ライフサイエンスコーパス: phospholipid binding

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

2 affect SNARE complex binding, but decreases phospholipid binding.

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

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

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

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

7 ation is synergistically coupled to membrane phospholipid binding.

8 n homology domain mutants exhibited enhanced phospholipid binding.

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

10 n and demonstrated reduced calcium-sensitive phospholipid binding.

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

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

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

14 of hydrophobic side chains may contribute to phospholipid binding.

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

16 mino acids within the AHD were necessary for phospholipid binding.

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

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

19 te from novel ionic interactions and revised phospholipid binding.

20 2A domain becomes the primary determinant of phospholipid binding.

21 tein module which mediates calcium-dependent phospholipid binding.

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

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

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

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

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

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

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

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

30 observation, biochemical assays revealed no phospholipid binding activity.

31 We demonstrate that sulfide regulates ATG18a phospholipid-binding activity by reversible persulfidati

32 -1432, and Lys-1434, are responsible for the phospholipid binding affinity.

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

34 The phospholipid binding and aggregation activities of the S

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

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

37 Phospholipid binding and enzymatic activity of these mut

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

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

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

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

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

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

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

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

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

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

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

49 made in understanding mechanisms underlying phospholipid binding and transport across the membrane d

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

51 w that the N-terminal domain of proSP-B is a phospholipid-binding and -transfer protein whose activit

52 ed for virus infection, whereas the inositol phospholipid-binding and F-actin-binding domains were es

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

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

55 rated that a member of the Ca(2+) -dependent phospholipid binding annexins, Annexin A6 (AnxA6), regul

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

57 at domain of alpha-Syn, which interfere with phospholipid binding, are ineffective in enhancing CME.

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

59 Phospholipid binding assays were performed with a commer

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

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

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

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

64 Here, we show that the Ca(2+)-responsive phospholipid-binding BONZAI (BON) proteins are critical

65 rib does not require palmitoylation or polar phospholipid binding but instead an independent cortical

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

90 sized that peptide mimetics derived from the phospholipid binding domain of Myristoylated alanine-ric

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

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

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

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

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

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

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

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

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

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

101 We show here that phospholipid binding drives important conformational rea

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

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

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

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

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

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

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

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

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

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

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

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

114 Although phospholipid binding is central for the normal functions

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

116 Phospholipid binding led to changes in chemical shifts o

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

118 The complex phospholipid binding mode of synaptotagmins may be impor

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

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

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

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

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

124 2 domains of MCTPs actually function as Ca2+/phospholipid-binding modules, we analyzed their Ca2+ and

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

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

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

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

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

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

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

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

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

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

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

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

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

138 chanism that functions to open and close the phospholipid-binding pocket.

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

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

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

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

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

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

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

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

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

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

149 PI) is an abundant plasma protein displaying phospholipid-binding properties.

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

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

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

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

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

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

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

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

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

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

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

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

162 nature consistent with adipogenesis, and the phospholipid-binding protein annexin A3 (AnxA3), a negat

163 t cancer cells we show that the Ca(2+) - and phospholipid-binding protein annexin A7 is part of the p

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

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

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

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

168 Annexin A5 (AnxA5) is a Ca(2+)-dependent phospholipid-binding protein associated with the regulat

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

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

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

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

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

174 Copine-6 is a calcium-sensitive phospholipid-binding protein of the evolutionarily conse

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

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

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

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

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

180 Annexin A8 (AnxA8), a calcium-dependent phospholipid-binding protein, and canonical Wnt signalli

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

197 hat recognize cell surface phospholipids and phospholipid binding proteins.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

226 terminus that are linked to deafness disrupt phospholipid binding, sensitize the channel to PIP(2) de

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

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

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

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

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

232 leaflet site, and structural changes in the phospholipid binding site unique to the open-channel.

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

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

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

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

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

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

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

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

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

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

243 ional pores by interacting with Hla near the phospholipid-binding site.

244 requisite for pore assembly as mutation of a phospholipids-binding site in CelTOS resulted in loss of

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

246 Comparison of cholesterol poses with phospholipid binding sites suggests that binding of chol

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

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

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

250 membrane translocation, distinct from known phospholipid binding sites.

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

252 4 in the absence of ligand exposes potential phospholipid-binding sites that are positioned for membr

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

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

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

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

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

258 tivity analyses showed that permeability and phospholipid binding strongly influenced the elimination

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

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

261 (Syt1) is an integral membrane protein whose phospholipid-binding tandem C2 domains, C2A and C2B, act

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

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

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

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

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

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

268 Phospholipid binding to the C1 domain triggers the coope

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

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

271 Phospholipid binding to this site is probably mediated b

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

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

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

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

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

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

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

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

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

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

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