ライフサイエンスコーパス: phospholipid binding

1 in-labeled domains retained Ca(2+)-activated phospholipid binding.

2 GIVAPLA2 above and beyond its Ca2+-dependent phospholipid binding.

3 methionine 173, are also essential for tight phospholipid binding.

4 may be partially redundant in Ca2+-dependent phospholipid binding.

5 ation is synergistically coupled to membrane phospholipid binding.

6 main has been implicated in both peptide and phospholipid binding.

7 n and demonstrated reduced calcium-sensitive phospholipid binding.

8 d type II Ca2+ binding sites are involved in phospholipid binding.

9 ose of other ARF GEPs in regions involved in phospholipid binding.

10 n homology domain mutants exhibited enhanced phospholipid binding.

11 shown by mutagenesis to be also involved in phospholipid binding.

12 of hydrophobic side chains may contribute to phospholipid binding.

13 ll three Ca2+-binding sites are required for phospholipid binding.

14 Galpha(q/11) binding, Gbetagamma binding, or phospholipid binding.

15 he omega-loop that mediates Ca(2+)-dependent phospholipid binding.

16 te from novel ionic interactions and revised phospholipid binding.

17 2A domain becomes the primary determinant of phospholipid binding.

18 tein module which mediates calcium-dependent phospholipid binding.

19 C(2)B domains that exhibit Ca(2+)-dependent phospholipid binding.

20 actions in addition to its conserved role in phospholipid binding.

21 affect SNARE complex binding, but decreases phospholipid binding.

22 tion were analyzed for (1) calcium-dependent phospholipid binding, (2) calcium-dependent binding to s

23 Mutation in the PX domain that abolished its phospholipid binding ability not only disrupted CISK loc

24 curs partially through the calcium-dependent phospholipid-binding ability of annexin II since some an

25 Moreover, we show that both phospholipid-binding activities are essential for AtSfh1

26 igher-order multimers, and Ca(2+)-dependent, phospholipid binding activity with preference for negati

27 erine liposomes, ApB displays no discernible phospholipid binding activity.

28 s, however, suggests that ISPs do not retain phospholipid binding activity.

29 observation, biochemical assays revealed no phospholipid binding activity.

30 -1432, and Lys-1434, are responsible for the phospholipid binding affinity.

31 a or APC via the omega-loop, we predict that phospholipid binding also induces the functional Ca4 con

32 The phospholipid binding and aggregation activities of the S

33 l or core domain that confers Ca2+-dependent phospholipid binding and an N-terminal domain that is va

34 truncated complex lacks residues involved in phospholipid binding and denatures at a lower temperatur

35 Phospholipid binding and enzymatic activity of these mut

36 compared the role of basic residues in Ca2+/phospholipid binding and in release.

37 cid (Gla) domain of factor IX is involved in phospholipid binding and is required for activation by f

38 by the extreme NH2 terminus of GRK5 mediates phospholipid binding and is required for optimal recepto

39 The specificity of phospholipid binding and its potential regulation are in

40 ough synaptotagmin-SNARE interactions, while phospholipid binding and oligomerization trigger rapid f

41 e repeats did not effectively participate in phospholipid binding and organization.

42 e chains mutated in this study contribute to phospholipid binding and participate directly in intermo

43 g(23) is a major determinant for interfacial phospholipid binding and participates in an intermolecul

44 ation and also exhibited a partial defect in phospholipid binding and phospholipid-stimulated autopho

45 roles for SMP domains in ERMES assembly and phospholipid binding and suggest a structure-based mecha

46 find that PKC phosphorylation disrupts both phospholipid binding and the gamma-Pcdh inhibition of (b

47 , was proposed to function by Ca2+-dependent phospholipid binding and/or by Ca2+-dependent soluble N-

48 rophobic spikes are constituents of both the phospholipid-binding and vWf-binding motifs.

49 an explanation for how receptor recognition, phospholipid binding, and kinase activation are intimate

50 d patients reduces the level of annexin-V, a phospholipid-binding anticoagulant protein, on cultured

51 scopy, isothermal titration calorimetry, and phospholipid binding assay.

52 Phospholipid binding assays were performed with a commer

53 In addition, phospholipid-binding assays suggest that alpha-14 giardi

54 C(2) domain are capable of Ca(2+)-dependent phospholipid binding at micromolar concentrations of fre

55 ciated with mutations at the Met2199/Phe2200 phospholipid binding beta-hairpin (group AB MAbs) and at

56 l T3SS; in contrast, a predicted periplasmic phospholipid binding (BON) domain and a putative peripla

57 acts by a downstream mechanism that requires phospholipid binding by alpha-synuclein.

58 One of the key questions is whether phospholipid binding by C(2)-domains is primarily govern

59 Together these data indicate that phospholipid binding by the C(2)A-domain, although trigg

60 ed the mechanisms involved in Ca2+-dependent phospholipid binding by the C2A-domain of synaptotagmin

61 ed intrinsic Ca2+ binding and Ca2+-dependent phospholipid binding by the isolated C2A domain.

62 previous data showing that Ca(2+)-dependent phospholipid binding by the synaptotagmin C(2)A-domain i

63 Consequently, calcium-triggered phospholipid binding by this artificially dimerized C2A

64 activity is regulated by its Ca2+-dependent phospholipid binding C2 domain.

65 They contain two calcium-dependent phospholipid binding C2 domains at the amino terminus an

66 presence of two N-terminal calcium-dependent phospholipid binding C2 domains, a conserved GAP related

67 cloned plant PLDs contain a Ca(2+)-dependent phospholipid-binding C2 domain and require Ca(2+) for ac

68 and PLDbeta both contain a Ca(2+)-dependent phospholipid-binding C2 domain near their N termini.

69 mall proteins containing a calcium-dependent phospholipid-binding C2 domain.

70 erminus contains a regulatory Ca2+-dependent phospholipid-binding (C2) domain that is found in a numb

71 the free sterol; i.e., that in excess of the phospholipid binding capacity.

72 esting that domain interaction decreases the phospholipid-binding capacity of apoE4.

73 helical gate determines access to the Sec14p phospholipid binding cavity.

74 Second, the proticity profile along the phospholipid-binding cavity of Sec14p was characterized.

75 cate that aPL induced by immunization with a phospholipid-binding CMV peptide are pathogenic in vivo.

76 t advances in the recognition of the role of phospholipid-binding cofactors, primarily beta2GPI, as t

77 nd C2 domain of MCTP2 include a perfect Ca2+/phospholipid-binding consensus sequence.

78 rtant for APC cofactor function, but not for phospholipid binding, defines a novel function (other th

79 ecies arising from the loss of prothrombin's phospholipid binding domain (des F1 species).

80 two important structural domains in GRK5, a phospholipid binding domain (residues 552-562) and an au

81 ucture of EPCR alone and in complex with the phospholipid binding domain of protein C.

82 BON1 contains a Ca(2+)-dependent phospholipid-binding domain and is associated with the p

83 They have a Ca(2+) and phospholipid-binding domain consisting of two C2 domains

84 In contrast, mutation of the C2 phospholipid-binding domain had little effect on PTEN ac

85 membranes using a phosphorylation-dependent phospholipid-binding domain.

86 ive mutant results in destabilization of the phospholipid-binding domain.

87 yl-beta-D-glucopyranoside and represents the phospholipid-binding domain.

88 ion mutant of GAP1(m), in which the putative phospholipid-binding domains (C2A and C2B) have been rem

89 in modules that generally act as Ca(2+)- and phospholipid-binding domains and/or as protein-protein i

90 f1 requires both its ubiquitin-ligase and C2 phospholipid-binding domains, and involves K48- rather t

91 We show here that phospholipid binding drives important conformational rea

92 Despite the importance of phospholipid binding for Dbs function in vivo, we found

93 vel function (other than Ca(2+) coordination/phospholipid binding) for a Gla residue in vitamin K-dep

94 To investigate the structural basis of phospholipid binding further, GM2AP was cocrystallized w

95 By virtue of its phospholipid-binding FYVE domain, CARP-2 localized to en

96 domain that has been shown to play a role in phospholipid binding in other myosin-I proteins.

97 ic residues in the region that overlays with phospholipid binding in related pleckstrin homology doma

98 ace and conformational changes upon a single phospholipid binding in the absence of a lipid surface.

99 t point mutations in the pocket that abolish phospholipid binding in vitro ablate the ability of Dock

100 pids, and mutations that reduce or eliminate phospholipid binding in vitro inactivate Spo20p in vivo.

101 loops of the PH domain resulted in impaired phospholipid binding in vitro, yet full guanine nucleoti

102 residues within the PTB domain critical for phospholipid binding in vitro.

103 uscular dystrophy in which calcium-regulated phospholipid binding is abnormal, leading to defective m

104 Although phospholipid binding is central for the normal functions

105 2)-domain proteins, the precise mechanism of phospholipid binding is unclear.

106 Phospholipid binding led to changes in chemical shifts o

107 ed by the Akt proto-oncogene is activated by phospholipid binding, membrane translocation and phospho

108 The complex phospholipid binding mode of synaptotagmins may be impor

109 Previously, we reported on multiple distinct phospholipid binding modes of alphaS with slow binding k

110 eal clear distinctions in the Ca2+-dependent phospholipid binding modes of the synaptotagmin 1 C2 dom

111 sults provide evidence for multiple distinct phospholipid-binding modes of alphaS.

112 , and a C2 domain, which is a Ca2+-triggered phospholipid-binding module.

113 Phospholipid-binding modules such as PH, C1, and C2 doma

114 2 domains of MCTPs actually function as Ca2+/phospholipid-binding modules, we analyzed their Ca2+ and

115 regions and represent Ca(2+)-binding but not phospholipid-binding modules.

116 horylates a serine residue situated within a phospholipid binding motif at the shared gamma-Pcdh C te

117 ivity to the voltage sensor is mediated by a phospholipid-binding motif at the interface between volt

118 for vegetal cortical targeting, including a phospholipid-binding motif near the N-terminus.

119 vacuolar protein-sorting (Vps)5p, contain a phospholipid-binding motif termed the phox homology (PX)

120 de a structural basis for the more efficient phospholipid binding of lactadherin as compared with fac

121 eckstrin homology fold often associated with phospholipid binding or protein-protein interactions.

122 en cells of PL/J mice immunized with TIFI, a phospholipid-binding peptide spanning Thr(101)-Thr(120)

123 une disease require the participation of the phospholipid binding plasma protein beta2 glycoprotein I

124 rombin and beta2-glycoprotein I beta2GPI), a phospholipid-binding plasma protein whose physiological

125 Beta2-glycoprotein I is an anionic phospholipid-binding plasma protein, and the phospholipi

126 The data further suggest that the Sec14p phospholipid binding pocket provides a polarity gradient

127 FYF motif, located in the inner walls of the phospholipid-binding pocket of the ITK PH domain, are co

128 Comparison of the phospholipid binding pockets in E2 and E1 conformations

129 Simultaneous occupancy of the two phospholipid-binding pockets radically increases membran

130 As a result, Ca(2+)-dependent phospholipid binding proceeds by a multimodal mechanism

131 with the patient mutations and examined the phospholipid binding profile of pleckstrin homology doma

132 We characterized the phorbol ester and phospholipid binding properties of a glutathione S-trans

133 Here, we report the phospholipid binding properties of the disease variants,

134 ombinant protein exhibited calcium-dependent phospholipid binding properties similar to those of Para

135 -binding modules, we analyzed their Ca2+ and phospholipid binding properties.

136 Importantly, we confirm that the reported phospholipid-binding properties of AVR3a are mediated by

137 ounted for, at least in part, by the unusual phospholipid-binding properties of its double C2A/B-doma

138 sional structure of alpha-14 giardin and its phospholipid-binding properties.

139 AnxA2 is a Ca(2+)-dependent phospholipid binding protein and serves as an extracellu

140 In the presence of apolipoprotein C-II, a phospholipid binding protein, a series of lipid molecule

141 murine macrophages deficient in the membrane phospholipid binding protein, annexin A2 (ANXA2), we obs

142 face tissue factor pathway inhibitor and the phospholipid binding protein, annexin V.

143 dies, those against Beta 2 glycoprotein I, a phospholipid binding protein, is now being recognized.

144 These included fatty acid binding protein, phospholipid binding protein, phospholipid synthesis pro

145 Annexin V is a Ca2+-dependent phospholipid binding protein.

146 st beta2-glycoprotein I (beta2GPI), a plasma phospholipid binding protein.

147 combined with MS, we discovered that calcium phospholipid-binding protein (CPBP), a homologue of elon

148 protein I (beta(2)GPI) is an abundant plasma phospholipid-binding protein and an autoantigen in the a

149 tor Sox9 and suppression of the proapoptotic phospholipid-binding protein Annexin A1 that link early

150 endothelial cells via the calcium-regulated phospholipid-binding protein annexin II, an interaction

151 In the present study, the Ca(2+)-sensitive phospholipid-binding protein annexin VI was purified fro

152 cell surface, followed by deposition of the phospholipid-binding protein annexin-1 and then transglu

153 Annexin 1 (AnxA1) is a multifunctional phospholipid-binding protein associated with the develop

154 calpactin I, a heterotetrameric, Ca(2+)- and phospholipid-binding protein complex that regulates memb

155 amer (AII(t)) is a member of the Ca(2+)- and phospholipid-binding protein family and is implicated in

156 Annexin XI, a member of the Ca2+-dependent, phospholipid-binding protein family, is an example of su

157 amer (AIIt), a member of the Ca2+- dependent phospholipid-binding protein family.

158 Synaptotagmin, an abundant calcium- and phospholipid-binding protein of synaptic vesicles, has b

159 ter from synaptic vesicles requires the Ca2+/phospholipid-binding protein synaptotagmin 1.

160 Annexin A2 is a phospholipid-binding protein that forms a heterotetramer

161 Annexin A1 is an intracellular calcium/phospholipid-binding protein that is involved in membran

162 ive factor attachment protein receptor)- and phospholipid-binding protein that localizes to and prime

163 Levels of annexin V, a phospholipid-binding protein with potent anticoagulant a

164 AnxA2) is a multifunctional Ca(2+)-dependent phospholipid-binding protein, and its overexpression is

165 Here, we report that the phospholipid-binding protein, annexin A2 (ANXA2) functio

166 he membrane of human macrophages through the phospholipid-binding protein, annexin II.

167 n this study we identify copine-I, a calcium phospholipid-binding protein, as a novel repressor that

168 Annexin II (AXII), a calcium-dependent phospholipid-binding protein, has been recently found to

169 Annexin A2, a calcium-dependent phospholipid-binding protein, is abundantly expressed in

170 Dysferlin, a type-II transmembrane phospholipid-binding protein, is hypothesized to regulat

171 Annexin A2 (AnxA2), a Ca(2+)-dependent phospholipid-binding protein, is known to associate with

172 Annexin A4 (AnxA4), a Ca(2+)- and phospholipid-binding protein, is up-regulated in the hum

173 Annexin V, a calcium-dependent anionic-phospholipid-binding protein, was expressed and isolated

174 Synexin, a Ca(2+)- and phospholipid-binding protein, was one of the proteins id

175 s syndrome are directed against a variety of phospholipid binding proteins of which beta2-glycoprotei

176 ent specific manner but not to other anionic phospholipid binding proteins such as beta2-glycoprotein

177 newly identified class of calcium-dependent, phospholipid binding proteins that are present in a wide

178 ns included extracellular matrix components, phospholipid binding proteins, enzymes, and cytoskeletal

179 holipids, lipid-protein adducts, and certain phospholipid binding proteins.

180 xins comprise a multigene family of Ca2+ and phospholipid- binding proteins.

181 ersistent presence of autoantibodies against phospholipid-binding proteins (aPLs), such as beta2 glyc

182 e, monoclonal antibodies to GP Ib or anionic phospholipid-binding proteins (beta2-glycoprotein I or a

183 ngs to a large family of calcium-binding and phospholipid-binding proteins and may act as an endogeno

184 hogenesis, and differentiation; calcium- and phospholipid-binding proteins and signal transducers; an

185 We revealed that the two phospholipid-binding proteins annexin A2 and A5 are, bes

186 pines are a novel group of Ca(2+)-dependent, phospholipid-binding proteins first isolated from Parame

187 use antibodies to phospholipids (aPA) and/or phospholipid-binding proteins have been associated with

188 Copines are calcium-responsive, phospholipid-binding proteins involved in cellular signa

189 Annexins are a family of calcium- and phospholipid-binding proteins involved with numerous cel

190 aptotagmins are synaptic vesicle-associated, phospholipid-binding proteins most commonly associated w

191 mined for the presence of calcium-dependent, phospholipid-binding proteins of the annexin class.

192 dely distributed class of calcium-dependent, phospholipid-binding proteins of undetermined biological

193 Annexins (ANXs) are a family of calcium- and phospholipid-binding proteins that have been implicated

194 ng processes in ciliates, calcium-dependent, phospholipid-binding proteins were isolated from extract

195 The majority of APLAs are directed against phospholipid-binding proteins, particularly beta(2)-glyc

196 These Abs are primarily directed against phospholipid-binding proteins, particularly beta(2)GPI,

197 Annexins are a large family of intracellular phospholipid-binding proteins, yet several extracellular

198 I, a member of a family of Ca(2+)-dependent phospholipid-binding proteins.

199 s, cytoskeletal proteins, phospholipids, and phospholipid-binding proteins.

200 he annexins are a family of Ca(2+)-dependent phospholipid-binding proteins.

201 While cellular acidic phospholipid-binding proteins/domains, such as the PI(4,

202 showed that O-phospho-l-serine binds to the phospholipid-binding region in the C2 domain, and this i

203 ng site consists of a conserved non-specific phospholipid-binding region in the TMD and a specific ph

204 in all vinculins and is present in an acidic phospholipid-binding region of alpha-catenin, is distinc

205 de 296 but does not contain the lysine-rich, phospholipid-binding region.

206 modimers, which are asymmetric, we show that phospholipid binding results in a domain-swapped symmetr

207 like fragment with a specialized protein- or phospholipid-binding role for muscle membrane repair.

208 clearance assay, we show that the identified phospholipid binding sequences all map to the surface of

209 beta2-Glycoprotein I (beta2GPI), a phospholipid-binding serum protein, is involved in aPL b

210 te that aPL induced by immunization with the phospholipid binding site of beta2GPI are thrombogenic a

211 rovide the first molecular insights into the phospholipid binding site of calreticulin as a key ancho

212 Although the fatty acid/phospholipid binding site structurally overlaps that for

213 To characterize further this phospholipid binding site, we have used hydrophobic phot

214 ed recognize an epitope distinct from the C1 phospholipid binding site.

215 ite separate from the type II Ca2+-dependent phospholipid binding site.

216 ndent of PtdIns(3,5)P(2), as mutation of the phospholipid-binding site in Atg18 does not prevent vacu

217 that TgISPs have functionally repurposed the phospholipid-binding site likely to coordinate protein p

218 The structure reveals a putative phospholipid-binding site near the N terminus of GRK6 an

219 which shares structural similarity with the phospholipid-binding site of beta(2)-glycoprotein I (bet

220 whether aPL induced by immunization with the phospholipid-binding site of beta2GPI are thrombogenic a

221 main of human beta2GPI, which represents the phospholipid-binding site of beta2GPI.

222 en-residue peptide derived from the inositol-phospholipid-binding site of gelsolin.

223 inhibits prothrombin activation by blocking phospholipid binding sites for the prothrombinase comple

224 2)), which has been shown to contain several phospholipid binding sites that dramatically affect acti

225 d is bound to low-affinity inner sarcolemmal phospholipid binding sites within the cleft.

226 orcine, murine, and canine fVIII at proposed phospholipid binding sites, were expressed.

227 sonance experiments, revealed two classes of phospholipid-binding sites having K(d) values of 4.8 and

228 4 in the absence of ligand exposes potential phospholipid-binding sites that are positioned for membr

229 By replacing lysine residues at proposed phospholipid-binding sites with glutamines, the two site

230 d from each other both on the basis of their phospholipid binding specificities and by their substant

231 ned phospholipid composition to quantify the phospholipid binding specificities of these seven clotti

232 The phospholipid-binding specificities of C(2) domains, wide

233 rs onto the synaptotagmin 1 C(2)A domain the phospholipid binding specificity of the cPLA(2) C(2) dom

234 and likely represents a third type of acidic phospholipid-binding structure.

235 erize the Arabidopsis (Arabidopsis thaliana) phospholipid binding Synaptotagmin1 (SYT1) as a plant or

236 or phosphorylation, likely via disruption of phospholipid binding, that was reversed by Gbetagamma.

237 In biological studies, Mg(2+) enhanced phospholipid binding to FVIIa and APC at physiological C

238 ransmitter release involves Ca(2+)-dependent phospholipid binding to its two C(2) domains, but this a

239 co-activate Ca2+-dependent and -independent phospholipid binding to synaptotagmin 1, but the effects

240 However, it is unclear how phospholipid binding to synaptotagmin is coupled to SNAR

241 a very high membrane affinity and dominates phospholipid binding to Syt7 in the presence or absence

242 Phospholipid binding to the C1 domain triggers the coope

243 Ca2+-dependent phospholipid binding to the C2A and C2B domains of synap

244 rent from that reported for photoactivatable phospholipid binding to the nAChR.

245 Phospholipid binding to this site is probably mediated b

246 the secretory granule Atp8a1 is activated by phospholipids binding to a specific site whose propertie

247 veral recently reported examples of inositol phospholipids binding to pleckstrin homology (PH) domain

248 e properties: charge-based binding to acidic phospholipids, binding to plasma membrane but not DCV me

249 operate in a common activity, Ca2+-dependent phospholipid binding, to trigger neurotransmitter releas

250 inding by native synaptotagmin-1, but leaves phospholipid binding unchanged.

251 erlin, bound 50% phosphatidylserine and that phospholipid binding was regulated by calcium concentrat

252 etely inactive in factor VIIIa inactivation; phospholipid binding was, however, normal.

253 y the site on Factor IX that is required for phospholipid binding, we have determined the three-dimen

254 No decreases in exchange due to phospholipid binding were seen in the ankyrin repeat dom

255 agmins IV and XI exhibited no Ca2+-dependent phospholipid binding, whereas mutant C2A-domains bound p

256 tructure identifies residues responsible for phospholipid binding, which when mutated in cells impair