ライフサイエンスコーパス: RAMP

1 RAMPs (1-3) are single transmembrane accessory proteins

2 RAMPs (receptor activity modifying proteins) impart rema

3 RAMPs are required to transport CRLR to the plasma membr

4 with receptor activity-modifying protein 1 (RAMP 1).

5 both receptor activity-modifying protein-1 (RAMP-1) and calcitonin receptor gene (CT-R) expression i

6 ing body development and EPS production in a RAMP-dependent manner.

7 ally to the cell surface in these cells in a RAMP-independent manner, resulting in both free and RAMP

8 All RAMP 1 mutants were able to associate with CRLR with ful

9 d specificity, we have co-expressed CRLR and RAMP proteins in the yeast Saccharomyces cerevisiae, whi

10 en other members of this receptor family and RAMP proteins.

11 dependent manner, resulting in both free and RAMP-associated receptor on the cell surface.

12 amily of receptors displays both ligand- and RAMP-dependent signaling bias among the Galphas, Galphai

13 d found expression correlation for GPCRs and RAMPs.

14 We applied RAMP to examine how endonucleolytic cleavages of the mou

15 We benchmark RAMP against traditional FBA on genome-scale metabolic r

16 otif, present as five tandem repeats in both RAMP and DXS6673E.

17 iomarkers, were determined in each sample by RAMP immunoassay.

18 as the stochastic elements dissipate, and C) RAMP can identify biologically tolerable diversity of a

19 atures of the crRNAs associated with the Cas RAMP module (Cmr) effector complex, which cleaves target

20 e synthesis factor produces a characteristic RAMP profile that exhibits consistency across a range of

21 These different CLR-RAMP interactions yield discrete receptor pharmacology a

22 nd may inform drug development targeting CLR:RAMP complexes.

23 rgy homeostasis, but the significance of CNS RAMPs in the control of energy balance remains unknown.

24 uman RAMP 1, three mutants were constructed: RAMP 1 without the cytoplasmic tail, a chimera consistin

25 constructions of native type III Cmr (CRISPR RAMP module) complexes in the absence and presence of ta

26 the CRLR-RAMP3 complex and NHERF-1, the CRLR-RAMP complex desensitizes but is unable to internalize u

27 y, we observed that in HEK293 cells the CRLR-RAMP complex undergoes agonist-stimulated desensitizatio

28 The internalization of the CRLR-RAMP complex was not affected by NHERF-1 when CRLR was c

29 agonist-induced internalization of the CRLR-RAMP complex.

30 odifying proteins (RAMPs) showed that a CRLR/RAMP receptor complex is required for intermedin signali

31 rtensive rats via interactions with the CRLR/RAMP receptor complexes.

32 ide family capable of signaling through CRLR/RAMP receptor complexes provides an additional player in

33 8p11, to a novel gene at 13q11-12 designated RAMP .

34 ells to characterize the effect of different RAMP and ligand combinations on this pathway.

35 During RAMP, nicotine increased the initial SkBF at 42 degrees

36 ells in the presence or absence of exogenous RAMP transfection, although the secretin receptor traffi

37 -R and suggest a broader regulatory role for RAMPs in receptor trafficking.

38 How peptides selectively bind GPCR:RAMP complexes is unknown.

39 Hospital RAMP outlier status is a rectal cancer surgery composite

40 results reveal unexpected differences in how RAMPs determine CTR and CLR peptide selectivity and supp

41 ransmembrane, TM; and tail domains) of human RAMP 1, three mutants were constructed: RAMP 1 without t

42 Although the three known mammalian RAMPs differ in their sequences and tissue expression, r

43 this requires the reference standard method (RAMP(R) immunoassay)) or alternatively on the basis of t

44 Heating occurred at one site over 15 min (RAMP) and over 90 s (STEP) at another site, and was main

45 Moreover, RAMP has the properties that: A) metabolic states are (L

46 , high outlier (worse than expected), or non-RAMP outlier using standard observed-to-expected methodo

47 variability in model performance, our novel RAMP approach is able to extract more information in ter

48 t in which the N-terminal 641 amino acids of RAMP become joined to the tyrosine kinase domain of FGFR

49 The results are discussed in the context of RAMP interactions probed through molecular modeling and

50 rived growth factor receptor, and the ECD of RAMP 1 alone.

51 mic tail, a chimera consisting of the ECD of RAMP 1 and the TM and tail of the platelet-derived growt

52 In conclusion, the ECD of RAMP 1 is sufficient for normal CRLR association and eff

53 The C-terminal tail of RAMP 1 is unnecessary for CRLR function.

54 ding the molecular details of the effects of RAMPs on CLR.

55 In contrast, expression of RAMPs 1, 2, and 3 was unaffected by low oxygen tension.

56 Such previously unrecognized functions of RAMPs highlight the need to consider all receptor-intera

57 s study further highlights the importance of RAMPs to CLR pharmacology and to bias in general, as wel

58 f Nt-CRLR to bind CGRP and AM independent of RAMPs was determined by studying inhibition of (125)I-CG

59 of CRLR was not affected by the presence of RAMPs in yeast, indicating that glycosylation of CRLR is

60 To analyze the role of RAMPs in determining ligand specificity, we have co-expr

61 m of this study was to determine the role of RAMPs in receptor trafficking.

62 lled receptor-activity-modifying proteins or RAMPs, are expressed.

63 suggesting that CLR may associate with other RAMPs in these tissues to form a receptor for additional

64 lem shows that FBA is a limiting case of our RAMP method.

65 cts a robust analysis of metabolic pathways (RAMP).

66 Regionalized Air Quality Model Performance (RAMP) approach to integrate chemical transport model (CT

67 call Ratio Analysis of Multiple Precursors (RAMP).

68 The predicted RAMP protein exhibits strong homology to the product of

69 the receptor (CRLR), the chaperone protein (RAMP), and RCP that couples the receptor to the cellular

70 equires receptor activity modifying protein (RAMP) 1 to give a calcitonin gene-related peptide (CGRP)

71 called receptor activity-modifying protein (RAMP) 1.

72 of the receptor activity modifying protein (RAMP) family, which results in the formation of two diff

73 ncoding receptor activity-modifying protein (RAMP)-like triterpene glycoside receptor (RL-TGR), a nov

74 rafish, receptor activity modifying protein (RAMP)-like triterpene glycoside receptor (RL-TGR), was p

75 ferent receptor activity modifying proteins (RAMP) to become a functional calcitonin gene-related pep

76 Receptor activity-modifying proteins (RAMPs 1-3) are single transmembrane accessory proteins c

77 Receptor activity-modifying proteins (RAMPs) 1, 2, and 3 are unusual accessory proteins that d

78 Receptor activity-modifying proteins (RAMPs) are widely expressed in human tissues and, in som

79 ), and receptor activity modifying proteins (RAMPs) have become recognized as integral components of

80 three receptor activity-modifying proteins (RAMPs) have been recognized as being important for the t

81 three receptor activity-modifying proteins (RAMPs) showed that a CRLR/RAMP receptor complex is requi

82 three receptor activity-modifying proteins (RAMPs).

83 g the repeat-associated mysterious proteins (RAMPs).

84 spital risk-adjusted margin positivity rate (RAMP) that allows identification of performance-based ou

85 further explore the utility of the receptor-RAMP interface as a pharmacological target.

86 Consequently, the receptor-RAMP interface represents an attractive pharmacological

87 None of the mutations significantly reduced RAMP expression.

88 ferred conformation of peptides that require RAMPs; CGRP, AM, and amylin.

89 In addition, the resulting RAMP-GPCR interaction map suggests that RAMP1 and RAMP3

90 (R)-1-amino-2-methoxymethylpyrrolidine (SAMP/RAMP)hydrazones.

91 ocedure involving the metalation of the SAMP/RAMP hydrazones of N-Boc-azetidin-3-one, reaction with a

92 (up to 84% ee) by the metalation of the SAMP/RAMP hydrazones of oxetan-3-one, followed by reaction wi

93 Tethering RAMPs to CTR enhanced binding of rAmy, CGRP, and the AMY

94 We discovered that RAMPs and GPCRs tend to have orthologs in the same speci

95 selectivity and support the hypothesis that RAMPs allosterically modulate CTR peptide affinity.

96 These data indicate that RAMPs are necessary and sufficient to determine ligand s

97 ency for CGRP signaling and binding, and the RAMP 1-ECD mutant had a 4000-fold decrease in potency.

98 med prokaryotic silencing (psi)RNAs) and the RAMP module (or Cmr) Cas proteins.

99 in represents a nonselective agonist for the RAMP coreceptors.

100 However, the RAMP 1/platelet-derived growth factor receptor chimera d

101 a TM domain and the specific sequence of the RAMP 1 TM domain contribute to CGRP affinity and potency

102 pendent on the intramembranous region of the RAMP and TM6 and TM7 of this receptor.

103 ng and molecular dynamics simulations of the RAMP-GPCR-G protein complexes.

104 By analogy with these, we propose that the RAMP-FGFR1 fusion product will contribute to progression

105 ozone observations only in contrast with the RAMP and a Constant Air Quality Model Performance (CAMP)

106 The RAMPs augment the binding site with distinct contacts to

107 These RAMP 1 mutants were examined for their ability to associ

108 These RAMP genes are indispensable for CRISPR3* to affect deve

109 In humans, there are three RAMPs and over 800 expressed GPCRs, making direct experi

110 be structurally and functionally related to RAMPs, a family of coreceptors that physically associate

111 t-mediated receptor-actin-myosin polarity (W-RAMP) structure accumulates asymmetrically at the cell p

112 However, whether RAMP-GPCR interactions are widespread, and the nature of

113 It is unclear whether RAMPs use a similar mechanism to modulate CTR affinity f

114 hypothesis that GPCRs interact globally with RAMPs in cellular signaling pathways.

115 ucts of two, highly homologous genes: ZNF198/RAMP/FIM and ZNF261/DXS6673E.