ライフサイエンスコーパス: Hsp70 family

1 for this unique member of the membrane-bound Hsp70 family.

2 cture model of the peptide binding domain of Hsp70 family.

3 PA), and the up-regulation of members of the HSP70 family.

4 esentation by Ydj1p to the chaperones of the Hsp70 family.

5 Hsp110s, which are themselves members of the Hsp70 family.

6 e two genes distant members of the mammalian Hsp70 family.

7 ation and root growth for this member of the hsp70 family.

8 te, much like Kar2p and other members of the hsp70 family.

9 otic cells and is a diverged relative of the hsp70 family.

10 quired for two separate functions of a yeast Hsp70 family.

11 balance between chaperones of the Hsp100 and Hsp70 families.

12 ent, overexpression of SSA2, a member of the Hsp70 family and a prominent candidate for the feedback

13 is a significantly diverged subgroup of the hsp70 family and has been found in organisms as diverse

14 he plant heat shock response, especially the HSP70 family and jasmonic acid production.

15 -associated proteins included members of the HSP70 family and various single-stranded DNA and RNA bin

16 constitutively bound to members of the Hsp40/Hsp70 family, and we found that heat shock-induced TDP-4

17 , a member of the 70 kDa heat shock protein (hsp70) family, and its complexes with substrate proteins

18 These results suggest that chaperones of the HSP70 family are required for nairovirus replication and

19 ass of cofactors of the eukaryotic chaperone Hsp70 family) are similar.

20 SPA2, highly homologous members of the HSPA (HSP70) family, are often overexpressed in non-small cell

21 Chaperones of the Hsp70 family bind to unfolded or partially folded polype

22 Here, we show that the Ssb1/2p member of the hsp70 family can form a stable, ATP-sensitive complex wi

23 Chaperones of the Hsp70 family can further disaggregate otherwise irrevers

24 trate that highly homologous variants in the Hsp70 family can have opposing effects on tau clearance

25 In agreement, GRP78, the major HSP70 family chaperone in the ER, is upregulated in Clcc

26 y showed that Mycoplasma fermentans DnaK, an HSP70 family chaperone protein, hampers the activity of

27 The mechanisms by which Hsp70 family chaperones are regulated, however, are only

28 Other HSP70 family chaperones could not effectively replace mo

29 Although Hsp70 family chaperones have been extensively examined f

30 Ssa1 and Ssa2 are Hsp70 family chaperones that generally cause pro-[PSI(+)

31 primary components of the liquid core to be HSP70 family chaperones, whose adenosine triphosphate (A

32 stimulate the protein refolding activity of Hsp70 family chaperones.

33 n recruiting and stimulating the activity of Hsp70 family chaperones.

34 for approximately 70-kDa heat shock protein (hsp70) family chaperones in regulating the quality and l

35 ng liquid outer shells and liquid centres of HSP70-family chaperones, cytoplasmic aggregates of TDP-4

36 The metazoan 70-kDa heat shock protein (HSP70) family contains several members localized in diff

37 lar chaperones of the heat shock protein 70 (Hsp70) family counteract protein misfolding in a variety

38 s illustrate the evolutionary history of the HSP70 family, encouraging us to propose a new nomenclatu

39 Chaperones of the heat shock protein 70 (Hsp70) family engage in protein-protein interactions wit

40 ese three sequences and known members of the HSP70 family from plants, these cDNAs were identified as

41 The HSP40/HSP70 family genes DNAJB1 and HSPA6 were found to be cri

42 Members of the hsp70 family have been reported to be immunoreactive.

43 emonstrate that various members of the yeast Hsp70 family have diverged from each other in regard to

44 interactions in the complex may model other Hsp70 family heterodimers in which two Hsp70s reciprocal

45 h the completion of the genome sequence, the hsp70 family in Arabidopsis consists of 14 members unequ

46 fragment represented a second member of the HSP70 family in this organism.

47 proteins from the 70-kDa heat shock protein (HSP70) family in MCF7 cells.

48 undant variant of the heat shock protein 70 (Hsp70) family in the brain, heat shock cognate 70 protei

49 SP70B', a poorly characterized member of the HSP70 family, in response to oxidatively modified LDL (o

50 nserved nature of the heat shock protein 70 (Hsp70) family, in conjunction with mutant analysis, perm

51 The extreme C terminus of the Hsp70 family is required for substrate targeting and het

52 ly recognized property of the members of the Hsp70 family is their ability to interact with lipids, o

53 A-5 (hsp70), which we believe is part of the hsp70 family, is induced during bradyzoite development.

54 und that mortalin (HSPA9/GRP75), a member of HSP70 family, is upregulated in human MTC tissues and th

55 o at least two sites on the Escherichia coli Hsp70 family member DnaK: under the ATPase domain in a c

56 Cripto forms a cell surface complex with the HSP70 family member glucose-regulated protein-78 (GRP78)

57 We have studied the interaction of BiP, an Hsp70 family member in the lumen of the endoplasmic reti

58 also required for the full repression of the HSP70 family member SSA1.

59 clin that represses the transcription of the HSP70 family member SSA1.

60 h copurifies with Flag-Dcp1p as the abundant Hsp70 family member Ssa1p/2p.

61 We also discovered that HSPA1L (HSP70 family member) and BAG4 have mutually opposing rol

62 the interaction between the Escherichia coli Hsp70 family member, DnaK, and its cochaperone partner D

63 ase activity of the constitutively expressed Hsp70 family member, Hsc70, together with the J domain p

64 The ER heat shock protein 70 (Hsp70) family member BiP is an ATP-dependent chaperone t

65 LXXLL motif that is required for binding of Hsp70 family members and cooperation with Hsp90 to regul

66 We compared C-terminal sequences of 730 Hsp70 family members and identified a novel conservation

67 found to catalyze trimethylation of various Hsp70 family members both in vitro and in vivo, and the

68 e expression of the inducible, antiapoptotic HSP70 family members HSPA1L and HSPA2, the latter of whi

69 enzyme, consistent with a proposed role for Hsp70 family members in tyrosinase post-translational mo

70 f BiP-assisted folding in the ER but also on Hsp70 family members that reside throughout the cell.

71 Hsp70 family members together with their Hsp40 cochapero

72 Like all Hsp70 family members, the ability of BiP to bind and rel

73 t binds to the nucleotide-binding domains of Hsp70 family members.

74 t are cell specific and discriminate between Hsp70 family members.

75 restored by ATP-dependent chaperones such as Hsp70 family members.

76 rotective proteins that bind to and regulate Hsp70 family molecular chaperones.

77 Heat Shock Protein 70 kDa (Hsp70) family molecular chaperones play critical roles i

78 As a characteristic of the Hsp70 family, multiple DnaJ-like co-factors can target s

79 ctin-binding proteins is mediated by BAG3, a HSP70 family nucleotide exchange factor that regulates t

80 Members of the Hsp90 and Hsp70 families of molecular chaperones are imp\ortant fo

81 ese genes, Hspa13 (Stch), is a member of the Hsp70 family of ATPase heat shock proteins, which have b

82 Proteins of the Hsp70 family of ATPases interact with a conserved domain

83 Proteins of the Hsp70 family of ATPases, such as BiP, function together

84 ain-binding protein (BiP) is a member of the hsp70 family of chaperones and one of the most abundant

85 , which lacks two cytoplasmic members of the hsp70 family of chaperones.

86 Since members of the hsp70 family of eucaryotic proteins are associated with

87 The HSC70/HSP70 family of heat shock proteins are evolutionarily c

88 In this regard, members of the Hsp70 family of heat shock proteins have been observed i

89 The Hsp70 family of molecular chaperones acts to prevent pro

90 endoplasmic reticulum (ER) orthologue of the Hsp70 family of molecular chaperones and is intricately

91 strate that the virus-specific member of the HSP70 family of molecular chaperones functions in interc

92 Members of the hsp70 family of molecular chaperones interact with and s

93 Protein folding mediated by the Hsp70 family of molecular chaperones requires both ATP a

94 ively recognized and bound by members of the HSP70 family of molecular chaperones, but the binding si

95 rowing evidence that members of the extended Hsp70 family of molecular chaperones, including the Hsp1

96 well-characterized, essential member of the Hsp70 family of molecular chaperones, Kar2p.

97 iding in the ER lumen that is related to the hsp70 family of molecular chaperones.

98 073) that would encode a novel member of the Hsp70 family of molecular chaperones.

99 PDR gene family that encodes a member of the Hsp70 family of proteins found in this organism.

100 81-kD stromal polypeptide is a member of the Hsp70 family of stress-related proteins.

101 it interacts with the heat shock protein 70 (Hsp70) family of chaperone proteins.

102 The 70 kDa heat shock protein (HSP70) family of chaperones are the front line of protec

103 The 70-kDa heat shock protein (Hsp70) family of chaperones bind cognate substrates to p

104 terest are the heat shock protein of 70 kDa (Hsp70) family of chaperones.

105 tile functions of the heat shock protein 70 (Hsp70) family of molecular chaperones rely on allosteric

106 antibodies to the 70-kD heat shock protein (HSP70) family of molecular chaperones.

107 that are part of the heat shock protein 70 (Hsp70) family of proteins that bind and fold a large pro

108 up-regulated Hsps include two members of the Hsp70 family, one member of the Hsp60 family (TCP-1), at

109 roup and others suggests that members of the Hsp70 family play a significant role in Tau regulation.

110 , a member of the 70 kDa heat shock protein (HSP70) family, plays an important role in spermatogenesi

111 ers of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and

112 levels of Hsp72, a heat-inducible member of Hsp70 family, protect cells against a variety of stresse

113 ], overproduction of the Ssa1 protein of the Hsp70 family protects [PSI] from the curing effect of Hs

114 ous overexpression of Ssa1, a protein of the Hsp70 family, protects [PSI] from curing by overexpressi

115 normal clam hemocytes) of human mortalin, an Hsp70 family protein.

116 Hsp70 family proteins are highly conserved chaperones in

117 NT-modified enolase, ATP5b, alpha-actin, and Hsp70 family proteins including Hspa5 and Hsp74.

118 f post-translational modifications (PTMs) on Hsp70 family proteins that include phosphorylation, acet

119 the dominant stress-inducible member of the HSP70 family, rather than constitutively expressed HSC70

120 emonstrate that BiP (Kar2p), a member of the Hsp70 family resident in the ER lumen, acts as a molecul

121 e we demonstrate that another protein of the Hsp70 family, Ssb, previously implicated in nascent poly

122 ikely chaperone proteins: two members of the HSP70 family, three alpha B-crystallin-related small hea

123 ative CCHFV N and cellular chaperones of the HSP70 family was confirmed during live CCHFV infection.

124 e protein (Hsc70) as a representative of the Hsp70 family, we have characterized the effect of mutati

125 cytosolic chaperones Ssa1 and Ssb1/2 of the Hsp70 family were previously shown to exhibit "pro-[PSI(

126 ral cellular mRNAs, including members of the Hsp70 family whose export was inhibited under some, but