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1 ortant for the initial addition of the first glutamate residue.
2  caps the chain with a single alpha-linked l-glutamate residue.
3 ated version of the SH3 domain lacking a key glutamate residue.
4 -quinone cross-linked to the side chain of a glutamate residue.
5 obe the functional importance of a conserved glutamate residue.
6  was confirmed by mutagenesis of a conserved glutamate residue.
7 ion, where most myosins have an aspartate or glutamate residue.
8  interactions with the conserved active site glutamate residue.
9 han that of removal of a single gamma-linked glutamate residue.
10 ive to modifications in either metal-binding glutamate residue.
11 ase using this mechanism, is an aspartate or glutamate residue.
12 r is composed of six conserved histidine and glutamate residues.
13 terminal sequence mutation to add additional glutamate residues.
14 these roles frequently include aspartate and glutamate residues.
15 agenesis of a critical Lys(882) residue to a glutamate residue abolished all evidence of kinase activ
16                                            A glutamate residue adjacent to the box2 region in IFNLR1
17 lecular interaction between partially buried glutamate residues adjacent to the active site of Escher
18 es of the putative zipper were replaced with glutamate residues also failed to form stable rings.
19 C-tail clusters require Tha4's transmembrane glutamate residue and its amphipathic helix, both of whi
20 n, were mutated to alanine; in addition, the glutamate residue and one aspartate residue were mutated
21                                          The glutamate residue and the aromatic pteridine ring intera
22 om a neutral histidine residue to a negative glutamate residue and the disruption of the "dilysine tr
23 nts to a position that engages the catalytic glutamate residue and would block cognate protein substr
24 The mutants include the conversion of all 20 glutamate residues and 24 of the 25 aspartate residues i
25  cluster ligated by three histidine and four glutamate residues and activates dioxygen to perform its
26       Analysis of six conserved aspartate or glutamate residues and an additional 18 disease-causing
27 tions such as those caused by methylation of glutamate residues and by ligand-induced conformational
28 te-directed mutagenesis of nine aspartate or glutamate residues and four histidine residues to leucin
29         Cleavage occurs between cysteine and glutamate residues and results in a pyroglutamate produc
30 ormation: a gamma-glutamyl ligase adds 1-3 l-glutamate residues and the ATP-grasp-type ligase describ
31                  Mouse CCP5 removes multiple glutamate residues and the branch point glutamate from t
32 lpolyglutamate synthetase (FPGS), which adds glutamate residues, and gamma-glutamyl hydrolase (GGH),
33 ids 24-48) that is enriched in aspartate and glutamate residues, and we previously speculated that th
34 wn, it is unknown whether single or multiple glutamate residues are added following each folate bindi
35                                              Glutamate residues are commonly found surrounding the me
36 ach active site, the catalytic histidine and glutamate residues are contributed by one monomer, and t
37 s, and two cytoplasmic amino-terminal domain glutamate residues are essential for this inhibitory act
38  the clan of GH-A enzymes, the two catalytic glutamate residues are located on strand 4 (the acid/bas
39 tallographic data suggested that neighboring glutamate residues associated with two of these tyrosine
40     We recently reported the importance of a glutamate residue at position 257 in the binding and tra
41  the E257D mutant protein also showed that a glutamate residue at position 257 of this permease is sp
42  the torsinA gene resulting in the loss of a glutamate residue at position 302 or 303 (torsinA DeltaE
43       Furthermore, potentiation required the glutamate residue at position 493.
44 l ATP sensitivity, while the mutation of the glutamate residue at position 51 to glycine (E51G) did n
45 electrostatic repulsions between the peptide glutamate residue at position 7 and 152D of the MHC mole
46 sine deaminase (ADA) contains an active site glutamate residue at position-217 that is highly conserv
47 fm-AAs) through the coupling reaction with a glutamate residue at the C-terminus and a glycine at the
48 eolytic cleavage site to acquire the optimal glutamate residue at the N-terminus.
49 ts of the substrate specificity, including a glutamate residue at the rim of the channel entrance tha
50 tion E262 shows that the naturally occurring glutamate residue at this position provides the optimal
51  domain elements and containing "activating" glutamate residues at loop and autophosphorylation sites
52                                              Glutamate residues at positions 9 and 13 and a basic ami
53 nels have a ring of eight negatively charged glutamate residues at the entrance to the intracellular
54 apore H3 domain modified by two gamma-linked glutamate residues at the epsilon-amino group of the COO
55 pends not only on the presence of a specific glutamate residue but also the presence of Cl(-) ions.
56       DRONC autoprocesses itself following a glutamate residue, but processes a second caspase, drICE
57 f variants with all possible combinations of glutamate residues changed to glutamine and arginine cha
58 son with prokaryotic CLC shows that a gating glutamate residue changes conformation and suggests a ba
59 nation of mutations that included a specific glutamate residue, conserved in all known Tim9 and Tim10
60 P(1) study identified that the corresponding glutamate residue, conserved in all S1P receptors, ion p
61              Mutant analysis showed that the glutamate residue corresponding to Asp(85) in bacteriorh
62                                         This glutamate residue corresponds to one of the residues cau
63 .5 MOPS buffer, suggesting that the original glutamate residue could be substituted with other ioniza
64 st evidence that the conserved aspartate and glutamate residues could be involved in the catalysis or
65 the oligomerization domain) was mutated to a glutamate residue, CPS formed an (alphabeta)2 dimer in t
66 ded phytochrome superfamily has identified a glutamate residue critical for bilin binding.
67  (AdoHcy) at 2.8 A resolution and identify a glutamate residue critical for its monomethylation behav
68 ciated with the deletion of one of a pair of glutamate residues (DeltaE302/303) near the C terminus o
69  However, the replacement of Thr(318) with a glutamate residue demonstrated that the simple addition
70                          Loss of this single glutamate residue disrupts favorable electrostatic inter
71         However, the mutation of Tyr992 to a glutamate residue does not alter the receptor internaliz
72      Replacement of serines 152 and 153 with glutamate residues down-regulates the activity of NET1 a
73  V13'T in M2 together with neutralization of glutamate residues (E-1'A) and the adjacent insertion of
74 ribution due to a ring of negatively charged glutamate residues (E-2') at the narrow intracellular en
75                              The role of two glutamate residues (E164 and E144) in the active site of
76 d at the bottom of this cleft is a conserved glutamate residue (E173) that is in position to play an
77       Site-directed mutagenesis of these two glutamate residues (E181A and E182A) along with another
78                    Moreover, in RNase H, the glutamate residue E188 has been shown to be essential fo
79                                          Two glutamate residues, E199 and E408, align with the conser
80 nsport involves protonation of the conserved glutamate residue E373.
81 K+-binding site comprising four co-ordinated glutamate residues (E423 and E426 from each monomer) at
82               Three aspartate residues and a glutamate residue: E424, D498, D500 and D502, thought to
83 4938, D4945, D4953) with asparagine and four glutamate residues (E4942, E4948, E4952, E4955) with glu
84 ucrose synthase 3 (RSuS3), the two conserved glutamate residues (E678 and E686) in this motif and a p
85                    Replacement of two unique glutamate residues, E9 and E13, from the cytoplasmic ami
86                                         Four glutamate residues (EEEE locus) are essential for ion se
87 a channels contain a cluster of four charged glutamate residues (EEEE locus), which seem essential fo
88 mental evidence that protonation of Glu37, a glutamate residue embedded in a hydrophobic pocket of Hd
89    In the Ca(2+)-binding site, two essential glutamate residues exhibit different conformations compa
90 ration, which appears to prime the catalytic glutamate residue for ATP hydrolysis.
91                      The predicted catalytic glutamate residue for transglycosylase activity of bacte
92  on the top face of the Kelch domain and the glutamate residues form multiple hydrogen bonds with hig
93                      The invariant catalytic glutamate residue found in lysozyme and various bacteria
94                     Mutation of an invariant glutamate residue found within the catalytic domain of g
95 es; in particular, the conserved active site glutamate residues found in retaining glycosidases are p
96 S metal ion in a manner similar to that of a glutamate residue from collagen.
97                                 Removal of a glutamate residue from the binding site resulted in the
98 tive mutation in most cases is deletion of a glutamate residue from the carboxy terminal of torsinA,
99             The enzyme also removed multiple glutamate residues from side chains and C termini of pac
100 aGH) catalyze the hydrolysis of gamma-linked glutamate residues from the polyglutamyl of folates and
101 site-directed mutagenesis to include the two glutamate residues functioning in acid/base catalysis in
102 residues in Sso7d (D16 and D35) and a single glutamate residue (G54) showed significantly perturbed p
103 ng S2 cells, DIAP1 is cleaved by DRONC after glutamate residue Glu-205, located between the first and
104 a mechanism according to which the invariant glutamate residue (Glu-243) acts as a general base catal
105 rystal structure of T7 helicase shows that a glutamate residue (Glu-343), located at the subunit inte
106  docking studies have implicated a conserved glutamate residue (Glu-348) as a general base in the syn
107  Mutational analysis identified a titratable glutamate residue (Glu-536) in the linker between TM3 an
108 transient coordination to a highly conserved glutamate residue (Glu-67) during the catalytic cycle.
109       Mutagenesis of either of two conserved glutamate residues (Glu(66) and Glu(70)) within the Nudt
110 of betaS fibril structures indicate that key glutamate residues (Glu-31 and Glu-61) in these domains
111 vitro binding assays, we have identified two glutamate residues (Glu-849 and Glu-902) in beta(2)-adap
112  the role of the highly conserved C-terminal glutamate residue, Glu-590, on catalysis and malonyl-CoA
113 port the effects of mutations of active site glutamate residues, Glu(78) and Glu(122), on reactant bi
114 tions of two symmetry-related, lumen-exposed glutamate residues, Glu-122 and Glu-226.
115 e and that this caused the relocation of two glutamate residues (Glu181 and Glu182) into the proximit
116 diated by a single, evolutionarily conserved glutamate residue (Glu373) at a position where synapsin
117    As an alternative explanation, a specific glutamate residue (Glu59 in this flavodoxin), which is h
118  residues (His78, His161 and His225) and one glutamate residue (Glu77).
119 equence in Rad30, in which the aspartate and glutamate residues have each been changed to alanine.
120 is of a selection of conserved aspartate and glutamate residues, identified aspartate 145 as being es
121                  Replacement of the external glutamate residue in domain II by cysteine reduces sodiu
122 ified that catalyze the epimerization of the glutamate residue in L-Ala-D/L-Glu.
123 dentified the amino-terminal neighbor of the glutamate residue in motif III as a determinant of pore
124 tributed to an additional negatively charged glutamate residue in PaNhaP.
125  In addition, we show the importance of this glutamate residue in sigma(54).DNA conformation sensing,
126 esidue at the end of the beta10 strand and a glutamate residue in the beta1-beta2 linker.
127                                  A conserved glutamate residue in the inhibitory helix motif was prev
128 ant role in histone substrate binding, and a glutamate residue in the protein core as playing an esse
129    We have now identified a highly conserved glutamate residue in the transmembrane region of E. coli
130  enzyme for collagen and the importance of a glutamate residue in the unique catalytic triad (Ser(278
131 cid with only one methyl group less than the glutamate residue in the wild-type enzyme, resulted in c
132                            Mutations of this glutamate residue in Torpedo ray ClC channels alter gati
133 vidence of a H-bond between the ligand and a glutamate residue in transmembrane helix 3, which is con
134                                          The glutamate residue in turn might be further polarized thr
135 affects channel selectivity, suggesting that glutamate residues in both TM1 and TM3 face the lumen of
136                                      Exposed glutamate residues in CaM (Glu(11), Glu(14), Glu(84), an
137                                      Exposed glutamate residues in CaM (Glu-11, Glu-14, Glu-84, and G
138 GGCX), the enzyme responsible for converting glutamate residues in certain proteins to gamma-carboxyg
139              The enzyme has the expected two glutamate residues in close proximity to one another in
140 e show that a pair of invariant arginine and glutamate residues in each receptor alpha-subunit electr
141 ally mimicked for NCX3-B by mutating several glutamate residues in its cytoplasmic loop.
142 eriments show that aspargine, glutamine, and glutamate residues in MSP are perturbed by photooxidatio
143                 We find that two consecutive glutamate residues in NOD2 are required for interaction
144 , 5 histidine, and 4 of the 28 aspartate and glutamate residues in the 202 residue VanX protein.
145 f methylation and demethylation of conserved glutamate residues in the Bacillus subtilis chemotaxis r
146 ent Cxs shows the presence of well conserved glutamate residues in the C terminus of TM-1; only Cx26
147 rected mutagenesis of conserved arginine and glutamate residues in the parasite-specific third cGMP s
148 ein and produces F420with predominantly 5-7l-glutamate residues in the poly-gamma-glutamate tail.
149                                         Four glutamate residues in the prototypic gamma-class carboni
150  By comparison, mutagenesis of aspartate and glutamate residues in the putative linker regions showed
151 functionally replaces one of the active site glutamate residues in the reactions catalyzed by crotona
152 catalyzed methylation (and demethylation) of glutamate residues in the signaling domains of methyl-ac
153 his study, we assessed the role of conserved glutamate residues in the Walker B domain of the two ATP
154 yotic Na(+)-channels is the presence of four glutamate residues in their selectivity filter.
155 e side-chain resonances of the aspartate and glutamate residues in uniformly (13)C-labeled alpha-lyti
156 s have confirmed that this unusual "bridging glutamate" residue in CntA is essential in catalysis and
157 likely filled by the analogous aspartate (or glutamate) residue in protein disulfide isomerase, DsbA,
158 backbone of rabbit CYP4B1; (ii) this I-helix glutamate residue influences substrate orientation in th
159  with this possibility, merely introducing a glutamate residue into the active site of a PTPS protein
160 n outside the cyclodextrin cavity, while the glutamate residue is anchored in the interior of the alp
161 d region includes a GIXE motif, in which the glutamate residue is completely conserved among the perm
162 ur interpretation is that this region of the glutamate residue is crucial in relaying the activating
163 al modification - polyglutamylation, where a glutamate residue is enzymatically linked to the gamma-c
164                                            A glutamate residue is identified as the key contact with
165 activity, respectively, indicating that this glutamate residue is important but not critical to catal
166                        A conserved essential glutamate residue is involved in this interaction.
167 of an E809A mutant showed that the conserved glutamate residue is not relevant for the PatZ catalytic
168                                   However, a glutamate residue is not the only residue capable of fun
169 rom Escherichia coli indicate an unspecified glutamate residue is phosphorylated.
170                We show that a single anionic glutamate residue is responsible for maintaining the dis
171 de that the steric hindrance provided by the glutamate residue is responsible for the heme orientatio
172        The water molecule, which bridges two glutamate residues, is reminiscent of the enolase active
173 nt protein shows that the negatively charged glutamate residue lies on the surface of the N-terminal
174         However, mutation at two consecutive glutamate residues located within the hinge between the
175     Glutamine substitutions in two conserved glutamate residues, located within predicted transmembra
176 erefore, the protonation of aspartate and/or glutamate residues must provide an additional driving fo
177 ene, which changes the charge at a conserved glutamate residue near the outer mouth of the pore, has
178 ing and selectivity, a set of four conserved glutamate residues near the external mouth of the pore.
179        These roles include polarization by a glutamate residue of a water molecule for the attack on
180                              We found that a glutamate residue of GIRK2 (E315), located on a hydropho
181  mutagenesis, we demonstrated that the first glutamate residue of the conserved DEIDFEFL motif (E97)
182                                          The glutamate residue of the HXE motif is catalytically requ
183 7 transgenes were mutagenized to replace the glutamate residue of the HXE motif, and transgenic plant
184 the posttranslational modification of select glutamate residues of its vitamin K-dependent substrates
185  the mannitol permease and the corresponding glutamate residues of other PTS permeases play important
186 out the spatial arrangement of two conserved glutamate residues of rat liver enoyl-CoA hydratase to w
187          In vertebrates, the modification of glutamate residues of target proteins is facilitated by
188 e of Glu181, the second of the two invariant glutamate residues of the double E loop that coordinate
189 lpha-helix-turn-beta-strand motifs, with the glutamate residues of the EEEE motif located in the turn
190                  Furthermore, we show that a glutamate residue on E3 is involved in catalyzing ubiqui
191 from its catalytic histidine to aspartate or glutamate residues on 43-kDa membrane proteins.
192                                    A ring of glutamate residues on its extracellular side forms the s
193                 Along with neutralization of glutamate residues on the B loop, these changes cause a
194 in ligation with the burial of three charged glutamate residues on the same helix.
195            The high density of aspartate and glutamate residues on the surface follow a helical patte
196 , we measured acid dissociation constants of glutamate residues on troponin C and of histidine on ske
197             These results indicate that both glutamate residues play crucial roles in the hydration c
198 2 form extensive hydrogen-bond networks with glutamate residues predominantly in the unstructured, ac
199 3 into the FtsY active site orients a single glutamate residue provided by Ffh (E277), triggering GTP
200                  A close approach of two key glutamate residues provides an elegant mechanism for the
201          Substitution of arginine 282 with a glutamate residue (R282E-PepT1) gave a protein at the pl
202 ltetrahydropterin synthase (PTPS) in which a glutamate residue replaces or accompanies the catalytic
203 eaction in the absence of a highly conserved glutamate residue seen in Gcn5-related N-acetyltransfera
204  mutant in which histidine was replaced by a glutamate residue showed preferential heterodimer format
205 S of an altered conformation, in which a key glutamate residue swings out toward one of the heme prop
206                   The active site contains a glutamate residue that contacts the substrate, but, beca
207            The E166A mutant lacks a critical glutamate residue that has a key role in the deacylation
208               Each subunit contains a buried glutamate residue that is essential for function, and th
209 ime identified and characterized a catalytic glutamate residue that is involved in the energy transdu
210 is known only inferentially by two conserved glutamate residues that act as way-stations for H(+) in
211            MH1 and MH2 contain glutamine and glutamate residues that are subject to deamidation, meth
212 ficance of strategically placed arginine and glutamate residues that form interacting pairs in respon
213 tituting each of the four negatively charged glutamate residues that form the ion selectivity filter
214 e occurrence of carboxylate shifts involving glutamate residues that ligate the catalytic iron atoms.
215 res are characterised by conserved aspartate/glutamate residues that provide ligands for metal bindin
216 nsity of acidic residues, including specific glutamate residues that serve as receptor adaptation sit
217                     Ca channels rely on four glutamate residues (the EEEE locus), whose carboxyl side
218 E144A, we studied the effect of shifting the glutamate residue to all sites within helix V and three
219               We show that the enzyme adds a glutamate residue to both F(420)-0 and F(420)-1 in two d
220   In contrast, modification of either of the glutamate residues to alanine caused a dramatic decrease
221 he processive addition of approximately four glutamate residues to DDAH 4PteGlu 1.
222 atalyses the GTP-dependent addition of two L-glutamate residues to F(420)-0 to form F(420)-2.
223 ynthesis pathway by successive additions ofl-glutamate residues to F420-0, producing a poly-gamma-glu
224 nstrate that full-length FbiB adds multiplel-glutamate residues to F420-0in vitroto produce F420-5 af
225 -translational conversion of certain protein glutamate residues to gamma-carboxyglutamate.
226 ational modification, gamma-carboxylation of glutamate residues to Gla.
227 with the known ability of negatively charged glutamate residues to substitute functionally, in some c
228 FB, an enzyme that catalyzes the addition of glutamate residues to the folate molecule to form folylp
229 red", electrostatic networks of arginine and glutamate residues to the surfaces of the coiled-coil bu
230 ical disorder caused by deletion of a single glutamate residue (torsinA DeltaE) in the C-terminal reg
231 licated in substrate binding were changed to glutamate residues using PCR based site-directed mutagen
232  not completely abolished when the invariant glutamate residue was altered.
233    It was found that protonation of a single glutamate residue was enough to modify the conformation
234 t and for both mu and delta receptors when a glutamate residue was incorporated into the extracellula
235                                              Glutamate residues were also introduced mutagenically as
236  residue (F680) that resides between the two glutamate residues were changed by site-directed mutagen
237 1p and Phr2p was conducted and two conserved glutamate residues were shown to be essential for activi
238                         Hence, aspartate and glutamate residues were systematically substituted with
239 31 novel lipophilic TS inhibitors, lacking a glutamate residue, were synthesized; 26 of them had in c
240 s the charge-charge repulsion from the three glutamate residues when carbamate passes through the tun
241 -CRD interface, is coordinated by a triad of glutamate residues which are, to some extent, neutralise
242 ring aspartate substitutions for each of the glutamate residues which normally undergo gamma-carboxyl
243 een the positively charged drug and a buried glutamate residue, which is the key to cation selectivit
244  SASP-C of Bacillus megaterium two conserved glutamate residues, which form part of the germination p
245                          The presence of one glutamate residue with its chain directed toward the int
246 ring penetrates into the CD cavity while the glutamate residue with the aminobenzoic part of FA is ex
247  inability of K(+) to fit between a plane of glutamate residues with the preferred solvation geometry
248                        We further identify a glutamate residue within a conserved region adjacent to
249 in EmrE is defined by two negatively charged glutamate residues within a hydrophobic pocket formed fr
250     The ion selectivity locus comprises four glutamate residues within the channel's pore.
251  involves reversible methylation of specific glutamate residues within the cytoplasmic domains of met
252 modified by carboxyl methylation of specific glutamate residues within their cytoplasmic domains.

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