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1 ty, properties that arise from its conserved AAA domain.
2 may be a general feature of ATP-hydrolyzing AAA domains.
3 ism for long-range communication between the AAA domains.
4 NifL-resistant phenotype of mutations in the AAA+ domain.
5 alpha-helix in the C-terminal portion of the AAA+ domain.
6 protein ClpB to provide a model of torsinA's AAA+ domain.
7 pha/beta and alpha-helical subdomains of the AAA+ domain.
8 coiled-coil domain intercalated between the AAA+ domains.
9 s at the top of the cylinder followed by two AAA+ domains.
10 terminal domain, an M-domain, and two tandem AAA(+) domains.
12 ontains an N-terminal domain (NSF-N) and two AAA domains, a catalytic NSF-D1 and a structural NSF-D2.
15 crystal structure of the Drosophila spastin AAA domain and provide a model for the active spastin he
17 nits contain calcium-signaling motifs and/or AAA domains and are nearly ubiquitous in species with mo
18 ormational changes that propagate to all six AAA domains and cause a large movement of the "linker,"
19 nucleotide binding or hydrolysis in the four AAA domains and examined the ability of the mutant dynei
20 ct double-stranded DNA through an N-terminal AAA(+) domain and a C-terminal winged-helix domain (WHD)
21 binding proteins (bEBPs) oligomerize through AAA(+) domains and use ATP hydrolysis-driven energy to i
23 es in controlling the oligomerization of the AAA+ domain and modulating interactions with sigma54 in
24 amino acid substitutions cluster within the AAA(+) domain at residues near the ATP-binding pocket.
25 reveals a closure of the motor's ring of six AAA+ domains (ATPases associated with various cellular a
27 ments show that the helicase activity of the AAA+ domain can be stimulated by addition of the isolate
35 receptor trafficking: Thorase (ATPase family AAA domain-containing protein 1), soluble N-ethylmaleimi
36 n-containing proteins, such as ATPase family AAA domain-containing protein 2 (ATAD2), isoform A, have
39 -terminal domain (N-domain) and the adjacent AAA domain (D1), resulting in a reduced affinity for ADP
41 conserved Arg(359) and Arg(362) in the first AAA domain, D1 and Arg(635) and Arg(638) in the second A
43 otation of more than 90 degrees for the Orc1 AAA+ domain disrupts interactions with catalytic amino a
46 binding and hydrolysis in each of these four AAA domains has constituted an important and unresolved
48 FIGL-1-AAA), in clear contrast to homologous AAA domains, has an unusually high ATPase activity and f
49 results show that the four conserved dynein AAA domains have distinct functions in dynein's mechanoc
50 minal Allosteric Communication Loop with the AAA+ domain helix-2-insert (h2i); and 3) a recessed bind
53 to a cysteine change upstream of the second AAA+ domain in the temperature sensitive TgNoAP1 allele
55 down experiments show that the DnaC and DnaA AAA+ domains interact in a nucleotide-dependent manner.
57 minate prematurely, suggesting that the DctD AAA+ domain interfered with transcription elongation.
60 imply that the wave's propagation within the AAA+ domains is not necessarily coupled with a strictly
61 domain, formed by a ring-like arrangement of AAA+ domains, is located approximately 280 A away from t
62 GAF domain restores inhibition by NifL to an AAA+ domain mutation, E356K, in response to fixed nitrog
67 n experiments also showed that the catalytic AAA domain of FtsH contains a chaperone-like activity, h
70 f P-loop function within the first and third AAA domains of the Drosophila cytoplasmic dynein heavy c
71 support current models in which the multiple AAA domains of the dynein heavy chain interact to suppor
73 ce of MgADP, and we show that the N-terminal AAA(+) domain of ChlD mediates this process, in agreemen
75 x high resolution structures (<2.1 A) of the AAA(+) domain of EBP phage shock protein F (PspF) includ
76 nit dynamics and nucleotide occupancy of the AAA(+) domain of one well-studied bEBP in complex with i
77 describe the first structure of the central AAA(+) domain of the flagellar regulatory protein FlrC (
79 inimal functional C-terminal boundary of the AAA+ domain of DctD as being located between Gly-381 and
80 report that Soj directly interacts with the AAA+ domain of DnaA and specifically regulates DnaA heli
83 idence for a DNA-interacting activity in the AAA+ domain of PspF was obtained, suggesting that PspF m
86 howing that the ADP.AlF(x) bound form of the AAA+ domain of the transcriptional activator protein Psp
87 vely removes the hydrophobic domain from the AAA+ domain of TorsinA, which retains catalytic activity
91 associated with various cellular activities (AAA+) domain of the Escherichia coli activator protein,
93 Structures of the sigma(54) activator PspF AAA+ domain (PspF(1-275)) bound to sigma(54) show two lo
96 ween two helical pentamers of ATP-associated AAA+ domains, sharply bending the duplex into a 180 degr
97 l ATPase associated with various activities (AAA) domain, specifically alpha-helices 7 and 9, as rele
98 Through proposed fitting of representative AAA domain structures, we show that the nucleotide catal
100 -1-AAA are not conserved in other homologous AAA domains that have relatively low ATPase activities.
101 share two domains: a modified version of the AAA(+) domain that characterizes the SF3 family of helic
102 NorR by characterizing substitutions in the AAA+ domain that bypass repression by the regulatory dom
104 built upon interactions between neighbouring AAA+ domains, that in vitro stretches DNA to promote rep
105 ows that CsoCbbQ is a hexamer of the typical AAA+ domain; the additional C-terminal domain, diagnosti
107 a continuous surface that allows successive AAA+ domains to bind and extend single-stranded DNA segm
113 the GAF domain regulates the activity of the AAA+ domain, we screened for second-site mutations that
114 of site-specifically modified, cross-linked AAA+ domains, we found that the conserved arginine pair
116 al DNA contacts are made with the N-terminal AAA+ domain, which inserts into the minor groove at a ch
117 ynein motor domain consists of a ring of six AAA domains with a protruding microtubule-binding stalk
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