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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 in or peptides resulting from deamidation of asparagine residues.
7 ed for the related motifs with aspartate and asparagine residues.
8 ecognition motifs, lacking both tyrosine and asparagine residues.
9 ide-activated monosaccharides to glycosylate asparagine residues.
10 g units that feature conserved glutamine and asparagine residues.
11 ay be a result of nonenzymatic truncation at asparagine residues.
12  both of which were replaced individually to asparagine residues.
13 ly reported the extracellular orientation of asparagine residues 182, 239, and 298 of the P2X2 recept
14 d that the lumenal domain is glycosylated at asparagine residues 2249 and 2252.
15                                              Asparagine residues 246 and 259 were completely deamidat
16       Site-directed mutagenesis of conserved asparagine residue 301 abolished esterase activity but p
17 ined by using site-directed mutagenesis that asparagine residues 40, 88, and 96 of rat ZIP8 are glyco
18 EDTA treatment, by a cleavage that occurs at asparagine residue 681.
19 has seven potential N-glycosylation sites at asparagine residues 73, 226, 291, 333, 375, 429, and 458
20 osylation site of triadin 1 was localized to asparagine residue 75, and its bitopic arrangement in th
21  at the three remaining glycosylation sites, asparagine residues 96, 155, and 192, in each of the two
22 bond that normally forms between the beta102 asparagine residue and the alpha94 aspartate residue in
23 sidic linkages with glucose and galactose at asparagine residues and di-glucose linkages at sites of
24      Most reported inteins have a C-terminal asparagine residue, and it has been shown that cyclizati
25                            Nonetheless, this asparagine residue appears to constitute an important co
26  activity, but only mutants of two invariant asparagine residues are completely inactive even in the
27  with AP sites and identifies an active site asparagine residue as an important component of AP site
28                                           An asparagine residue (Asn-106) in transmembrane segment 2
29 ll known mammalian orthologs of AQP6 have an asparagine residue (Asn-60) at the position correspondin
30  Site-directed mutagenesis revealed that two asparagine residues (Asn(585) and Asn(592)) are glycosyl
31 erved element of the type 1 architecture, an asparagine residue (Asn38) adjacent to one of the ligati
32                                           An asparagine residue (Asn485) at the active site is believ
33 t not for DNA binding, and that an invariant asparagine residue (Asn73) is required for optimal activ
34 empferol, consistent with the presence of an asparagine residue at a location known to determine subs
35 finity toward gallamine, suggesting that the asparagine residue at M(2)(419) is responsible for galla
36                       Misincorporation of an asparagine residue at multiple serine positions was dete
37 between His119 and either an aspartate or an asparagine residue at position 121.
38 between His119 and either an aspartate or an asparagine residue at position 121.
39 ng the -1 and +1 amino acids relative to the asparagine residue at position 162.
40 -binding protein Rac (Rac N17, containing an asparagine residue at position 17) was found to block v-
41 missense mutation replacing a lysine with an asparagine residue at position 201 (K201N) of STAT1.
42 n 1 reveals that a glycan emanating from the asparagine residue at position 25 (Asn-25) is located wi
43 e, substitution of a cysteine residue for an asparagine residue at position 260 of the cyclin T2a and
44 : A/WSN/33; N31S-M2WSN, a mutant in which an asparagine residue at position 31 in the M2 TM domain wa
45 tion 101 changed to cysteine (R101C), or the asparagine residue at position 414 changed to serine (N4
46                 In this study, the conserved asparagine residue at position 510 in choline oxidase wa
47             A mutation of a highly conserved asparagine residue at position 70 (N70A) delays ribosome
48              Amino acid substitutions of the asparagine residue at position 72, which is located at t
49 ral or cationic residue at position 91 or an asparagine residue at position 89 virtually eliminated t
50  other Db-binding peptides by its lack of an asparagine residue at position five, which had been prev
51                          We propose that the asparagine residue at the contact point between TM2 and
52                          Hydroxylation at an asparagine residue at the COOH-terminal activation domai
53                                 They include asparagine residues at amino acid positions 109, 118, 11
54 our Hex(8-16)GlcNAc2 modifications involving asparagine residues at positions 20, 25, 141, and 181.
55 A nuclease A in vitro after phenylalanine or asparagine residues at the -1 position.
56 ties determined by the positioning of buried asparagine residues at the a positions.
57 y introducing multiple negatively charged or asparagine residues at the edges of CDR3, whereas other
58 mutagenesis to replace six deamidation-prone asparagine residues, at positions 408, 466, 537, 601, 71
59         We also show that N-glycosylation of asparagine residues blocks AEP action in vitro.
60           Peptides with deamidation sites at asparagine residues but lacking a typical asparagine-X-s
61 function and suggest that introduction of an asparagine residue can cause sufficient stabilization of
62      Previous studies have demonstrated that asparagine residues can drive transmembrane helix associ
63                         Determination of the asparagine residues carrying carbohydrate moieties in PD
64 e chains make base-specific contacts, and an asparagine residue contacts a G.A base pair.
65 tic subunits so far characterized contain an asparagine residue corresponding to residue 681 of CelS.
66                   In addition, we identified asparagine residues essential for TSC2 GAP activity.
67 t because the decisive role of the conserved asparagine residue for determining sugar specificity has
68 dolichylpyrophosphate oligosaccharides to an asparagine residue found in the sequon Asn-Xaa-Thr/Ser o
69 nding of the conserved histidine, lysine and asparagine residues found among all PLD family members.
70 n-enriched antibody population showed that 4 asparagine residues: heavy chain Asn-162, Asn-360, and l
71 e at position 355 (T355) is replaced with an asparagine residue (i.e., a T355N mutant).
72 position of this fragment, bridging to a key asparagine residue, improving enzyme inhibition, and lea
73                  Deamidation of one specific asparagine residue in an alpha/beta-type small, acid-sol
74 e activity, as did mutation of the conserved asparagine residue in motif C, an observation indicating
75  that would result in the substitution of an asparagine residue in place of aspartic acid at position
76 dent acyltransferase and identified a unique asparagine residue in the acyltransferase domain of KATm
77                     Replacing Arg172 with an asparagine residue in the APX3M background generates a m
78  the transfer of a carbohydrate moiety to an asparagine residue in the consensus sequence Asn-Xaa-Thr
79         Both patients harbour deletion of an asparagine residue in the epsilon subunit (epsilonN436de
80 saC(N92A), with a substitution of a critical asparagine residue in the kinase domain, we infer that t
81                     Mutation of an invariant asparagine residue in the N-terminal extension, however,
82 idney 293 cells, Orai1 is glycosylated at an asparagine residue in the predicted second extracellular
83                We have identified a critical asparagine residue in the second TM helix of PhoQ.
84 erature-sensitive mutant, a highly conserved asparagine residue in the sensor I motif was changed to
85 inked oligosaccharide and its transfer to an asparagine residue in the sequon NX(S/T) of a secreted p
86 gests a more specific role for the wild-type asparagine residue in the utilization of isopropylmalate
87 ariants had a mutation at either a conserved asparagine residue in transmembrane helix 8 or a threoni
88 tuted both separately and simultaneously the asparagine residues in all three putative N-linked glyco
89 onal glycosylation of specific extracellular asparagine residues in Ca(V)3.2 channels accelerates cur
90                            The reactivity of asparagine residues in Cu, Zn superoxide dismutase (SOD1
91 IF (FIH) catalyzes the beta-hydroxylation of asparagine residues in HIF-alpha transcription factors a
92 l as the donor for N-linked glycosylation of asparagine residues in N-X-T/S consensus sites in newly
93 h transfers preassembled glycans to specific asparagine residues in target proteins.
94 erred by an increased number of arginine and asparagine residues in the heavy chain third complementa
95    Mass spectrometry analysis identified two asparagine residues in the helicase 2i domain of RIG-I t
96 sults suggest a vital role for the conserved asparagine residues in the leucine-rich repeats of GP Ib
97 endopeptidase (AEP), which targets different asparagine residues in the lumenal domain of human and m
98 nown that N-linked glycans usually attach to asparagine residues in the N-X-S/T motifs of proteins.
99                                     Although asparagine residues in the pore-forming M2 regions of NR
100 attachment of an oligosaccharide to selected asparagine residues in the sequence N-X-S/T (X not equal
101 ized computational methods to identify three asparagine residues in wild-type (WT) SOD1 (i.e., N26, N
102 covery of proteins that cleave themselves at asparagine residues indicates that not all peptide bond
103 vated EcPlt toxin modifies a proximal lysine/asparagine residue instead.
104 -stage pentapeptide in order to transform an asparagine residue into a diaminopropanoic acid residue.
105 ion was predicted to result in conversion of asparagine residues into aspartic acid residues.
106                           A highly conserved asparagine residue is contained in the consensus site se
107    Here we show that a strictly conserved E2 asparagine residue is critical for catalysis of E2- and
108                              A conserved CTE asparagine residue is required for ubiquitylation and de
109 for a mutant retropeptide, in which a single asparagine residue is restored to the characteristic hep
110 lin showed that deamidation of glutamine and asparagine residues is a principal modification.
111 eraction between the D-loop aspartate and an asparagine residue located in Walker A loop of the oppos
112                The cleavage is at a specific asparagine residue located within CDR1 and occurs with c
113 e at sites located close to the glycosylated asparagine residue may result from steric blocking by th
114 ge-dependent deamidation of glutamine and/or asparagine residues may play an important role in the tu
115 ary N-linked oligosaccharide attached to the asparagine residue N45.
116 r study on one peptide (PepB2) pinpointed an asparagine residue necessary for CPP activity.
117 gosaccharide structures can be present on an asparagine residue not adhering to the consensus site mo
118 id-linked oligosaccharide (LLO) donor to the asparagine residue of a nascent polypeptide chain is cat
119          The binding models suggest that the asparagine residue of the mutant receptor can form hydro
120 s hydrogen bonded to a conserved active site asparagine residue of the phosphate binding loop.
121                               Deamidation of asparagine residues of biological pharmaceuticals is a m
122 d high mannose oligosaccharides onto certain asparagine residues of nascent polypeptides.
123                                              Asparagine residues of the consensus sequences (Asn-Xaa-
124         The side-chain pockets and conserved asparagine residues of the DR1 molecule are well-positio
125  been found to hydroxylate aspartic acid and asparagine residues on epidermal growth factor (EGF)-dom
126 ing the transfer of Glc(3)Man(9)GlcNAc(2) to asparagine residues on nascent polypeptides.
127 network (asparagine ladder) formed among the asparagine residues on the concave surfaces of neighbori
128 tudy suggest that spontaneous deamidation of asparagine residues predicted to occur during storage of
129 ubunit Zn2+-binding site, for the equivalent asparagine residue present in GlyR alpha2 and alpha3, re
130  site of CheB, Asp54, had been mutated to an asparagine residue, provided the enzyme was sufficiently
131 ed by hydroxylation of conserved proline and asparagine residues, respectively.
132 elop a bidentate interaction with a critical asparagine residue resulted in the incorporation of a py
133 ecule coordinated by conserved histidine and asparagine residues seems to serve as the catalytic base
134 d tryptic digestion, only 4 of a possible 25 asparagine residues showed deamidation, demonstrating th
135 s was originally identified, at an invariant asparagine residue that, when mutated in orthologous kin
136 nt receptor is related to the ability of the asparagine residue to hydrogen bond with the ether oxyge
137 -dependent posttranslational modification of asparagine residues to aspartic acid.
138 H-bond donor interactions of the NPA motif's asparagine residues to passing water molecules; observe
139 typically involved mutating the glycosylated asparagine residues to structurally similar glutamines o
140 ward vaccinia virus is dominated by a shared asparagine residue, together with other shared structura
141 sed phosphorylation site was converted to an asparagine residue was generated.
142 ne of six highly conserved aspartic acid and asparagine residues were required for GTP binding.
143 T1 at position 261 rather than a tyrosine or asparagine residue which are found in the murine cyclin
144 asaccharide with a beta-glucose linked to an asparagine residue which is not located in the typical s
145 e uses nucleotide-activated sugars to modify asparagine residues with single monosaccharides.
146 an oligosaccharide from a lipid carrier onto asparagine residues within a consensus sequon is catalyz
147 en bloc transfer of the glycan to particular asparagine residues within acceptor proteins.
148 endrocyte glycoprotein, two Ags that contain asparagine residues within or in proximity to the releva
149 es reveals a length polymorphism in a run of asparagine residues within the coding region.

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