ライフサイエンスコーパス: Asp

1 Asp and Ala, in the selectivity motif DEKA, line the wal

2 Asp(22) is part of the proton-binding site of GlcP(Se) a

3 Asp-82 also enhanced the function of Tyr as a redox-acti

4 acellular ligand-binding repeats at Gly(171) Asp(172).

5 nserved negatively charged residues Glu-179, Asp-180, and Asp-181 that could contribute to non-bonded

6 3) The DC pair residue Asp(196) (Asp(156) in CrChR2) deprotonates in N --> O transition.

7 We conclude that CaV1.2 Asp-181 anchors the physical interaction that facilitate

8 Substitutions of CaV1.2 Asp-181 impaired the co-immunoprecipitation of CaVbeta/C

9 hat is not hydrolyzed in the absence of O(2) Asp-678 resides near the quinone moiety of PlGoxA, and a

10 bipyramid geometry with His(117), His(257), Asp(116), Asn(216), and a water/hydroxide as ligands.

11 2) The counter-ion Asp(293) (Asp(253) in CrChR2) receives the retinal Schiff base pro

12 ymic metal ligands in MPE: Asp(33), His(35), Asp(78), Asn(112), His(124), His(146), and His(158) A sw

13 both thrombin exosite I with segment Glu-35-Asp-47 and the catalytic site with the region Pro-49-Arg

14 Three aspartate residues in Cx30 (Asp-50, Asp-172, and Asp-179) have been implicated previously in

15 ree highly conserved residues - Gln(232/585)-Asp(262)/Asn(623)-Tyr(322/666) (the constriction triads)

16 dynamic upon substitution of catalytic acid Asp-239 by alanine.

17 Acidic amino acids, aspartic acid (Asp) and glutamic acid (Glu) can enhance the solubility

18 n of peptides that employs an aspartic acid (Asp) as a native directing motif, which directs the site

19 n (4S)-aminoproline (Amp) and aspartic acid (Asp) that directs the composition and register-specific

20 model system consisting of l-aspartic acid (Asp) which when added to the precipitation solution of c

21 utant EWSR1/FLI1-T79D (Thr to aspartic acid (Asp)) retained the high activity as wild-type EWSR1/FLI1

22 analogues bearing basic (Lys, Orn) or acid (Asp or Glu) function.

23 DC1 in wri1-1 decreased indole-3-acetic acid-Asp content and partially rescued its short-root phenoty

24 length and elevation of indole-3-acetic acid-Asp levels relative to the wild type.

25 ues with less hydrophobic residues or acidic Asp.

26 ion of the protein, encompassing amino acids Asp-31-Arg-62, is the region mainly responsible for alph

27 simply by adding chiral acidic amino acids (Asp and Glu).

28 A key patch of amino acids, Asp-Phe-Asp (the 'DFD patch'), situated at the mouth of

29 rted by the NMR structure of the less active Asp-58-IGF-1 variant.

30 lex with type I inhibitors assume an active "Asp-Phe-Gly (DFG)-in" and "alphaC-in" conformation.

31 Systematic mutagenesis of His583 to Ala, Asp, Asn, Glu, Gln, Lys, Phe, Tyr, and Trp showed that a

32 ic samples (seven enantiomer pairs d/l-Ala, -Asp, -Glu, -His, -Leu, -Ser, -Val and the three achiral

33 on of the gene encoding the sole Asp-Glu-Ala-Asp (DEAD)-box RNA helicase in Synechocystis sp. PCC 680

34 Here we report that a charge-altering Asp-to-His mutant (D46H) expands native cholesterylation

35 and a homologous aspartate aminotransferase (Asp-AT) from Escherichia coli as a control.

36 This Amp-Asp salt bridge allowed for the rational design of stran

37 es near the quinone moiety of PlGoxA, and an Asp is structurally conserved in this position in all tr

38 one active site is recognized in trans by an Asp-274 from the opposing half, which is positioned to s

39 cinimide, which is hydrolyzed to generate an Asp or isoAsp containing peptide.

40 Target of Egr1 (TOE1) is an Asp-Glu-Asp-Asp (DEDD) domain containing deadenylase tha

41 mple where a general base substitution of an Asp for His preserves both the structure and activity as

42 The simulations suggested that an Asp-156-Arg-39-Tyr-202 triad creates a hydrogen-bonded n

43 Furthermore, His(100) and Asp(171) were preferential affinity sites for Cu(II) and

44 wo conserved aspartate residues, Asp-163 and Asp-164, are essential for transport and are candidates

45 rtate residues in Cx30 (Asp-50, Asp-172, and Asp-179) have been implicated previously in the Ca(2+) s

46 sis of Nef amino acids Arg-134, Glu-174, and Asp-175, which stabilize Nef for AP-2 alpha-sigma2 bindi

47 ively charged residues Glu-179, Asp-180, and Asp-181 that could contribute to non-bonded interactions

48 amino acid residues (Cys-1865, His-1955, and Asp-1975).

49 e hypothesis that replacement of Arg-213 and Asp-143 with the corresponding RF1 residues will reduce

50 active site residues identified Asn(24) and Asp(39) as being essential for activity.

51 etween the active-site residues His(265) and Asp(267) In OTUB2, however, the arrangement of the catal

52 l group oxygen and nitrogen with Lys-343 and Asp-320, respectively.

53 oteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death.

54 Both the single Tyr-41 and Asp-82 constructs lowered the oxygen affinity of HbS but

55 Some acquired residues (e.g. Pro(52) and Asp(55)) are conserved in naturally efficient CMs, but m

56 rtate modification introduced at Asp(58) and Asp(91), respectively.

57 ding required key residues Asp-179(4.60) and Asp-275(6.58) (residue numbering follows the Ballesteros

58 omers through the interaction of Arg-742 and Asp-113 is essential for catalytic activity and nuclear

59 torial proton path in BR in which Asp-85 and Asp-96 serve as acceptor and donor, respectively, of the

60 ed two central aspartate residues Asp-99 and Asp-219 as essential for catalytic activity.

61 in which the His acts as a Bronsted acid and Asp as a Bronsted base in a single-displacement mechanis

62 The results also indicate that both Asn and Asp can restore the activity of Val-inhibited PKM2.

63 structures of the Eb/O-PLP-AFPA complex and Asp-AT-PLP-AFPA complex revealed that GabR is incapable

64 directs PARP-1 catalytic activity to Glu and Asp residues.

65 substituting key charged Arg, Lys, Glu, and Asp residues by Gly or His.

66 n N-terminal extension containing a His- and Asp/Glu-rich hypervariable region followed by a highly c

67 not conserved in E. coli OtsA (His, Leu, and Asp, respectively), providing a rationale for the purine

68 Ins, Cho, Cr, PCr, Tau, GABA, Lac, NAAG, and Asp.

69 Ins, Cho, Cr, PCr, Tau, GABA, Lac, NAAG, and Asp.

70 We found that Asn (polar) and Asp (charged) activate PKM2 and that Val (hydrophobic) i

71 Another similar pair is Leu-126 in RF1 and Asp-143 in RF2, which are also conserved within their re

72 Third, an Arg-Asp dipeptide immediately preceding the ZF helix, conser

73 This Arg-Asp conformational switch allows identical ZF modules to

74 are cysteine proteases which break Asx (Asn/Asp)-Xaa bonds in acidic conditions.

75 boosts the synthesis of cytosolic aspartate (Asp) and NAA, which is impeded by aralar deficiency, pre

76 s), arginine (Arg), lysine (Lys), aspartate (Asp), glutamate (Glu) and cysteine (Cys) phosphorylation

77 etons, with the amino acid data rich in Asx (Asp + Asn) and Glx (Glu + Gln) typical of invertebrate s

78 roteins are cleaved by caspases-1 and -11 at Asp-276.

79 Intramolecular self-cleavage at Asp-193 evoked higher solvent exposure in the regions of

80 tivity by proteolytically processing HOIP at Asp-348 and Asp-387 during the execution of cell death.

81 he l-isoaspartate modification introduced at Asp(58) and Asp(91), respectively.

82 extents of oxidation at beta-His-77 and beta-Asp-99 of globin were significantly elevated in oral can

83 ase, demonstrates the potential of the beta2-Asp to take either one of these two roles.

84 n N-proteinases ADAMTS2 and ADAMTS14 between Asp-218 and Tyr-219, 50 amino acids downstream of the BM

85 r release from the ER, a salt bridge between Asp-17 and Arg-57 is essential.

86 identified a network of salt bridges between Asp(1261) and the rest of A1 that lock the N-terminal li

87 position of the proton that resides between Asp-222 and the pyridinyl nitrogen.

88 Although brain Asp and NAA levels did not change by betaOHB administrat

89 s suggest that the lack of increase in brain Asp and NAA is possibly because of its active utilizatio

90 in the active-site region and coordinated by Asp(320) Using constructs to produce either recombinant

91 mes complementary to trypsin, such as Glu-C, Asp-N, Lys-N, Arg-C, LysargiNase has been reported.

92 ir (G-Arg interaction) to a G:C base pair (C-Asp interaction).

93 Catalytic Asp-239 controls hMGL allosteric communications and may

94 nsmembrane proteins that possess a catalytic Asp-His-His-Cys cysteine-rich domain (DHHC-CRD).

95 eutral replacement of the negatively charged Asp(22) led to positive charge displacements over the en

96 utoacylated at a site defined by a conserved Asp-His-His-Cys motif.

97 because it capitalizes on a highly conserved Asp-Ser-Leu-Asp amino acid sequence in ACPs to which acy

98 BsPdaC retains the conserved Asp-His-His metal-binding triad characteristic of CE4 en

99 ations to reposition a universally conserved Asp (D) residue involved in catalysis.

100 eacetylases that lack the metal-coordinating Asp residue.

101 The sodium-coupled Asp symporter, Glt(Ph) is an archaeal homolog of glutama

102 Three aspartate residues in Cx30 (Asp-50, Asp-172, and Asp-179) have been implicated previ

103 eration of a mixture of unusual isoAsp and d-Asp residues that may impact health.

104 preexposure to the amino acid D-aspartate (D-Asp).

105 Interestingly at equimolar combinations, D-Asp and D-Glu were able to significantly disperse (at 20

106 The anti-biofilm activity of D-Asp and D-Glu was studied on Staphylococcus aureus biofi

107 Using D-Asp as a "false" GT, we determined the extent of local n

108 Using D-Asp, it was possible to investigate the effects of speci

109 so possible in simulations with deprotonated Asp.

110 a unique DFG-out/alpha-C state formed as DFG-Asp is moved into a back pocket forming a salt bridge wi

111 is how key titratable residues, such as DFG-Asp, alphaC-Glu, and HRD-Asp, change protonation states

112 PRUNE is a member of the DHH (Asp-His-His) phosphoesterase protein superfamily of mole

113 ved Arg residues that might contact the DIME-Asp.

114 lu-Arg (ER); and two non-arginyl dipeptides: Asp-Asp (DD) and Glu-Asp (ED).

115 CP-REDOR NMR reveals that each Asp is embedded in a perturbed occlusion shell of ~8 dis

116 c and polar residues, substitution of either Asp-219 or Glu-447 with any other residues resulted in r

117 y additional in silico digestion with either Asp-N, Arg-C, Glu-C, Lys-C, or Lys-N.

118 ments generated by trypsin plus endoprotease-Asp-N.

119 for the FraB-catalyzed deglycation of 6-P-F-Asp (via an enaminol intermediate) to glucose-6-phosphat

120 substrate 6-phosphofructose-aspartate (6-P-F-Asp).

121 Next, Ala-scanning of the five Asp residues preceding the activation site Lys revealed

122 ve composite gels composed of Fmoc-Lys(Fmoc)-Asp and a conductive polymer exhibit excellent DNA bindi

123 Fmoc-Lys(Fmoc)-Asp exhibits the lowest CGC and highest mechanical prope

124 imalistic, de novo dipeptide, Fmoc-Lys(Fmoc)-Asp, as an hydrogelator with the lowest CGC ever reporte

125 sults suggest a putative pH-sensing role for Asp-219 and Glu-447 in hENT3 and that the size, ionizati

126 pexin-like (HX) domain, with a group of four Asp carboxylate groups.

127 es even when using the central cE5 fragment (Asp-31-Arg-62) alone.

128 f preselected to carry at least one A118G G (Asp) allele, were randomized to naltrexone (50 mg) or pl

129 ns of nuclease enzymes suggest that this Glu(Asp)-mediated mechanism for third ion recruitment and nu

130 he N, S, and O side chains of His, Cys, Glu, Asp, and Lys residues.

131 The peptides were rich in Glu, Asp, Lys, Gly and Leu, and also exhibited diverse bioact

132 non-arginyl dipeptides: Asp-Asp (DD) and Glu-Asp (ED).

133 Target of Egr1 (TOE1) is an Asp-Glu-Asp-Asp (DEDD) domain containing deadenylase that is mut

134 r, bound adjacent to a conserved Glu-Arg-Glu/Asp ionic network in the enzyme's active site.

135 ependently of IGF binding through an Arg-Gly-Asp (RGD) integrin-binding motif.

136 C3 harbors an Arg-Gly-Asp (RGD) motif, which is the major integrin-binding sit

137 ration by targeting integrins, using Arg-Gly-Asp (RGD) peptide-functionalized gold nanorods.

138 Cyclic peptides containing the Arg-Gly-Asp (RGD) sequence have been shown to specifically bind

139 intermediates for the preparation of Arg-Gly-Asp (RGD)-based cyclopentapeptides (cRGD) with nanomolar

140 In contrast, the putative Arg-Gly-Asp (RGD)-binding alphaPAT-2/betaPAT-3 integrin was acti

141 sses of integrins: collagen-binding, Arg-Gly-Asp (RGD)-binding, laminin-binding, and leukocyte integr

142 higher affinity compared with other Arg-Gly-Asp binding integrins.

143 l cells, BA increased beta1-integrin-Arg-Gly-Asp-peptide affinity by 18% with a transition from singl

144 XAT contains a canonical Gly-Asp-Ser-Leu (GDSL) motif and is encoded by a member of t

145 gs drives the expansion of KP expressing Gly-Asp insertion mutants, despite an associated fitness cos

146 Additionally, the Gly-Asp insertion impairs bacterial growth in lactose-contai

147 ighly preferred for binding to conserved Gly:Asp:Asn residues.

148 intact Glu-Arg-Glu network, as only Glu --> Asp substitutions retain activity.

149 nes with a protonable side chain, i.e., His, Asp, and Glu, were able to mediate electron transfer at

150 ghly active cysteine-lipase having a Cys-His-Asp catalytic triad and additional mutations W104V/A281Y

151 part of the characteristic catalytic Cys-His-Asp triad of Cys proteases.

152 lacement bi-bi mechanism involving a Ser-His-Asp catalytic triad and unconventionally uses an Arg res

153 (CALB) as the model enzyme with the Ser-His-Asp catalytic triad, a highly active cysteine-lipase hav

154 anniversary of the discovery of the Ser-His-Asp catalytic triad, perhaps the most unusual variation

155 monstrated that substitutions in its Ser-His-Asp triad, proposed to serve a general acid-base role, m

156 GEs contain a Ser-His-Asp/Glu catalytic triad, but the location of the catalyt

157 inverting mechanism, EnvSia156 reveals a His/Asp active center in which the His acts as a Bronsted ac

158 o contain a conserved and functional Ser/His/Asp catalytic triad.

159 sidues, such as DFG-Asp, alphaC-Glu, and HRD-Asp, change protonation states dependent on the DFG, alp

160 -GE) and low indole-3-acetate aspartate (IAA-Asp) and isopentenyladenine (iP) contents in BS berries

161 ion-existing either as fused domains (IbetaH(Asp)) at the carboxyl terminus of a nonribosomal peptide

162 and site-directed mutagenesis, we identified Asp(230) in the extracellular loop-2 as being critical f

163 and manganese complex with asparagine Mn(II)(Asp)(2).

164 After the addition of IDL (Ile-Asp-Leu) to the C terminus of CHR peptide WQ or MT-WQ, t

165 ol, neurons led to a substantial increase in Asp (3-fold) and NAA (4-fold) levels.

166 ave high selectivity for the proximal Tyr in Asp-directed Tyr modification.

167 whereas in the other (G329D), the introduced Asp mimicked the presence of pyruvate.

168 2) The counter-ion Asp(293) (Asp(253) in CrChR2) receives the retinal Schif

169 er characterized triose-phosphate isomerase (Asp t 36), one of the dominant IgE (IgE)-reactive protei

170 OTCH3 N terminus at the peptide bond joining Asp(80) and Pro(81) Cleavage at this site was predicted

171 mediates of PGA with canonical substrates (L-Asp and L-Glu) and an opportunistic ligand, a citrate an

172 of these occlusion units suggests that large Asp-free domains drive the vaterite to calcite transform

173 eatment of TCam-2 cells with the peptide Leu-Asp-Phe-Ile (LDFI), a full leptin-receptor antagonist, c

174 apitalizes on a highly conserved Asp-Ser-Leu-Asp amino acid sequence in ACPs to which acyl groups att

175 table, while vaterite grown at 10-fold lower Asp concentration, yet 2-fold less in the crystal, spont

176 receptor, which recognises a C-terminal Lys-Asp-Glu-Leu (KDEL) sequence.

177 ndent recognition of a carboxyl-terminal Lys-Asp-Glu-Leu (KDEL) signal by the KDEL receptor.

178 o bind the minimal FLAG peptide (Asp-Tyr-Lys-Asp) were grafted onto a single-chain variable fragment

179 -MG11 ((177)Lu-DOTA-dGlu-Ala-Tyr-Gly-Trp-Met-Asp-Phe-NH(2)) and (177)Lu-DOTA-PP-F11 ((177)Lu-DOTA-(dG

180 ((177)Lu-DOTA-(dGlu)(6)-Ala-Tyr-Gly-Trp-Met-Asp-Phe-NH(2)), and whether the use of protease inhibito

181 s achieved mostly by introducing d- N-methyl-Asp instead of Asp at the penultimate position of CCK-8.

182 eaving enzyme 1 (BACE1) cleaves APP at minor Asp(1) site to generate C99 for amyloid beta protein (Ab

183 yses reveal that a conserved diacidic motif (Asp-Glu) in these proteins is necessary for their export

184 y serve as the enzymic metal ligands in MPE: Asp(33), His(35), Asp(78), Asn(112), His(124), His(146),

185 ethods: DOTA-D-Glu-Ala-Tyr-Gly-Trp-(N-Me)Nle-Asp-1-Nal-NH(2) (DOTA-MGS5) radiolabeled with (111)In, (

186 ((177)Lu-DOTA-(dGlu)(6)-Ala-Tyr-Gly-Trp-Nle-Asp-Phe-NH(2)) performs better than reference analogs wi

187 (177)Lu-DOTA-(d-Glu)(6)-Ala-Tyr-Gly-Trp-Nle-Asp-PheNH(2) ((177)Lu-PP-F11N) is a suitable agent for t

188 tion of Nt-Asn, arginylation of resulting Nt-Asp, binding of resulting (conjugated) Nt-Arg to the UBR

189 the anion in place of the commonly observed Asp, reminding us that even well-trodden scientific grou

190 The embedding shell and the occluded Asp act as an integral until which minimally rearranges

191 hange the microenvironment, but the pK(a) of Asp(22) corresponded to that of the WT.

192 ng morphology is induced by L-enantiomers of Asp and Glu, whereas 'left-handed' (clockwise) morpholog

193 yzes the post-translational hydroxylation of Asp and Asn residues in epidermal growth factor-like dom

194 xylase (AspH) catalyses the hydroxylation of Asp/Asn-residues in epidermal growth factor-like domains

195 ly by introducing d- N-methyl-Asp instead of Asp at the penultimate position of CCK-8.

196 th mass spectrometry showed that mutation of Asp(21) promoted disorder in the N-terminal helices of 1

197 In this study, mutation of Asp-678 in PlGoxA did not abolish CTQ formation.

198 s to bind nitric oxide, a single mutation of Asp-96 to Val in mitoNEET or Asp-123 to Val in Miner1 fa

199 ed Lys-300 residue, a salt bridge partner of Asp-163.

200 r results reveal the immunogenic property of Asp t 36, a major allergen from A. terreus, and define a

201 long-standing hypothesis that protonation of Asp favors the DFG-out state and explain why DFG flip is

202 tion triggered by the Glu-145 replacement of Asp.

203 of the WT reflects the protonation state of Asp(22) We expected that the substitution of the residue

204 site and perturbed the protonation state of Asp(22), with the latter now exhibiting a pK(a) of 6.4.

205 hENT3 revealed that the ionization states of Asp-219 and Glu-447, and not His, strongly determined th

206 d each directs opposite stereoselectivity of Asp beta-hydroxylation.

207 ogy-based model of the tertiary structure of Asp t 36.

208 gether with the simultaneous substitution of Asp-163 with Asn, and characterized these transporter va

209 Dual substitution of Asp-219 and Glu-447 to Ala sustained pH-independent acti

210 ) or 3-methoxyaspartate (MeOAsp) with Asn or Asp, respectively, in A5D is more detrimental to activit

211 th HOAsn and MeOAsp are replaced with Asn or Asp, respectively.

212 demonstrates that peptides containing Glu or Asp that are preorganized to adopt beta-hairpin structur

213 gle mutation of Asp-96 to Val in mitoNEET or Asp-123 to Val in Miner1 facilitates nitric oxide bindin

214 and Val) are similar in S. venezuelae OtsA (Asp, Ser, and Phe, respectively) but not conserved in E.

215 used IQF substrates to re-investigate the P1-Asp characteristic of caspases, thus demonstrating that

216 whether the Lys-300 residue and its partner Asp-163 are essential for the electrogenicity of EcNhaA.

217 predicted to bind the minimal FLAG peptide (Asp-Tyr-Lys-Asp) were grafted onto a single-chain variab

218 A key patch of amino acids, Asp-Phe-Asp (the 'DFD patch'), situated at the mouth of the BchL

219 Although the aspartate at position Asp-50 was indispensable for divalent cation-dependent g

220 with a flexible loop and a conserved His-Pro-Asp motif required for ATP hydrolysis by Hsp70s) and als

221 ysates, we explored the use of the proteases Asp-N and Glu-C and a nonenzymatic acid induced cleavage

222 The residue H75 defines a cross-protomer Asp-His-Trp triad, which potentially serves as a pH-depe

223 murine model displayed that the recombinant Asp t 36 was able to stimulate airway inflammation, as d

224 al of the crucial Na(+)-coordinating residue Asp(926) This mechanistic model is consistent with exper

225 3) The DC pair residue Asp(196) (Asp(156) in CrChR2) deprotonates in N --> O tr

226 ational dynamics of a single active residue, Asp-103, promotes large electric field fluctuations that

227 The presence of acidic residues Asp and Glu near the peptide N-terminus is by far the mo

228 ts identified two central aspartate residues Asp-99 and Asp-219 as essential for catalytic activity.

229 This network, which involves residues Asp-222, His-143, Thr-139, His-189, and structural water

230 CXCL12 binding required key residues Asp-179(4.60) and Asp-275(6.58) (residue numbering follo

231 th assays demonstrate that MazF-mt6 residues Asp-10, Arg-13, and Thr-36 are critical for RNase activi

232 We find that while the active site residues Asp-40 and Tyr-16 maintain their electric field contribu

233 ty depends on the conserved acidic residues, Asp-189 and Glu-247.

234 Two conserved aspartate residues, Asp-163 and Asp-164, are essential for transport and are

235 6) pocket, forming a salt bridge with ProT's Asp(194), thereby stabilizing the active conformation.

236 tably, the pyrimidine containing prodrug (S)-Asp-FPMPC is the only congener within this series to dem

237 n its ion transport pathway a unique Thr-Ser-Asp (TSD) motif, which is involved in the binding of a c

238 Phylogenetic analysis showed Asp t 36 to be highly conserved with close similarity to

239 s amine group with the conserved active-site Asp is essential for activity and likely dictates its or

240 , accumulation of the gene encoding the sole Asp-Glu-Ala-Asp (DEAD)-box RNA helicase in Synechocystis

241 DHHC3), a cellular Golgi apparatus-specific Asp-His-His-Cys (DHHC) zinc finger protein.

242 known as DHHC3), a Golgi apparatus-specific Asp-His-His-Cys (DHHC) zinc finger protein; (ii) a GODZ

243 hnRACs reveal a distinct feature of stacking Asp residues, which contributes to fibril reversibility

244 c DxE ER export signal, because substituting Asp-211 and Glu-213 with alanine induced retention of th

245 ase (NRPS) or as stand-alone enzymes (TbetaH(Asp))-and each directs opposite stereoselectivity of Asp

246 ctrostatic interaction between an N-terminal Asp of the pheromone and Arg-153 within the proposed phe

247 ction effect of the side chain of N-terminal Asp reduces the basicity of the N-terminal amino group a

248 These studies confirm that Asp(22) is the proton-binding residue in GlcP(Se) and sh

249 py on the immobilized GlcP(Se) We found that Asp(22) has a pK(a) of 8.5 +/- 0.1, a value consistent w

250 We found that Asp-30 of WW1 and His-75 of WW2 interact through a hydro

251 Quantum chemical calculations indicate that Asp-222, which is directly coupled to the pyridinyl nitr

252 These results indicate that Asp-678 is involved in the initial deprotonation of the

253 Biophysical analysis indicated that Asp t 36 shows similar secondary structure content and t

254 d free-energy surface studies indicated that Asp-168 is important in anchoring Arg-155 for ligand bin

255 In those other enzymes, mutation of that Asp results in no or negligible CTQ formation.

256 with site-directed mutagenesis revealed that Asp(147) or Asn(169) of RIPK1 are key for ceramide bindi

257 tracentrifugation, our results revealed that Asp(21) and Glu(89) both play key roles in dimer dynamic

258 ant XoxF1 or its D320A variant, we show that Asp(320) is needed for in vivo catalytic function, in vi

259 Solid-state NMR shows that Asp is sparsely occluded within vaterite and calcite.

260 The structures also suggest that Asp-678 is acting as a proton relay that directs these p

261 veral WER variants with substitutions at the Asp-105 position, and these exhibited a variety of gene

262 leaves along with mutual effects between the Asp family and SMM pathways operating in these tissues.

263 pathological fibril formation caused by the Asp mutations identified in familial ALS.

264 esent in Hb Mequon; the second contained the Asp (K82D) found in the beta cleft of Hb Providence; and

265 onation of the GtCCR2 SB occurs not from the Asp-96 homolog, but by proton return from the earlier pr

266 he contributions of the activation loop, the Asp-Phe-Gly (DFG) motif, the regulatory spine, and the g

267 In GtCCR2, deprotonation of the Asp-96 homolog is required for cation channel opening an

268 cate that, contrary to previous reports, the Asp(614)Gly mutation in the spike glycoprotein (S) likel

269 ic channel to cations in GtCCR2 requires the Asp-96 homolog to be unprotonated, as has been proposed

270 of BACE1 in APP from the Glu(11) site to the Asp(1) site both in male and female transgenic mice in v

271 BACE1 cleavage site from the Glu(11) to the Asp(1) site, resulting in much higher C99 level and C99/

272 e SB chromophore rapidly deprotonates to the Asp-85 homolog, as in BR.

273 d that Ca(2+) binding was perturbed when the Asp and Glu residues in the motif were substituted by al

274 Mutation of this Asp residue in nSMase2 disrupts catalysis, allosteric ac

275 n amino acids, including Gly, Ala, Ser, Thr, Asp, and Glu, which are relatively silent with regard to

276 hereas phosphomimetic mutation of Ser-357 to Asp did not.

277 located within hydrogen-bonding distance to Asp(22), would change the microenvironment, but the pK(a

278 the N terminus at position 1 (equivalent to Asp-221 in the Fc of IgG1) dramatically enhances overall

279 Effects of Ser to Asp phosphomimetic substitutions in the M-domain of C0-C

280 (Gly), tRNA(Lys), tRNA(Val), tRNA(His), tRNA(Asp), and tRNA(SeC) to produce tRNA halves and tRF-5s th

281 oding RNAs and reduced the stability of tRNA(Asp(GTC)) We also demonstrate the importance of m(5)C in

282 The C-terminal region of LRRK2 is a Trp-Asp-40 (WD40) domain with poorly defined biological func

283 domain and implicate a previously unexamined Asp-Thr dyad in catalysis of the cyclodehydration reacti

284 Lys-343 access to the bound ligand, whereas Asp-320 lies in an extended loop proximal to the ligand-

285 ine the vectorial proton path in BR in which Asp-85 and Asp-96 serve as acceptor and donor, respectiv

286 Substitution of RIN4 Thr-166 with Asp enhanced the association of AtRIN4 with EXO70E2, whi

287 Phosphomimetic substitution of Thr-38 with Asp increased co-immunoprecipitation of the CAR DBD with

288 we report that substitution of Gly-4941 with Asp or Lys results in functional channels as indicated b

289 to E88D selectins that replaced Glu-88 with Asp.

290 for instance, appeared to be associated with Asp(808) protonation.

291 hat Ser-6 in Pep8 forms a hydrogen bond with Asp-202 in eIF4E.

292 rg-742 of a monomer forms a salt bridge with Asp-113 of another monomer.

293 stability is tunable, as vaterite grown with Asp at high concentration is both thermally and temporal

294 subsite and electrostatic interactions with Asp(125) of the S2' subsite.

295 Substitution of Ser-6 with Lys, but not with Asp, enhanced the ability of Pep8 to inhibit the Rbm38-e

296 f the possible antiparallel structures (with Asp(15) and Phe(19) aligned), are highly stable and orde

297 phosphorylation sites were substituted with Asp) perturbed self-association and inhibited DEAD-box h

298 , Ser-3 modification (i.e. substitution with Asp or phosphorylation) "undocks" and repositions the co

299 and the integrity of its binding motif His-X-Asp, which is conserved in Fe-dependent dioxygenases(3).

300 lacing a single asparagine residue in ZnT10 (Asp-43) with threonine (ZnT10 N43T) converted the Mn(2+)