ライフサイエンスコーパス: Glu residue

1 12 was substituted by the negatively charged Glu residue.

2 ompared to the same interactions made by the Glu residue.

3 s similar to those of the negatively charged Glu residue.

4 , including the invariant putative catalytic Glu residue.

5 c+59 ions may also be generated at the gamma-Glu residue.

6 gen bonding changes of additional Asp and/or Glu residues.

7 rahedrally bound by symmetry-related His and Glu residues.

8 Glu-Xaa-Xaa-His sequences and by two further Glu residues.

9 carboxyl groups from these conserved Asp and Glu residues.

10 and tyrosine phosphorylation sites from Asp/Glu residues.

11 ific nor without interference from the gamma-Glu residues.

12 meters for confident identification of gamma-Glu residues.

13 istence and locate the position of the gamma-Glu residues.

14 coil structure and sequence spacing of Asp, Glu residues.

15 arboxy terminus and alternating Neu2en and L-Glu residues.

16 the carboxylate groups of four Asp and four Glu residues.

17 ding five Cys, three His, nine Asp and eight Glu residues.

18 for PepB are peptides with N-terminal Asp or Glu residues.

19 hare the common sequence Val-Val-Cys-Met-Ile-Glu (residues 178-183).

20 th the most abundant peptide commencing with Glu (residue 3 in Abeta1-40/1-42) that is present as pyr

21 The clustering of Asp and Glu residues along the sequence was suggested to limit p

22 nteract favorably only with surface e' or g' Glu residues also impart structural uniqueness to a desi

23 nesis was used to replace Ser14 with Asp and Glu residues, analogs of the phosphoserine, that might b

24 ond network that includes water molecules, a Glu residue, and an Asn residue.

25 get labeled at their C-terminus, at Asp and Glu residues, and at carboxymethylated cysteine residues

26 , which contains two sets of two consecutive Glu residues, and fibrinopeptide A and fibrinopeptide B,

27 The pK(a) values of many solvent-exposed Glu residues are anomalously high and close to the bindi

28 These Glu residues are close to one another on the surface of

29 lf-channel and subsequent deprotonation of a Glu residue at a luminal half-channel.

30 n to class I sequences, which must display a Glu residue at P-3 and a Thr residue at P-2 By means of

31 (1) A Glu residue at position 2 of the gp41 fusion peptide is

32 The conserved Glu residue at position 5 (E5) of mature (pseudo)pilins

33 , but there is an absolute requirement for a Glu residue at position 6.

34 sis-driven rotation causing protonation of a Glu residue at the cytoplasmic half-channel and subseque

35 A systematic study of Lys, Asp, and Glu residues at 25 internal positions in staphylococcal

36 PAI-1 contains Glu residues at both the P4' and P5' positions, and prev

37 Undercarboxylation of Glu residues at positions 33 and 34 may result in an und

38 p in FXa is highly acidic and contains three Glu residues at positions 36, 37, and 39.

39 op is highly acidic in FXa, containing three Glu residues at positions 36, 37, and 39.

40 X-ray quality crystals, are bound to His and Glu residues at the crystal packing interfaces of both s

41 e very similar for the central P2 Val to P2' Glu residues, but show more variation for the distal P3

42 show that substitution of the PsbX C-domain Glu residues by Val leads to a burial of the cleavage si

43 The two Glu residues can be replaced with neutral or with positi

44 We propose that the engineered Asp or Glu residue changes the cofactor chemistry by stabilizin

45 n the conserved Nudix motif and is missing a Glu residue characteristic of the Nudix signature sequen

46 Here, we identify a Glu residue conserved in B' regulatory subunits that is

47 contacts the gamma-phosphate of ATP and the Glu residue contacts a basic residue located in the pept

48 s known from earlier work that two conserved Glu residues, designated "catalytic carboxylates," are c

49 Furthermore, amidation of the d-Glu residue did not alter NOD2 activation.

50 extent Gln-450) to Ala, Asn, or Met (but not Glu) residues disrupt a bifurcated hydrogen bond between

51 Mature conantokin-G peptide containing Glu residues (E.Con-G) in place of Gla is a poor substra

52 l activity was localized to an extracellular Glu residue (E600) in the region linking the fifth trans

53 ghly active on glutathione, transferring its Glu residue either to a water molecule or to the Gly-L-L

54 nstrate a role for CCP1 in the processing of Glu residues from beta- as well as alpha-tubulin in vitr

55 In addition, CCP1 removed Glu residues from the polyglutamyl side chains of porcin

56 entre was coordinated by the two His and two Glu residues from two conserved Glu-Xaa-Xaa-His sequence

57 nal receiver motif of AccR to a phosphomimic Glu residue generates a constitutively active derivative

58 usters of Glu residues to gamma-carboxylated Glu residues (Glas) in VKD proteins, which is required f

59 By homology modeling, we identified two Glu residues (Glu-145 and Glu-172) in the second extrace

60 ce of water, with only the carboxy groups on Glu residues hydrated.

61 racellular channel entrance near the ring of Glu residues identified in the crystal structure, wherea

62 smatch-containing DNA duplex reveal that the Glu residue in a conserved Phe-X-Glu motif participates

63 nism that depends on its C2 domain, a unique Glu residue in its activation loop, intrinsic catalytic

64 ed, a RIG-I mutant carrying a phosphomimetic Glu residue in place of Thr-170 loses TRIM25 binding, Ly

65 revealing the chemical participation of this Glu residue in the catalytic mechanism.

66 tudies reveal a novel role for the conserved Glu residue in the establishment of mismatch discriminat

67 Mutation of a single Glu residue in the S3-S4 linker and a His residue in the

68 in 101 (Hsp101) gene, converting a conserved Glu residue in the second ATP-binding domain to a Lys re

69 The Glu residue in this peptide was required for activity, a

70 t the involvement of invariant Ser, His, and Glu residues in metal coordination.

71 s region that form salt bridges with Asp and Glu residues in NEIL1.

72 ptide activity, we hypothesized that Asp and Glu residues in pro-Crp4(20-43) neutralize Crp4 Arg side

73 N-terminal Gln and Glu residues in proteins or peptides have been reported

74 en-bond number for buried, protonated Asp or Glu residues in proteins.

75 Mutation of the Glu residues in the EX(7)E motif of the N-terminal WbdA(

76 N-terminal five positions, a lack of Asp or Glu residues in the first 12 positions, and amphipathici

77 Finally, we show that substitution of the Glu residues in the lumenal A2 loop of the PsbY polyprot

78 In contrast, mutation of the Glu residues in the motif of the C-terminal WbdA(O9a) do

79 to from favorable interactions with g' or e' Glu residues in the parallel and antiparallel orientatio

80 S6 were mutated to alanine and the conserved Glu residues in the pore region of each homologous domai

81 e side-chain carboxyl carbons of all Asp and Glu residues in the reduced and oxidized states of human

82 sts that this region and, more specifically, Glu residues in the repeats may be important in regulati

83 The Glu residues in the transforming isolates often exhibite

84 A mutagenic survey of all eight Asp and Glu residues in this region reveals that only two (E376

85 arboxylase that uses the base to carboxylate Glu residues in VKD proteins, rendering them active in h

86 Quantitation of gla, asp, and glu residues indicated 3 mol gla/mol carboxylase.

87 at is critical for inactivation, MscSP has a Glu residue instead of an Asn in a position that was rec

88 n bond network the neurokinin-1 has a unique Glu residue instead of the highly conserved AspII:10 (2.

89 We propose that mutations of the catalytic Glu residues interfere with formation and characteristic

90 separated from peptides with multiple Asp or Glu residues, interfering with the identification of pho

91 Deprotonation of at least one Asp/Glu residue is detected in the transducer-free receptor

92 localization, of HMA4 in planta, whereas the Glu residue is important but not essential.

93 a measurable rate, indicating that the gamma-Glu residue is important for efficient transport.

94 in, a peptide that contains a string of five Glu residues, is an excellent substrate for meprin beta,

95 eptide indicates that the first two flanking Glu residues lie in a position favorable to form salt br

96 esenting binding of excess Cd(II) to surface Glu residues located at the helical interfaces.

97 tion of the phosphorylation sites to Asp and Glu residues mimicked the effect of receptor phosphoryla

98 Mutation of these sites to phosphomimetic Glu residues negatively shifted I(Na) availability witho

99 on of proton-carrying Glu residues, with the Glu residue of subunit c'' interacting with Arg735 of su

100 Our results suggest that the second Glu residue of the EX7E motif in Gpi3p is of greater imp

101 rmed between the Lys residues of FPR and Asp/Glu residues of FdI.

102 osine-1 phosphate (S1P) to conserved Arg and Glu residues present at the extracellular face of the th

103 On the other hand, mutation of Met and Glu residues proposed to be part of the metal exit site

104 matic (Phe, Tyr, Trp) or negatively charged (Glu) residues reduce V(1b) affinity.

105 a form of alpha-tubulin with two C-terminal Glu residues removed (delta3-tubulin).

106 Substitution of Asp(313) to His or Glu residues restored pH sensitivity of the receptor.

107 ll the side chain carboxyl groups of Asp and Glu residues revealed that Asp 23 and Glu 9 have an upsh

108 The presence of Glu residue(s) may be inferred from the observation of a

109 of aspartic acid (Asp) and/or glutamic acid (Glu) residues, since their negatively charged side chain

110 Most importantly, a Glu residue situated near the peroxide binding site coul

111 In the absence of Cd(II), the Glu residues stabilize the three-helical structure thoug

112 the active site to form a salt bridge with a Glu residue that is conserved in all astacins.

113 cteria identified 10 conserved His, Asp, and Glu residues that might play catalytic roles.

114 h includes the previously identified Asp and Glu residues, that is required for efficient exit of VSV

115 Using transmembrane domains with two Glu residues, the spacing between these was systematical

116 Two of 25 Glu residues titrated with normal pK(a) near 4.5; the ot

117 essor mutant enabling an unidentified Asp or Glu residue to substitute for Glu96 in positioning Mg2+

118 inding, we have mutated 11 conserved Asp and Glu residues to Ala in Escherichia coli IMPDH.

119 ndent (VKD) carboxylase converts clusters of Glu residues to gamma-carboxylated Glu residues (Glas) i

120 ne in a manner that allows conserved Lys and Glu residues to interact with the zwitterionic headgroup

121 rg/Lys residues were changed to Asp, and Asp/Glu residues to Lys.

122 Change of the Glu residues to other amino acids results in reduction o

123 the differentiation of the alpha- and gamma-Glu residues, using three human Crystallin peptides (alp

124 zinc binding site involving two His and one Glu residue was identified crystallographically in the N

125 ive atypical NAT harboring a catalytic triad Glu residue was recently identified in Bacillus cereus (

126 The role of the strictly conserved His-Glu residues was evaluated by site-directed mutagenesis.

127 -A and FLAG-hkor-EE, in which one Ala or two Glu residues were added to the C terminus, respectively.

128 Similar results were also obtained when Glu residues were replaced with Ala (E556A and E1201A).

129 terminal flanking sequence, and a downstream Glu residue, were found to be important for DQ2 binding.

130 activities localized six additional Asp and Glu residues which reduced Ni(2+) transport by >90% when

131 de bond predominantly on the carboxy side of Glu residues while hydrolysis on the carboxyl side of As

132 ed form is polyglutamylated with one to four Glu residues, while the Delta2 tubulin is polyglycylated

133 n asymmetric distribution of proton-carrying Glu residues, with the Glu residue of subunit c'' intera

134 negative protein pocket (four conserved Asp/Glu residues within 12 A) and the dielectric of the prot

135 These results demonstrated that some of the Glu residues within the repeats can have significant eff

136 were unique in that they contained multiple Glu residues within the transmembrane domain.