ライフサイエンスコーパス: AAA protein

1 associated with diverse cellular activities (AAA proteins).

2 of evolutionary change that characterize the AAA proteins.

3 dopting a conserved mechanism shared by many AAA proteins.

4 exameric ring organisation characteristic of AAA proteins.

5 tide-related allosteric signals in a class-1 AAA+ protein.

6 ilarity with the large and diverse family of AAA+ proteins.

7 ns, aligns with a key catalytic Arg found in AAA+ proteins.

8 insights into the mechanisms of MgsA family AAA+ proteins.

9 stinguishes it from other clamp loader clade AAA+ proteins.

10 ary dystonia, is called the torsin family of AAA+ proteins.

11 (54) activators as pre-sensor 1 beta-hairpin AAA+ proteins.

12 reviously found only in distinct families of AAA+ proteins.

13 similar to adaptor-binding domains of other AAA(+) proteins.

14 e to identify similar residue pairs in other AAA(+) proteins.

15 orII helix in PspF, which may apply to other AAA(+) proteins.

16 vation in the origin of those events amongst AAA(+) proteins.

17 Rubisco activase is an AAA(+) protein, a superfamily with members that use a "S

18 hown that the modular domain architecture of AAA proteins allows for precise control of cellular acti

19 dentification of an evolutionarily conserved AAA+ protein, ANCCA/pro2000, endowed with a bromodomain

20 During photosynthesis the AAA+ protein and essential molecular chaperone Rubisco a

21 multiple cell types appear to utilize torsin AAA+ proteins and differential expression of torsinB may

22 The common oligomeric structures of AAA+ proteins and the creation of the active site for AT

23 ing and helical lid domains (conserved among AAA+ proteins) and a tetramerization domain.

24 tor bound to spastin, a microtubule-severing AAA protein, and characterize the residues involved in i

25 Torsins are developmentally essential AAA+ proteins, and mutation of human torsinA causes the

26 Other AAA+ proteins appear to cycle through states that are an

27 The AAA proteins are characterized by the presence of a 230

28 spindle formation, but functions for the SF7 AAA proteins are largely unknown.

29 AAA proteins are molecular chaperones that facilitate a

30 AAA proteins are oligomeric and often have multiple ATPa

31 AAA(+) proteins are ubiquitous mechanochemical ATPases t

32 associated with diverse cellular activities (AAA+ proteins) are macromolecular machines that convert

33 r II helix that has been implicated in other AAA+ proteins as sensing changes in the nucleotide durin

34 Mutations in the AAA+ protein (ATPase associated with a variety of cellul

35 The AAA proteins (ATPases Associated with a variety of cellu

36 that bears similarity to the FtsH family of AAA proteins (ATPases associated with diverse cellular a

37 ted open complex formation requires specific AAA+ proteins (ATPases Associated with diverse cellular

38 They belong to the family of AAA+ proteins (ATPases associated with various cellular

39 hI and BchD subunits belong to the family of AAA+ proteins (ATPases associated with various cellular

40 AAA+ proteins (ATPases associated with various cellular

41 The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitoc

42 ymes as members of the clamp loader clade of AAA+ proteins, but structural information defining the f

43 However, we do not know how AAA proteins can be activated by small molecules.

44 of particular interest for understanding how AAA+ proteins carry out multiple ATP driven functions.

45 2.2- angstrom crystal structure of the MoxR AAA+ protein CbbQ2 from Acidithiobacillus ferrooxidans r

46 VAT), the archaeal homolog of the ubiquitous AAA+ protein Cdc48/p97, functions in concert with the 20

47 o this event, two of the three subunits, the AAA(+) proteins ChlI and ChlD, form a ChlID-MgATP comple

48 ication factor C (RFC) is a heteropentameric AAA+ protein clamp loader of the proliferating cell nucl

49 l partially explained by the presence of the AAA(+) protein ComGA, which is also required for the bin

50 gation, we have explored Hsp104, a hexameric AAA+ protein disaggregase from yeast.

51 The AAA+ protein disaggregase Hsp104 can sever the amyloid f

52 Hsp104 is an AAA+ protein disaggregase that solubilizes and reactivat

53 The AAA+ protein disaggregase, Hsp104, increases fitness und

54 ome formation and identified novel mammalian AAA+ protein disaggregases RuvbL1 and RuvbL2.

55 ot have a C-terminal helical domain as other AAA proteins do.

56 associated with various cellular activities (AAA) proteins, especially in the mononucleotide binding

57 These activators belong to the large AAA protein family and the majority of them consist of a

58 t AMP-AlF(x) is a powerful new tool to study AAA(+) protein family members and, more generally, Walke

59 transcription activators that belong to the AAA(+) protein family.

60 e ATPase associated with diverse activities (AAA) protein family and is involved in mitochondrial mor

61 associated with diverse cellular activities (AAA) protein family, and contains a microtubule interact

62 r the C terminus of torsinA, a member of the AAA+ protein family (ATPases associated with a variety o

63 r binding proteins (bEBP) are members of the AAA+ protein family and have a highly conserved 'DE' Wal

64 ic peptidase B homolog ClpB, a member of the AAA+ protein family.

65 associated with various cellular activities (AAA+) protein family, are required to remodel the transc

66 classifying this gene as a new member of the AAA-protein family (ATPase associated with diverse activ

67 ontrast, Methanosarcina mazei contains seven AAA proteins, five of which, both PAN proteins, two out

68 Many other AAA proteins form ring-shaped hexamers and contain pore

69 Fidgetin is the first mutant AAA protein found in a mammalian developmental mutant, t

70 is a dynamic ring translocase and hexameric AAA+ protein found in yeast, which couples ATP hydrolysi

71 Hsp104, a conserved hexameric AAA+ protein from yeast, solubilizes disordered aggregat

72 Many other AAA+ proteins function by threading macromolecules throu

73 we review how substrate-bound structures of AAA+ proteins have expanded our understanding of ATP-dri

74 AAA+ proteins have key functionalities encompassing unfo

75 -over-hand mechanism proposed for many other AAA+ proteins, highlighting the versatile mechanisms uti

76 nt hydrogen exchange results for the typical AAA+ protein Hsp104 with prior information on several ne

77 The homologous hexameric AAA(+) proteins, Hsp104 from yeast and ClpB from bacteri

78 NSF and p97 are related AAA proteins implicated in membrane trafficking and orga

79 a new member of the cdc48p/VCP subfamily of AAA proteins in Drosophila.

80 o the threading mechanism widely employed by AAA proteins in substrate translocation, subunits of Bcs

81 p97(E578Q)) to compare the function of these AAA proteins in the secretory pathway of mammalian cells

82 mutation (WB(EQ)) that typically stabilizes AAA+ proteins in a substrate-bound state causes torsinA

83 dimer adopts a novel oligomeric assembly for AAA+ proteins in which the arginine finger, crucial for

84 to the establishment of different functional AAA proteins, including proteasomal regulatory, NSF/Sec,

85 Several AAA+ proteins, including ClpB/Hsp104, possess a pair of

86 A feature common to AAA+ proteins is the formation of oligomeric rings that

87 greatest similarity to the VCP subfamily of AAA proteins, is widely expressed, and encodes a nuclear

88 tumor antigen (LTag) of simian virus 40, an AAA(+) protein, is a hexameric helicase essential for vi

89 amma/delta' hydroxyl group that 99% of other AAA+ proteins lack.

90 TorsinA is an AAA(+) protein located predominantly in the lumen of the

91 TorsinA is an AAA+ protein located predominantly in the lumen of the e

92 The human mitochondrial AAA+ protein LONP1 is a critical quality control proteas

93 g/remodeling by this conserved and essential AAA+ protein machine and their adaption and possible bio

94 The GTP-specific AAA + protein McrB powers translocation along DNA and it

95 nce when considering how activities of other AAA(+) proteins might be controlled.

96 n motor domain is constructed from a ring of AAA protein modules, with the C-terminal module position

97 The superfamily of massively large AAA+ protein molecular machines functions to convert the

98 The AAA protein Msp1 extracts mislocalized tail-anchored mem

99 Akin to other AAA proteins, Msp1 forms hexameric spirals that transloc

100 ciated with the diverse cellular activities (AAA+) protein, N-ethylmaleimide-sensitive factor (NSF/Se

101 Here, we reveal mechanistic details of AAA+ protein NSF (N-ethylmaleimide sensitive factor) and

102 ease is allosterically activated by HslU, an AAA protein of the Clp/Hsp100 family consisting of three

103 Human AAA(+) protein p97 consists of an N-domain and two tande

104 iated with diverse cellular Activities plus (AAA+) protein p97.

105 For one type of member AAA(+) protein (phage shock protein F, PspF), we identif

106 For example, AAA+ proteins play a prominent role in cellular proteost

107 AAA+ proteins play crucial roles in diverse biological p

108 c AAA ATPase p97 is perhaps the best studied AAA protein, playing an essential role in various import

109 dent interactions and consideration of other AAA+ proteins provide insight into activator mechanochem

110 ssociated with assorted cellular activities (AAA+) proteins, raising the possibility that expression

111 Here, we investigated the mechanism of the AAA+ protein Rubisco activase (Rca) in metabolic repair

112 AAA proteins share a conserved active site for ATP hydro

113 matching the magnitude of force produced by AAA proteins similar to Mdn1, enhance the MIDAS domain b

114 Here, we establish that a mitochondrial AAA+ protein, Skd3 (human ClpB), couples ATP hydrolysis

115 Precedence to other AAA(+) proteins suggests that Mcm ATPase active sites ar

116 associated with diverse cellular activities (AAA+ proteins) termed Rubisco activases (Rcas).

117 p60 katanin, an AAA protein that severs and depolymerizes microtubules,

118 TIP48 and TIP49 are two related AAA(+) proteins that are essential for the formation of

119 trates a reverse-chaperoning activity for an AAA+ protein that can act as a template for the assembly

120 Regulatory ATPase variant A (RavA) is a MoxR AAA+ protein that functions together with a partner prot

121 Regulatory ATPase variant A (RavA) is a MoxR AAA+ protein that functions together with a partner prot

122 re, our data suggest a mechanism of the bEBP AAA+ protein that is distinct from the hand-over-hand me

123 similarity of Aquifex aeolicus DnaA to other AAA+ proteins that are oligomeric, it was proposed that

124 -coupler are present in related, switch-like AAA+ proteins that control replicative helicase loading

125 tivators of the bacterial sigma(54)-RNAP are AAA+ proteins that couple ATP hydrolysis to restructure

126 A subgroup of the AAA+ proteins that reside in the endoplasmic reticulum a

127 taining Domain (CAD) proteins (also known as AAA proteins) that are involved in a wide variety of cel

128 Mutational studies show that, unlike other AAA+ proteins, the catalytic Walker B aspartate is requi

129 TorsinA is an "AAA" protein thought to reside in the endoplasmic reticu

130 hydrolysis of ATP is universally required by AAA+ proteins to underpin their mechano-chemical work.

131 sH, Lon, 26S proteasome) use AAA+ domains or AAA+ proteins to unfold protein substrates (using energy

132 By contrast to other AAA+ proteins, torsin proteins contain two conserved cys

133 A glutamic acid deletion (DeltaE) in the AAA+ protein torsinA causes DYT1 dystonia.

134 We demonstrate that the AAA+ protein torsinA, whose dysfunction causes the neuro

135 03)) in the carboxyl-terminal portion of the AAA+ protein, torsinA.

136 Here, we discuss repurposing AAA+ protein translocases Hsp104 and proteasome-activati

137 c coupling may apply generally in organizing AAA+ protein translocases into their active conformation

138 rally applicable to the examination of other AAA+ protein translocases involved in a variety of impor

139 d high-resolution structure determination of AAA+ proteins trapped in the act of processing substrate

140 previously discovered that the mitochondrial AAA+ protein unfoldase ClpX (mtClpX) activates the initi

141 f structural and energetic events that carry AAA+ proteins unidirectionally around a functional cycle

142 associated with various cellular activities (AAA) protein Vps4.

143 4 is a member of the CDC48p/VCP subfamily of AAA proteins which are involved in homotypic fusion of t

144 ollows the general principle established for AAA proteins while adopting several structural features

145 two related and highly conserved eukaryotic AAA(+) proteins with an essential biological function an

146 chitectural principles established for other AAA proteins yet specializes Msp1 for its unique role in