ライフサイエンスコーパス: homodimerize

1 GT1A8, UGT1A9, and UGT1A10 self-oligomerize (homodimerize).

2 e active site mutant retained its ability to homodimerize.

3 nsmembrane domain were independently able to homodimerize.

4 that S100A2 displays a strong propensity to homodimerize.

5 nd Ku70 formed only heterodimers and did not homodimerize.

6 Cx26 pore domain, had a strong propensity to homodimerize.

7 chorismate, and TyrA) domain is licensed to homodimerize.

8 dimerize with each other in vivo, as well as homodimerize.

9 Kfyve regulator ArPIKfyve and its ability to homodimerize.

10 nto model membranes where it was observed to homodimerize.

11 lity to promote MC2 receptor trafficking and homodimerize.

12 rated the potential of each UGT1A protein to homodimerize.

13 ains its phylogenetically ancient ability to homodimerize.

14 Furthermore, AtMinE1 has the ability to homodimerize.

15 ed localization and possesses the ability to homodimerize.

16 mediates only heterodimerization; it cannot homodimerize.

17 easing the capacity of the mutant protein to homodimerize.

18 t physiological temperatures, alphaE-catenin homodimerizes 10x more weakly than does alphaN-catenin b

19 Its chromo shadow domain (CSD) homodimerizes, a requirement for binding protein partner

20 Full-length Mlh1p alone, which can homodimerize, also binds to DNA.

21 lular domain of the EPO receptor should also homodimerize and activate.

22 ogether with the fact that E2F7 and E2F8 can homodimerize and are expressed in the same adult tissues

23 Unexpectedly, phyC and phyE do not homodimerize and are present in seedlings only as hetero

24 is highly expressed in erythroid cells, can homodimerize and assemble [2Fe-2S] in vitro.

25 able from max with respect to its ability to homodimerize and bind DNA.

26 ERK2 has been proposed to homodimerize and bind only to cytoplasmic but not nuclea

27 the BH3 domain of Bax ablated its ability to homodimerize and completely abrogated lethality in yeast

28 ucine zippers of GCN4 and of EB1 exclusively homodimerize and do not form dimers with other bZip prot

29 omoter was located to -55/-46, where p50 can homodimerize and form a complex with the transcriptional

30 ding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty ac

31 DTX family members homodimerize and heterodimerize in vivo, suggesting that

32 Nore and RASSF1A can each efficiently homodimerize and heterodimerize with each other through

33 ar, serotonin (5-HT) receptors were shown to homodimerize and heterodimerize with other GPCRs, althou

34 All of the NodD1 mutant proteins can homodimerize and heterodimerize with wild-type NodD1.

35 Upon ligand binding, TLR/IL-1Rs hetero- or homodimerize and recruit MyD88 through their respective

36 ) proteins (APC7, APC3, APC6, and APC8) that homodimerize and stack with quasi-2-fold symmetry.

37 The ability of alphaCPs to homodimerize and their reported association with additio

38 The longer isoform (GABPbeta1L) can homodimerize and thus form alpha(2)beta(2) tetramers dep

39 ransfer experiments demonstrated that MARCH1 homodimerizes and also forms heterodimers with others fa

40 ther members of the myc network, max readily homodimerizes and binds to identical E-box sites in vitr

41 CASTOR1 homodimerizes and can also heterodimerize with the relat

42 thyl epoxyfarnesoate, whereupon the receptor homodimerizes and changes tertiary conformation, includi

43 Over time 14-3-3gamma homodimerizes and dissociates from STAR, allowing this p

44 helix domain, our article shows that MAPKBP1 homodimerizes and heterodimerizes with WDR62.

45 embedded in the mitochondrial inner membrane homodimerizes and homo-oligomerizes.

46 An N-terminal domain homodimerizes and interacts with H3-H4 independently of

47 ests that the small transmembrane E5 protein homodimerizes and physically interacts with the transmem

48 ro cross-linking analysis indicate that Mst1 homodimerizes and that the extreme COOH-terminal 57 amin

49 Here, we show that PTEN homodimerizes and, in this active conformation, exerts l

50 t-lived nuclear proteins that are capable of homodimerizing and heterodimerizing.

51 randed DNA in a sequence-independent manner, homodimerize, and bind proteins containing a LEM domain.

52 , the leucine zipper domain enables c-Cbl to homodimerize, and homodimerization influences Cbl's sign

53 smembrane domain, that the ESyts hetero- and homodimerize, and that ESyt2 homodimerization in vivo re

54 cannot simultaneously bind beta-catenin and homodimerize, and that the dynamics of binding and unbin

55 Dug2p was also shown to be able to homodimerize, and this was mediated by its M20A peptidas

56 tly in mitochondrial membranes, where it was homodimerized as assessed by homobifunctional cross-link

57 The p62 PB1 domain homodimerizes as well as heterodimerizes with other PB1

58 ears that A.thaliana define many families of homodimerizing B-ZIP proteins by having long leucine zip

59 n the a position helps define 14 families of homodimerizing B-ZIP proteins in A.thaliana, in contrast

60 ke alphaE-catenin in the CCC, these chimeras homodimerize, bind F-actin strongly, and inhibit the Arp

61 These proteins can only homodimerize but do not heterodimerize, and lacking sign

62 D68A) and Bax(E69A), retained the ability to homodimerize but failed to interact with Bcl-2 as determ

63 e pathogenic DJ-1/E163K variant is unable to homodimerize but is retained in the cytosol upon wild-ty

64 Viruses expressing mutants that failed to homodimerize but were able to form heterodimeric complex

65 Based on bacterial two-hybrid assays, CelR homodimerizes but does not interact with DivK.

66 ADSF-hFc not only homodimerizes but heterooligomerizes with ADSF/resistin

67 Nrf2 does not homodimerize, but CNC-bZIP.small Maf protein heterodimer

68 n is thought to arise from their property to homodimerize, but how dimerization influences their func

69 ecule that could be conditionally induced to homodimerize by adding the FKBP ligand AP1510, or instea

70 Refolded Bcl-2(1-203) showed no tendency to homodimerize by gel filtration or analytical ultracentri

71 Max readily homodimerizes, competes with C-myc-Max heterodimers, and

72 The homodimerized compounds actively inhibited chymotrypsin-

73 everal Bax mutants which retained ability to homodimerize (deltaBH1, deltaBH2, and delta1-58) also re

74 purpose of demonstration we use a set of 50 homodimerizing enzymes which were co-crystallized with t

75 one ATP-binding domain, ABCG2 is thought to homodimerize for function.

76 ed with multidrug resistance that presumably homodimerizes for function.

77 r forced dimerization by tagging it with the homodimerizing Fv domain.

78 nfirmed by in vitro analysis, HAND2 fails to homodimerize in a mammalian two-hybrid assay but demonst

79 onstrate the v-erbB products can efficiently homodimerize in all three target tissues, that this dime

80 process in that BAX did not redistribute or homodimerize in response to a death signal.

81 that various isoforms of CD45 differentially homodimerize in T cells.

82 otein was expressed in yeast, it was able to homodimerize in the nucleus.

83 vely spliced isoforms of human SH2-B readily homodimerize in yeast two-hybrid and cellular transfecti

84 Like TNFR1, WSL-1 will homodimerize in yeast.

85 Cbh2p and Abp1p homodimerized in the budding yeast two-hybrid assay, but

86 on enhancement experiments confirm that NBD1 homodimerizes in solution in the expected head-to-tail o

87 e that the BRCA1 NH2-terminal domain readily homodimerizes in solution.

88 glycoprotein of the thyroid gland, folds and homodimerizes in the endoplasmic reticulum (ER) before i

89 ocess in which the IRAK4 kinase domain first homodimerizes in the Myddosome, leading to its trans-aut

90 Neither Dpb3p nor Dpb2p homodimerizes in the two-hybrid assay.

91 rize and show that although PAK3a is able to homodimerize, it is more likely to form heterodimeric co

92 indicates that 75% of the beta-hairpins have homodimerized N strands and C strands in the anionic mem

93 The CB-MyoD fusion appears to divert homodimerizing native MyoD from its usual nuclear destin

94 or LAZ-3/BCL-6, BTB/POZ domain could readily homodimerize, no heterodimerization was detected in vivo

95 Interestingly, KS-bcl-2 neither homodimerizes nor heterodimerizes with other Bcl-2 famil

96 t destabilize TAK1, or impair its ability to homodimerize or bind TAB2, but it does increase TAK1 aut

97 nt RASSF1C exhibits a much weaker ability to homodimerize or heterodimerize; thus the binding of RASS

98 Boo inhibits apoptosis, homodimerizes or heterodimerizes with some death-promoti

99 ates a range of cellular processes by either homodimerizing or heterodimerizing with other basic HLH-

100 uced a functional kinase that preferentially homodimerized over interacting with EnvZ.

101 3 kDa protein (g-sept), which along with the homodimerized p-sept form a 56 kDa multimer (observed as

102 al 29 kDa protein (n-sept) that binds to the homodimerized p-sept, and together they form a 62 kDa mu

103 We elucidate a p110alpha-independent role of homodimerized p85alpha in the positive regulation of PTE

104 K-bZIP is a homodimerizing protein of 237 amino acids with a prototy

105 n was slightly more error prone than that of homodimerized pseudodiploid vectors.

106 ZIP proteins has led to leucine zippers that homodimerize rather than heterodimerize.

107 ly identical to that of classic caspases and homodimerizes similarly to form an active protease.

108 We show that TBR1 homodimerizes, that it interacts with FOXP2, a transcrip

109 bacteria, hibernation-promoting factor (HPF) homodimerizes the 70S ribosomes to form a translationall

110 heir complexes, we find that SYG-1 orthologs homodimerize through a common, bispecific interface that

111 Moreover, FOXP3 was found to homodimerize through its leucine zipper.

112 Furthermore, Dok can homodimerize through its phosphotyrosine binding domain

113 They have potential to both hetero- and homodimerize through their bHLHLZ domains, so it has bee

114 rength in noncrowded conditions, CA subunits homodimerize through this CTD-CTD interface, but do not

115 Here we report that RUNX1 homodimerizes through a mechanism involving C terminus-C

116 imer initiation site (DIS), that efficiently homodimerizes through a palindromic base sequence in its

117 c/DIABLO at 2.2 A resolution reveals that it homodimerizes through an extensive hydrophobic interface

118 sed, constitutively nuclear polypeptide that homodimerizes through its amino terminus and binds MST1

119 This arrangement suggests that RUNX1 could homodimerize to bring and hold together distant chromati

120 six transmembrane-spanning domains and must homodimerize to form the active membrane transporter.

121 We show that ARF DNA-binding domains also homodimerize to generate cooperative DNA binding, which

122 Lis1 must be able to homodimerize to stimulate dynein, because a C-terminal f

123 Both alpha- and beta-liprins homodimerize via their N-terminal, coiled coil regions.

124 or Cdc12, respectively) retain an ability to homodimerize via their so-called G interface, thereby al

125 with the ability of the inhibitor protein to homodimerize via this domain.

126 In addition, Kaiso homodimerized via its POZ domain but it did not heterodi

127 The domain homodimerizes via an antiparallel coiled coil with an ad

128 79mer has three internal disulfide bonds and homodimerizes via another disulfide bridge.

129 p110alpha-free p85alpha homodimerizes via two intermolecular interactions (SH3:p

130 The ability of the mutants to homodimerize was gauged by gel filtration and/or PAGE un

131 , I show that alpha-catenin must transiently homodimerize while bound to beta-catenin in order for ho

132 The pro-apoptotic protein Bax can homodimerize with itself and heterodimerize with the ant

133 Kar3 does not homodimerize with itself but forms a heterodimer with ei

134 model in which two molecules of SH2-B or APS homodimerize with their SH2 domains bound to two JAK2 mo

135 tant Bax proteins were tested for ability to homodimerize with themselves and to heterodimerize with

136 TF(L)LZ homodimerized with a K(d) similar to that of the LZ pept

137 or FKBP-rapamycin-binding domain [FRB]) were homodimerized with the bivalent FKBP ligand AP1510 and h

138 tracellular sialylation and O-glycosylation--homodimerizes with the highest efficiency, resulting in

139 tif, Bax(DeltaIGDE), was incapable of either homodimerizing with itself or heterodimerizing with Bcl-

140 All three dsRBPs are reported to homodimerize, with the Dicer-binding region implicated i

141 the first direct evidence that procaspase-9 homodimerizes within the apoptosome, markedly increasing

142 r cannot functionally substitute for another homodimerizing zipper domain in domain-swapping experime