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1 isingly, without the involvement of the Vps4 AAA-ATPase.
2 ocess and may shed light on studies of other AAA ATPases.
3 bl1) and Reptin (Ruvbl2) are closely related AAA ATPases.
4 ly applicable to other protein-translocating AAA ATPases.
5 g ATPase cycle, which is likely conserved in AAA-ATPases.
6 veals an additional regulatory mechanism for AAA+ ATPases.
7 licative hexameric helicases onto origins by AAA+ ATPases.
8 gnition of genomic sites, termed origins, by AAA+ ATPases.
9 the presence of RuvBL1-RuvBL2, two essential AAA+ ATPases.
10 lpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases.
11 of protein translocation by Cdc48 and other AAA+ ATPases.
12 tion mechanism is likely conserved for other AAA+ ATPases.
13 ay reflect an entirely new characteristic of AAA + ATPases.
14 sinA, an endoplasmic reticulum (ER) resident AAA(+) ATPase.
15 ndent on clpV, a gene that likely encodes an AAA(+) ATPase.
16 uding dynamic conformations similar to other AAA(+) ATPases.
17 lexes that require activation by specialized AAA(+) ATPases.
18 rotein (RIME) assay, we identified RuvB-like AAA ATPase 1 (RUVBL1/Pontin) and enhancer of rudimentary
19 ponents are investigated including HSP101 (a AAA(+) ATPase), a protein of no known function termed PT
21 motor domain of dynein contains three active AAA+ ATPases (AAA1, 3, and 4), only the functions of AAA
24 a single-stranded DNA coil, akin to the way AAA+ ATPases (adenosine triphosphatases) unfold peptides
31 associated with diverse cellular activities (AAA) ATPase and to evaluate its potential to be a therap
33 Potentiated variants of Hsp104, a hexameric AAA+ ATPase and protein disaggregase from yeast, have be
34 er-order assembly and client engagement by a AAA+ ATPase and suggest a mechanistic model where IstB b
37 o VI is necessary for the full activation of AAA-ATPase and a set of (1)O(2)-responsive transcripts i
39 d from MCC by the joint action of the TRIP13 AAA-ATPase and the Mad2-binding protein p31(comet) Now w
40 associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or w
43 massive (>500 kDa) protein has an N-terminal AAA (ATPase associated with diverse cellular activities)
50 charomyces cerevisiae) is a highly conserved AAA(+) (ATPases associated with multiple cellular activi
51 nding proteins (bEBPs) are a subclass of the AAA(+) (ATPases Associated with various cellular Activit
52 Escherichia coli is carried out by ClpB, an AAA(+) (ATPases associated with various cellular activit
53 ctor (NSF) is a homo-hexameric member of the AAA(+) (ATPases associated with various cellular activit
55 sed of four heptameric rings, and one or two AAA+ (ATPase associated with a variety of cellular activ
56 t is predicted to adopt a fold resembling an AAA+ (ATPase associated with a variety of cellular activ
57 l channel of the OEM, and CDC48, a cytosolic AAA+ (ATPase associated with diverse cellular activities
59 e report that the nuclear envelope-localized AAA+ (ATPase associated with various cellular activities
61 bacterium tuberculosis collaborates with the AAA+ (ATPases associated with a variety of cellular acti
62 rom the Orc1-5 subunits sits atop a layer of AAA+ (ATPases associated with a variety of cellular acti
64 gradation in vivo, and LonA is the principal AAA+ (ATPases associated with diverse cellular activitie
65 he bromodomain region of human ATPase family AAA+ (ATPases associated with diverse cellular activitie
67 of chemical energy into mechanical force by AAA+ (ATPases associated with diverse cellular activitie
70 Midasin, an essential approximately 540-kDa AAA+ (ATPases associated with diverse cellular activitie
71 all organisms, initiator proteins possessing AAA+ (ATPases associated with various cellular activitie
72 ancer binding protein (bEBP), members of the AAA+ (ATPases Associated with various cellular Activitie
73 binding domains, cellular initiators possess AAA+ (ATPases associated with various cellular activitie
75 ase with distinct N-terminal, transmembrane, AAA+ (ATPases associated with various cellular activitie
77 t targeted deletion of the gene encoding the AAA+-ATPase Atad3a hyperactivated mitophagy in mouse hem
78 xameric protein p97, a very abundant type II AAA ATPase (ATPase associated with various cellular acti
80 dentify Msp1, a conserved, membrane-anchored AAA-ATPase (ATPase associated with a variety of cellular
83 sly, we and others have reported that TRIP13 AAA-ATPase binds to the mitotic checkpoint-silencing pro
84 ring-shaped cylindrical oligomer like other AAA(+) ATPases, but this has been difficult to directly
86 st-fusion, the complex is disassembled by an AAA+ ATPase called N-ethylmaleimide-sensitive factor (NS
87 asis of phylogenetic classification of their AAA ATPase cassette, include four relatively well charac
90 1 (LAP1), an activator of ER-resident Torsin AAA+-ATPases, causes a failure in membrane removal from
91 Raman et al. and Franz et al. establish the AAA ATPase CDC-48/p97 as an essential regulator of eukar
93 rate that UBXN-2, a substrate adaptor of the AAA ATPase Cdc48/p97, is required to coordinate centroso
95 stress induces selective recruitment of the AAA(+) ATPase Cdc48/p97 to catalyze dissociation of the
100 g anaphase B, Imp1-mediated transport of the AAA-ATPase Cdc48 protein at the MMD allows this disassem
104 0 and serves as a recruitment signal for the AAA-ATPase Cdc48/p97, which actively disassembles the co
107 regulator of Arabidopsis CDC48, an essential AAA-ATPase chaperone that mediates diverse cellular acti
110 Here, we show that the RuvBL1 and RuvBL2 AAA+ ATPases co-purify with FA core complex isolated und
111 nknown, but it is thought to involve the p97 AAA-ATPase complex and bears a topological equivalence t
112 Moreover, we found involvement of the Cdc48 AAA-ATPase complex members Ufd1 and Npl4, as well as the
113 n addition to a role for the Cdc48-Npl4-Ufd1 AAA-ATPase complex, Doa1 and a mitochondrial pool of the
119 echanistically, this is dependent on SAF-A's AAA(+) ATPase domain, which mediates cycles of protein o
120 leQ, the second messenger interacts with the AAA+ ATPase domain at a site distinct from the ATP bindi
122 The viral protein binds to the loader's AAA+ ATPase domain, allowing binding of the host replica
129 The transcription factor FleQ is a bacterial AAA+ ATPase enhancer-binding protein that is the master
130 ionarily conserved microtubule (MT)-severing AAA-ATPase enzyme Katanin is emerging as a critical regu
131 ved and essential residue in many GTPase and AAA+ ATPase enzymes that completes the active site from
132 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of
133 s a highly abundant protein belonging to the AAA ATPase family involved in a number of essential cell
134 ein (VCP), also known as p97, is a member of AAA ATPase family that is involved in several biological
135 t GENERAL CONTROL NONREPRESSIBLE4 (GCN4), an AAA(+)-ATPase family protein, as one of the key proteins
137 ATPases are the only representatives of the AAA+ ATPase family that reside in the lumen of the endop
143 aplegia protein M1 Spastin, a membrane-bound AAA ATPase found on LDs, coordinates fatty acid (FA) tra
144 It is not understood how Hsp104, a hexameric AAA+ ATPase from yeast, disaggregates diverse structures
146 trol of the promoter of a (1)O(2)-responsive AAA-ATPase gene (At3g28580) and isolating second-site mu
147 me, above the N-terminal coiled coils of the AAA-ATPase heterodimers Rpt4/Rpt5 and Rpt1/Rpt2, respect
149 onserved bromodomain-containing protein with AAA-ATPase homology originally implicated in heterochrom
152 ay could shed light on a general role of 19S AAA ATPases in processing tight protein-DNA complexes du
154 Each RP is believed to include six different AAA+ ATPases in a heterohexameric ring that binds the CP
155 97 or N-ethylmaleimide-sensitive factor (two AAA ATPases involved in membrane fusion) and their cofac
156 identify a new VBP1 binding partner, p97, an AAA(+) ATPase involved in protein degradation and DNA da
159 r DNA damage, little is known about how this AAA-ATPase is involved in the transcriptional process.
160 served nonstructural protein 2C, which is an AAA+ ATPase, is a promising target for drug development.
161 now define the decameric organization of the AAA+ ATPase IstB, unveiling key insights into its target
167 striking, unifying feature of meiotic clade AAA ATPases may be their MIT domain, which is a module t
169 ations indicate a general mechanism by which AAA+ ATPases may translocate a variety of substrates tha
170 for the construction of atomic models of the AAA(+) ATPase module as it progresses through the functi
171 ase of the RP is formed by a heterohexameric AAA(+) ATPase module, which unfolds and translocates sub
173 amer, which connects to the CP and roofs the AAA-ATPase module, positioning the Rpn8/Rpn11 heterodime
177 Valosin-containing protein (VCP)/p97 is an AAA ATPase molecular chaperone that regulates vital cell
178 by mutations in the evolutionarily conserved AAA-ATPase molecular chaperone, CDC48A, homologous to ye
184 s are recognized and unfolded by a dedicated AAA+ ATPase (Mycobacterium proteasomal AAA+ ATPase; ATPa
185 on, the SNARE complex is disassembled by the AAA-ATPase N-ethylmaleimide-sensitive factor that requir
186 in of Rpn11 is positioned directly above the AAA-ATPase N-ring suggesting that Rpn11 deubiquitylates
187 solically dislocated, in cells deficient for AAA-ATPases of the proteasome 19 S regulatory particle.
189 The essential and highly abundant hexameric AAA ATPase p97 is perhaps the best studied AAA protein,
190 TRIM21 or chemical inhibition of either the AAA ATPase p97/valosin-containing protein (VCP) or the p
191 rough the activity of the proteasome and the AAA ATPase p97/VCP in a similar manner to infectious vir
193 he unexpected collaboration of the cytosolic AAA-ATPase p97 and the luminal quality control factor UD
194 t was unclear whether they would require the AAA-ATPase p97 chaperone complex that retrotranslocates/
198 ting inhibition of a conserved Dictyostelium AAA ATPase, p97, a homolog of the human transitional end
200 an essential role for the ubiquitin-directed AAA-ATPase, p97, in the clearance of damaged lysosomes b
203 tures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase).
205 Signaling is attenuated by a homolog of the AAA+ ATPase Pch2/TRIP13, which binds and disassembles th
209 tly phosphorylates parasite RPT1, one of six AAA(+) ATPases present in the 19S regulatory particle of
210 report that Isu is degraded by the Lon-type AAA+ ATPase protease of the mitochondrial matrix, Pim1.
213 pendent Esigma(54) and its cognate activator AAA+ ATPase protein, before ADP+P(i) formation, using a
214 uvBL1/RuvBL2 or pontin/reptin) are enigmatic AAA(+) ATPase proteins that are present in multiple cell
216 mingly incompatible symmetries-the hexameric AAA+ ATPase RavA and the decameric inducible lysine deca
218 show that p37/UBXN2B, a cofactor of the p97 AAA ATPase, regulates spindle orientation in mammalian c
219 ent ubiquitylation also involves VCP/p97, an AAA ATPase regulating the folding of various cellular su
223 mily; Bro1, a homolog of Alix; and Vps4, the AAA-ATPase required for ESCRT function in all contexts/o
225 E) mutation in TOR1A, which encodes torsinA, AAA(+) ATPase resident in the lumen of the endoplasmic r
227 ns between the lid subunit Rpn5 and the base AAA+ ATPase ring are important for stabilizing the subst
228 roteasome contains a heterohexameric ring of AAA-ATPases (RPT1-6) that unfolds and inserts substrates
229 function of the subunit regulatory particle AAA ATPase (RPT2a) causes a weak defect in 26S proteasom
234 ing known regulators, we discovered that the AAA+ ATPase RUVBL1 is necessary for Nrf1's transcription
236 hancer-binding protein (bEBP) with a central AAA+ ATPase sigma(54)-interaction domain, flanked by a C
240 easome, the 20S particle is regulated by six AAA ATPase subunits and, in archaea, by a homologous rin
242 a bacterial enhancer-binding protein of the AAA+ ATPase superfamily, is inhibited by an unprecedente
247 r protein sorting 4 (Vps4), which encodes an AAA ATPase that interacts with the ESCRT-III complex to
249 uble-stranded DNA (dsDNA) viruses contain an AAA(+) ATPase that assembles into oligomers, often hexam
252 charomyces cerevisiae) is a highly conserved AAA(+)-ATPase that regulates a wide array of cellular pr
253 transcriptional activators forms a hexameric AAA+ ATPase that acts through conformational changes bro
256 p97 is a highly abundant, homohexameric AAA+ ATPase that performs a variety of essential cellula
258 n (DeltaE) at position 302/303 of TorsinA, a AAA+ ATPase that resides in the endoplasmic reticulum.
259 LAP1 binds to and activates torsinA, an AAA+ ATPase that resides in the perinuclear space and co
260 equires the activity of Rubisco activase, an AAA+ ATPase that utilizes chemo-mechanical energy to cat
262 s tubular lysosomal network requires VCP, an AAA-ATPase that, when mutated, causes degenerative disea
263 s - katanin, spastin, fidgetin - are related AAA-ATPases that cut microtubules into shorter filaments
266 erstood endoplasmic reticulum (ER)-localized AAA+ ATPases, through a conserved, perinuclear domain.
268 Pase domain, the Ies2 and Ies6 proteins, the AAA(+) ATPases Tip49a and Tip49b, and the actin-related
275 ive oxidase1a, NADH dehydrogenaseB2, and the AAA ATPase Ubiquinol-cytochrome c reductase synthesis1),
277 ugh poorly defined reactions mediated by the AAA-ATPase valosin-containing protein (VCP)/p97 and augm
279 protein that we termed VWA interacting with AAA+ ATPase (ViaA) containing a von Willebrand Factor A
282 sport III (ESCRT-III) subunit CHMP2A and the AAA ATPase VPS4, but their regulatory mechanisms remain
286 e effects of inhibiting the ESCRT-associated AAA+ ATPase VPS4 on EV release from cultured cells using
287 rsions of peptides bind to the S. cerevisiae AAA+ ATPase Vps4 with similar affinities, and determined
290 r transport (ESCRT)-III subunit Snf7 and the AAA-ATPase Vps4 to destabilize and clear defective NPC a
293 dodecamer, and argue that, like other type I AAA ATPases, Vps4 functions as a single ring with six su
295 ssociated with various cellular activities" (AAA(+)) ATPases, which use mechanical forces powered by
296 s the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembl
299 ), also named p97, is an essential hexameric AAA+ ATPase with diverse functions in the ubiquitin syst