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Mals Mariappan retweeted
Checkout the recent work from our lab that demonstrates how glucose attached to a protein can direct the protein folding and molecular choreography of nascent chains in the endoplasmic reticulum.
Online Now: ER chaperones use a protein folding and quality control glyco-code dlvr.it/SzhMDy
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Mals Mariappan retweeted
Nice reconstitution from @MariappanLab. Nascent proteins from stalled ribosomes are polyubiquitinated and then promptly deubiquitinated, giving a second chance to fold. If a protein still can't fold, it exposes a degron, is re-ubiquitinated and degraded. biorxiv.org/content/10.110…
We report that nascent chains ubiquitinated on stalled ribosomes undergo complete deubiquitination upon release from ribosomes. Deubiquitinated proteins can fold into mature proteins or be re-ubiquitinated in the cytosol for degradation if they misfold.
Nascent Chain Ubiquitination is Uncoupled from Degradation to Enable Protein Maturation biorxiv.org/content/10.110…
Mals Mariappan retweeted
We usually think of mRNAs carrying the information needed to make a protein (the central dogma...). But how can the encoded protein control the fate of its encoding mRNA? 🤔 Check out our review on the topic 👇 cell.com/molecular-cell…
Mals Mariappan retweeted
Mechanisms of readthrough mitigation reveal principles of GCN1-mediated translational quality control: Cell cell.com/cell/fulltext/…
Mals Mariappan retweeted
🚨Out now!🚨 Check out how cells adjust their tubulin mRNA levels in response to excess free tubulin. A 40-year-old puzzle solved! Wonderful collaboration with @AbsmeierEva, @lapassmore & @Ivana_Gasic 🧵 1/ cell.com/molecular-cell…
Mals Mariappan retweeted
🎉We are thrilled to share our exciting new collaboration with @inada_lab and @jingdongcheng on how Otu2 recognizes and deubiquitinates 40S ribosomes after translation. Here is a thread with the most interesting findings:👇 #ribosome #ubiquitin #cryoEM
Mals Mariappan retweeted
A beautiful story from @LukeChaoSun and @erin_schuman on how 19S proteasome caps can independently regulate aspects of synaptic biology. lovely to see it out!! science.org/doi/10.1126/sc…
Very nice paper from the Zhang group
UBE4A catalyzes NRF1 ubiquitination and facilitates DDI2-mediated NRF1... sciencedirect.com/science/articl…
Mals Mariappan retweeted
Check out the preview of our latest story at news.stanford.edu/2023/04/20/stu…
Mals Mariappan retweeted
New work from Ron Kopito and @scafrancesco1 reveal that UFMylation of ER translocon-bound 60S ribosome subunits promotes proteasome-mediated degradation of arrest polypeptides following ribosome stalling. 👏 biorxiv.org/content/10.110…
Mals Mariappan retweeted
.@udi_yael et al. @RoutLab_RU @RockefellerUniv present a new method for quantitative subcellular fractionation of a wide range of mammalian cells while maintaining nuclear integrity. bit.ly/404Jvpr @innalax #Biochemistry #Trafficking #Organelles
Mals Mariappan retweeted
Multiple job opportunites in the @YaleWestCampus Cores - mass spec & flow cytometry. Join an established team of staff scientists in support of research across campus. Please RT buff.ly/3lbi9i8 #research #hiring #yale @YWCimagingcore
Yale Cell Biology Seminar Series: "Molecular Origami: The Delicate Art of Protein Folding and Misfolding and Its Relevance to Health and Disease" m.yale.edu/bmps via @yalemed
Mals Mariappan retweeted
Honored & excited to be selected for Best of @BiophysJ symposium @BiophysicalSoc #BPS2023 Shout out to @MariappanLab & @MoitrayeeLab for their pivotal contributions @YaleCellBio biophysics.org/2023meeting/pr…
Mals Mariappan retweeted
This week's fanart is by Sha Sun, Xia Li, and Malaiyalam Mariappan ° #biology #research #cell #compbio #ER #structural #protein #folding #communication #sciart
The Get1/2 insertase forms a channel to mediate the insertion of tail-... sciencedirect.com/science/articl…
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