Results 211 to 220 of about 234,152 (246)
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AAA ATPase conformational high jinks

Science, 2016
Structural Biology The protein p97 is an AAA adenosine triphosphatase (ATPase) that uses energy from ATP hydrolysis to regulate substrates involved in intracellular protein quality control. Its role in this central process makes it a target for cancer chemotherapy. Banerjee et al.
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MoxR AAA+ ATPases: A novel family of molecular chaperones?

Journal of Structural Biology, 2006
The MoxR AAA+ family is a large, diverse group of ATPases that, so far, has been poorly studied. Members of this family are found throughout the Bacteria and Archaea superkingdoms, but have not yet been detected in Eukaryota. The limited experimental data available to date suggest that members of this family might have chaperone-like activities.
Jamie, Snider, Walid A, Houry
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AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery

Traffic, 2007
AAA+ adenosine triphosphatases (ATPases) are molecular machines that perform a wide variety of cellular functions. For instance, they can act in vesicle transport, organelle assembly, membrane dynamics and protein unfolding. In most cases, the ATPase domains of these proteins assemble into active ring‐shaped hexamers.
Susan Roehl, White, Brett, Lauring
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AAA ATPases

2021
The AAA (ATPases associated with diverse cellular activities) protein family encompasses a large group of enzymes in all domains of life. AAA proteins assemble into oligomeric rings and undergo conformational changes during nucleotide hydrolysis cycles, exerted by highly conserved ATPase modules.
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Evolutionary history and higher order classification of AAA+ ATPases

Journal of Structural Biology, 2004
The AAA+ ATPases are enzymes containing a P-loop NTPase domain, and function as molecular chaperones, ATPase subunits of proteases, helicases or nucleic-acid-stimulated ATPases. All available sequences and structures of AAA+ protein domains were compared with the aim of identifying the definitive sequence and structure features of these domains and ...
Lakshminarayan M, Iyer   +3 more
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[AAA ATPases and hereditary spastic paraplegia].

Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics, 2009
The hereditary spastic paraplegias (HSPs or SPGs) are clinically and genetically highly heterogeneous neurodegenerative disorders mainly characterized by progressive spasticity and weakness in the lower limbs. The inheritance mode includes autosomal dominant(AD-HSP), autosomal recessive(AR-HSP) and X-linked recessive(XR-HSP). Thirty-five loci have been
Yin-guang, Wang, Lu, Shen
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Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins

Nature Structural & Molecular Biology, 2020
L. Kater   +5 more
semanticscholar   +1 more source

AAA-ATPases

2013
J. Martin, A.N. Lupas
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The AAA-ATPase p97 in mitosis and fertilization

2007
Late mitotic events are chiefly controlled by proteolysis of key regulatory proteins via the ubiquitin-proteasome pathway. In this pathway ubiquitin ligases modify substrates by attachment of ubiquitin (“ubiquitylation”), which usually results in their subsequent degradation by the 26S proteasome.
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