Results 31 to 40 of about 3,365 (168)
The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1
eLife, 2018 The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors.
Piotr Sosnowski +6 more
doaj +1 more source
Hierarchical Binding of Cofactors to the AAA ATPase p97 [PDF]
Structure, 2011 The hexameric AAA ATPase p97 is involved in several human proteinopathies and mediates ubiquitin-dependent protein degradation among other essential cellular processes. Via its N-terminal domain (N domain), p97 interacts with multiple regulatory cofactors including the UFD1/NPL4 heterodimer and members of the "ubiquitin regulatory X" (UBX) domain ...
Hänzelmann, Petra +2 more
openaire +2 more sources
AAA + ATPase Thorase inhibits mTOR signaling through the disassembly of the mTOR complex 1
Nature Communications, 2022 Signaling via the mTOR complex 1 (mTORC1) maintains cellular and organismal homeostasis. Here the authors show that the AAA + ATPase Thorase binds mTOR to promote disassembly and inactivation of mTORC1 to fine tune TOR signaling according to amino acid ...
George K. E. Umanah +15 more
doaj +1 more source
The emerging role of E3 ubiquitin ligase RNF213 as an antimicrobial host determinant
Frontiers in Cellular and Infection Microbiology, 2023 Ring finger protein 213 (RNF213) is a large E3 ubiquitin ligase with a molecular weight of 591 kDa that is associated with moyamoya disease, a rare cerebrovascular disease. It is located in the cytosol and perinuclear space.
Yulu Zhang +11 more
doaj +1 more source
Assembly of the AAA ATPase Vps4 on ESCRT-III [PDF]
Molecular Biology of the Cell, 2010 Vps4 is a key enzyme that functions in endosomal protein trafficking, cytokinesis, and retroviral budding. Vps4 activity is regulated by its recruitment from the cytoplasm to ESCRT-III, where the protein oligomerizes into an active ATPase. The recruitment and oligomerization steps are mediated by a complex network of at least 12 distinct interactions ...
Shestakova, Anna +6 more
openaire +2 more sources
The role of the N-D1 linker of the N-ethylmaleimide-sensitive factor in the SNARE disassembly. [PDF]
PLoS ONE, 2013 N-ethylmaleimide-sensitive factor (NSF) is a member of the type II AAA+ (ATPase associated with various cellular activities) family. It plays a critical role in intracellular membrane trafficking by disassembling soluble NSF attachment protein receptor ...
Cui-Cui Liu, Shan Sun, Sen-Fang Sui
doaj +1 more source
Cryo-EM structures reveal high-resolution mechanism of a DNA polymerase sliding clamp loader
eLife, 2022 Sliding clamps are ring-shaped protein complexes that are integral to the DNA replication machinery of all life. Sliding clamps are opened and installed onto DNA by clamp loader AAA+ ATPase complexes.
Christl Gaubitz +6 more
doaj +1 more source
In the absence of ATPase activity, pre-RC formation is blocked prior to MCM2-7 hexamer dimerization [PDF]
, 2013 26.03.14 KB.
Brill, S +17 more
core +1 more source
Proteasomal AAA-ATPases: Structure and function
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012 The 26S proteasome is a chambered protease in which the majority of selective cellular protein degradation takes place. Throughout evolution, access of protein substrates to chambered proteases is restricted and depends on AAA-ATPases. Mechanical force generated through cycles of ATP binding and hydrolysis is used to unfold substrates, open the gated ...
Bar-Nun, Shoshana, Glickman, Michael H.
openaire +2 more sources
Structural and biochemical studies of MCM proteins [PDF]
, 2010 The eukaryotic MCM2-7 replicative helicase is a hetero-complex composed by 6 homologues belonging to the AAA+ ATPase superfamily. These proteins form a ring-like structure which is essential for the initiation and the progression of the replication fork.
Medagli, Barbara
core +1 more source