Results 11 to 20 of about 3,365 (168)

AAA-ATPases in Protein Degradation [PDF]

Frontiers in Molecular Biosciences, 2017
Proteolytic machineries containing multisubunit protease complexes and AAA-ATPases play a key role in protein quality control and the regulation of protein homeostasis. In these protein degradation machineries, the proteolytically active sites are formed
Ravikiran S. Yedidi, Petra Wendler, Cordula Enenkel   +2 more
doaj   +5 more sources

Structural basis for inhibition of the AAA-ATPase Drg1 by diazaborine [PDF]

Nature Communications, 2021
The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large subunit. Here the authors report the structure of Drg1 in complex with its specific inhibitor diazaborine and provide insight into ...
Michael Prattes, Irina Grishkovskaya, Victor-Valentin Hodirnau, Ingrid Rössler, Isabella Klein, Christina Hetzmannseder, Gertrude Zisser, Christian C. Gruber, Karl Gruber, David Haselbach, Helmut Bergler   +10 more
doaj   +5 more sources

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+
Tainer, John A, Perry, J Jefferson P, Williams, Gareth J, Tsai, Chi-Lin   +3 more
core   +6 more sources

Bromodomain AAA+ ATPases get into shape [PDF]

Nucleus, 2020
Bromodomain AAA+ ATPases (ATPases associated with diverse cellular activities) are emerging as oncogenic proteins and compelling targets for anticancer therapies. However, structural and biochemical insight into these machines is missing.
Magdalena Murawska, Andreas G. Ladurner
doaj   +3 more sources

Optimization of Phenyl Indole Inhibitors of the AAA+ ATPase p97 [PDF]

ACS Medicinal Chemistry Letters, 2018
Optimization of the side-chain of a phenyl indole scaffold identified from a high-throughput screening campaign for inhibitors of the AAA+ ATPase p97 is reported.
Tsui-Fen Chou (214740), William J. Moore, Celeste Alverez (1398700), Neal Green, Alverez, Celeste, James C. Burnett, Shan Li (110392), R. Jeffrey Neitz, Matthew G. LaPorte, James C. Burnett (246494), Wipf, Peter, Huryn, Donna M, Peter Wipf, Peter Wipf (134666), Burnett, James C, Tsui-Fen Chou, Moore, William J, William J. Moore (1464922), Yue, Zhizhou, Raffaele Colombo (1464925), Chou, Tsui-Fen, Michelle R. Arkin (114394), Zhizhou Yue, R. Jeffrey Neitz (772019), Neal Green (1398688), Colombo, Raffaele, Zhizhou Yue (1464910), Matthew G. LaPorte (1443652), Donna M. Huryn (243231), Michelle R. Arkin, Donna M. Huryn, Stacie L. Bulfer, Celeste Alverez, Li, Shan, Neitz, R Jeffrey, Arkin, Michelle R, LaPorte, Matthew G, Green, Neal, Raffaele Colombo, Bulfer, Stacie L, Shan Li, Stacie L. Bulfer (1398706)   +41 more
core   +6 more sources

Regulation | 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 ...
Jörg Martin, Martin, J. ; https://orcid.org/   +1 more
core   +2 more sources

Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway

Nature Communications
The Cdc48 AAA+ ATPase is an abundant and essential enzyme that unfolds substrates in multiple protein quality control pathways. The enzyme includes two conserved AAA+ ATPase motor domains, D1 and D2, that assemble as hexameric rings with D1 stacked above
Ian Cooney, Heidi L. Schubert, Karina Cedeno, Olivia N. Fisher, Richard Carson, John C. Price, Christopher P. Hill, Peter S. Shen   +7 more
doaj   +2 more sources

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, Shaw, Anthony, Bates, Paul A., Newman, Richard H., Gowen, Brent, Orlova, Elena, Gorman, Michael A., Kondo, Hisao, Dokurno, Pawel, Lally, John, Leonard, Gordon, Meyer, Hemmo, van Heel, Marin, Freemont, Paul S.   +13 more
openaire   +2 more sources

AAA+ ATPase Mechanism [PDF]

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, Sysoeva, Tatyana A., Chen, Baoyu, Chowdhury, Saikat, Guo, Liang, De Carlo, Sacha, Hanson, Jeffrey, Yang, Haw   +7 more
openaire   +1 more source

The AAA+ ATPase p97, a cellular multitool [PDF]

Biochemical Journal, 2017
The AAA+ (ATPases associated with diverse cellular activities) ATPase p97 is essential to a wide range of cellular functions, including endoplasmic reticulum-associated degradation, membrane fusion, NF-κB (nuclear factor kappa-light-chain-enhancer of activated B cells) activation and chromatin-associated processes, which are regulated by ubiquitination.
Freemont, P, Stach, L
openaire   +3 more sources