ライフサイエンスコーパス: AAA-ATPase

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 tion mechanism is likely conserved for other AAA+ ATPases.

6 the presence of RuvBL1-RuvBL2, two essential AAA+ ATPases.

7 lpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases.

8 tamate switch" in six of the seven clades of AAA+ ATPases.

9 esolution reveals that Hda resembles typical AAA+ ATPases.

10 re highly conserved in the ClpX subfamily of AAA+ ATPases.

11 licative hexameric helicases onto origins by AAA+ ATPases.

12 gnition of genomic sites, termed origins, by AAA+ ATPases.

13 ndent on clpV, a gene that likely encodes an AAA(+) ATPase.

14 sinA, an endoplasmic reticulum (ER) resident AAA(+) ATPase.

15 lexes that require activation by specialized AAA(+) ATPases.

16 uding dynamic conformations similar to other AAA(+) ATPases.

17 encoding the Proteosomal Regulatory Particle AAA-ATPase-3 (RPT3).

18 ponents are investigated including HSP101 (a AAA(+) ATPase), a protein of no known function termed PT

19 Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellul

20 p97, a AAA+ ATPase, accumulates on mitochondria upon uncoupling

21 complexes through its remodelling by cognate AAA+ ATPase activators.

22 The evolutionarily conserved AAA ATPase ANCCA (AAA nuclear coregulator cancer-associa

23 independent mechanism that requires only 19S AAA ATPases and 20S proteasome.

24 hromosome maintenance) complex is a toroidal AAA(+) ATPase and the putative eukaryotic replicative he

25 Finally, the p97 AAA(+)-ATPase and its cofactor UFD1 are required for pro

26 associated with diverse cellular activities (AAA) ATPase and to evaluate its potential to be a therap

27 ANCCA is an AAA+ ATPase and a bromodomain-containing nuclear coactiv

28 Potentiated variants of Hsp104, a hexameric AAA+ ATPase and protein disaggregase from yeast, have be

29 er-order assembly and client engagement by a AAA+ ATPase and suggest a mechanistic model where IstB b

30 DnaA is an AAA+ ATPase and the conserved replication initiator in b

31 Like other AAA+ ATPases and self-compartmentalising proteases, Lon

32 o VI is necessary for the full activation of AAA-ATPase and a set of (1)O(2)-responsive transcripts i

33 Topo VI binds to the promoter of the AAA-ATPase and other (1)O(2)-responsive genes, and hence

34 d from MCC by the joint action of the TRIP13 AAA-ATPase and the Mad2-binding protein p31(comet) Now w

35 associated with diverse cellular activities (AAA+ ATPase) and forms ATP-dependent filaments with or w

36 Homohexameric ring AAA(+) ATPases are found in all kingdoms of life and are

37 r results identify a member of the Afg2/Spaf AAA ATPases as a critical in vivo inhibitor of this kina

38 ber of the Afg2/Spaf subfamily of Cdc48-like AAA ATPases as an essential inhibitor of AIR-2 stability

39 The type I AAA (ATPase associated with a variety of cellular activi

40 The p97 AAA (ATPase associated with diverse cellular activities)

41 The AAA (ATPase associated with diverse cellular activities)

42 The FIGL-1 protein contains an AAA (ATPase associated with various activities) domain a

43 protein (VCP) belongs to a highly conserved AAA (ATPases associated with a variety of activities) fa

44 Mutations in p97, a major cytosolic AAA (ATPases associated with a variety of cellular activ

45 Yme1, an AAA (ATPases associated with diverse cellular activities

46 vide evidence for the involvement of the 19S AAA (ATPases associated with diverse cellular activity)

47 Proteins of the AAA (ATPases associated with various cellular activities

48 The AAA(+) (ATPases associated with a variety of cellular ac

49 TorsinA is an essential AAA(+) (ATPases associated with a variety of cellular ac

50 sinA DeltaE) in the C-terminal region of the AAA(+) (ATPases associated with a variety of cellular ac

51 elocalization, as are ClpP and either of the AAA(+) (ATPases associated with a variety of cellular ac

52 charomyces cerevisiae) is a highly conserved AAA(+) (ATPases associated with multiple cellular activi

53 nding proteins (bEBPs) are a subclass of the AAA(+) (ATPases Associated with various cellular Activit

54 Escherichia coli is carried out by ClpB, an AAA(+) (ATPases associated with various cellular activit

55 ctor (NSF) is a homo-hexameric member of the AAA(+) (ATPases associated with various cellular activit

56 h distinct roles for the conserved catalytic AAA(+) (ATPases associated with various cellular activit

57 p97/VCP is a member of the AAA+ (ATPase associated with a variety of activities) pr

58 p97/VCP is a member of the AAA+ (ATPase associated with a variety of activities) pr

59 sed of four heptameric rings, and one or two AAA+ (ATPase associated with a variety of cellular activ

60 t is predicted to adopt a fold resembling an AAA+ (ATPase associated with a variety of cellular activ

61 e report that the nuclear envelope-localized AAA+ (ATPase associated with various cellular activities

62 DnaA protein, a member of the AAA+ (ATPase associated with various cellular activities

63 TorsinA is a membrane-associated AAA+ (ATPases associated with a variety of cellular acti

64 The AAA+ (ATPases associated with a variety of cellular acti

65 rom the Orc1-5 subunits sits atop a layer of AAA+ (ATPases associated with a variety of cellular acti

66 We find that purified Pch2 is an AAA+ (ATPases associated with diverse cellular activitie

67 of chemical energy into mechanical force by AAA+ (ATPases associated with diverse cellular activitie

68 p97/VCP, a member of the AAA+ (ATPases associated with diverse cellular activitie

69 logous to DnaA), a protein homologous to the AAA+ (ATPases associated with diverse cellular activitie

70 Midasin, an essential approximately 540-kDa AAA+ (ATPases associated with diverse cellular activitie

71 gradation in vivo, and LonA is the principal AAA+ (ATPases associated with diverse cellular activitie

72 he bromodomain region of human ATPase family AAA+ (ATPases associated with diverse cellular activitie

73 ancer binding protein (bEBP), members of the AAA+ (ATPases Associated with various cellular Activitie

74 binding domains, cellular initiators possess AAA+ (ATPases associated with various cellular activitie

75 bEBPs are members of the AAA+ (ATPases associated with various cellular activitie

76 Force generation originates from a tandem AAA+ (ATPases associated with various cellular activitie

77 ClpB and Hsp104 are members of the AAA+ (ATPases associated with various cellular activitie

78 lysis and also the helicase function of this AAA+ (ATPases associated with various cellular activitie

79 04, a yeast protein-remodeling factor of the AAA+ (ATPases associated with various cellular activitie

80 all organisms, initiator proteins possessing AAA+ (ATPases associated with various cellular activitie

81 Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellular activities)

82 t targeted deletion of the gene encoding the AAA+-ATPase Atad3a hyperactivated mitophagy in mouse hem

83 only known enzyme in the ESCRT pathway, the AAA ATPase (ATPase associated with diverse cellular acti

84 xameric protein p97, a very abundant type II AAA ATPase (ATPase associated with various cellular acti

85 VPS4B, an AAA ATPase (ATPase associated with various cellular acti

86 dentify Msp1, a conserved, membrane-anchored AAA-ATPase (ATPase associated with a variety of cellular

87 cated AAA+ ATPase (Mycobacterium proteasomal AAA+ ATPase; ATPase forming ring-shaped complexes).

88 Meiotic clade AAA ATPases (ATPases associated with diverse cellular ac

89 The loss of a glutamic acid residue in the AAA-ATPase (ATPases associated with diverse cellular act

90 sly, we and others have reported that TRIP13 AAA-ATPase binds to the mitotic checkpoint-silencing pro

91 ring-shaped cylindrical oligomer like other AAA(+) ATPases, but this has been difficult to directly

92 Msp1 is a transmembrane AAA-ATPase, but its role in TA protein clearance is not

93 st-fusion, the complex is disassembled by an AAA+ ATPase called N-ethylmaleimide-sensitive factor (NS

94 asis of phylogenetic classification of their AAA ATPase cassette, include four relatively well charac

95 and trafficking) domain followed by a single AAA ATPase cassette.

96 also relieves autoinhibition and primes the AAA ATPase cassettes for substrate binding.

97 Raman et al. and Franz et al. establish the AAA ATPase CDC-48/p97 as an essential regulator of eukar

98 rms a SUMO-specific ternary complex with the AAA ATPase Cdc48 and an adaptor, Doa1.

99 rate that UBXN-2, a substrate adaptor of the AAA ATPase Cdc48/p97, is required to coordinate centroso

100 We identify the AAA(+) ATPase Cdc48 and its cofactors as the Ub receptor

101 stress induces selective recruitment of the AAA(+) ATPase Cdc48/p97 to catalyze dissociation of the

102 associated with diverse cellular activities (AAA(+)) ATPase Cdc48.

103 ese processes are catalyzed by the conserved AAA-ATPase Cdc48 (also known as p97).

104 The AAA-ATPase Cdc48 and the Hsp70 chaperone Ssa1 are crucia

105 The yeast AAA-ATPase Cdc48 and the ubiquitin fusion degradation (U

106 g anaphase B, Imp1-mediated transport of the AAA-ATPase Cdc48 protein at the MMD allows this disassem

107 ylation, we demonstrated that Rbd2 binds the AAA-ATPase Cdc48 through a C-terminal SHP box.

108 found associated, together with Ltn1 and the AAA-ATPase Cdc48, to 60S ribosomal subunits.

109 nd functionally interacts with the conserved AAA-ATPase Cdc48.

110 c complementation to a gene encoding a novel AAA-ATPase/CDC48 family member called TgNoAP1.

111 retrotranslocation, which required ATP, the AAA-ATPase Cdc48p, and its receptor Ubx2p.

112 The hexameric AAA-ATPase, Cdc48p, catalyzes an array of cellular activ

113 CDC48/p97 is a conserved homohexameric AAA-ATPase chaperone required for a variety of cellular

114 regulator of Arabidopsis CDC48, an essential AAA-ATPase chaperone that mediates diverse cellular acti

115 Bacterial AAA+ ATPase ClpB cooperates with DnaK during reactivatio

116 The AAA(+) ATPase ClpV disassembles the contracted sheath, w

117 Here, we show that the RuvBL1 and RuvBL2 AAA+ ATPases co-purify with FA core complex isolated und

118 nknown, but it is thought to involve the p97 AAA-ATPase complex and bears a topological equivalence t

119 heat shock protein 101 (HSP101), a ClpB-like AAA+ ATPase component of PTEX.

120 t vaccinia virus (VACV) to identify the VACV AAA+ ATPase D5 as the poxvirus uncoating factor.

121 Dedicated AAA+ ATPases deposit hexameric ring-shaped helicases ont

122 An AAA+ ATPase, DnaC, delivers DnaB helicase at the E. coli

123 echanistically, this is dependent on SAF-A's AAA(+) ATPase domain, which mediates cycles of protein o

124 leQ, the second messenger interacts with the AAA+ ATPase domain at a site distinct from the ATP bindi

125 Crystal structures of FleQ's AAA+ ATPase domain in its apo-state or bound to ADP or A

126 The viral protein binds to the loader's AAA+ ATPase domain, allowing binding of the host replica

127 ive interactions between the large and small AAA ATPase domains of adjacent Vps4 subunits, suggesting

128 Previous studies of AAA(+) ATPase domains from sigma(54) activators have sho

129 l DNA binding elements, initiators use their AAA+ ATPase domains to recognize origin DNA.

130 Here we identify the AAA-ATPase Drg1 as a target of diazaborine.

131 The AAA-ATPase Drg1 is essential for the release of several

132 ubiquitin-system or a HORMA domain-PCH2-like AAA+ ATPase dyad.

133 The transcription factor FleQ is a bacterial AAA+ ATPase enhancer-binding protein that is the master

134 ved and essential residue in many GTPase and AAA+ ATPase enzymes that completes the active site from

135 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of

136 s a highly abundant protein belonging to the AAA ATPase family involved in a number of essential cell

137 p is an abundant and conserved member of the AAA ATPase family of molecular chaperones.

138 ein (VCP), also known as p97, is a member of AAA ATPase family that is involved in several biological

139 t GENERAL CONTROL NONREPRESSIBLE4 (GCN4), an AAA(+)-ATPase family protein, as one of the key proteins

140 A (also known as ATAD2), a new member of the AAA+ ATPase family proteins, as a novel AR coactivator.

141 ATPases are the only representatives of the AAA+ ATPase family that reside in the lumen of the endop

142 is a highly expressed member of the type II AAA+ ATPase family.

143 The flagella export AAA+ ATPase FliI was identified as a result of this scre

144 uch as Mu, Tn7, and IS21, require regulatory AAA+ ATPases for function.

145 It is not understood how Hsp104, a hexameric AAA+ ATPase from yeast, disaggregates diverse structures

146 Meiotic clade AAA ATPases function as hexamers that can cycle between

147 trol of the promoter of a (1)O(2)-responsive AAA-ATPase gene (At3g28580) and isolating second-site mu

148 me, above the N-terminal coiled coils of the AAA-ATPase heterodimers Rpt4/Rpt5 and Rpt1/Rpt2, respect

149 eals previously unidentified features of the AAA-ATPase heterohexamer.

150 We previously identified the AAA+ ATPase homolog ruvb-1 as a potent suppressor of pha

151 onserved bromodomain-containing protein with AAA-ATPase homology originally implicated in heterochrom

152 , the J-protein Sis1, the Hsp70 Ssa, and the AAA+ ATPase Hsp104, act sequentially in the fragmentatio

153 1, an Ssa Hsp70 co-chaperone, as well as the AAA+ ATPase, Hsp104, for its propagation.

154 TorsinA is a membrane-tethered AAA+ ATPase implicated in nuclear envelope dynamics as w

155 Msp1 is a conserved AAA ATPase in budding yeast localized to mitochondria wh

156 ay could shed light on a general role of 19S AAA ATPases in processing tight protein-DNA complexes du

157 O-GlcNAcylation of Rpt2, one of the AAA ATPases in the 19 S regulatory cap, shuts off the pr

158 A AAA+ ATPase in the clamp loader clade, RarA protein is p

159 TorsinA (TorA) is an AAA+ ATPase in the endoplasmic reticulum (ER) lumen that

160 Each RP is believed to include six different AAA+ ATPases in a heterohexameric ring that binds the CP

161 ersions of ESCRT-III components and the VPS4 AAA ATPase, indicating that Itch-mediated correction of

162 ng revealed the presence of p97, a cytosolic AAA ATPase instrumental in the extraction and delivery o

163 and katanin are related microtubule-severing AAA ATPases involved in constructing neuronal and non-ce

164 97 or N-ethylmaleimide-sensitive factor (two AAA ATPases involved in membrane fusion) and their cofac

165 identify a new VBP1 binding partner, p97, an AAA(+) ATPase involved in protein degradation and DNA da

166 actly where the arginine finger of canonical AAA+ ATPases is found.

167 r DNA damage, little is known about how this AAA-ATPase is involved in the transcriptional process.

168 now define the decameric organization of the AAA+ ATPase IstB, unveiling key insights into its target

169 Receptor Interacting Protein 13 (TRIP13), an AAA-ATPase known to interact with p31(comet).

170 H domain, while one, L738P, localized to the AAA ATPase-like domain within the C-terminal half of Sir

171 TorsinA is an AAA+ ATPase located within the lumen of the endoplasmic

172 striking, unifying feature of meiotic clade AAA ATPases may be their MIT domain, which is a module t

173 ults suggest that the functionality of other AAA+ ATPases may be also optimized by interaction and sy

174 erved, opening up the possibility that other AAA+ ATPases may respond to c-di-GMP.

175 for the construction of atomic models of the AAA(+) ATPase module as it progresses through the functi

176 ase of the RP is formed by a heterohexameric AAA(+) ATPase module, which unfolds and translocates sub

177 Its AAA-ATPase module adopts essentially the same topology t

178 amer, which connects to the CP and roofs the AAA-ATPase module, positioning the Rpn8/Rpn11 heterodime

179 mmitment and prior to their unfolding by the AAA-ATPase module.

180 nd a regulatory particle (RP) containing the AAA-ATPase module.

181 Valosin-containing protein (VCP)/p97 is an AAA ATPase molecular chaperone that regulates vital cell

182 by mutations in the evolutionarily conserved AAA-ATPase molecular chaperone, CDC48A, homologous to ye

183 tered abundance of transport proteins having AAA-ATPase motifs.

184 The AAA+ ATPase motor cytoplasmic dynein regulates ciliary t

185 We show that the AAA+ ATPase Msp1 limits the accumulation of mislocalized

186 Spastin, an AAA ATPase mutated in the neurodegenerative disease here

187 s are recognized and unfolded by a dedicated AAA+ ATPase (Mycobacterium proteasomal AAA+ ATPase; ATPa

188 on, the SNARE complex is disassembled by the AAA-ATPase N-ethylmaleimide-sensitive factor that requir

189 in of Rpn11 is positioned directly above the AAA-ATPase N-ring suggesting that Rpn11 deubiquitylates

190 of the amino-terminal domain of an archaeal AAA ATPase of unknown function shows that it is closely

191 solically dislocated, in cells deficient for AAA-ATPases of the proteasome 19 S regulatory particle.

192 The human AAA ATPase p97 is a molecular chaperone essential in cel

193 -associated degradation, the multifunctional AAA ATPase p97 is part of a protein degradation complex.

194 The essential and highly abundant hexameric AAA ATPase p97 is perhaps the best studied AAA protein,

195 islocation reaction, including the cytosolic AAA ATPase p97, the membrane protein Derlin-1, and the E

196 TRIM21 or chemical inhibition of either the AAA ATPase p97/valosin-containing protein (VCP) or the p

197 rough the activity of the proteasome and the AAA ATPase p97/VCP in a similar manner to infectious vir

198 chinery that includes ubiquitin ligase gp78, AAA ATPase p97/VCP, and the putative channel Derlin1.

199 he unexpected collaboration of the cytosolic AAA-ATPase p97 and the luminal quality control factor UD

200 t was unclear whether they would require the AAA-ATPase p97 chaperone complex that retrotranslocates/

201 The AAA-ATPase p97 plays vital roles in mechanisms of protei

202 that DNA-locked Ku rings are released by the AAA-ATPase p97.

203 the cytosol in a manner that depends on the AAA-ATPase p97/VCP [3].

204 Cisternal membrane fusion requires two AAA ATPases, p97 and NSF (N-ethylmaleimide-sensitive fus

205 an essential role for the ubiquitin-directed AAA-ATPase, p97, in the clearance of damaged lysosomes b

206 We show that an AAA-ATPase, p97, is required for the proteasomal degrada

207 rm a complex with Derlin-1 and an associated AAA-ATPase, p97.

208 Exclusion requires the AAA+-ATPase Pch2 and is directly coupled to synaptonemal

209 The widely conserved AAA+-ATPase Pch2 mediates this pattern, likely by means

210 The traffic AAA-ATPase PilF is essential for pilus biogenesis and na

211 Our results suggest that 19S AAA ATPases play a dual role in sensing the Top2beta cle

212 report that Isu is degraded by the Lon-type AAA+ ATPase protease of the mitochondrial matrix, Pim1.

213 13 ortholog PCH-2, revealing a new family of AAA+ ATPase protein remodelers.

214 pendent Esigma(54) and its cognate activator AAA+ ATPase protein, before ADP+P(i) formation, using a

215 uvBL1/RuvBL2 or pontin/reptin) are enigmatic AAA(+) ATPase proteins that are present in multiple cell

216 xes at chromatin is a process facilitated by AAA+ ATPase proteins.

217 mingly incompatible symmetries-the hexameric AAA+ ATPase RavA and the decameric inducible lysine deca

218 a mechanochemical process through which the AAA ATPase Rea1 induces release of an assembly protein c

219 until remodeling of the pre-ribosome by the AAA-ATPase Rea1 (Midasin).

220 In cells, dedicated AAA+ ATPases regulate loading, however, the mechanism by

221 show that p37/UBXN2B, a cofactor of the p97 AAA ATPase, regulates spindle orientation in mammalian c

222 ent ubiquitylation also involves VCP/p97, an AAA ATPase regulating the folding of various cellular su

223 Multimeric AAA ATPases represent a structurally homologous yet func

224 VPS4 proteins are AAA(+) ATPases required to form multivesicular bodies, r

225 Pex1 and Pex6 are Type-2 AAA+ ATPases required for the de novo biogenesis of pero

226 mily; Bro1, a homolog of Alix; and Vps4, the AAA-ATPase required for ESCRT function in all contexts/o

227 E) mutation in TOR1A, which encodes torsinA, AAA(+) ATPase resident in the lumen of the endoplasmic r

228 Torsins are membrane-tethered AAA+ ATPases residing in the nuclear envelope (NE) and e

229 three-dimensional structure comparisons with AAA+ ATPases revealed the presence of Walker A (GPPGVGKT

230 roteasome contains a heterohexameric ring of AAA-ATPases (RPT1-6) that unfolds and inserts substrates

231 function of the subunit regulatory particle AAA ATPase (RPT2a) causes a weak defect in 26S proteasom

232 2/p27, binds to the C-terminal region of the AAA-ATPase Rpt5.

233 f the GABAB2 C terminus with the proteasomal AAA-ATPase Rpt6.

234 We have tested this method on the AAA+ ATPase Rubisco activase (Rca).

235 proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2.

236 ing 14 different polypeptides, including the AAA+ ATPases Rvb1 and Rvb2.

237 hancer-binding protein (bEBP) with a central AAA+ ATPase sigma(54)-interaction domain, flanked by a C

238 The AAA ATPase Spastin severs microtubules along their lengt

239 h the phosphorylation at Ser(120) of another AAA ATPase subunit, Rpt6.

240 ve NADH binding motif (GxGxxG) including the AAA-ATPase subunit, Psmc1 (Rpt2).

241 easome, the 20S particle is regulated by six AAA ATPase subunits and, in archaea, by a homologous rin

242 and may guide the development of additional AAA+ ATPase superfamily inhibitors.

243 a bacterial enhancer-binding protein of the AAA+ ATPase superfamily, is inhibited by an unprecedente

244 en five RavA rings is unique for the diverse AAA+ ATPase superfamily.

245 id deletion in torsinA (TA), a member of the AAA+ ATPase superfamily.

246 in the SF3 helicase family, a subset of the AAA+ ATPase superfamily.

247 Helices unique to the microtubule-severing AAA ATPases surround the entrances to the pore on either

248 r protein sorting 4 (Vps4), which encodes an AAA ATPase that interacts with the ESCRT-III complex to

249 Spastin is a hexameric ring AAA ATPase that severs microtubules.

250 uble-stranded DNA (dsDNA) viruses contain an AAA(+) ATPase that assembles into oligomers, often hexam

251 Magnesium chelatase is an AAA(+) ATPase that catalyzes the first committed step in

252 Magnesium chelatase is an AAA(+) ATPase that catalyzes the first step in chlorophy

253 charomyces cerevisiae) is a highly conserved AAA(+)-ATPase that regulates a wide array of cellular pr

254 transcriptional activators forms a hexameric AAA+ ATPase that acts through conformational changes bro

255 DnaA is the widely conserved bacterial AAA+ ATPase that functions as both the replication initi

256 p97/VCP is an essential, abundant AAA+ ATPase that is conserved throughout eukaryotes, wit

257 This study identifies an AAA+ ATPase that plays a critical role in regulating the

258 n (DeltaE) at position 302/303 of TorsinA, a AAA+ ATPase that resides in the endoplasmic reticulum.

259 osome DNA replication is mediated by DnaA, a AAA+ ATPase that unwinds the origin of replication.

260 equires the activity of Rubisco activase, an AAA+ ATPase that utilizes chemo-mechanical energy to cat

261 Torsin proteins are AAA+ ATPases that localize to the endoplasmic reticular/

262 s tubular lysosomal network requires VCP, an AAA-ATPase that, when mutated, causes degenerative disea

263 Pex1 and Pex6 are two AAA-ATPases that play a crucial role in peroxisome bioge

264 Here we describe and characterize the AAA+ ATPase Thorase, which regulates the expression of s

265 substrate interacts with Rv3868, a cytosolic AAA ATPase, through its C-terminus.

266 erstood endoplasmic reticulum (ER)-localized AAA+ ATPases, through a conserved, perinuclear domain.

267 The AAA-ATPase thyroid hormone receptor interacting protein

268 Pase domain, the Ies2 and Ies6 proteins, the AAA(+) ATPases Tip49a and Tip49b, and the actin-related

269 Saunders et al. show that the AAA+ ATPase torsinA and its partner LAP1 are required fo

270 The AAA+ ATPase TRIP13 regulates both MAD2 and meiotic HORMA

271 Here, we report that the conserved AAA+ ATPase TRIP13(PCH-2) localizes to unattached kineto

272 Here we describe a mechanism where the AAA-ATPase TRIP13 promotes treatment resistance.

273 ive oxidase1a, NADH dehydrogenaseB2, and the AAA ATPase Ubiquinol-cytochrome c reductase synthesis1),

274 strates depends on its being partnered by an AAA+ ATPase/unfoldase, ClpA or ClpX.

275 ugh poorly defined reactions mediated by the AAA-ATPase valosin-containing protein (VCP)/p97 and augm

276 C1orf124 also binds to the AAA-ATPase valosin-containing protein via its SHP domain

277 protein that we termed VWA interacting with AAA+ ATPase (ViaA) containing a von Willebrand Factor A

278 The AAA ATPase Vps4 disassembles the membrane-bound ESCRT-II

279 The hexameric AAA ATPase Vps4 drives membrane fission by remodeling an

280 The AAA ATPase Vps4 is recruited to membrane necks shortly b

281 A component of this pathway, the AAA ATPase Vps4, provides energy for pathway progression

282 y of the ESCRT-III complex by recruiting the AAA ATPase Vps4.

283 in disassembly of ESCRT-III polymers by the AAA ATPase Vps4.

284 The ESCRT machinery along with the AAA+ ATPase Vps4 drive membrane scission for trafficking

285 e effects of inhibiting the ESCRT-associated AAA+ ATPase VPS4 on EV release from cultured cells using

286 The AAA+ ATPase VPS4 plays an essential role in multivesicul

287 The AAA-ATPase Vps4 catalyzes disassembly of the ESCRT-III c

288 The AAA-ATPase Vps4 is critical for function of the MVB sort

289 The AAA-ATPase Vps4 is required for ESCRT function, and its

290 The AAA-ATPase Vps4 is required for ESCRT-III disassembly, h

291 r transport (ESCRT)-III subunit Snf7 and the AAA-ATPase Vps4 to destabilize and clear defective NPC a

292 ruiting Vps2, which subsequently engages the AAA-ATPase Vps4 to dissociate ESCRT-III.

293 their disassembly requires the action of the AAA-ATPase Vps4.

294 The vacuolar protein sorting 4 AAA-ATPase (Vps4) recycles endosomal sorting complexes r

295 dodecamer, and argue that, like other type I AAA ATPases, Vps4 functions as a single ring with six su

296 As an AAA-ATPase, Vps4 is important for function of multivesic

297 ssociated with various cellular activities" (AAA(+)) ATPases, which use mechanical forces powered by

298 s the formation of a heterohexameric ring of AAA-ATPases, which is guided by at least four RP assembl

299 This reaction is catalyzed by VPS4, an AAA-ATPase whose activity is tightly regulated by a host

300 p97 is a AAA-ATPase with multiple cellular functions, one of whic