コーパス検索結果 (1語後でソート)
通し番号をクリックするとPubMedの該当ページを表示します
1 re for a PAR2 antagonist competing against a tethered ligand.
2 ond both to exogenous SFLLRN and to a second tethered ligand.
3 tivation of a chemokine receptor by a pseudo-tethered ligand.
4 by proteolysis of the N terminus to expose a tethered ligand.
5 s at a conserved target arginine to reveal a tethered ligand.
6 by proteolysis of the N terminus to reveal a tethered ligand.
7 red testisin specifically releases the PAR-2 tethered ligand.
8 MrgprC11 did not involve the generation of a tethered ligand.
9 proteolytic cleavage and the unmasking of a tethered ligand.
10 4 activation by both agonist peptide and the tethered ligand.
11 ytic cleavage, PAR(2) is activated through a tethered ligand.
12 by proteolytic cleavage and generation of a tethered ligand.
13 or 2 (PAR-2), via cleavage and exposure of a tethered ligand.
14 y cleavage of the amino terminus to unmask a tethered ligand.
15 tivated by proteolytic exposure of an occult tethered ligand.
16 placement of diffusible Netrin-B by membrane-tethered ligands.
17 ated by proteolytic shedding of its membrane-tethered ligands.
18 functionalized Au surfaces with three thiol-tethered ligands: 2-mercaptopropionic acid, 4-pyridinyle
27 the hexapeptide SFFLRN (that functions as a tethered ligand) and was blocked by the thrombin inhibit
30 pecific labeling is achieved by presenting a tethered ligand at the synapses of genetically defined n
31 However, targeting PAR1 with an orthosteric-tethered ligand binding-site antagonist results in bleed
32 lithium compounds have been prepared with a tethered ligand, (CH(3)OCH(2)CH(2))(2)NCH(2)C(CH(3))(2)-
34 ived agonist peptide (TRAP, a portion of the tethered ligand created by thrombin's proteolytic activi
35 a new amino terminus which then serves as a tethered ligand, docking intramolecularly to the body of
36 fication of the docking interactions between tethered ligand domain and receptor is critical for unde
38 of PAR1 antagonists, which compete with the tethered ligand domain rather than preventing PAR1 cleav
41 for thrombin, which is also activated by the tethered-ligand domain sequence (SFLLRN) and which promo
42 ast cells, and peptides corresponding to the tethered ligand domains of PAR-1 and PAR-2 increased [Ca
43 Synthetic "agonist peptides" that mimic the tethered ligand domains of thrombin receptor and PAR2 ac
44 ases cleave PARs at specific sites to expose tethered ligand domains that bind to and activate the cl
47 eptor-1 (PAR-1) can be activated by both the tethered ligand exposed by thrombin cleavage and a synth
48 ized complement component C5 and unmasks the tethered ligand for EC-expressed protease-activated rece
51 tide (GYPGQV) representing the newly exposed tethered ligand from the amino terminus of PAR4 after pr
53 ity behavior would be expected for a matrix-"tethered" ligand; i.e., a ligand which acts from the mat
54 rin receptors dissociate streptavidin-biotin tethered ligands in focal adhesions within 60 min of cel
56 equilibrium system the compound with the exo-tethered ligand inverts faster than its endo analog.
58 nd release from the cell surface of membrane-tethered ligands is an important mechanism of regulating
60 aved at an N-terminal arginine to unmask its tethered ligand, is generally regarded as a target for t
62 psin, SLIGRL-NH2 (corresponding to the PAR-2 tethered ligand), mast cell tryptase, and a filtrate of
65 c trypsin and a peptide corresponding to the tethered ligand of PAR-2, which is exposed by trypsin cl
67 vation because peptides corresponding to the tethered ligand of the thrombin receptor were also able
70 lasmin-cleavage sites removes the N-terminal tethered ligand or preligand, thereby providing an effec
71 let [Ca2+]i induced by alpha-thrombin or the tethered ligand peptide (TLP; SFLLRNPNDKYEPF) have been
72 s agonists for probing PAR function, but the tethered ligand peptide for PAR4, GYPGKF, lacks potency
73 o-terminal domain, but Ca2+ responses to the tethered ligand peptide SFLLRNPNDKYEPF were not affected
85 ceptors can be conjugated to photoswitchable tethered ligands (PTLs) to enable photoactivation, or ph
86 PAR2) is a 7-transmembrane G-protein-coupled tethered ligand receptor that is expressed by pancreatic
87 s to utilize mechanism(s) independent of its tethered ligand receptor to selectively prime phospholip
89 o the functioning G protein-linked thrombin (tethered ligand) receptor in human platelet membranes.
91 essions that relate key properties of single-tethered ligand-receptor interactions to multiple bond f
93 ated PAR1 and PAR2 bound to their endogenous tethered ligands, revealing a shallow and constricted or
95 h sequences derived from these novel exposed tethered ligands, selectively stimulated PAR1-mediated m
96 cleavage and a synthetic peptide having the tethered ligand sequence (thrombin receptor agonist pept
97 nthetic agonist peptides (AP) that share the tethered ligand sequence also activate PAR2, often measu
99 ird residues of the human thrombin receptor "tethered ligand" sequence (SFLLR) led to a series of ago
100 vated by proteolytic-mediated exposure of a "tethered ligand" sequence and can also be activated by t
101 in the amino acid sequence of the receptors' tethered ligand sequences suggest that their respective
102 AP or SLIGRL-NH2, corresponding to the PAR-2 tethered ligand) stimulated both an 125I- efflux inhibit
103 d a decapeptide mimicking the Cat-S-revealed tethered ligand-stimulated PAR2 coupling to Galphas and
106 Proteolytic cleavage of PAR(2) reveals a tethered ligand that activates PAR(2) and two major down
107 the extracellular domain of PAR1 generates a tethered ligand that activates PAR1 in an unusual intram
108 trypsin within the NH2-terminus, exposing a tethered ligand that binds and activates the receptor.
109 a new N-terminal domain that functions as a tethered ligand that binds intermolecularly to activate
110 their amino-terminal exodomains to unmask a tethered ligand that binds intramolecularly to the body
111 ls the receptor-activating motif, termed the tethered ligand that binds intramolecularly to the recep
112 )) at Arg(36) downward arrowSer(37) reveal a tethered ligand that binds to the cleaved receptor.
113 ough cleavage of the N-terminus, unmasking a tethered ligand that can then interact with the receptor
115 2) at R(36) downward arrowS(37) and reveal a tethered ligand that excites nociceptors, causing neurog
116 ctivating peptide (AP), corresponding to the tethered ligand that is exposed upon trypsin cleavage, a
117 major product of III-beta1a processing is a tethered ligand that may act as a cell surface signaling
118 ical site, exposing a previously undescribed tethered ligand that triggers biased G-protein agonism a
119 noncanonical sites, which result in distinct tethered ligands that activate G-protein signaling pathw
120 AR1 signaling and we describe a novel set of tethered ligands that are distinct from the classical te
121 ivated receptors (PARs) to expose N-terminal tethered ligands that bind and activate the cleaved rece
124 gamma-thrombin, which does not stimulate the tethered ligand thrombin receptor and caused little or n
127 volving sequestration or modification of the tethered ligand to prevent or terminate its function.
128 or peptidomimetics can mimic binding of the tethered ligand to stimulate signaling without the nonsp
132 hereby exposing a new N-terminal sequence, a tethered ligand, which initiates a cascade of molecular
136 s retained efficacy against both soluble and tethered ligands with lower cLogP values and an increase