ライフサイエンスコーパス: homomer

1 ve to inhibition compared to the GlyR alpha2 homomer.

2 fferent functional properties than the CNGA1 homomer.

3 less affected by many startle mutations than homomers.

4 eromers give much larger currents than ASIC3 homomers.

5 KA2, which prevent surface expression of KA2 homomers.

6 ng only opioid receptor heterodimers but not homomers.

7 e and do not exhibit significant function as homomers.

8 , such as heteromeric complexes favored over homomers.

9 ely, affected these events when expressed as homomers.

10 able differences compared to wild-type CNGA1 homomers.

11 is intermediate between wild-type and mutant homomers.

12 eta subunits is shifted toward that of alpha homomers.

13 GC-E and GC-F appear to preferentially form homomers.

14 ome and 20% of two eukaryotic proteomes form homomers.

15 replaces embryonically expressed GlyRalpha2 homomers.

16 tructure, and membrane organization of K-Ras homomers.

17 undergo a reverse transition back to enzyme homomers.

18 a heteromers together with ASIC1a and ASIC2a homomers.

19 ular weight species compared with A4V and WT homomers.

20 onectin, but heteromers separate faster than homomers.

21 lutamate concentrations, compared with GluK2 homomers.

22 e of cell surface D(2long) and D(3) receptor homomers.

23 shifted TEA sensitivity compared with KCNQ2 homomers.

24 of internalization of R1b, compared with R1b homomers.

25 ) K(+) channels, most probably KCNQ5 (Kv7.5) homomers.

26 aptic insertion and phosphorylation of GluA1 homomers.

27 annels is as effective as for TRPV1 or TRPA1 homomers.

28 meric channels compared with KCNQ2 and KCNQ3 homomers.

29 aptic AMPARs by providing stability to GluR1 homomers.

30 g alpha7 subunits are thought to assemble as homomers.

31 protruding height when compared with the PC2 homomers.

32 ld potentially be arranged either as a GluK2 homomer alongside a GluK5 homomer or as two GluK2/K5 het

33 current detection of each of M2-M2 and M3-M3 homomers alongside M2-M3 heteromers at the surface of st

34 The mutant D(2)R homomers also exhibited bias towards recruitment of the

35 in-protein interaction domain which mediates homomer and heteromer formation with each family member.

36 t in the wild-type condition, when both ISA1 homomer and ISA1/ISA2 heteromer are present.

37 2 immunoprecipitates contain functional HAS2 homomers and also heteromers with HAS3.

38 ariants expressed in Xenopus oocytes both as homomers and as heteromeric NR1/NR2A or NR1/NR2B complex

39 We investigated how ASIC1a homomers and ASIC1a/2a heteromers respond to brief stimu

40 ow desensitzation enables recombinant ASIC1a homomers and ASIC1a/2a heteromers, as well as native ASI

41 edly higher glutamate sensitivity than GluK2 homomers and did not desensitize at low glutamate concen

42 ents surface expression of nonfunctional KA2 homomers and ensures a high level of GluR6/KA2 heteromer

43 expressing each subtype a complex mixture of homomers and heteromers co-exists at steady state.

44 owed by Western analysis confirmed that both homomers and heteromers could be formed.

45 nvironment-driven transitions between enzyme homomers and heteromers during their trafficking within

46 G-protein coupled receptors (GPCRs) can form homomers and heteromers in addition to functioning as si

47 idence that AtSUN1 and AtSUN2 are present as homomers and heteromers in vivo, and that the coiled-coi

48 g a reconstitution of function approach both homomers and heteromers of D(2long) and D(3) receptors w

49 Such homomers and heteromers were found to co-exist and using

50 inant ASIC1b- and ASIC3-containing channels (homomers and heteromers) is lost on mutation of a putati

51 ine D(2long) and D(3) receptors to form both homomers and heteromers, and show that in cells expressi

52 By forming both homomers and heteromers, the hdeltaOR-Cys-27 variant may

53 teraction and are able to bind each other as homomers and heteromers, they are structurally plastic a

54 KCNQ1 and KCNQ4 homomers and KCNQ2/3 heteromers yield large currents, wh

55 which are small compared with those of KCNQ4 homomers and KCNQ2/Q3 heteromers.

56 membrane domain are active at both mGlu(4/4) homomers and mGlu(2/4) heteromers, while those that bind

57 All three proteins were also able to form homomers and MtCRN and MtCLV2 also interact with each ot

58 nto the assembly of functional human alpha10 homomers and provide tools for the development of alpha1

59 dence indicates that they function as enzyme homomers and/or heteromers in the living cell.

60 luR2 heteromeric receptors behave like GluR2 homomers, and endogenous AMPA receptors show differentia

61 Molecular mass, polydispersity of homomers, and the rate of subunit exchange with WT-alpha

62 interplay and show that glycosyltransferase homomers are assembled in the endoplasmic reticulum.

63 oteins that assemble into different types of homomers are associated with different biological functi

64 that the folds of single-domain MBS and SBS homomers are different, and SBS homomers are likely to b

65 Upon transport to the Golgi, the majority of homomers are disassembled to allow the formation of enzy

66 MBS and SBS homomers are different, and SBS homomers are likely to be folded cotranslationally, whil

67 ly to be folded cotranslationally, while MBS homomers are more likely to form post-translationally an

68 itatively different from monomers, while SBS homomers are much less distinct, supporting the hypothes

69 nge of such binding pockets, ligands of such homomers are much more likely to bind their homologs tha

70 addition, our findings demonstrate that MBS homomers are qualitatively different from monomers, whil

71 We show that Kv1.2 homomers are responsible for two-thirds of presynaptic l

72 c efficiently to the plasma membrane, hERG1b homomers are retained in the endoplasmic reticulum (ER).

73 We conclude that KCNQ3 homomers are well expressed at the plasma membrane, but

74 Homomers are widespread, with 50-70% of proteins with a

75 ntly incorporates into and inactivates OCR-2 homomers as well as heteromers with the TRPV subunits OC

76 examined the responses of recombinant ASIC1a homomers, ASIC1a/2a heteromers and native ASICs from sen

77 involvement of transmembrane domains in AT1R homomer assembly with the goal of identifying hydrophobi

78 about the mechanisms that drive formation of homomers at the level of evolution and assembly in the c

79 ere used to develop one maize line with ISA1 homomer but lacking heteromeric ISA and a second line wi

80 e in blocking heterologously expressed TRPC5 homomers but also TRPC1:TRPC5 heteromers as well as nati

81 et within the same domain are efficacious in homomers but not heteromers.

82 roximately 20-fold lower levels versus Kv1.4 homomers but they were trans-Golgi glycosylated.

83 se-type debranching activity present is ISA1 homomer, but not in the wild-type condition, when both I

84 9 families, which do not generate functional homomers, but instead assemble and modify the function o

85 profile of this conductance excludes TASK-3 homomers, but rather implicates TASK-1-containing channe

86 ion of heteromers and their coexistence with homomers by electrophysiology, but could not determine w

87 effectively converted from heteromers to 1a homomers by expressing a fragment corresponding to the 1

88 nt heteromeric GlyRs were less impaired than homomers by this mutation when we measured their respons

89 tion analyses suggested an increase in GluA4 homomers (Ca(2+)-permeable AMPAR) and immunohistochemica

90 nction of protein complexes, particularly in homomers-complexes comprising multiple copies of the sam

91 lpha and beta subunits at a ratio of 2:1 and homomers composed of only alpha subunits.

92 tic enhancement of the contribution of GluR1 homomers, concentrated at the largest synapses.

93 om this data that PC12 BgtRs and alpha7/5HT3 homomers contain at least three distinguishable agonist

94 While homomers containing 5-HT(3A) subunits form functional li

95 but also how GluA2-lacking, Ca(2+)-permeable homomers could form, which are induced under specific ph

96 The GlyRs expressed as alpha1 homomers either in HEK-293 cells or at presynaptic termi

97 pproaches demonstrated that the D(2)R mutant homomers exhibited greater stability.

98 ], has low nanomolar affinity for rat alpha7 homomers expressed in Xenopus laevis oocytes, and antago

99 irement of mutations of Trp175(4.64) in both homomers for disrupting dimerization.

100 dition, we present evidence that beta(2)L99C homomers form spontaneously open channels.

101 1 interacts with SRK and interferes with SRK homomer formation.

102 binding cooperativity was observed for BgtR homomers formed from chimeric alpha7/5HT3 subunits expre

103 We observe that homomers from different symmetry groups are significantl

104 When expressed in cell lines these homomers had very different trans-Golgi glycosylation ef

105 strategies and the generation of asymmetric homomers have started to provide information on the cont

106 al model of the D2 dopamine receptor (D(2)R) homomer identified distinct combinations of substitution

107 The alpha7 subunit appears to exist as a homomer in the posterior post-acrosomal and neck regions

108 sion when they were transiently expressed as homomers in cell lines.

109 M378R) that also form constitutive CRY2-CRY2 homomers in dark, suggesting they adopt global conformat

110 Whole-cell recording studies of iGluR3 homomers in HEK293 cells revealed that neither iGluR3-M7

111 eover, we found that the assembly of ST6GAL1 homomers in the endoplasmic reticulum before ST6GAL1 act

112 jority of GC-E and GC-F were precipitated as homomers in the eye.

113 rm heteromeric channels that differ from the homomers in their unitary conductance, kinetic behavior,

114 The ERECTA family forms receptor homomers in vivo.

115 the role of presynaptic GlyRs, likely alpha homomers, in diseases.

116 siological analysis of surface-expressed KA2 homomers indicates that they do not form functional ion

117 ructure are monomers, while in the cytoplasm homomers, indicating that the evolution of oligomers is

118 hromatography of D393S shows the presence of homomers instead of a monomer in the dark, providing sup

119 f the M2 receptor resulted in enhanced M2-M2 homomer interactions but decreased M2-M3 heteromer inter

120 A homomer is formed by self-interacting copies of a protei

121 es and show that the quaternary structure of homomers is conserved in over 70% of protein pairs shari

122 structurally crucial because mis-assembly of homomers is implicated in disease.

123 the evolution of quaternary structure in SBS homomers is significantly influenced by stochastic proce

124 The resulting SRK homomer levels would be sensed by the common pollen reje

125 bservation that nmrASIC3 forms nonfunctional homomers may reflect a further adaptation of the naked m

126 he maximum decrease in chaperone activity in homomers occurred on deamidation of N123 residue, but it

127 man recombinant 5-HT3 receptors assembled as homomers of 5-HT3A subunits, or heteromers of 5-HT3A and

128 Recombinant homomers of alpha- or beta-CaM kinase II, as well as of

129 nAChR subtypes exist as homomers of alpha-subunits or heteromers composed of alp

130 vity of the heterocomplex, without effect on homomers of either receptor, and reduced SCT-stimulated

131 tor subunits can form functional channels as homomers of GluK1, GluK2 or GluK3, or as heteromeric com

132 Homomers of human alpha1 GlyR were recombinantly express

133 al data suggesting differing stabilities for homomers of the cognate human beta1- and beta2-adrenergi

134 The homomer-only line had smaller, more numerous granules.

135 either as a GluK2 homomer alongside a GluK5 homomer or as two GluK2/K5 heterodimers.

136 tor did not significantly alter either M3-M3 homomer or M2-M3 heteromer interactions.

137 is not glycosylated at Asn(132), either as a homomer or when coexpressed with GIRK1.

138 tained current occurs with ASIC1a (either as homomers or 1a/3 heteromers), whereas ASIC2a/3 heteromer

139 Expression of alpha7 homomers or alpha/beta pairs (alpha2, alpha3, alpha4, or

140 te, and some members have been shown to form homomers or heteromeric complexes with catalytically ina

141 type II TGF-beta receptor cytoplasmic domain homomers or heteromers can be examined.

142 GPCR homomers or heteromers have been explored widely for GPC

143 tect Galphaq or Galpha11 protein coupling to homomers or heteromers of D1 or D2 receptors using a var

144 still unknown whether AdipoR2 may also form homomers or heteromers with AdipoR1 or if such interacti

145 ggested that GC-E and GC-F could form either homomers or heteromers, at least when overexpressed in C

146 ; and the helical sequences can be the same (homomers) or different (heteromers).

147 X(1) heteromer compared with the OX(1)-OX(1) homomer present in the same cells and the effects of CB(

148 evolution of enzymes in circumstances where homomers rarely evolve.

149 All GIRK1-containing channels, but not GIRK2 homomers, recruited Gbetagamma to the plasma membrane.

150 In alpha1 homomers, removal of the hydroxyl group by mutation of r

151 rs and that TGF beta receptor heteromers and homomers show distinct trafficking behavior.

152 tematic analysis of the relationship between homomer structure and function.

153 ch deviate substantially from existing GluA2 homomer structures.

154 ar relationship between protein function and homomer symmetry that has important implications for und

155 Relative to WT-alphaA homomers, the mutant proteins exhibited major structural

156 ent for specific binding, and FBI-1 can form homomers through its POZ domain and, in vivo, through it

157 NQ2/3 heteromers and KCNQ2-5, but not KCNQ1, homomers to muscarinic inhibition, manifested by shifts

158 Ca(2+)-permeable (CP) AMPARs, such as GluR1 homomers, to synapses likely via lateral diffusion from

159 IJ has high affinity, and a putative K(v)1.2 homomer, toward which kappaM-RIIIJ is less potent.

160 While hERG1a homomers traffic efficiently to the plasma membrane, hER

161 mal cultures where ligand bound to TGF-betaR homomers was internalized, yet the receptors were not do

162 rrent, spontaneously gated by beta 3 subunit homomers, was enhanced by pentobarbitone and inhibited b

163 Kv1 homomers were absent from bushy cell somata (from which

164 alpha10 homomers were blocked by alpha-bungarotoxin but were ins

165 currently not well understood, especially in homomers, where quaternary structure might frequently ev

166 opy structures of the Ca(2+)-permeable GluA3 homomer, which substantially diverges from other AMPARs.

167 their homologs than ligands of monomers, or homomers with a single-chain binding site.

168 ceptor mutation affects the assembly of AT1R homomers with a specific focus on hydrophobic residues.

169 Here we show that a particular class of homomers with binding sites spanning multiple protein ch

170 assembly into multimeric structures, usually homomers with even numbers of subunits all derived from

171 Previously, we have shown that homomers with multichain binding sites (MBSs) are charac

172 itatively different allosteric pathways than homomers with single-chain binding sites (SBSs) or monom

173 ield large currents, whereas KCNQ2 and KCNQ3 homomers yield small currents.