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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
20                         Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellul
21 motor domain of dynein contains three active AAA+ ATPases (AAA1, 3, and 4), only the functions of AAA
22                                       p97, a AAA+ ATPase, accumulates on mitochondria upon uncoupling
23 complexes through its remodelling by cognate AAA+ ATPase activators.
24  a single-stranded DNA coil, akin to the way AAA+ ATPases (adenosine triphosphatases) unfold peptides
25 f substrate translocation proposed for other AAA+ ATPases (adenosine triphosphatases).
26                 The evolutionarily conserved AAA ATPase ANCCA (AAA nuclear coregulator cancer-associa
27 independent mechanism that requires only 19S AAA ATPases and 20S proteasome.
28                                          The AAA(+) ATPase and bromodomain factor ATAD2/ANCCA is over
29                      Since Yta7(ATAD2) is an AAA(+) ATPase and potential hexameric unfoldase, our res
30                             Finally, the p97 AAA(+)-ATPase and its cofactor UFD1 are required for pro
31 associated with diverse cellular activities (AAA) ATPase and to evaluate its potential to be a therap
32                                  ANCCA is an AAA+ ATPase and a bromodomain-containing nuclear coactiv
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
35                                   DnaA is an AAA+ ATPase and the conserved replication initiator in b
36                                   Like other AAA+ ATPases and self-compartmentalising proteases, Lon
37 o VI is necessary for the full activation of AAA-ATPase and a set of (1)O(2)-responsive transcripts i
38         Topo VI binds to the promoter of the AAA-ATPase and other (1)O(2)-responsive genes, and hence
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
41                           Homohexameric ring AAA(+) ATPases are found in all kingdoms of life and are
42                                      The p97 AAA (ATPase associated with diverse cellular activities)
43 massive (>500 kDa) protein has an N-terminal AAA (ATPase associated with diverse cellular activities)
44                                          The AAA (ATPase associated with diverse cellular activities)
45               The FIGL-1 protein contains an AAA (ATPase associated with various activities) domain a
46          Mutations in p97, a major cytosolic AAA (ATPases associated with a variety of cellular activ
47                                     Yme1, an AAA (ATPases associated with diverse cellular activities
48                              Proteins of the AAA (ATPases associated with various cellular activities
49                                          The AAA(+) (ATPases associated with a variety of cellular ac
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
54                   p97/VCP is a member of the AAA+ (ATPase associated with a variety of activities) pr
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
58                DnaA protein, a member of the AAA+ (ATPase associated with various cellular activities
59 e report that the nuclear envelope-localized AAA+ (ATPase associated with various cellular activities
60                                          The AAA+ (ATPases associated with a variety of cellular acti
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
63             TorsinA is a membrane-associated 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
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                                              AAA+ (ATPases associated with diverse cellular activitie
69                     p97/VCP, a member of the 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
74                     bEBPs are members of the AAA+ (ATPases associated with various cellular activitie
75 ase with distinct N-terminal, transmembrane, AAA+ (ATPases associated with various cellular activitie
76           Dynein contains four AAA+ ATPases (AAA: ATPase associated with various cellular activities)
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
79                                    VPS4B, an AAA ATPase (ATPase associated with various cellular acti
80 dentify Msp1, a conserved, membrane-anchored AAA-ATPase (ATPase associated with a variety of cellular
81 cated AAA+ ATPase (Mycobacterium proteasomal AAA+ ATPase; ATPase forming ring-shaped complexes).
82                                Meiotic clade AAA ATPases (ATPases associated with diverse cellular ac
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
85                      Msp1 is a transmembrane AAA-ATPase, but its role in TA protein clearance is not
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
88 and trafficking) domain followed by a single AAA ATPase cassette.
89  also relieves autoinhibition and primes the AAA ATPase cassettes for substrate binding.
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
92 rms a SUMO-specific ternary complex with the AAA ATPase Cdc48 and an adaptor, Doa1.
93 rate that UBXN-2, a substrate adaptor of the AAA ATPase Cdc48/p97, is required to coordinate centroso
94                              We identify the AAA(+) ATPase Cdc48 and its cofactors as the Ub receptor
95  stress induces selective recruitment of the AAA(+) ATPase Cdc48/p97 to catalyze dissociation of the
96 associated with diverse cellular activities (AAA(+)) ATPase Cdc48.
97 ese processes are catalyzed by the conserved AAA-ATPase Cdc48 (also known as p97).
98                                          The AAA-ATPase Cdc48 and the Hsp70 chaperone Ssa1 are crucia
99                                    The yeast AAA-ATPase Cdc48 and the ubiquitin fusion degradation (U
100 g anaphase B, Imp1-mediated transport of the AAA-ATPase Cdc48 protein at the MMD allows this disassem
101 ylation, we demonstrated that Rbd2 binds the AAA-ATPase Cdc48 through a C-terminal SHP box.
102 found associated, together with Ltn1 and the AAA-ATPase Cdc48, to 60S ribosomal subunits.
103 nd functionally interacts with the conserved AAA-ATPase Cdc48.
104 0 and serves as a recruitment signal for the AAA-ATPase Cdc48/p97, which actively disassembles the co
105 c complementation to a gene encoding a novel AAA-ATPase/CDC48 family member called TgNoAP1.
106                                The hexameric AAA-ATPase, Cdc48p, catalyzes an array of cellular activ
107 regulator of Arabidopsis CDC48, an essential AAA-ATPase chaperone that mediates diverse cellular acti
108                                              AAA+ ATPase ClpB is a promising target for the developme
109                                          The AAA(+) ATPase ClpV disassembles the contracted sheath, w
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
114 heat shock protein 101 (HSP101), a ClpB-like AAA+ ATPase component of PTEX.
115 t vaccinia virus (VACV) to identify the VACV AAA+ ATPase D5 as the poxvirus uncoating factor.
116                                    Dedicated AAA+ ATPases deposit hexameric ring-shaped helicases ont
117                          In cells, dedicated AAA+ ATPases deposit hexameric, ring-shaped helicases on
118                                           An AAA+ ATPase, DnaC, delivers DnaB helicase at the E. coli
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
121                 Crystal structures of FleQ's AAA+ ATPase domain in its apo-state or bound to ADP or A
122      The viral protein binds to the loader's AAA+ ATPase domain, allowing binding of the host replica
123 eted ORC5, the protein would lack 80% of the AAA+ ATPase domain, including the Walker A motif.
124                          Previous studies of AAA(+) ATPase domains from sigma(54) activators have sho
125 s) DNA are bound within the C-tier of MCM2-7 AAA+ ATPase domains.
126                         Here we identify the AAA-ATPase Drg1 as a target of diazaborine.
127                                          The AAA-ATPase Drg1 is essential for the release of several
128 ubiquitin-system or a HORMA domain-PCH2-like AAA+ ATPase dyad.
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
136                          Many members of the AAA+ ATPase family function as hexamers that unfold thei
137  ATPases are the only representatives of the AAA+ ATPase family that reside in the lumen of the endop
138  is a highly expressed member of the type II AAA+ ATPase family.
139                          The flagella export AAA+ ATPase FliI was identified as a result of this scre
140 uch as Mu, Tn7, and IS21, require regulatory AAA+ ATPases for function.
141                                         Many AAA+ ATPases form hexamers that unfold protein substrate
142                            RUVBL1 and RUVBL2 AAA-ATPases form an hetero-hexameric ring that is part o
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
145                                Meiotic clade AAA ATPases function as hexamers that can cycle between
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
148 eals previously unidentified features of the AAA-ATPase heterohexamer.
149 onserved bromodomain-containing protein with AAA-ATPase homology originally implicated in heterochrom
150               TorsinA is a membrane-tethered AAA+ ATPase implicated in nuclear envelope dynamics as w
151                          Msp1 is a conserved AAA ATPase in budding yeast localized to mitochondria wh
152 ay could shed light on a general role of 19S AAA ATPases in processing tight protein-DNA complexes du
153                                            A AAA+ ATPase in the clamp loader clade, RarA protein is p
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
157                p97 is an essential hexameric AAA+ ATPase involved in a wide range of cellular process
158 actly where the arginine finger of canonical AAA+ ATPases is found.
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
162                                          The AAA ATPase katanin severs microtubules.
163 Receptor Interacting Protein 13 (TRIP13), an AAA-ATPase known to interact with p31(comet).
164       The structure establishes that type II AAA-ATPases lacking the aromatic-hydrophobic motif withi
165               Msp1 is a conserved eukaryotic AAA+ ATPase localized to the outer mitochondrial membran
166                                TorsinA is an AAA+ ATPase located within the lumen of the endoplasmic
167  striking, unifying feature of meiotic clade AAA ATPases may be their MIT domain, which is a module t
168 erved, opening up the possibility that other AAA+ ATPases may respond to c-di-GMP.
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
172                                          Its AAA-ATPase module adopts essentially the same topology t
173 amer, which connects to the CP and roofs the AAA-ATPase module, positioning the Rpn8/Rpn11 heterodime
174 nd a regulatory particle (RP) containing the AAA-ATPase module.
175 mmitment and prior to their unfolding by the AAA-ATPase module.
176 a 20S proteolytic core particle (CP), and an AAA-ATPase module.
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
179 tered abundance of transport proteins having AAA-ATPase motifs.
180                                          The AAA+ ATPase motor cytoplasmic dynein regulates ciliary t
181                            The mitochondrial AAA ATPase Msp1 is well known for extraction of mislocal
182                             We show that the AAA+ ATPase Msp1 limits the accumulation of mislocalized
183                            The mitochondrial AAA-ATPase Msp1 removes mislocalized TA proteins from th
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.
188                                    The human AAA ATPase p97 is a molecular chaperone essential in cel
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
192 y described as inhibitor leads for the human AAA+ ATPase p97, an antitumor target.
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/
195                                          The AAA-ATPase p97 plays vital roles in mechanisms of protei
196 that DNA-locked Ku rings are released by the AAA-ATPase p97.
197  the cytosol in a manner that depends on the AAA-ATPase p97/VCP [3].
198 ting inhibition of a conserved Dictyostelium AAA ATPase, p97, a homolog of the human transitional end
199                                          The AAA+ ATPase, p97, also referred to as VCP, plays an esse
200 an essential role for the ubiquitin-directed AAA-ATPase, p97, in the clearance of damaged lysosomes b
201                              We show that an AAA-ATPase, p97, is required for the proteasomal degrada
202 rm a complex with Derlin-1 and an associated AAA-ATPase, p97.
203 tures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase).
204                   We show that the conserved AAA-ATPase PCH-2/TRIP13, which remodels the checkpoint e
205  Signaling is attenuated by a homolog of the AAA+ ATPase Pch2/TRIP13, which binds and disassembles th
206                       Exclusion requires the AAA+-ATPase Pch2 and is directly coupled to synaptonemal
207                                  The traffic AAA-ATPase PilF is essential for pilus biogenesis and na
208                 Our results suggest that 19S AAA ATPases play a dual role in sensing the Top2beta cle
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.
211 is dependent on the conserved inner-membrane AAA+ ATPase/protease, FtsH.
212 13 ortholog PCH-2, revealing a new family of AAA+ ATPase protein remodelers.
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
215                                          The AAA + ATPase R2TP complex facilitates assembly of a numb
216 mingly incompatible symmetries-the hexameric AAA+ ATPase RavA and the decameric inducible lysine deca
217  until remodeling of the pre-ribosome by the AAA-ATPase Rea1 (Midasin).
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
220                                   Multimeric AAA ATPases represent a structurally homologous yet func
221                            VPS4 proteins are AAA(+) ATPases required to form multivesicular bodies, r
222                     Pex1 and Pex6 are Type-2 AAA+ ATPases required for the de novo biogenesis of pero
223 mily; Bro1, a homolog of Alix; and Vps4, the AAA-ATPase required for ESCRT function in all contexts/o
224                 Rix7 is an essential type II AAA-ATPase required for the formation of the large ribos
225 E) mutation in TOR1A, which encodes torsinA, AAA(+) ATPase resident in the lumen of the endoplasmic r
226                Torsins are membrane-tethered AAA+ ATPases residing in the nuclear envelope (NE) and e
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
230 2/p27, binds to the C-terminal region of the AAA-ATPase Rpt5.
231 f the GABAB2 C terminus with the proteasomal AAA-ATPase Rpt6.
232            We have tested this method on the AAA+ ATPase Rubisco activase (Rca).
233  proteins as follows: Pih1D1, RPAP3, and the AAA(+)-ATPases RUVBL1 and RUVBL2.
234 ing known regulators, we discovered that the AAA+ ATPase RUVBL1 is necessary for Nrf1's transcription
235 ing 14 different polypeptides, including the AAA+ ATPases Rvb1 and Rvb2.
236 hancer-binding protein (bEBP) with a central AAA+ ATPase sigma(54)-interaction domain, flanked by a C
237                                          The AAA ATPase Spastin severs microtubules along their lengt
238                                          The AAA+ ATPase spastin remodels microtubule arrays through
239 ve NADH binding motif (GxGxxG) including the AAA-ATPase subunit, Psmc1 (Rpt2).
240 easome, the 20S particle is regulated by six AAA ATPase subunits and, in archaea, by a homologous rin
241  and may guide the development of additional AAA+ ATPase superfamily inhibitors.
242  a bacterial enhancer-binding protein of the AAA+ ATPase superfamily, is inhibited by an unprecedente
243 en five RavA rings is unique for the diverse AAA+ ATPase superfamily.
244 id deletion in torsinA (TA), a member of the AAA+ ATPase superfamily.
245  in the SF3 helicase family, a subset of the AAA+ ATPase superfamily.
246                        TorsinA is an unusual AAA + ATPase that needs an external activator.
247 r protein sorting 4 (Vps4), which encodes an AAA ATPase that interacts with the ESCRT-III complex to
248                  Spastin is a hexameric ring AAA ATPase that severs microtubules.
249 uble-stranded DNA (dsDNA) viruses contain an AAA(+) ATPase that assembles into oligomers, often hexam
250                    Magnesium chelatase is an AAA(+) ATPase that catalyzes the first committed step in
251                    Magnesium chelatase is an AAA(+) ATPase that catalyzes the first step in chlorophy
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
254       DnaA is the widely conserved bacterial AAA+ ATPase that functions as both the replication initi
255            p97/VCP is an essential, abundant AAA+ ATPase that is conserved throughout eukaryotes, wit
256      p97 is a highly abundant, homohexameric AAA+ ATPase that performs a variety of essential cellula
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      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
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 s - katanin, spastin, fidgetin - are related AAA-ATPases that cut microtubules into shorter filaments
264                        Pex1 and Pex6 are two AAA-ATPases that play a crucial role in peroxisome bioge
265        Here we describe and characterize the AAA+ ATPase Thorase, which regulates the expression of s
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 glutamic acid codon in the gene encoding the AAA+ ATPase TorsinA (TorA).
270                Saunders et al. show that the AAA+ ATPase torsinA and its partner LAP1 are required fo
271                                 In turn, the AAA+ ATPase torsinA is thought to regulate force transmi
272                                          The AAA+ ATPase TRIP13 regulates both MAD2 and meiotic HORMA
273           Here, we report that the conserved AAA+ ATPase TRIP13(PCH-2) localizes to unattached kineto
274       Here we describe a mechanism where the AAA-ATPase TRIP13 promotes treatment resistance.
275 ive oxidase1a, NADH dehydrogenaseB2, and the AAA ATPase Ubiquinol-cytochrome c reductase synthesis1),
276 strates depends on its being partnered by an AAA+ ATPase/unfoldase, ClpA or ClpX.
277 ugh poorly defined reactions mediated by the AAA-ATPase valosin-containing protein (VCP)/p97 and augm
278                   C1orf124 also binds to the AAA-ATPase valosin-containing protein via its SHP domain
279  protein that we termed VWA interacting with AAA+ ATPase (ViaA) containing a von Willebrand Factor A
280                                The hexameric AAA ATPase Vps4 drives membrane fission by remodeling an
281                                          The AAA ATPase Vps4 is recruited to membrane necks shortly b
282 sport III (ESCRT-III) subunit CHMP2A and the AAA ATPase VPS4, but their regulatory mechanisms remain
283             A component of this pathway, the AAA ATPase Vps4, provides energy for pathway progression
284  in disassembly of ESCRT-III polymers by the AAA ATPase Vps4.
285           The ESCRT machinery along with the AAA+ ATPase Vps4 drive membrane scission for trafficking
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
288                                          The AAA-ATPase Vps4 is required for ESCRT function, and its
289                                          The AAA-ATPase Vps4 is required for ESCRT-III disassembly, h
290 r transport (ESCRT)-III subunit Snf7 and the AAA-ATPase Vps4 to destabilize and clear defective NPC a
291 their disassembly requires the action of the AAA-ATPase Vps4.
292               The vacuolar protein sorting 4 AAA-ATPase (Vps4) recycles endosomal sorting complexes r
293 dodecamer, and argue that, like other type I AAA ATPases, Vps4 functions as a single ring with six su
294                                        As an AAA-ATPase, Vps4 is important for function of multivesic
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
297       This reaction is catalyzed by VPS4, an AAA-ATPase whose activity is tightly regulated by a host
298                    TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results i
299 ), also named p97, is an essential hexameric AAA+ ATPase with diverse functions in the ubiquitin syst
300                                     p97 is a AAA-ATPase with multiple cellular functions, one of whic

 
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