with the Arctic mutation from human and mouse brains #AD | biorxiv Surprisingly, two types of Arctic Aβ filaments were observed from human brains, differ from murine Arctic fold.⁦ biorxiv.org/content/10.1101/…
Cryo-EM Structures of Amyloid-β Filaments With the Arctic Mutation (E22G) From Human and Mouse...

Cryo-EM Structures of Amyloid-β Filaments With the Arctic Mutation (E22G) From Human and Mouse...

The Arctic mutation, encoding E693G in the amyloid precursor protein (APP) gene [E22G in amyloid-β (Aβ)], causes dominantly inherited Alzheimer’s disease. Here we report the high-resolution cryo-EM...

biorxiv.org
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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.
Image from Yang Yang (@yyang_cella)
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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.
Image from Yang Yang (@yyang_cella)
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New paper from @yyang_cella @MichelGoed & colleagues reports that the cryo-EM structures of α-synuclein filaments from the brains of individuals with #Parkinsons, PD dementia & dementia with Lewy bodies are made of a single protofilament; Different to #MSA nature.com/articles/s41586-0…
Image from The Science of Parkinson's (@ScienceofPD)
Image from The Science of Parkinson's (@ScienceofPD)
Image from The Science of Parkinson's (@ScienceofPD)
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We extracted filaments from 3 individuals with PD or PDD, and 3 individuals with DLB. The structures are identical with 'Lewy fold', which indicates the diseases are closely related.
Image from Yang Yang (@yyang_cella)
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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.
Image from Yang Yang (@yyang_cella)
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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.
Image from Yang Yang (@yyang_cella)
Image from Yang Yang (@yyang_cella)
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Scientists at @MRC_LMB published on @ScienceMagazine high-resolution #cryoEM structures of Aβ42 fibrils coming from 10 human brains. They found two types of S-shaped filaments (type I and II), each consisting of two identical protofilaments.
Image from 3D Protein Imaging (@proteinimaging)
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Cryo-EM Unveils Distinct Aβ42 Fibril Structures for Sporadic, Familial AD | ALZFORUM alzforum.org/news/research-n…
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