Results 31 to 40 of about 234,152 (246)
An AAA-ATPase links mitochondrial division with DNA nucleoids. [PDF]
Proc Natl Acad Sci U S A, 2022 Yeung N, Iijima M, Sesaki H.
europepmc +3 more sources
Biophysical Journal, 2011 AAA+ ATPases contribute to nearly all cellular activities. Nature builds these machines as homomeric rings with catalytic sites residing between each protomer. A highly conserved catalytic core is modified with task-specific structural elements to generate a myriad of functions.
Nixon, B. Tracy +7 more
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ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP
eLife, 2020 AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase.
Sora Kim +4 more
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Torsins: not your typical AAA+ ATPases [PDF]
Critical Reviews in Biochemistry and Molecular Biology, 2015 Torsin ATPases (Torsins) belong to the widespread AAA+ (ATPases associated with a variety of cellular activities) family of ATPases, which share structural similarity but have diverse cellular functions. Torsins are outliers in this family because they lack many characteristics of typical AAA+ proteins, and they are the only members of the AAA+ family ...
April E, Rose +2 more
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Crystal structure of the ATPase domain of the human AAA+ protein paraplegin/SPG7. [PDF]
PLoS ONE, 2009 Paraplegin is an m-AAA protease of the mitochondrial inner membrane that is linked to hereditary spastic paraplegias. The gene encodes an FtsH-homology protease domain in tandem with an AAA+ homology ATPase domain.
Tobias Karlberg +6 more
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An AAA+ ATPase Clamshell Targets Transposition [PDF]
Cell, 2015 DNA transposition plays key roles in genome diversity, pathogenesis, and evolution. Yet, structural and mechanistic information on transposition targeting and regulation is limited. Arias-Palomo and Berger now define the decameric organization of the AAA+ ATPase IstB, unveiling key insights into its targeting and regulation of IstA transposase activity.
Tsai, Chi-Lin +3 more
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Structure of the AAA ATPase p97 [PDF]
Molecular Cell, 2000 p97, an abundant hexameric ATPase of the AAA family, is involved in homotypic membrane fusion. It is thought to disassemble SNARE complexes formed during the process of membrane fusion. Here, we report two structures: a crystal structure of the N-terminal and D1 ATPase domains of murine p97 at 2.9 A resolution, and a cryoelectron microscopy structure ...
Zhang, Xiaodong +13 more
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Structure of the AAA protein Msp1 reveals mechanism of mislocalized membrane protein extraction. [PDF]
, 2020 The AAA protein Msp1 extracts mislocalized tail-anchored membrane proteins and targets them for degradation, thus maintaining proper cell organization.
Myasnikov, Alexander +3 more
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Development of p97 AAA ATPase inhibitors [PDF]
Autophagy, 2011 Specific p97 inhibitors are valuable research tools to carry out mechanistic and cellular investigations of p97 biology. p97 is an abundant, ubiquitin-selective chaperone that has multiple functions and is essential for life. Therefore, genetic methods that require long incubations like siRNA or expression of dominant-negative p97 mutants are likely to
Chou, Tsui-Fen, Deshaies, Raymond J.
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Journal of Biological Research, 2019 Asthenozoospermia is the most frequent sperm motility disorder, but there are other more extreme sperm motility disorders, namely oligo-astheno-teratozoospermia (OAT) and necrozoospermia.
Silvia W. Lestari +3 more
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