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ProteomicsRecruitment of trimeric eIF2 by phosphatase non-catalytic subunit PPP1R15B
HDX-MS of R15B and it's interactions with trimeric eIF2 substrate. Here we integrated diverse approaches to elucidate how the PP1 non-catalytic subu-nit PPP1R15B (R15B) captures its full trimeric eIF2 substrate. We found that the substrate recruitment module of R15B is largely disordered with three...
ORGANISM(S): Homo sapiens (Human) 
2024-05-22 | PXD047538 | Pride
Hdx-ms Hd-ms 
ProteomicsAssembly and phospho-regulatory mechanisms of the budding yeast outer kinetochore KMN complex
Crosslinking of KMN outer kinetochore complex. During mitosis and meiosis kinetochores mediate interactions between chromosomes and spindle microtubules. Kinetochores are multi-megadalton protein complexes essential for chromosome segregation in all eukaryotes, however recent structural, functional,...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2026-03-16 | PXD072662 | Pride
Kinetochore Cl-ms Crosslinking 
ProteomicsHow Myosin VI Traps its Off-State, is Activated and Dimerizes
Myosin VI (Myo6) is the only minus-end directed nanomotor on actin, allowing it to uniquely contribute to numerous cellular functions. As for other nanomotors, proper functioning of Myo6 relies on precise spatio-temporal control of motor activity via a poorly defined off-state and interactions with ...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD044767 | Pride
Myosin vi Human Clms Cross linking mass spectromety 
ProteomicsRECQL5 and transcription-coupled DNA repair complex coordinate to regulate transcription elongation
The RECQL5 helicase is crucial for maintaining genome stability and functions at the intersection of transcription, replication, and DNA repair. RECQL5 associates with RNA15 polymerase II (Pol II) to modulate transcription elongation, yet the underlying mechanism remains unclear. Here, we report cry...
ORGANISM(S): Homo sapiens (Human) 
2025-09-22 | PXD062042 | Pride
Recql5 Transcription Crosslinking 
UnknownCOVID-19 in patients with pulmonary alveolar proteinosis: a European multicentre study.
Not available
S-EPMC9271262 | biostudies-literature
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