ライフサイエンスコーパス: aspartate residue

1 es induced by phosphorylation of a conserved aspartate residue.

2 ognate sensor histidine kinase to a specific aspartate residue.

3 orylated by the sensor kinase at a conserved aspartate residue.

4 been proteolytically cleaved at an internal aspartate residue.

5 specificity for peptidyl sequences with a P1 aspartate residue.

6 p, where FGFR-1, but not FGFR-4, bears a key aspartate residue.

7 peptide to Ld is dependent primarily on a P8 aspartate residue.

8 version of the translated methionine into an aspartate residue.

9 equence, was mutated to either an alanine or aspartate residue.

10 f the kinase and contains a phosphorylatable aspartate residue.

11 sequences, including a completely conserved aspartate residue.

12 rtance of a proposed lanthanide-coordinating aspartate residue.

13 preQ(1)-recognition site by pushing back an aspartate residue.

14 marily directs PAR modification to glutamate/aspartate residues.

15 posed of 40% alanine, 36% histidine, and 11% aspartate residues.

16 Thr-174 were substituted with phosphomimetic aspartate residues.

17 x thioethers linking the beta carbons of six aspartate residues.

18 ase shows that the active site contains four aspartate residues.

19 dged by a water (hydroxide) molecule and two aspartate residues.

20 cleavage of multiple substrates at specific aspartate residues.

21 cysteine protease by processing at internal aspartate residues.

22 proteases, cleave their substrates following aspartate residues.

23 geminal fluorine atoms, and the active-site aspartate residues.

24 proteases, cleave their substrates following aspartate residues.

25 phosphorylation sites with either alanine or aspartate residues.

26 rodimeric enzymes after cleavage at specific aspartate residues.

27 city for cleaving synthetic substrates after aspartate residues.

28 ding a series of critical negatively charged aspartate residues.

29 ive site of each monomer involving conserved aspartate residues.

30 y conserved negatively charged glutamate and aspartate residues.

31 Replacement of aspartate residue 541 by alanine (D541A) in the pore of

32 ve virus containing an integrase mutation at aspartate residue 64.

33 ge of the amyloid precursor protein (APP) at aspartate residue 664 by caspases may play a key role in

34 ither internal tandem duplications (ITDs) or aspartate residue 835 (D835) point mutations, are presen

35 l data, lithium binds to site II, coupled to aspartate residues 84, 87, and 212.

36 r-filled pocket surrounding an nNOS-specific aspartate residue (absent in eNOS).

37 en directly attacks the phosphorus, with the aspartate residue acting as a H-bond acceptor.

38 One of the beta1 subunits possesses an aspartate residue and N-glycosylation sites hitherto sho

39 Three aspartate residues and a glutamate residue: E424, D498,

40 Mapping these two aspartate residues and a highly conserved lysine onto th

41 g domains and four 'U-motifs' with conserved aspartate residues and a QxxRW motif that are essential

42 d reveals that the active site comprises two aspartate residues and an arginine residue.

43 a factor family revealed a conserved pair of aspartate residues and an arginine that are important fo

44 o the transmembrane domains contain multiple aspartate residues and are found to play an important ro

45 , that binds at least two Ca2+ ions via five aspartate residues and is conserved in most C2-domains.

46 domain, named after conserved histidine and aspartate residues; and two C-terminal ACT domains, name

47 oordinated by two histidine residues and one aspartate residue approximately 14 angstroms into the li

48 e wild-type periplasmic domain structure two aspartate residues are bound per dimer, but with differe

49 Corresponding aspartate residues are completely conserved throughout t

50 results indicate that the two transmembrane aspartate residues are critical for both presenilin-1 en

51 mical studies, suggests that the active site aspartate residues are in proximity to the S1/S1' bindin

52 Aspartate residues are involved in coordination of the n

53 Four aspartate residues are located at the bottom of the cavi

54 sequence SxHxxGxAxD, in which histidine and aspartate residues are putative zinc ligands, identified

55 ive sodium ion bound to the highly conserved aspartate residue Asp(2.50).

56 osis in S2 cells, DIAP1 is cleaved following aspartate residue Asp-20 by the effector caspase DrICE.

57 Aspartate residues Asp-16* and Asp-271 individually prov

58 active site variants identified two central aspartate residues Asp-99 and Asp-219 as essential for c

59 ge to one side-chain oxygen atom of a buried aspartate residue (Asp(89)), whereas the other oxygen is

60 distal side of the heme molecule, a flexible aspartate residue (Asp-168) plays a key role in catalysi

61 49, and phosphoryl groups are transferred to aspartate residues (Asp-52 and Asp-220) in the two recei

62 Two conserved aspartate residues, Asp-163 and Asp-164, are essential f

63 has lost direct ligation to the active-site aspartate residue, Asp127.

64 I manganese stabilizing protein, contains an aspartate residue [Asp157 (spinach numbering)], which is

65 that the protonation states of two catalytic aspartate residues, Asp25 and Asp125, strongly influence

66 An essential calcium-binding aspartate residue, Asp307Ala, was disrupted by a c.920A>

67 d by multiple caspases at a highly conserved aspartate residue (Asp421) in its C terminus in vitro an

68 forms a salt bridge with a conserved, buried aspartate residue (Asp51), which suggests that the amino

69 amino-terminus (Pro1) and a highly conserved aspartate residue (Asp51).

70 on to the vital hydrogen bonding between the aspartate residue (Asp53) of beta2M and methionine (Met9

71 corporated into peptidoglycan.Mutation of an aspartate residue (Asp59) of His-tagged VanXY(C) corresp

72 Mutation of a conserved aspartate residue associated with human disease (MPS-4-D

73 aled the electronic quenching dynamics by an aspartate residue at a hydrogen bond distance in 275-615

74 otein, but not to a mutant form in which the aspartate residue at amino acid position 54 has been cha

75 ization of a mutant RecA protein wherein the aspartate residue at position 100 within the ATP binding

76 An aspartate residue at position 102 (position 89 in the Es

77 A variant of t-PA containing an aspartate residue at position 144, for example, exhibite

78 f ORF57 in the cytoplasm by caspase-7 at the aspartate residue at position 33 from the N terminus.

79 psbd41 contains a buried aspartate residue at position 34 that may provide stabil

80 nt, RR06(D51A), with a point mutation in the aspartate residue at position 51 (a predicted major phos

81 rifugation, we identified a highly conserved aspartate residue at the boundary of the M3-M4 loop and

82 imer interface; (2) KGPDC and OMPDC share an aspartate residue at the end of the first beta-strand an

83 mutagenesis, a NodWD70N mutant in which the aspartate residue at the proposed phosphorylation site w

84 y in other DFRs, whereas MtDFR2 contained an aspartate residue at the same site and was only marginal

85 ly specific requirement for an asparagine or aspartate residue at this position may indicate a key ro

86 enrichment, confirming the importance of an aspartate residue at this site.

87 SLRPs since it possesses a unique stretch of aspartate residues at its N terminus.

88 We found that both glutamate and aspartate residues at position 64 are efficient proton s

89 -site cysteine of the CED-3 protease and the aspartate residues at sites of processing of the CED-3 p

90 As the pH decreases, the aspartate residue becomes protonated and deltadeltaG(o)

91 creased when Asn-106 was substituted with an aspartate residue, but decreased in mutants with alanine

92 Substitution of the aspartate residue by alanine or arginine results in sign

93 lization resulting from the partially buried aspartate residue cannot be offset by ion pair formation

94 ins and a cluster of conserved histidine and aspartate residues capable of binding two metal atoms in

95 gment, which contains numerous glutamate and aspartate residues, caused a 55% decrease in trans-activ

96 ains, based on rapid chemical proteolysis at aspartate residues combined with immunoprecipitation and

97 Our studies suggest that this aspartate residue contributes to a selectivity filter ne

98 A magnesium ion bound by these aspartate residues could therefore mediate the DNA cleav

99 Using site-directed mutagenesis, two aspartate residues crucial for nucleic acid synthesis an

100 P) with Asp-to-Asn substitution at the first aspartate residue (D117N) of this motif could not be gen

101 contained mutations in close proximity to an aspartate residue (D121) believed to form part of the ca

102 mutations were made at two species-invariant aspartate residues, D174 and D231.

103 re of the postfusion E1 trimer shows that an aspartate residue, D188, is positioned in the central co

104 Recently, a conserved aspartate residue (D303, or D46) of hedgehog was identif

105 the present study, we show that a conserved aspartate residue, D46 of the Hh autoprocessing domain,

106 A conserved active-site aspartate residue, D46, plays a key catalytic role in Hh

107 Here, we substituted three aspartate residues (D4938, D4945, D4953) with asparagine

108 The block is mediated by a cytosolic aspartate residue, D633, situated between the terminatio

109 The coiled coil contains a rare aspartate residue (D69) in the normally hydrophobic d po

110 K+ channel crystal structure, the equivalent aspartate residue (D80) does not directly interact with

111 A highly conserved aspartate residue (D89) that is near the agonist binding

112 All three receptors contain a conserved aspartate residue (D98) at the extracellular boundary of

113 Mutation of S368 and S372 to a phosphomimic aspartate residue decreases the association of GGA3 with

114 , whereas their conversion to phosphomimetic aspartate residues decreases cell migration.

115 in enzyme activity, suggesting that the two aspartate residues did not play a pivotal role in cataly

116 The active sites of FBPAs contain an aspartate residue equivalent to Asp255 of glFBPA, wherea

117 The GT-C motif contains two aspartate residues essential for function in the DDX mot

118 e studies identified conserved histidine and aspartate residues essential for the catalytic activity

119 onversion are modulated by protonation of an aspartate residue, establishing the power of MD & MSMs i

120 screening the electrostatic effects that the aspartate residue exerts on the nearby PIP2-interacting

121 iation constant)-perturbed pair of conserved aspartate residues explains the pH dependence of this tr

122 ed by site-directed mutagenesis of three key aspartate residues flanking the conserved C93 which were

123 to phytaspases hydrolyzed prosystemin at two aspartate residues flanking the systemin sequence.

124 Such pathways utilize two histidine and two aspartate residues for signal transduction.

125 The side chains of histidine and aspartate residues form a hydrogen bond in the active si

126 idine residues from one molecule and another aspartate residue from the next molecule, thus forming a

127 y of the YMDD loop and prevent the catalytic aspartate residues from adopting their metal-binding con

128 sium ion surrounded by four highly conserved aspartate residues from helices TM2 and TM3.

129 An aspartate residue, from the CDR3 loop of the antibody he

130 Four glutamate/aspartate residues (Glu151, Glu161, Glu169, and Asp170)

131 erved sequence contains adjacent glycine and aspartate residues (Gly226 and Asp227).

132 table in a mutant RecB(N)protein in which an aspartate residue has been changed to alanine.

133 lobin; the results indicate that none of the aspartate residues has a strongly depressed pKa in N, as

134 ate in long-lived proteins, isomerization at aspartate residues has been shown to be extensive throug

135 eltaN or SleB-DeltaC, in which glutamate and aspartate residues have individually been changed to ala

136 ation of Ser471 to a phosphorylation mimetic aspartate residue impaired REL's transforming ability, e

137 ediates the conversion of a highly conserved aspartate residue in a cyclic substrate into a succinimi

138 nsmembrane domain with phosphorylation of an aspartate residue in a cytoplasmic domain.

139 active site and specific interactions of an aspartate residue in a polar loop and two phenylalanines

140 Phosphorylation of an aspartate residue in a receiver domain modulates the fun

141 appear to use a highly conserved active site aspartate residue in covalent catalysis.

142 sults suggest that the role of the conserved aspartate residue in loop 2/3 is to influence the topolo

143 highlights the critical role of a conserved aspartate residue in mediating the first-order hydrolyti

144 An invariant aspartate residue in MotB (Asp32 in the protein of E. co

145 in tRNA, and RimO, which modifies a specific aspartate residue in ribosomal protein S12.

146 An aspartate residue in the 8-9 loop that has no counterpar

147 , D1866Y, alters an evolutionarily conserved aspartate residue in the C-terminal cytoplasmic domain o

148 Together, the data indicate that the aspartate residue in the His ...

149 Phosphorylation of an aspartate residue in the N-terminal receiver domain of N

150 , coinciding with lack of specificity for an aspartate residue in the neutralization core of BnAb 2F5

151 bind xanthine nucleotides when the conserved aspartate residue in the NKXD motif was changed to aspar

152 The role of the conserved aspartate residue in the phosphorylation of AlgB was exa

153 e beta102 asparagine residue and the alpha94 aspartate residue in the Re state.

154 a the transfer of the phosphoryl group to an aspartate residue in the receiver domain of NodW.

155 When a specific aspartate residue in the receiver domain of NtrC is phos

156 Phosphorylation of an aspartate residue in the receiver domain, usually via ph

157 group that is subsequently transferred to an aspartate residue in the response regulator protein.

158 The aspartate residue in the second putative transmembrane s

159 ctivities are obliterated by mutation of the aspartate residue in the V2 peptide to alanine.

160 mutated protein, we found that the conserved aspartate residue in the Walker B motif plays a role in

161 lase activity for purine ribosides, while an aspartate residue in this position confers high activity

162 acid asparagine 285, which is replaced by an aspartate residue in type P(O) SadP, was required for bi

163 Site-directed mutagenesis of glutamate and aspartate residues in a conserved acidic patch (region 2

164 ative charge on Ser(982)-phosphate and three aspartate residues in a D986NDD custer in altering the s

165 hypothesize that spontaneous cyclization of aspartate residues in amyloidogenic proteins can serve a

166 e molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the fie

167 f all 20 glutamate residues and 24 of the 25 aspartate residues in CcP, one at a time, to lysine resi

168 within the lens wherein the isomerization of aspartate residues in crystallin peptides differentially

169 Three aspartate residues in Cx30 (Asp-50, Asp-172, and Asp-179

170 signal is insensitive to 13C-labeling of the aspartate residues in Hb, and cannot arise from protonat

171 Like other calcium channels, RyR has four aspartate residues in its GGGIGDE selectivity filter.

172 ects of mutating the conserved histidine and aspartate residues in methionine synthase have recently

173 f either of two conserved transmembrane (TM) aspartate residues in presenilin-1, Asp 257 (in TM6) and

174 Biochemical data reveal that conserved aspartate residues in PRORP1 are important for catalytic

175 Two aspartate residues in Sso7d (D16 and D35) and a single g

176 ed to study the protonation of histidine and aspartate residues in the acid-induced unfolding of reco

177 0' and Asp-179 and with nickel ions bound to aspartate residues in the acidic cluster.

178 variety of organisms, candidates for two key aspartate residues in the active site are identified at

179 TTQ biogenesis and to define novel roles for aspartate residues in the biogenesis of a protein-derive

180 show that mutating two of the Ca(2+)-binding aspartate residues in the C(2)B domain (D(416,418)N in D

181 ulation, with crucial roles for these single aspartate residues in the communication and functional i

182 ite-directed mutagenesis indicate that three aspartate residues in the conserved phosphoesterase moti

183 transport was observed when any of the five aspartate residues in the cytoplasmic loop were converte

184 Replacement of five aspartate residues in the e2 loop with lysyl residues si

185 utative active site motif with two conserved aspartate residues in the large (XseA/TM1768) subunit.

186 Three conserved aspartate residues in the largest subunit of multisubuni

187 Expression of a gp5 variant in which aspartate residues in the metal-binding site of the poly

188 Mutation to glutamate of each of the three aspartate residues in the Mg(2+)-binding aspartate-rich

189 were inversely proportional to the number of aspartate residues in the peptide.

190 The roles of the conserved aspartate residues in the phosphorylation of AlgR were a

191 n include PARPs, enzymes known to ribosylate aspartate residues in the process of poly(ADP-ribosyl)at

192 By mutating one of the critical aspartate residues in the proposed Ca(2+)-channel pore i

193 ycosylation profiling to show that conserved aspartate residues in the tetratricopeptide repeat (TPR)

194 rane environment near a ring of four charged aspartate residues in the trimer, namely Asp36, Asp38, A

195 Mutation of the lysine and aspartate residues in TMDs II and IV, respectively, can

196 horylation by mutation to positively charged aspartate residues increases basal transactivation.

197 nteractions in the vicinity of the catalytic aspartate residues, increasing the distance between them

198 ee distinct highly conserved arginine and/or aspartate residues inside or flanking these TM helices a

199 pha1(A322D)) introduces a negatively charged aspartate residue into the hydrophobic M3 transmembrane

200 An aspartate residue, invariant in all Pcls, acts as a surr

201 The D163-168A mutant modifies aspartate residues involved in Ca(2+) binding, whereas t

202 The histidine and aspartate residues involved in iron-binding in ETHE1, oc

203 dine nitrogen of the cofactor to a conserved aspartate residue is 2.6 A in AATase and 3.8 A in ACC sy

204 transduction systems, phosphorylation of an aspartate residue is coupled to a change from an inactiv

205 This essential catalytic aspartate residue is present in all PTPs and has structu

206 c triad, and in some enzymes the role of the aspartate residue is replaced by a main-chain carbonyl o

207 essential amino acid motif (DGXD) containing aspartate residues is located in the first transmembrane

208 This glutamate (or aspartate) residue is conserved in all members of the Ki

209 enriched in alternating lysine and glutamate/aspartate residues (KEKE motifs).

210 Engineered substitutions of this aspartate residue led to complete inactivation, which wa

211 contrast, substitutions with phosphomimetic aspartate residues led to a complete recovery of the tra

212 d naphthalene dioxygenase (NDO), a conserved aspartate residue lies between the mononuclear and Riesk

213 e effect on antigen binding of an isomerized aspartate residue located in the complementarity-determi

214 e I' band and the side-chain absorbances for aspartate residues located almost exclusively at the cal

215 protease, and mutation of either of the two aspartate residues located in adjacent transmembrane dom

216 t bridges formed by arginine, glutamate, and aspartate residues located in helices D, E, F, and G.

217 Six other aspartate residues located near the conserved Asp(142) w

218 the coordination of two calcium ions by five aspartate residues located on two separate loops.

219 Sixteen glutamate and aspartate residues, located in the first two thirds of t

220 t109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit in

221 ons all lend weight to the proposal that the aspartate residues mediate substrate binding by chelatio

222 The essential aspartate residue might be required for coordination of

223 tivity, whereas mutation to negative charged aspartate residues (mimicking receptor phosphorylation)

224 Phosphorylation at the conserved aspartate residue modulates the activity of the response

225 In particular, a conserved aspartate residue near the middle of M6 has been found t

226 alytic GGEEF motif, as well as the conserved aspartate residue of a CheY-like receiver domain, for st

227 that an alanine substitution of a conserved aspartate residue of Csm3 eliminates the 6-nucleotide in

228 histidine and then transfer phosphate to an aspartate residue of DosR.

229 We recently showed that a conserved aspartate residue of GAT-1, Asp-451, whose LeuT equivale

230 Substitution of a key aspartate residue of ISU is found to decrease the rate o

231 mechanism in which the ions interact with an aspartate residue of MotB to drive conformational change

232 Furthermore, the second aspartate residue of this motif is the likely candidate

233 receptor that is homologous to the essential aspartate residue of TM3 in the biogenic amine receptors

234 thus point mutations in the phosphoaccepting aspartate residues of FrzZ and demonstrated the respecti

235 E477 and K505 may help to position the three aspartate residues of the IMTD(Q/A)DXD motif for magnesi

236 utophosphorylation and phosphotransfer to an aspartate residue on a receiver molecule have only recen

237 rapidly transferred from phospho-FixL to an aspartate residue on FixJ.

238 ansfer of phosphate from the histidine to an aspartate residue on the cognate response regulator (RR)

239 Transient phosphorylation at an aspartate residue on the Spo0F protein is a central step

240 In both acidic clusters, the first aspartate residue played a more important role in CAII b

241 the negatively charged carboxyl group of the aspartate residue plays a critical role at the active si

242 substitutions of two conserved transmembrane aspartate residues ("PS1 aspartate variants") leads to t

243 The critical aspartate residue required for eicosanoid sensitivity is

244 Ho & Murrell-Lagnado recently identified an aspartate residue responsible for gating these K+ channe

245 Rapid chemical proteolysis at aspartate residues results in K63-linked peptides with t

246 H(+)-ATPase isoform 2 (AHA2) consists of an aspartate residue serving as key proton donor/acceptor (

247 The obligate kinase subunits have aspartate residues substituted for threonine at position

248 whereas the mutation of calcium-coordinating aspartate residues (syt-D3,4N) alters endocytic rate but

249 anionic uracil leaving group and a conserved aspartate residue that are located on opposite faces of

250 ption is abolished by either mutation of the aspartate residue that is conserved among response regul

251 h PIP2, are localized next to the identified aspartate residue that is responsible for the Na+ effect

252 evealed the presence of a water-coordinating aspartate residue that limits esterase activity.

253 ysis of ALG6 variants identified a catalytic aspartate residue that probably acts as a general base.

254 taining proteins revealed that the conserved aspartate residue that usually interacts with the Mg(2+)

255 Binding involves one serine and five aspartate residues that are conserved in numerous C2-dom

256 Aspartate residues that are incorporated in long buried

257 main does not contain the full complement of aspartate residues that commonly mediate Ca2+ binding at

258 cterized by a conserved set of histidine and aspartate residues that coordinate an active site metall

259 the decarboxylation of several glutamate and aspartate residues that mediate contacts between moving

260 Numerous aspartate residues that might inhibit DNA binding by the

261 In particular, both aspartate residues that occupy the positions of the chro

262 an unusual repeat sequence of histidine and aspartate residues that occur in pairs: NPVDDHHDDHHDAPIV

263 directed mutagenesis of two highly conserved aspartate residues that play important structural and/or

264 , and others, is hydrogen bonding of the key aspartate residue, the counterion to the retinal Schiff

265 cavity allows access to a strictly conserved aspartate residue thought to coordinate ion binding dire

266 dichroism showed that neutralization of the aspartate residue through the formation of a methyl este

267 yzes the rearrangement of a highly conserved aspartate residue to a beta-amino acid, isoaspartate, in

268 We mutated this aspartate residue to alanine and assessed the elastogeni

269 backbone fold and the use of an active site aspartate residue to mediate catalysis with the 4-hydrox

270 ctivity whereas conversion of other selected aspartate residues to alanine had less effect, consisten

271 Mutating the two aspartate residues to alanine rendered the peptides inac

272 On separate mutation of two of these aspartate residues to cysteine or histidine, the metal i

273 that require accurate processing at internal aspartate residues to generate the two-chain active enzy

274 ns that in turn require cleavage at internal aspartate residues to generate the two-subunit active en

275 otein through ester links from glutamate and aspartate residues to the heme 1- and 5-methyl groups an

276 rs, it has been assumed that two ion-binding aspartate residues transport the two protons that are la

277 Moreover, a conserved aspartate residue trigger was found to affect mitochondr

278 sole constriction is lined by a ring of six aspartate residues, two in each of the three identical m

279 with 2 or more C-terminal glutamate (but not aspartate) residues (V(max) for 3 glutamates is approxim

280 trate-trapping mutant, in which an invariant aspartate residue was changed to alanine (D811A in PTPH1

281 d by site-directed mutagenesis in which each aspartate residue was individually replaced by glutamate

282 sbd41Asn was synthesized in which the buried aspartate residue was mutated to asparagine.

283 ective cleavage at only 6 solvent accessible aspartate residues was observed.

284 h conserved glycine 176 was replaced with an aspartate residue, was not able to support CO(2)-depende

285 ; in addition, the glutamate residue and one aspartate residue were mutated to glutamine and asparagi

286 Contrary to earlier findings where conserved aspartate residues were found crucial for iron release,

287 s activity was eliminated when the catalytic aspartate residues were replaced with alanine.

288 e largely focused on invariant histidine and aspartate residues which may be involved in metal bindin

289 an unusual "bridging" glutamate but not the aspartate residue, which is believed to facilitate inter

290 osphotransfer from the sensor to a conserved aspartate residue, which is present in the amino terminu

291 omplished by removing the negatively charged aspartate residue, which normally participates in a conf

292 bution of electron density for the catalytic aspartate residues, which is discussed in relation to th

293 A conserved TM10 aspartate residue, whose LeuT counterpart participates i

294 Upon phosphorylation of a specific aspartate residue within the regulatory domain, the C-te

295 to enable alignment with oppositely charged aspartate residues within CD3zeta and activation of CD3z

296 Rat VAChT has a number of aspartate residues within its predicted transmembrane do

297 nal studies showed that two highly conserved aspartate residues within putative transmembrane domains

298 for binding to trkB, two negatively charged aspartate residues within the 11 amino acid motif of FL

299 In contrast, aspartate residues within the CDRs were almost entirely

300 The negative charge of two aspartate residues within this stretch is crucial for li