Results 71 to 80 of about 234,152 (246)
Autophagy, 2017 Peroxisome biogenesis disorders (PBDs) are metabolic disorders caused by the loss of peroxisomes. The majority of PBDs result from mutation in one of 3 genes that encode for the peroxisomal AAA ATPase complex (AAA-complex) required for cycling PEX5 for ...
Kelsey B. Law +8 more
semanticscholar +1 more source
Nucleotide‐dependent conformational changes of the AAA+ ATPase p97 revisited
FEBS Letters, 2016 The ubiquitous AAA‐ATPase p97 segregates ubiquitylated proteins from their molecular environment. Previous studies of the nucleotide‐dependent conformational changes of p97 were inconclusive. Here, we determined its structure in the presence of ADP, AMP‐PNP, or ATP‐γS at 6.1–7.4 Å resolution using single particle cryo‐electron microscopy.
J. Schuller +4 more
semanticscholar +5 more sources
ATPase-deficient mitochondrial inner membrane protein ATAD3A disturbs mitochondrial dynamics in dominant hereditary spastic paraplegia [PDF]
, 2017 De novo mutations in ATAD3A (ATPase family AAA-domain containing protein 3A) were recently found to cause a neurological syndrome with developmental delay, hypotonia, spasticity, optic atrophy, axonal neuropathy, and hypertrophic cardiomyopathy.
Auranen, Mari +15 more
core +1 more source
A CDK-regulated chromatin segregase promoting chromosome replication
Nature Communications, 2021 How cells coordinate chromatin dynamics with the cell cycle machinery to promote genome duplication during S phase is still a matter of study. Here the authors reveal by in vitro reconstitution assays that the AAA + -ATPase containing Yta7 protein in S ...
Erika Chacin +11 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
Ubiquitin-Independent Disassembly by a p97 AAA-ATPase Complex Drives PP1 Holoenzyme Formation.
Molecules and Cells, 2018 The functional diversity of protein phosphatase-1 (PP1), with its countless substrates, relies on the ordered assembly of alternative PP1 holoenzymes. Here, we show that newly synthesized PP1 is first held by its partners SDS22 and inhibitor-3 (I3) in an
Matthias Weith +11 more
semanticscholar +1 more source
Is PCNA unloading the central function of the Elg1/ATAD5 replication factor C-like complex? [PDF]
, 2013 This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.Peer ...
Donaldson, Anne D +2 more
core +1 more source
Frontiers in Molecular Biosciences, 2017 ClpX is a member of the Clp/Hsp100 family of ATP-dependent chaperones and partners with ClpP, a compartmentalized protease, to degrade protein substrates bearing specific recognition signals.
Christopher J. LaBreck +4 more
doaj +1 more source
An empirical energy landscape reveals mechanism of proteasome in polypeptide translocation
eLife, 2022 The ring-like ATPase complexes in the AAA+ family perform diverse cellular functions that require coordination between the conformational transitions of their individual ATPase subunits (Erzberger and Berger, 2006; Puchades et al., 2020).
Rui Fang +3 more
doaj +1 more source
Structure of the active form of human origin recognition complex and its ATPase motor module
eLife, 2017 Binding of the Origin Recognition Complex (ORC) to origins of replication marks the first step in the initiation of replication of the genome in all eukaryotic cells.
Ante Tocilj +7 more
doaj +1 more source