ライフサイエンスコーパス: homomer

1 ve to inhibition compared to the GlyR alpha2 homomer.

2 , such as heteromeric complexes favored over homomers.

3 ely, affected these events when expressed as homomers.

4 able differences compared to wild-type CNGA1 homomers.

5 is intermediate between wild-type and mutant homomers.

6 eta subunits is shifted toward that of alpha homomers.

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

8 undergo a reverse transition back to enzyme homomers.

9 a heteromers together with ASIC1a and ASIC2a homomers.

10 onectin, but heteromers separate faster than homomers.

11 lutamate concentrations, compared with GluK2 homomers.

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

13 shifted TEA sensitivity compared with KCNQ2 homomers.

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

15 of internalization of R1b, compared with R1b homomers.

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

17 aptic insertion and phosphorylation of GluA1 homomers.

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

19 meric channels compared with KCNQ2 and KCNQ3 homomers.

20 aptic AMPARs by providing stability to GluR1 homomers.

21 g alpha7 subunits are thought to assemble as homomers.

22 protruding height when compared with the PC2 homomers.

23 eromers give much larger currents than ASIC3 homomers.

24 KA2, which prevent surface expression of KA2 homomers.

25 ng only opioid receptor heterodimers but not homomers.

26 e and do not exhibit significant function as homomers.

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

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

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

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

31 2 immunoprecipitates contain functional HAS2 homomers and also heteromers with HAS3.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

80 We observe that homomers from different symmetry groups are significantl

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

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

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

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

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

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

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

88 The ERECTA family forms receptor homomers in vivo.

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

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

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

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

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

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

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

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

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

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

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

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

101 Homomers of human alpha1 GlyR were recombinantly express

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

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

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

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

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

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

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

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

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

111 GPCR homomers or heteromers have been explored widely for GPC

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

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

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

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

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

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

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

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

120 ch deviate substantially from existing GluA2 homomer structures.

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

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

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

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

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

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

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

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

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

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

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