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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 ase shows that the active site contains four aspartate residues.
13 dged by a water (hydroxide) molecule and two aspartate residues.
14 cleavage of multiple substrates at specific aspartate residues.
15 cysteine protease by processing at internal aspartate residues.
16 proteases, cleave their substrates following aspartate residues.
17 geminal fluorine atoms, and the active-site aspartate residues.
18 proteases, cleave their substrates following aspartate residues.
19 rodimeric enzymes after cleavage at specific aspartate residues.
20 city for cleaving synthetic substrates after aspartate residues.
21 tion of the initial protonation state of the aspartate residues.
22 ding a series of critical negatively charged aspartate residues.
23 ive site of each monomer involving conserved aspartate residues.
24 y conserved negatively charged glutamate and aspartate residues.
25 phosphorylation sites with either alanine or aspartate residues.
26 posed of 40% alanine, 36% histidine, and 11% aspartate residues.
29 ge of the amyloid precursor protein (APP) at aspartate residue 664 by caspases may play a key role in
30 ither internal tandem duplications (ITDs) or aspartate residue 835 (D835) point mutations, are presen
36 g domains and four 'U-motifs' with conserved aspartate residues and a QxxRW motif that are essential
38 a factor family revealed a conserved pair of aspartate residues and an arginine that are important fo
39 o the transmembrane domains contain multiple aspartate residues and are found to play an important ro
40 , that binds at least two Ca2+ ions via five aspartate residues and is conserved in most C2-domains.
41 domain, named after conserved histidine and aspartate residues; and two C-terminal ACT domains, name
42 oordinated by two histidine residues and one aspartate residue approximately 14 angstroms into the li
43 e wild-type periplasmic domain structure two aspartate residues are bound per dimer, but with differe
45 results indicate that the two transmembrane aspartate residues are critical for both presenilin-1 en
46 mical studies, suggests that the active site aspartate residues are in proximity to the S1/S1' bindin
49 sequence SxHxxGxAxD, in which histidine and aspartate residues are putative zinc ligands, identified
51 osis in S2 cells, DIAP1 is cleaved following aspartate residue Asp-20 by the effector caspase DrICE.
53 ge to one side-chain oxygen atom of a buried aspartate residue (Asp(89)), whereas the other oxygen is
54 distal side of the heme molecule, a flexible aspartate residue (Asp-168) plays a key role in catalysi
56 49, and phosphoryl groups are transferred to aspartate residues (Asp-52 and Asp-220) in the two recei
58 I manganese stabilizing protein, contains an aspartate residue [Asp157 (spinach numbering)], which is
59 that the protonation states of two catalytic aspartate residues, Asp25 and Asp125, strongly influence
61 d by multiple caspases at a highly conserved aspartate residue (Asp421) in its C terminus in vitro an
62 forms a salt bridge with a conserved, buried aspartate residue (Asp51), which suggests that the amino
64 corporated into peptidoglycan.Mutation of an aspartate residue (Asp59) of His-tagged VanXY(C) corresp
66 aled the electronic quenching dynamics by an aspartate residue at a hydrogen bond distance in 275-615
67 otein, but not to a mutant form in which the aspartate residue at amino acid position 54 has been cha
68 ization of a mutant RecA protein wherein the aspartate residue at position 100 within the ATP binding
71 f ORF57 in the cytoplasm by caspase-7 at the aspartate residue at position 33 from the N terminus.
73 nt, RR06(D51A), with a point mutation in the aspartate residue at position 51 (a predicted major phos
74 rifugation, we identified a highly conserved aspartate residue at the boundary of the M3-M4 loop and
75 imer interface; (2) KGPDC and OMPDC share an aspartate residue at the end of the first beta-strand an
76 mutagenesis, a NodWD70N mutant in which the aspartate residue at the proposed phosphorylation site w
77 y in other DFRs, whereas MtDFR2 contained an aspartate residue at the same site and was only marginal
78 ly specific requirement for an asparagine or aspartate residue at this position may indicate a key ro
82 -site cysteine of the CED-3 protease and the aspartate residues at sites of processing of the CED-3 p
84 creased when Asn-106 was substituted with an aspartate residue, but decreased in mutants with alanine
86 lization resulting from the partially buried aspartate residue cannot be offset by ion pair formation
87 gment, which contains numerous glutamate and aspartate residues, caused a 55% decrease in trans-activ
88 ains, based on rapid chemical proteolysis at aspartate residues combined with immunoprecipitation and
92 P) with Asp-to-Asn substitution at the first aspartate residue (D117N) of this motif could not be gen
93 contained mutations in close proximity to an aspartate residue (D121) believed to form part of the ca
95 re of the postfusion E1 trimer shows that an aspartate residue, D188, is positioned in the central co
97 the present study, we show that a conserved aspartate residue, D46 of the Hh autoprocessing domain,
101 K+ channel crystal structure, the equivalent aspartate residue (D80) does not directly interact with
103 All three receptors contain a conserved aspartate residue (D98) at the extracellular boundary of
104 Mutation of S368 and S372 to a phosphomimic aspartate residue decreases the association of GGA3 with
106 in enzyme activity, suggesting that the two aspartate residues did not play a pivotal role in cataly
109 e studies identified conserved histidine and aspartate residues essential for the catalytic activity
110 onversion are modulated by protonation of an aspartate residue, establishing the power of MD & MSMs i
111 screening the electrostatic effects that the aspartate residue exerts on the nearby PIP2-interacting
112 iation constant)-perturbed pair of conserved aspartate residues explains the pH dependence of this tr
113 ed by site-directed mutagenesis of three key aspartate residues flanking the conserved C93 which were
117 idine residues from one molecule and another aspartate residue from the next molecule, thus forming a
118 y of the YMDD loop and prevent the catalytic aspartate residues from adopting their metal-binding con
124 lobin; the results indicate that none of the aspartate residues has a strongly depressed pKa in N, as
125 eltaN or SleB-DeltaC, in which glutamate and aspartate residues have individually been changed to ala
127 ation of Ser471 to a phosphorylation mimetic aspartate residue impaired REL's transforming ability, e
129 active site and specific interactions of an aspartate residue in a polar loop and two phenylalanines
131 26 shows an abnormally high pKa value for an aspartate residue in all states of human thioredoxin, wi
133 sults suggest that the role of the conserved aspartate residue in loop 2/3 is to influence the topolo
134 highlights the critical role of a conserved aspartate residue in mediating the first-order hydrolyti
138 , D1866Y, alters an evolutionarily conserved aspartate residue in the C-terminal cytoplasmic domain o
141 , coinciding with lack of specificity for an aspartate residue in the neutralization core of BnAb 2F5
142 bind xanthine nucleotides when the conserved aspartate residue in the NKXD motif was changed to aspar
148 group that is subsequently transferred to an aspartate residue in the response regulator protein.
151 mutated protein, we found that the conserved aspartate residue in the Walker B motif plays a role in
152 lase activity for purine ribosides, while an aspartate residue in this position confers high activity
153 Site-directed mutagenesis of glutamate and aspartate residues in a conserved acidic patch (region 2
154 ative charge on Ser(982)-phosphate and three aspartate residues in a D986NDD custer in altering the s
155 hypothesize that spontaneous cyclization of aspartate residues in amyloidogenic proteins can serve a
156 ndividually mutated to serine, histidine, or aspartate residues in an attempt to identify the protein
157 e molecule is shown to bind to the catalytic aspartate residues in an unprecedented manner in the fie
158 f all 20 glutamate residues and 24 of the 25 aspartate residues in CcP, one at a time, to lysine resi
160 signal is insensitive to 13C-labeling of the aspartate residues in Hb, and cannot arise from protonat
162 ects of mutating the conserved histidine and aspartate residues in methionine synthase have recently
163 f either of two conserved transmembrane (TM) aspartate residues in presenilin-1, Asp 257 (in TM6) and
166 ed to study the protonation of histidine and aspartate residues in the acid-induced unfolding of reco
168 variety of organisms, candidates for two key aspartate residues in the active site are identified at
169 TTQ biogenesis and to define novel roles for aspartate residues in the biogenesis of a protein-derive
170 show that mutating two of the Ca(2+)-binding aspartate residues in the C(2)B domain (D(416,418)N in D
171 ulation, with crucial roles for these single aspartate residues in the communication and functional i
172 ite-directed mutagenesis indicate that three aspartate residues in the conserved phosphoesterase moti
173 transport was observed when any of the five aspartate residues in the cytoplasmic loop were converte
175 utative active site motif with two conserved aspartate residues in the large (XseA/TM1768) subunit.
177 Mutation to glutamate of each of the three aspartate residues in the Mg(2+)-binding aspartate-rich
180 n include PARPs, enzymes known to ribosylate aspartate residues in the process of poly(ADP-ribosyl)at
182 rane environment near a ring of four charged aspartate residues in the trimer, namely Asp36, Asp38, A
184 horylation by mutation to positively charged aspartate residues increases basal transactivation.
185 nteractions in the vicinity of the catalytic aspartate residues, increasing the distance between them
186 ee distinct highly conserved arginine and/or aspartate residues inside or flanking these TM helices a
187 pha1(A322D)) introduces a negatively charged aspartate residue into the hydrophobic M3 transmembrane
191 dine nitrogen of the cofactor to a conserved aspartate residue is 2.6 A in AATase and 3.8 A in ACC sy
192 transduction systems, phosphorylation of an aspartate residue is coupled to a change from an inactiv
194 c triad, and in some enzymes the role of the aspartate residue is replaced by a main-chain carbonyl o
195 essential amino acid motif (DGXD) containing aspartate residues is located in the first transmembrane
199 contrast, substitutions with phosphomimetic aspartate residues led to a complete recovery of the tra
200 d naphthalene dioxygenase (NDO), a conserved aspartate residue lies between the mononuclear and Riesk
201 e effect on antigen binding of an isomerized aspartate residue located in the complementarity-determi
202 e I' band and the side-chain absorbances for aspartate residues located almost exclusively at the cal
203 protease, and mutation of either of the two aspartate residues located in adjacent transmembrane dom
204 t bridges formed by arginine, glutamate, and aspartate residues located in helices D, E, F, and G.
208 t109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit in
209 ons all lend weight to the proposal that the aspartate residues mediate substrate binding by chelatio
211 tivity, whereas mutation to negative charged aspartate residues (mimicking receptor phosphorylation)
213 wn absolute stereochemistry, we find that an aspartate residue near the gorge entrance (D74) is respo
215 alytic GGEEF motif, as well as the conserved aspartate residue of a CheY-like receiver domain, for st
216 that an alanine substitution of a conserved aspartate residue of Csm3 eliminates the 6-nucleotide in
220 mechanism in which the ions interact with an aspartate residue of MotB to drive conformational change
222 receptor that is homologous to the essential aspartate residue of TM3 in the biogenic amine receptors
223 thus point mutations in the phosphoaccepting aspartate residues of FrzZ and demonstrated the respecti
224 E477 and K505 may help to position the three aspartate residues of the IMTD(Q/A)DXD motif for magnesi
225 utophosphorylation and phosphotransfer to an aspartate residue on a receiver molecule have only recen
227 ansfer of phosphate from the histidine to an aspartate residue on the cognate response regulator (RR)
230 the negatively charged carboxyl group of the aspartate residue plays a critical role at the active si
231 substitutions of two conserved transmembrane aspartate residues ("PS1 aspartate variants") leads to t
233 Ho & Murrell-Lagnado recently identified an aspartate residue responsible for gating these K+ channe
235 H(+)-ATPase isoform 2 (AHA2) consists of an aspartate residue serving as key proton donor/acceptor (
236 proton translocation between the active site aspartate residues simultaneously with carbonyl hydratio
238 whereas the mutation of calcium-coordinating aspartate residues (syt-D3,4N) alters endocytic rate but
239 anionic uracil leaving group and a conserved aspartate residue that are located on opposite faces of
240 ption is abolished by either mutation of the aspartate residue that is conserved among response regul
241 h PIP2, are localized next to the identified aspartate residue that is responsible for the Na+ effect
242 taining proteins revealed that the conserved aspartate residue that usually interacts with the Mg(2+)
245 main does not contain the full complement of aspartate residues that commonly mediate Ca2+ binding at
246 cterized by a conserved set of histidine and aspartate residues that coordinate an active site metall
247 the decarboxylation of several glutamate and aspartate residues that mediate contacts between moving
250 an unusual repeat sequence of histidine and aspartate residues that occur in pairs: NPVDDHHDDHHDAPIV
251 directed mutagenesis of two highly conserved aspartate residues that play important structural and/or
252 , and others, is hydrogen bonding of the key aspartate residue, the counterion to the retinal Schiff
253 cavity allows access to a strictly conserved aspartate residue thought to coordinate ion binding dire
254 dichroism showed that neutralization of the aspartate residue through the formation of a methyl este
256 backbone fold and the use of an active site aspartate residue to mediate catalysis with the 4-hydrox
257 ctivity whereas conversion of other selected aspartate residues to alanine had less effect, consisten
260 that require accurate processing at internal aspartate residues to generate the two-chain active enzy
261 ns that in turn require cleavage at internal aspartate residues to generate the two-subunit active en
262 otein through ester links from glutamate and aspartate residues to the heme 1- and 5-methyl groups an
263 rs, it has been assumed that two ion-binding aspartate residues transport the two protons that are la
265 sole constriction is lined by a ring of six aspartate residues, two in each of the three identical m
266 with 2 or more C-terminal glutamate (but not aspartate) residues (V(max) for 3 glutamates is approxim
267 trate-trapping mutant, in which an invariant aspartate residue was changed to alanine (D811A in PTPH1
268 d by site-directed mutagenesis in which each aspartate residue was individually replaced by glutamate
270 h conserved glycine 176 was replaced with an aspartate residue, was not able to support CO(2)-depende
271 ; in addition, the glutamate residue and one aspartate residue were mutated to glutamine and asparagi
272 Contrary to earlier findings where conserved aspartate residues were found crucial for iron release,
274 luster analysis (HCA), two glutamate and two aspartate residues were shown to be conserved in all of
275 e largely focused on invariant histidine and aspartate residues which may be involved in metal bindin
276 an unusual "bridging" glutamate but not the aspartate residue, which is believed to facilitate inter
277 osphotransfer from the sensor to a conserved aspartate residue, which is present in the amino terminu
278 omplished by removing the negatively charged aspartate residue, which normally participates in a conf
279 bution of electron density for the catalytic aspartate residues, which is discussed in relation to th
283 to enable alignment with oppositely charged aspartate residues within CD3zeta and activation of CD3z
285 nal studies showed that two highly conserved aspartate residues within putative transmembrane domains
286 for binding to trkB, two negatively charged aspartate residues within the 11 amino acid motif of FL
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