ライフサイエンスコーパス: asparagine residue

1 i in which His 353 has been replaced with an asparagine residue.

2 tively more stable than those containing the asparagine residue.

3 A protein in which Asp100 was replaced by an asparagine residue.

4 ch is consistent with the modification of an asparagine residue.

5 ive site histidine has been replaced with an asparagine residue.

6 modifications, including N-glycosylation of asparagine residues.

7 in or peptides resulting from deamidation of asparagine residues.

8 ed for the related motifs with aspartate and asparagine residues.

9 ecognition motifs, lacking both tyrosine and asparagine residues.

10 on and a flip in the orientation of two core asparagine residues.

11 ide-activated monosaccharides to glycosylate asparagine residues.

12 tact when Asp506 and Asp571 are mutated into asparagine residues.

13 g units that feature conserved glutamine and asparagine residues.

14 ay be a result of nonenzymatic truncation at asparagine residues.

15 both of which were replaced individually to asparagine residues.

16 ly reported the extracellular orientation of asparagine residues 182, 239, and 298 of the P2X2 recept

17 d that the lumenal domain is glycosylated at asparagine residues 2249 and 2252.

18 Asparagine residues 246 and 259 were completely deamidat

19 Site-directed mutagenesis of conserved asparagine residue 301 abolished esterase activity but p

20 ined by using site-directed mutagenesis that asparagine residues 40, 88, and 96 of rat ZIP8 are glyco

21 Asparagine residues 481 and 501 in the receptor-binding

22 EDTA treatment, by a cleavage that occurs at asparagine residue 681.

23 has seven potential N-glycosylation sites at asparagine residues 73, 226, 291, 333, 375, 429, and 458

24 osylation site of triadin 1 was localized to asparagine residue 75, and its bitopic arrangement in th

25 at the three remaining glycosylation sites, asparagine residues 96, 155, and 192, in each of the two

26 bond that normally forms between the beta102 asparagine residue and the alpha94 aspartate residue in

27 sidic linkages with glucose and galactose at asparagine residues and di-glucose linkages at sites of

28 Most reported inteins have a C-terminal asparagine residue, and it has been shown that cyclizati

29 Nonetheless, this asparagine residue appears to constitute an important co

30 activity, but only mutants of two invariant asparagine residues are completely inactive even in the

31 m intramolecular cyclization of glutamine or asparagine residues, are physiological degrons on substr

32 with AP sites and identifies an active site asparagine residue as an important component of AP site

33 An asparagine residue (Asn-106) in transmembrane segment 2

34 ll known mammalian orthologs of AQP6 have an asparagine residue (Asn-60) at the position correspondin

35 Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosyl

36 erved element of the type 1 architecture, an asparagine residue (Asn38) adjacent to one of the ligati

37 An asparagine residue (Asn485) at the active site is believ

38 t not for DNA binding, and that an invariant asparagine residue (Asn73) is required for optimal activ

39 empferol, consistent with the presence of an asparagine residue at a location known to determine subs

40 finity toward gallamine, suggesting that the asparagine residue at M(2)(419) is responsible for galla

41 Misincorporation of an asparagine residue at multiple serine positions was dete

42 between His119 and either an aspartate or an asparagine residue at position 121.

43 absence of hydrogen bonding with a conserved asparagine residue at position 132.

44 ng the -1 and +1 amino acids relative to the asparagine residue at position 162.

45 -binding protein Rac (Rac N17, containing an asparagine residue at position 17) was found to block v-

46 missense mutation replacing a lysine with an asparagine residue at position 201 (K201N) of STAT1.

47 n 1 reveals that a glycan emanating from the asparagine residue at position 25 (Asn-25) is located wi

48 e, substitution of a cysteine residue for an asparagine residue at position 260 of the cyclin T2a and

49 : A/WSN/33; N31S-M2WSN, a mutant in which an asparagine residue at position 31 in the M2 TM domain wa

50 tion 101 changed to cysteine (R101C), or the asparagine residue at position 414 changed to serine (N4

51 gene, leading to inclusion of an additional asparagine residue at position 417 (N417ins).

52 In this study, the conserved asparagine residue at position 510 in choline oxidase wa

53 A mutation of a highly conserved asparagine residue at position 70 (N70A) delays ribosome

54 Amino acid substitutions of the asparagine residue at position 72, which is located at t

55 ral or cationic residue at position 91 or an asparagine residue at position 89 virtually eliminated t

56 other Db-binding peptides by its lack of an asparagine residue at position five, which had been prev

57 We propose that the asparagine residue at the contact point between TM2 and

58 Hydroxylation at an asparagine residue at the COOH-terminal activation domai

59 They include asparagine residues at amino acid positions 109, 118, 11

60 our Hex(8-16)GlcNAc2 modifications involving asparagine residues at positions 20, 25, 141, and 181.

61 A nuclease A in vitro after phenylalanine or asparagine residues at the -1 position.

62 ties determined by the positioning of buried asparagine residues at the a positions.

63 y introducing multiple negatively charged or asparagine residues at the edges of CDR3, whereas other

64 mutagenesis to replace six deamidation-prone asparagine residues, at positions 408, 466, 537, 601, 71

65 We also show that N-glycosylation of asparagine residues blocks AEP action in vitro.

66 Peptides with deamidation sites at asparagine residues but lacking a typical asparagine-X-s

67 nsive modifications, including aspartate and asparagine residue C3-hydroxylations catalyzed by the 2-

68 function and suggest that introduction of an asparagine residue can cause sufficient stabilization of

69 Previous studies have demonstrated that asparagine residues can drive transmembrane helix associ

70 Determination of the asparagine residues carrying carbohydrate moieties in PD

71 Mutations in Walker A asparagine residues cause a severe reduction in substrat

72 e chains make base-specific contacts, and an asparagine residue contacts a G.A base pair.

73 tic subunits so far characterized contain an asparagine residue corresponding to residue 681 of CelS.

74 In addition, we identified asparagine residues essential for TSC2 GAP activity.

75 t because the decisive role of the conserved asparagine residue for determining sugar specificity has

76 dolichylpyrophosphate oligosaccharides to an asparagine residue found in the sequon Asn-Xaa-Thr/Ser o

77 nding of the conserved histidine, lysine and asparagine residues found among all PLD family members.

78 n-enriched antibody population showed that 4 asparagine residues: heavy chain Asn-162, Asn-360, and l

79 e at position 355 (T355) is replaced with an asparagine residue (i.e., a T355N mutant).

80 position of this fragment, bridging to a key asparagine residue, improving enzyme inhibition, and lea

81 Deamidation of one specific asparagine residue in an alpha/beta-type small, acid-sol

82 e activity, as did mutation of the conserved asparagine residue in motif C, an observation indicating

83 that would result in the substitution of an asparagine residue in place of aspartic acid at position

84 dent acyltransferase and identified a unique asparagine residue in the acyltransferase domain of KATm

85 Replacing Arg172 with an asparagine residue in the APX3M background generates a m

86 copper-dependent C(beta)-hydroxylation of an asparagine residue in the concatemeric repeats, followed

87 the transfer of a carbohydrate moiety to an asparagine residue in the consensus sequence Asn-Xaa-Thr

88 n in E2 enzymes remains unclear, although an asparagine residue in the conserved HPN motif of E2 enzy

89 Both patients harbour deletion of an asparagine residue in the epsilon subunit (epsilonN436de

90 saC(N92A), with a substitution of a critical asparagine residue in the kinase domain, we infer that t

91 Mutation of an invariant asparagine residue in the N-terminal extension, however,

92 idney 293 cells, Orai1 is glycosylated at an asparagine residue in the predicted second extracellular

93 T2 N722S mutation) which targets a conserved asparagine residue in the second PDZ domain of Mint2 tha

94 We have identified a critical asparagine residue in the second TM helix of PhoQ.

95 erature-sensitive mutant, a highly conserved asparagine residue in the sensor I motif was changed to

96 inked oligosaccharide and its transfer to an asparagine residue in the sequon NX(S/T) of a secreted p

97 gests a more specific role for the wild-type asparagine residue in the utilization of isopropylmalate

98 echanism, involving the outward motion of an asparagine residue in transmembrane helix 3, might be a

99 ariants had a mutation at either a conserved asparagine residue in transmembrane helix 8 or a threoni

100 ent of Ca(2+) Remarkably, replacing a single asparagine residue in ZnT10 (Asp-43) with threonine (ZnT

101 tuted both separately and simultaneously the asparagine residues in all three putative N-linked glyco

102 onal glycosylation of specific extracellular asparagine residues in Ca(V)3.2 channels accelerates cur

103 The reactivity of asparagine residues in Cu, Zn superoxide dismutase (SOD1

104 alyzes hydroxylations of conserved aspartate/asparagine residues in epidermal growth factor-like doma

105 IF (FIH) catalyzes the beta-hydroxylation of asparagine residues in HIF-alpha transcription factors a

106 l as the donor for N-linked glycosylation of asparagine residues in N-X-T/S consensus sites in newly

107 h transfers preassembled glycans to specific asparagine residues in target proteins.

108 We show that the serine and asparagine residues in the G5 motif likely play a role i

109 erred by an increased number of arginine and asparagine residues in the heavy chain third complementa

110 Mass spectrometry analysis identified two asparagine residues in the helicase 2i domain of RIG-I t

111 sults suggest a vital role for the conserved asparagine residues in the leucine-rich repeats of GP Ib

112 endopeptidase (AEP), which targets different asparagine residues in the lumenal domain of human and m

113 nown that N-linked glycans usually attach to asparagine residues in the N-X-S/T motifs of proteins.

114 Although asparagine residues in the pore-forming M2 regions of NR

115 attachment of an oligosaccharide to selected asparagine residues in the sequence N-X-S/T (X not equal

116 ized computational methods to identify three asparagine residues in wild-type (WT) SOD1 (i.e., N26, N

117 ite-directed mutagenesis of the glycosylated asparagine residues indicated that glycosylation of the

118 covery of proteins that cleave themselves at asparagine residues indicates that not all peptide bond

119 vated EcPlt toxin modifies a proximal lysine/asparagine residue instead.

120 -stage pentapeptide in order to transform an asparagine residue into a diaminopropanoic acid residue.

121 ion was predicted to result in conversion of asparagine residues into aspartic acid residues.

122 A highly conserved asparagine residue is contained in the consensus site se

123 Here we show that a strictly conserved E2 asparagine residue is critical for catalysis of E2- and

124 A conserved CTE asparagine residue is required for ubiquitylation and de

125 for a mutant retropeptide, in which a single asparagine residue is restored to the characteristic hep

126 lin showed that deamidation of glutamine and asparagine residues is a principal modification.

127 eraction between the D-loop aspartate and an asparagine residue located in Walker A loop of the oppos

128 The cleavage is at a specific asparagine residue located within CDR1 and occurs with c

129 e at sites located close to the glycosylated asparagine residue may result from steric blocking by th

130 ge-dependent deamidation of glutamine and/or asparagine residues may play an important role in the tu

131 ary N-linked oligosaccharide attached to the asparagine residue N45.

132 r study on one peptide (PepB2) pinpointed an asparagine residue necessary for CPP activity.

133 gosaccharide structures can be present on an asparagine residue not adhering to the consensus site mo

134 id-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is cat

135 The binding models suggest that the asparagine residue of the mutant receptor can form hydro

136 s hydrogen bonded to a conserved active site asparagine residue of the phosphate binding loop.

137 Deamidation of asparagine residues of biological pharmaceuticals is a m

138 on of C-terminal cyclic imides on C-terminal asparagine residues of CRBN substrates.

139 hat catalyses C3 hydroxylations of aspartate/asparagine residues of epidermal growth factor-like doma

140 d high mannose oligosaccharides onto certain asparagine residues of nascent polypeptides.

141 oligosaccharide from its lipid carrier onto asparagine residues of secretory proteins.

142 Asparagine residues of the consensus sequences (Asn-Xaa-

143 The side-chain pockets and conserved asparagine residues of the DR1 molecule are well-positio

144 on of a six-membered pyrimidone ring from an asparagine residue on the precursor peptide, and an acyl

145 been found to hydroxylate aspartic acid and asparagine residues on epidermal growth factor (EGF)-dom

146 ing the transfer of Glc(3)Man(9)GlcNAc(2) to asparagine residues on nascent polypeptides.

147 network (asparagine ladder) formed among the asparagine residues on the concave surfaces of neighbori

148 tudy suggest that spontaneous deamidation of asparagine residues predicted to occur during storage of

149 ubunit Zn2+-binding site, for the equivalent asparagine residue present in GlyR alpha2 and alpha3, re

150 site of CheB, Asp54, had been mutated to an asparagine residue, provided the enzyme was sufficiently

151 pendent hydroxylation of HIFs on proline and asparagine residues regulates protein stability and tran

152 ed by hydroxylation of conserved proline and asparagine residues, respectively.

153 elop a bidentate interaction with a critical asparagine residue resulted in the incorporation of a py

154 ecule coordinated by conserved histidine and asparagine residues seems to serve as the catalytic base

155 d tryptic digestion, only 4 of a possible 25 asparagine residues showed deamidation, demonstrating th

156 tructure of the mutant enzyme revealed a key asparagine residue that mediates a hydrogen bonding netw

157 s was originally identified, at an invariant asparagine residue that, when mutated in orthologous kin

158 nt receptor is related to the ability of the asparagine residue to hydrogen bond with the ether oxyge

159 of SKN-1A/Nrf1 by converting N-glycosylated asparagine residues to aspartate, which is necessary for

160 -dependent posttranslational modification of asparagine residues to aspartic acid.

161 tein by converting particular N-glycosylated asparagine residues to aspartic acid.

162 H-bond donor interactions of the NPA motif's asparagine residues to passing water molecules; observe

163 typically involved mutating the glycosylated asparagine residues to structurally similar glutamines o

164 ward vaccinia virus is dominated by a shared asparagine residue, together with other shared structura

165 sed phosphorylation site was converted to an asparagine residue was generated.

166 chain CDR2, which is the only CDR containing asparagine residues, was quite resistant to deamidation

167 ne of six highly conserved aspartic acid and asparagine residues were required for GTP binding.

168 T1 at position 261 rather than a tyrosine or asparagine residue which are found in the murine cyclin

169 asaccharide with a beta-glucose linked to an asparagine residue which is not located in the typical s

170 single point mutation of a highly conserved asparagine residue, which makes contact with the distal

171 ic acid (isoAsp) from aspartic acid (Asp) or asparagine residues, which tends to occur in long-lived

172 e uses nucleotide-activated sugars to modify asparagine residues with single monosaccharides.

173 an oligosaccharide from a lipid carrier onto asparagine residues within a consensus sequon is catalyz

174 en bloc transfer of the glycan to particular asparagine residues within acceptor proteins.

175 endrocyte glycoprotein, two Ags that contain asparagine residues within or in proximity to the releva

176 es reveals a length polymorphism in a run of asparagine residues within the coding region.

177 This modification targets asparagine residues within the consensus sequence, N-X-S