ライフサイエンスコーパス: exodomain

1 in-like region (Hir) located in the receptor exodomain.

2 as important LRRs spread throughout the FSHR exodomain.

3 50-amino acid-long, N-terminal extracellular exodomain.

4 vides a clue for the signal modulator in the exodomain.

5 ted when thrombin cleaves its amino-terminal exodomain.

6 eavage site generating transiently activated exodomain.

7 follicle-stimulating hormone binding to the exodomain.

8 ted when thrombin cleaves its amino-terminal exodomain.

9 loop 2 influences the hormone binding to the exodomain.

10 endodomain attenuates hormone binding at the exodomain.

11 repeats and is located in the middle of the exodomain.

12 king the kcat/Km the same as that of PAR1-wt exodomain.

13 rombin binding and cleavage of PAR1 and PAR4 exodomains.

14 c measurements using soluble PAR1 N-terminal exodomains.

15 The exodomain alone binds hormone with high affinity, wherea

16 like most seven-transmembrane receptors, the exodomain alone is responsible for high affinity hormone

17 350-amino acid-long N-terminal extracellular exodomain and a membrane-associated endodomain of simila

18 or domains of similar size, an extracellular exodomain and a membrane-associated endodomain which inc

19 inct functions: the N-terminal extracellular exodomain and C-terminal membrane-associated endodomain.

20 rminal region of exoloop 3 interact with the exodomain and constrain the hormone binding in the wild

21 is known about the relationship between the exodomain and endodomain.

22 orresponding to the N-terminal region of the exodomain and exoloop 3 of the endodomain.

23 urface plasmon resonance, we found that LDLR exodomain and its cluster of complement-type repeats (CR

24 30 amino acids, the N-terminal extracellular exodomain and membrane-associated endodomain including t

25 30 amino acids, the N-terminal extracellular exodomain and membrane-associated endodomain.

26 PAR1-wt exodomain and P4 and P3 mutants were noncompetitive inhi

27 of equal size, the N-terminal extracellular exodomain and the C-terminal membrane-associated endodom

28 o equal halves, the N-terminal extracellular exodomain and the C-terminal membrane-associated endodom

29 or the precise hormone contact points in the exodomain and the endodomain.

30 tracellular face of PAR2, its amino-terminal exodomain and three extracellular loops, for the cognate

31 3), Ile(584), and Lys(590) interact with the exodomain and/or the hormone.

32 o halves: the N-terminal extracellular half (exodomain) and C-terminal membrane-associated half (endo

33 rminal extracellular hormone binding domain (exodomain) and the C-terminal membrane-associated, signa

34 FSH initially binds to exodomain, and the resulting FSH/exodomain complex modul

35 Hormone binds to the exodomain, and the resulting hormone-exodomain complex m

36 an chorionic gonadotropin (hCG) binds to the exodomain, and then hCG/exodomain complex is thought to

37 er, the precise hormone contact sites in the exodomain are unclear.

38 er, the precise hormone contact sites in the exodomain are unknown.

39 Plasmin also cleaves the TR78 exodomain at the R41 thrombin-cleavage site generating t

40 nly plasmin can rapidly truncate the soluble exodomain at the R70/K76/K82 sites located on a linker r

41 As a result, the exodomain attains the maximal affinity for hormone bindi

42 This exodomain binds hormone with high affinity and specifici

43 The exodomain binds the hormone with high affinity, and the

44 activated through cleavage of the N-terminal exodomain by the serine protease thrombin.

45 The resulting hCG-exodomain complex adjusts the structure and its associat

46 n (hCG) binds to the exodomain, and then hCG/exodomain complex is thought to make a secondary contact

47 main, of its receptor, and the resulting hCG-exodomain complex is thought to modulate the membrane as

48 ly binds to exodomain, and the resulting FSH/exodomain complex modulates the endodomain and generates

49 to the exodomain, and the resulting hormone-exodomain complex modulates the endodomain to generate s

50 ith high affinity, and the resulting hormone/exodomain complex modulates the endodomain where recepto

51 The exodomain has seven to nine Leu-rich repeats, which are

52 Our results indicate that the region of the exodomain interacts with hCG and that the contact points

53 ly, the high affinity hormone binding at the exodomain is constrained by a group of amino acids, Ser4

54 The exodomain is exclusively responsible for high affinity h

55 Plasmin cleavage of the TR78 exodomain is nearly equivalent to that of thrombin cleav

56 The uniquely large exodomain is responsible for high affinity hormone bindi

57 The bulk of the exodomain is speculated to assume a crescent structure c

58 contact point (the signal modulator) in the exodomain is.

59 ta(40) ratio, indicating that the N-terminal exodomain of APP is not required for mutant PS1 to influ

60 edly, MMP-1 and MMP-13 cleave the N-terminal exodomain of PAR1 at noncanonical sites, which result in

61 (PAR4) due to a hirudin-like sequence in the exodomain of PAR1 that binds thrombin's exosite I.

62 A chimeric protein in which the N-terminal exodomain of PAR1 was fused to an unrelated transmembran

63 p(57), Asp(59), Glu(62), and Asp(65)) in the exodomain of PAR4 is examined for its influence on cleav

64 The N-terminal exodomain of protease-activated receptor-1 (PAR1), a G p

65 asis of a known amino acid difference in the exodomain of the DT receptor (proHB-EGF) of swine compar

66 ion are mediated by thrombin cleavage of the exodomain of the PAR1 receptor.

67 ctivates PAR1 by cleaving the amino-terminal exodomain of the receptor, which exposes a tethered pept

68 inds to the extracellular N-terminal domain, exodomain, of its receptor, and the resulting hCG-exodom

69 determine which subunit of FSH contacts the exodomain or endodomain and in what orientation FSH inte

70 y, substitution of either the amino-terminal exodomain or third extracellular loop alone caused marke

71 than the hirudin-like binding region on PAR1 exodomain predominate in influencing PAR1 cleavage on ce

72 Furthermore, the C-terminal exodomain product of thrombin cleavage, corresponding to

73 PAR1 shedding resides within its N-terminal exodomain rather than its heptahelical segment, that act

74 e in secretion of the soluble amino-terminal exodomain (s-APP alpha) derived from non-amyloidogenic p

75 The sequence alignment of the exodomain shows imperfectly matching eight to nine Leu-r

76 However, recombinant exodomain studies indicate that PAR4 does have extended

77 a2-binding IL-13 mutein to make a tandem CAR exodomain (TanCAR) and a CD28.zeta endodomain.

78 rombin cleaves the receptor's amino-terminal exodomain to reveal the new N-terminal sequence SFLLRN w

79 mbin binds to and cleaves its amino-terminal exodomain to unmask a new receptor amino terminus.

80 by specific cleavage of their amino-terminal exodomains to unmask a tethered ligand that binds intram

81 By using a soluble N-terminal exodomain (TR78) as a model for the full-length receptor

82 n cleavage of this receptor's amino-terminal exodomain unmasks a new amino terminus.

83 Specific cleavage of their amino-terminal exodomains unmasks a new amino terminus which then serve

84 ity was further improved by >3-fold when the exodomain was attached to the membrane-associated domain

85 Recombinant PAR1 wild-type (wt) exodomain was cleaved by alpha-thrombin with a Km of 28

86 Recombinant PAR4-wt exodomain was cleaved by alpha-thrombin with a Km of 61

87 To address these issues, the exodomain was examined by Ala scan and multiple substitu

88 It was reported that hormone binding to the exodomain was improved when the endodomain was truncated

89 result suggests that hormone binding to the exodomain was influenced by the endodomain.

90 When the FSH-R exodomain was prepared by truncating its endodomain, the

91 ediately downstream of the N terminus of the exodomain was shown to be crucial for hormone binding.

92 odomain, the hormone binding affinity of the exodomain was slightly improved, compared with the wild

93 All PAR4 exodomains were competitive inhibitors of alpha-thrombin

94 the upstream and downstream LRRs of the LHR exodomain, whereas important LRRs spread throughout the