Mals Mariappan (@mariappanlab) 's Twitter Profile
Mals Mariappan

@mariappanlab

ID: 1195511562720727041

linkhttps://www.mariappanlab.com/ calendar_today16-11-2019 01:19:14

103 Tweet

233 Followers

176 Following

Mals Mariappan (@mariappanlab) 's Twitter Profile Photo

A motor neuron disease-associated mutation produces non-glycosylated Seipin that induces ER stress and apoptosis by inactivating SERCA2b doi.org/10.7554/eLife.…

Art4Science (@rimatesa91) 's Twitter Profile Photo

This week's fanart is by Sha Sun, Xia Li, and Malaiyalam Mariappan ° #biology #research #cell #compbio #ER #structural #protein #folding #communication #sciart

This week's fanart is by Sha Sun, Xia Li, and Malaiyalam Mariappan
°
#biology #research #cell #compbio #ER #structural #protein #folding #communication #sciart
Mals Mariappan (@mariappanlab) 's Twitter Profile Photo

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

Chris Incarvito (@cincarvito) 's Twitter Profile Photo

Multiple job opportunites in the Yale West Campus 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

Journal of Cell Biology (@jcellbiol) 's Twitter Profile Photo

.yael udi et al. Rout Lab Rockefeller University present a new method for quantitative subcellular fractionation of a wide range of mammalian cells while maintaining nuclear integrity. bit.ly/404Jvpr Inna Ricardo-Lax #Biochemistry #Trafficking #Organelles

.<a href="/udi_yael/">yael udi</a> et al. <a href="/RoutLab_RU/">Rout Lab</a> <a href="/RockefellerUniv/">Rockefeller University</a> present a new method for quantitative subcellular fractionation of a wide range of mammalian cells while maintaining nuclear integrity. bit.ly/404Jvpr

<a href="/innalax/">Inna Ricardo-Lax</a> 
#Biochemistry #Trafficking #Organelles
James Olzmann (@olzmannlab) 's Twitter Profile Photo

New work from Ron Kopito and Francesco Scavone 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…

Kapil Ramachandran (@kvramachandran5) 's Twitter Profile Photo

A beautiful story from Chao Sun 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…

Beckmann Lab (@beckmannlab) 's Twitter Profile Photo

🎉We are thrilled to share our exciting new collaboration with Inada Lab and Jingdong Cheng on how Otu2 recognizes and deubiquitinates 40S ribosomes after translation. Here is a thread with the most interesting findings:👇 #ribosome #ubiquitin #cryoEM

Markus Höpfler (@markushopfler) 's Twitter Profile Photo

🚨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 Eva Absmeier, Lori Passmore & Ivana Gasic 🧵 1/ cell.com/molecular-cell…

WilsonLab (@wilsonlab2) 's Twitter Profile Photo

Mechanisms of readthrough mitigation reveal principles of GCN1-mediated translational quality control: Cell cell.com/cell/fulltext/…

Markus Höpfler (@markushopfler) 's Twitter Profile Photo

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…

Ishier Raote (@ishier_raote) 's Twitter Profile Photo

Nice reconstitution from Mals Mariappan. 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…

Nice reconstitution from <a href="/MariappanLab/">Mals Mariappan</a>. 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…
Dan Hebert (@hebert_lab) 's Twitter Profile Photo

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.