Manisha Kochar

PhD scholar at @IGIBSocial | Protein folding and proteostasis

[Manisha Kochar @ManishaKochar]

@ssiddhant_ @IGIBSocial @foldingINvivo @kausikigib @dkumar02 Thank you Siddhant!! 💖✨

[Manisha Kochar @ManishaKochar]

@Chet_Mishra @IGIBSocial @foldingINvivo @kausikigib @dkumar02 Thank you Chetan!!

[Manisha Kochar @ManishaKochar]

@dkumar02 @IGIBSocial @foldingINvivo @kausikigib Thank you so much for always supporting me in my little endeavours!! 💖🌸

[Manisha Kochar @ManishaKochar]

@shruthy_suresh @IGIBSocial @foldingINvivo @kausikigib @dkumar02 Thank you so much!!! 💖🌸

[Manisha Kochar @ManishaKochar]

Still in disbelief, but two weeks ago, I defended my PhD. 🎓✨
We explored how molecular chaperones evolve to support increasingly complex proteins.

I'm deeply grateful to everyone who supported & helped me get here.

#PhD 🥂
@IGIBSocial
@foldingINvivo
@kausikigib
@dkumar02

[ShorterLab @ShorterLab]

Mitochondria serve as a holdout compartment for aggregation-prone proteins hindering efficient degradation: https://t.co/uFAShqDAaE

[Manisha Kochar @ManishaKochar]

Last week was a roller coaster- equal parts exhaustion & relief. After years of late nights, setbacks & small wins, I finally submitted my PhD thesis.

Still letting it sink in… with gratitude, a little disbelief & a full heart✨
@IGIBSocial @foldingINvivo @kausikigib @dkumar02

[Manisha Kochar @ManishaKochar]

@AggarwalAyush_ Congratulations Ayush!!

[Marvin Tanenbaum @MarvinTanenbaum]

New lab paper!! We develop a technology for live-cell, single-molecule visualization of proteasomal substrate degradation. We find that the site of substrate engagement by the proteasome determines decay kinetics, efficiency and co-factor requirement.

https://t.co/FltQFPYs8h

[Manisha Kochar @ManishaKochar]

Pre-thesis colloquium ✔️

Presented my PhD work at CSIR-IGIB last month—grateful for the feedback and excited for the final stretch 🚀🧬

@foldingINvivo @IGIBSocial
#PhDLife #AcademicTwitter #GradSchool #ProteinFolding

[ShorterLab @ShorterLab]

Mitochondrial presequences harbor variable strengths to maintain organellar function: https://t.co/ksFHSGY33z

[BuchnerLab @buchnerlab_tum]

Happy to share our latest work, out now in Molecular Cell!
https://t.co/p23Vqy7lrj

[ShorterLab @ShorterLab]

A widespread protein misfolding mechanism is differentially rescued in vitro by chaperones based on gene essentiality: https://t.co/iLwra0XTf4

[Manisha Kochar @ManishaKochar]

Had a wonderful time earlier this month at the EMBO|India Lecture Series on “Structure, function and quality control of proteins in cell organelles” at @ccmb_csir. Great science, inspiring discussions, and a fun chance to explore the city as well.
#EMBOorganelles #EMBOCCMB2025

[Stephen Fried JHU @fried_lab]

How well do you think you understand chaperones? In our recent @MolSystBiol paper, @fried_lab's Divya Yadav shows that obligate chaperone clients in cells are totally different from the proteins that "need" chaperones during in vitro refolding.
https://t.co/EAeGVuDSld

[Stephen Fried JHU @fried_lab]

As the planet gets hotter & drier, can we make proteins & organisms more resilient to desiccation stress? Together with @shaharsu @SyracuseU & @alexholehouse @washumedicine, we show in @CellSystemsCP a sequence grammar encoding tolerance to dehydration.
https://t.co/6irXPGyfh3

[NatureStructMolBiol @NatureSMB]

New online! The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking https://t.co/5B8oN1eB5g

[Santosh Chauhan @Chauhanlab_ILS]

FROM CELL DEATH TO REGENERATION: What if dying cells -come back to life? Now online @embojournal I https://t.co/eOKTg6qVnk , we aim to answer this question. Here is the journey. If you🩷science, please dont 🛑till the end of 🧵, I promise you will not regret. 1/n

[Dilip Kumar Tiwari @dkumar02]

This EMBO practical course is one of the most comprehensive cryo-EM course. Please repost it and share with your colleagues. Deadline approaching soon!
@EMBO, @iitdelhi, @unescorcb, @aiims_newdelhi, #CEM3DIP

[Structura Biotechnology @structurabio]

Flexibility can be frustrating when processing a #cryoEM dataset. If your target has a wobbly domain, check out our new case study on FaNaC1 for continuous heterogeneity tips in #CryoSPARC!

https://t.co/I7FIqEGtFk