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1 ompared to the same interactions made by the Glu residue.
2 s similar to those of the negatively charged Glu residue.
3 , including the invariant putative catalytic Glu residue.
4 c+59 ions may also be generated at the gamma-Glu residue.
5 12 was substituted by the negatively charged Glu residue.
6 for PepB are peptides with N-terminal Asp or Glu residues.
7 gen bonding changes of additional Asp and/or Glu residues.
8 rahedrally bound by symmetry-related His and Glu residues.
9 Glu-Xaa-Xaa-His sequences and by two further Glu residues.
10 carboxyl groups from these conserved Asp and Glu residues.
11  were used to achieve a selective signal for Glu residues.
12 AMPylases with conserved active site Ser-His-Glu residues.
13 hich identified a catalytic triad of Tyr-His-Glu residues.
14 s contain a high percentage of Arg, Lys, and Glu residues.
15  and tyrosine phosphorylation sites from Asp/Glu residues.
16 ific nor without interference from the gamma-Glu residues.
17 meters for confident identification of gamma-Glu residues.
18 istence and locate the position of the gamma-Glu residues.
19  coil structure and sequence spacing of Asp, Glu residues.
20 arboxy terminus and alternating Neu2en and L-Glu residues.
21  the carboxylate groups of four Asp and four Glu residues.
22 ding five Cys, three His, nine Asp and eight Glu residues.
23 hare the common sequence Val-Val-Cys-Met-Ile-Glu (residues 178-183).
24 th the most abundant peptide commencing with Glu (residue 3 in Abeta1-40/1-42) that is present as pyr
25                    The clustering of Asp and Glu residues along the sequence was suggested to limit p
26 nteract favorably only with surface e' or g' Glu residues also impart structural uniqueness to a desi
27 nesis was used to replace Ser14 with Asp and Glu residues, analogs of the phosphoserine, that might b
28 ond network that includes water molecules, a Glu residue, and an Asn residue.
29  get labeled at their C-terminus, at Asp and Glu residues, and at carboxymethylated cysteine residues
30 , which contains two sets of two consecutive Glu residues, and fibrinopeptide A and fibrinopeptide B,
31     The pK(a) values of many solvent-exposed Glu residues are anomalously high and close to the bindi
32                                        These Glu residues are close to one another on the surface of
33 clear Zn coordination motif in which His and Glu residues are rigidly placed in a tetrahedral geometr
34 of a high percentage (>75%) of Arg, Lys, and Glu residues, are exceptions to this rule but have been
35 lf-channel and subsequent deprotonation of a Glu residue at a luminal half-channel.
36 n to class I sequences, which must display a Glu residue at P-3 and a Thr residue at P-2 By means of
37                                        (1) A Glu residue at position 2 of the gp41 fusion peptide is
38                                The conserved Glu residue at position 5 (E5) of mature (pseudo)pilins
39 , but there is an absolute requirement for a Glu residue at position 6.
40 sis-driven rotation causing protonation of a Glu residue at the cytoplasmic half-channel and subseque
41          A systematic study of Lys, Asp, and Glu residues at 25 internal positions in staphylococcal
42                               PAI-1 contains Glu residues at both the P4' and P5' positions, and prev
43                        Undercarboxylation of Glu residues at positions 33 and 34 may result in an und
44 p in FXa is highly acidic and contains three Glu residues at positions 36, 37, and 39.
45 op is highly acidic in FXa, containing three Glu residues at positions 36, 37, and 39.
46 X-ray quality crystals, are bound to His and Glu residues at the crystal packing interfaces of both s
47 e very similar for the central P2 Val to P2' Glu residues, but show more variation for the distal P3
48  show that substitution of the PsbX C-domain Glu residues by Val leads to a burial of the cleavage si
49 s alpha to the side-chain carboxylate of Asp/Glu residues C-terminal to the Cys residues.
50                                      The two Glu residues can be replaced with neutral or with positi
51        We propose that the engineered Asp or Glu residue changes the cofactor chemistry by stabilizin
52 n the conserved Nudix motif and is missing a Glu residue characteristic of the Nudix signature sequen
53                          Here, we identify a Glu residue conserved in B' regulatory subunits that is
54  contacts the gamma-phosphate of ATP and the Glu residue contacts a basic residue located in the pept
55 s known from earlier work that two conserved Glu residues, designated "catalytic carboxylates," are c
56              Furthermore, amidation of the d-Glu residue did not alter NOD2 activation.
57 extent Gln-450) to Ala, Asn, or Met (but not Glu) residues disrupt a bifurcated hydrogen bond between
58       Mature conantokin-G peptide containing Glu residues (E.Con-G) in place of Gla is a poor substra
59 upling/sensing requires two highly conserved Glu residues (E171 and E175) instead of one (E175) as im
60 l activity was localized to an extracellular Glu residue (E600) in the region linking the fifth trans
61 ghly active on glutathione, transferring its Glu residue either to a water molecule or to the Gly-L-L
62 nstrate a role for CCP1 in the processing of Glu residues from beta- as well as alpha-tubulin in vitr
63 wo Cys residues from one subunit and His and Glu residues from the other.
64                    In addition, CCP1 removed Glu residues from the polyglutamyl side chains of porcin
65 entre was coordinated by the two His and two Glu residues from two conserved Glu-Xaa-Xaa-His sequence
66 nal receiver motif of AccR to a phosphomimic Glu residue generates a constitutively active derivative
67 usters of Glu residues to gamma-carboxylated Glu residues (Glas) in VKD proteins, which is required f
68      By homology modeling, we identified two Glu residues (Glu-145 and Glu-172) in the second extrace
69 ce of water, with only the carboxy groups on Glu residues hydrated.
70 racellular channel entrance near the ring of Glu residues identified in the crystal structure, wherea
71 smatch-containing DNA duplex reveal that the Glu residue in a conserved Phe-X-Glu motif participates
72 nism that depends on its C2 domain, a unique Glu residue in its activation loop, intrinsic catalytic
73 ed, a RIG-I mutant carrying a phosphomimetic Glu residue in place of Thr-170 loses TRIM25 binding, Ly
74 ctional ligation; and (c) incorporation of a Glu residue in the assembly module of one machine to ena
75 revealing the chemical participation of this Glu residue in the catalytic mechanism.
76 tudies reveal a novel role for the conserved Glu residue in the establishment of mismatch discriminat
77                         Mutation of a single Glu residue in the S3-S4 linker and a His residue in the
78 in 101 (Hsp101) gene, converting a conserved Glu residue in the second ATP-binding domain to a Lys re
79                                          The Glu residue in this peptide was required for activity, a
80 Ser/Thr residues with negatively charged Asp/Glu residues in different regions of the protein.
81 t the involvement of invariant Ser, His, and Glu residues in metal coordination.
82 s region that form salt bridges with Asp and Glu residues in NEIL1.
83 ptide activity, we hypothesized that Asp and Glu residues in pro-Crp4(20-43) neutralize Crp4 Arg side
84                           N-terminal Gln and Glu residues in proteins or peptides have been reported
85 en-bond number for buried, protonated Asp or Glu residues in proteins.
86                              Mutation of the Glu residues in the EX(7)E motif of the N-terminal WbdA(
87  N-terminal five positions, a lack of Asp or Glu residues in the first 12 positions, and amphipathici
88    Finally, we show that substitution of the Glu residues in the lumenal A2 loop of the PsbY polyprot
89                 In contrast, mutation of the Glu residues in the motif of the C-terminal WbdA(O9a) do
90 a(2+) binding was perturbed when the Asp and Glu residues in the motif were substituted by alanine.
91 to from favorable interactions with g' or e' Glu residues in the parallel and antiparallel orientatio
92 S6 were mutated to alanine and the conserved Glu residues in the pore region of each homologous domai
93 e side-chain carboxyl carbons of all Asp and Glu residues in the reduced and oxidized states of human
94 sts that this region and, more specifically, Glu residues in the repeats may be important in regulati
95                                          The Glu residues in the transforming isolates often exhibite
96      A mutagenic survey of all eight Asp and Glu residues in this region reveals that only two (E376
97 arboxylase that uses the base to carboxylate Glu residues in VKD proteins, rendering them active in h
98                Quantitation of gla, asp, and glu residues indicated 3 mol gla/mol carboxylase.
99 at is critical for inactivation, MscSP has a Glu residue instead of an Asn in a position that was rec
100 n bond network the neurokinin-1 has a unique Glu residue instead of the highly conserved AspII:10 (2.
101   We propose that mutations of the catalytic Glu residues interfere with formation and characteristic
102 separated from peptides with multiple Asp or Glu residues, interfering with the identification of pho
103            Deprotonation of at least one Asp/Glu residue is detected in the transducer-free receptor
104 localization, of HMA4 in planta, whereas the Glu residue is important but not essential.
105 a measurable rate, indicating that the gamma-Glu residue is important for efficient transport.
106 , a cyclization product of N-terminal Gln or Glu residues, is a widespread post-translational modific
107 in, a peptide that contains a string of five Glu residues, is an excellent substrate for meprin beta,
108 eptide indicates that the first two flanking Glu residues lie in a position favorable to form salt br
109 esenting binding of excess Cd(II) to surface Glu residues located at the helical interfaces.
110 tion of the phosphorylation sites to Asp and Glu residues mimicked the effect of receptor phosphoryla
111    Mutation of these sites to phosphomimetic Glu residues negatively shifted I(Na) availability witho
112 on of proton-carrying Glu residues, with the Glu residue of subunit c'' interacting with Arg735 of su
113          Our results suggest that the second Glu residue of the EX7E motif in Gpi3p is of greater imp
114 rmed between the Lys residues of FPR and Asp/Glu residues of FdI.
115 e interaction between a highly conserved Trp/Glu residue pair in the lower pore is detrimental to gat
116 osine-1 phosphate (S1P) to conserved Arg and Glu residues present at the extracellular face of the th
117       On the other hand, mutation of Met and Glu residues proposed to be part of the metal exit site
118 matic (Phe, Tyr, Trp) or negatively charged (Glu) residues reduce V(1b) affinity.
119  a form of alpha-tubulin with two C-terminal Glu residues removed (delta3-tubulin).
120           Substitution of Asp(313) to His or Glu residues restored pH sensitivity of the receptor.
121 ll the side chain carboxyl groups of Asp and Glu residues revealed that Asp 23 and Glu 9 have an upsh
122                              The presence of Glu residue(s) may be inferred from the observation of a
123 of aspartic acid (Asp) and/or glutamic acid (Glu) residues, since their negatively charged side chain
124                          Most importantly, a Glu residue situated near the peroxide binding site coul
125                In the absence of Cd(II), the Glu residues stabilize the three-helical structure thoug
126 the active site to form a salt bridge with a Glu residue that is conserved in all astacins.
127 cteria identified 10 conserved His, Asp, and Glu residues that might play catalytic roles.
128 h includes the previously identified Asp and Glu residues, that is required for efficient exit of VSV
129         Using transmembrane domains with two Glu residues, the spacing between these was systematical
130                                    Two of 25 Glu residues titrated with normal pK(a) near 4.5; the ot
131 essor mutant enabling an unidentified Asp or Glu residue to substitute for Glu96 in positioning Mg2+
132 inding, we have mutated 11 conserved Asp and Glu residues to Ala in Escherichia coli IMPDH.
133 ion with atomic accuracy, preorganizing four Glu residues to form the desired dinuclear Cu(II) center
134 ndent (VKD) carboxylase converts clusters of Glu residues to gamma-carboxylated Glu residues (Glas) i
135 ne in a manner that allows conserved Lys and Glu residues to interact with the zwitterionic headgroup
136 rg/Lys residues were changed to Asp, and Asp/Glu residues to Lys.
137                                Change of the Glu residues to other amino acids results in reduction o
138  the differentiation of the alpha- and gamma-Glu residues, using three human Crystallin peptides (alp
139  zinc binding site involving two His and one Glu residue was identified crystallographically in the N
140 ive atypical NAT harboring a catalytic triad Glu residue was recently identified in Bacillus cereus (
141       The role of the strictly conserved His-Glu residues was evaluated by site-directed mutagenesis.
142 -A and FLAG-hkor-EE, in which one Ala or two Glu residues were added to the C terminus, respectively.
143      Similar results were also obtained when Glu residues were replaced with Ala (E556A and E1201A).
144 terminal flanking sequence, and a downstream Glu residue, were found to be important for DQ2 binding.
145  activities localized six additional Asp and Glu residues which reduced Ni(2+) transport by >90% when
146 de bond predominantly on the carboxy side of Glu residues while hydrolysis on the carboxyl side of As
147 ed form is polyglutamylated with one to four Glu residues, while the Delta2 tubulin is polyglycylated
148 n asymmetric distribution of proton-carrying Glu residues, with the Glu residue of subunit c'' intera
149  negative protein pocket (four conserved Asp/Glu residues within 12 A) and the dielectric of the prot
150                                          Key Glu residues within a Csm1 loop segment of Csm(crRNA) ad
151  These results demonstrated that some of the Glu residues within the repeats can have significant eff
152  were unique in that they contained multiple Glu residues within the transmembrane domain.

 
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