Results 131 to 140 of about 3,365 (168)
AAA ATPases widely exist in many organisms and function in various organelles. However, there is little information about AAA ATPase functioning in endocytosis.
カキモト, ケンイチ +11 more
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Pancreatic cancer presents as an almost invariably lethal malignancy. We show through analysis of genome-scale transposon screening that the AAA ATPase Fign collaborates with KrasG12D to drive pancreatic cancer dedifferentiation.
Widholz, Sebastian Alexander
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AAA+ ATPases in the Initiation of DNA Replication
Critical Reviews in Biochemistry and Molecular Biology, 2008All cellular organisms and many viruses rely on large, multi-subunit molecular machines, termed replisomes, to ensure that genetic material is accurately duplicated for transmission from one generation to the next. Replisome assembly is facilitated by dedicated initiator proteins, which serve to both recognize replication origins and recruit requisite ...
Karl E, Duderstadt, James M, Berger
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The AAA team: related ATPases with diverse functions
Trends in Cell Biology, 1998A new family of related ATPases has emerged, characterized by a highly conserved AAA motif. This motif forms a 230-amino-acid domain that contains Walker homology sequences and imparts ATPase activity. Homology between AAA-family members is confined mostly to the AAA domain, although additional homology outside the AAA motif is present among closely ...
S, Patel, M, Latterich
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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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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, 2004The 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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MoxR AAA+ ATPases: A novel family of molecular chaperones?
Journal of Structural Biology, 2006The 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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Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle
Nature Structural Biology, 2002p97 (also called VCP), a member of the AAA ATPase family, is involved in several cellular processes, including membrane fusion and extraction of proteins from the endoplasmic reticulum for cytoplasmic degradation. We have studied the conformational changes that p97 undergoes during the ATPase cycle by cryo-EM and single-particle analysis.
Isabelle, Rouiller +6 more
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AAA ATPase conformational high jinks
Science, 2016Structural 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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AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery
Traffic, 2007AAA+ 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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