Ekampreet Singh
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esingh.bsky.social
Ekampreet Singh
@esingh.bsky.social
42 followers 92 following 2 posts
PhD student at Schulman Lab, Max Planck Institute of Biochemistry.
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Reposted by Ekampreet Singh
biorxiv-biochem.bsky.social
Cysteine availability tunes ubiquitin signaling via inverse stability of LRRC58 E3 ligase and its substrate CDO1 https://www.biorxiv.org/content/10.1101/2025.11.14.688510v1
November 15, 2025 at 2:45 AM
esingh.bsky.social
Congratulations Caro!! ✨
August 7, 2025 at 11:20 AM
Reposted by Ekampreet Singh
carolinklose.bsky.social
Excited to share our latest study in @natcomms.nature.com , where we characterize the chaperone function of the ER membrane protein complex (EMC)—supporting membrane protein biogenesis beyond insertion!
1/9

www.nature.com/articles/s41...
The EMC acts as a chaperone for membrane proteins - Nature Communications
Membrane proteins are essential for any cell but difficult to fold. Here, the authors show that the EMC acts as a chaperone for membrane proteins. They dissect client recognition and provide a molecul...
www.nature.com
August 5, 2025 at 1:18 PM
esingh.bsky.social
Congratulations @samuelmaiwald.bsky.social on this wonderful story about ub chain formation. A must read! ✨
May 26, 2025 at 7:49 PM
Reposted by Ekampreet Singh
samuelmaiwald.bsky.social
Excited to share our latest study on how K29/K48-branched #ubiquitin chains are forged by the #E3 ligase TRIP12, and how this suggests a consensus mechanism for chain formation by HECT E3s!

@natsmb.nature.com

1/7

www.nature.com/articles/s41...
TRIP12 structures reveal HECT E3 formation of K29 linkages and branched ubiquitin chains - Nature Structural & Molecular Biology
Using biochemistry, chemical biology, and cryo-EM, Maiwald et al. elucidate how TRIP12 forms K29 linkages and K29/K48-linked branched ubiquitin chains, revealing a mechanism for polyubiquitylation sha...
www.nature.com
May 26, 2025 at 9:37 AM
Reposted by Ekampreet Singh
leokiss.bsky.social
Super excited to share our latest work on deciphering the #Ubiquitin Code

“𝗨𝗯𝗶𝗥𝗘𝗔𝗗 𝗱𝗲𝗰𝗶𝗽𝗵𝗲𝗿𝘀 𝗽𝗿𝗼𝘁𝗲𝗮𝘀𝗼𝗺𝗮𝗹 𝗱𝗲𝗴𝗿𝗮𝗱𝗮𝘁𝗶𝗼𝗻 𝗰𝗼𝗱𝗲 𝗼𝗳 𝗵𝗼𝗺𝗼𝘁𝘆𝗽𝗶𝗰 𝗮𝗻𝗱 𝗯𝗿𝗮𝗻𝗰𝗵𝗲𝗱 𝗞48 𝗮𝗻𝗱 𝗞63 𝘂𝗯𝗶𝗾𝘂𝗶𝘁𝗶𝗻 𝗰𝗵𝗮𝗶𝗻𝘀”

@cp-molcell.bsky.social

1/8

www.cell.com/molecular-ce...
UbiREAD deciphers proteasomal degradation code of homotypic and branched K48 and K63 ubiquitin chains
Ubiquitin chains determine the fates of their modified proteins, including proteasomal degradation. Kiss et al. present UbiREAD, a technology to monitor cellular degradation and deubiquitination at hi...
www.cell.com
March 24, 2025 at 2:54 PM