Frank Adolf ❄️🔬🧬
@frankadolf.bsky.social
Project Group Leader @MPI_Biochem | Department of Molecular Maschinens and Signaling | Schulman lab | Max Planck Institute of Biochemistry
Reposted by Frank Adolf ❄️🔬🧬
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
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
Reposted by Frank Adolf ❄️🔬🧬
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...
@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
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...
@natsmb.nature.com
1/7
www.nature.com/articles/s41...
Having a great time at #Ub&Friends25. Fantastic lineup of speakers. I hope I get the chance to come back to the beautiful #Vienna.
May 9, 2025 at 5:46 AM
Having a great time at #Ub&Friends25. Fantastic lineup of speakers. I hope I get the chance to come back to the beautiful #Vienna.
Reposted by Frank Adolf ❄️🔬🧬
UbiREAD deciphers proteasomal degradation code of homotypic and branched K48 and K63 ubiquitin chains
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 high temporal resolution after intracellular delivery of ubiquitinated proteins. This reveals a degradation code for ubiquitin chains varying by linkage, length, and topology.
dlvr.it
April 7, 2025 at 7:14 PM
UbiREAD deciphers proteasomal degradation code of homotypic and branched K48 and K63 ubiquitin chains
Reposted by Frank Adolf ❄️🔬🧬
It seems no starter pack exists yet for the migrated #TPD community - here is an attempt at one: go.bsky.app/FreGFDW
November 18, 2024 at 11:51 PM
It seems no starter pack exists yet for the migrated #TPD community - here is an attempt at one: go.bsky.app/FreGFDW
Reposted by Frank Adolf ❄️🔬🧬
New week, updated starter pack. Now with 69 profiles to follow if you are interested in anything #ubiquitin or #Ubl: signalling, structure and biochemistry, biology, mechanisms, proteostasis, TPD, chemical biology, etc. Let me know if you or anyone else is missing.
November 25, 2024 at 8:32 AM
New week, updated starter pack. Now with 69 profiles to follow if you are interested in anything #ubiquitin or #Ubl: signalling, structure and biochemistry, biology, mechanisms, proteostasis, TPD, chemical biology, etc. Let me know if you or anyone else is missing.