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1               The spontaneous degradation of asparaginyl and aspartyl residues to isoaspartyl residue
2                               Deamidation of asparaginyl and glutaminyl residues causes time-dependen
3 ssess the rare combination of discriminating asparaginyl and glutaminyl tRNA synthetase (AARS) togeth
4 es sequence and structural homology with the asparaginyl and histidinyl hydroxylase FIH-1 (factor inh
5  spontaneous and deleterious conversion of l-asparaginyl and l-aspartyl protein residues to l-iso-Asp
6                                            L-Asparaginyl and L-aspartyl residues in proteins are subj
7         Within proteins and peptides, both L-asparaginyl and L-aspartyl residues spontaneously degrad
8      FIH also catalyzes the hydroxylation of asparaginyl and other residues in ankyrin repeat domain-
9              AspH catalyses hydroxylation of asparaginyl- and aspartyl-residues in epidermal growth f
10            Many bacteria lack genes encoding asparaginyl- and/or glutaminyl-tRNA synthetase and conse
11 stability with respect to deamidation of the asparaginyl (Asn) residues in proteins is described.
12 art, mediated by a hydrogen bond between the asparaginyl beta-hydroxyl group and the side chain of a
13                        ASPH encodes aspartyl/asparaginyl beta-hydroxylase (ASPH), which has been foun
14 poxia-inducible factor (HIF)-1 (FIH-1) is an asparaginyl beta-hydroxylase enzyme that was initially f
15                  The S. typhimurium aspartyl/asparaginyl beta-hydroxylase homologue (designated lpxO)
16 ame(s) with similarity to mammalian aspartyl/asparaginyl beta-hydroxylases in bacteria known to make
17                                     A second asparaginyl beta-hydroxylation causes further stabilizat
18 l techniques are used to study the effect of asparaginyl beta-hydroxylation on the structure and stab
19 hysical insights into the mechanism by which asparaginyl beta-hydroxylation stabilizes the ARD protei
20                          The human aspartyl (asparaginyl) beta-hydroxylase (HAAH) is a highly conserv
21 ysis of several residues in bovine aspartyl (asparaginyl) beta-hydroxylase that are located in a regi
22 ed the antigen as the human form of aspartyl(asparaginyl)beta-hydroxylase.
23                                    Aspartyl-(asparaginyl)-beta-hydroxylase (ASPH) is a cell-surface e
24 ferating cell nuclear antigen, and aspartyl-(asparaginyl)-beta-hydroxylase, a gene associated with in
25 r isoD) via either aspartyl isomerization or asparaginyl deamidation alters protein structure and pot
26                                              Asparaginyl endopeptidase (AEP or legumain) is a lysosom
27  but not the terminal acyclic TI, depends on asparaginyl endopeptidase (AEP) for maturation.
28 ts AD pathologies, associated with C/EBPbeta/Asparaginyl endopeptidase (AEP) pathway upregulation, mi
29 ned competitive peptide inhibitors of B-cell asparaginyl endopeptidase (AEP) that specifically block
30                                              Asparaginyl endopeptidase (AEP) was shown to be involved
31 d approaches identified unique expression of asparaginyl endopeptidase (AEP), intercellular adhesion
32                                              Asparaginyl endopeptidase (AEP), which is overexpressed
33 nteric nervous system-specific expression of asparaginyl endopeptidase (AEP)-truncated alpha-syn and
34                                           An asparaginyl endopeptidase (legumain) also synergized wit
35  with kainic acid or pH 6.0 medium activated asparaginyl endopeptidase and consequently produced the
36 cemia as in diabetes, I2(PP2A) is cleaved by asparaginyl endopeptidase at Asn-175 into the N-terminal
37 he first time that legumain, a member of the asparaginyl endopeptidase family functioning as a stress
38                                              Asparaginyl endopeptidase from Alzheimer disease brain c
39                               Therefore, the asparaginyl endopeptidase is required for hexamer assemb
40     Here we show that the level of activated asparaginyl endopeptidase is significantly increased, an
41 gulates lysosomal cysteine proteases and the asparaginyl endopeptidase legumain.
42      Here, we showed that legumain, the only asparaginyl endopeptidase of the mammalian genome, is hi
43 phosphorylation of Tau, and the knockdown of asparaginyl endopeptidase with siRNA abolished this path
44              Expression of legumain, a novel asparaginyl endopeptidase, in tumors was identified from
45 cine, the mutants could be cyclized using an asparaginyl endopeptidase, in vitro with a yield of ~90%
46            A recombinant Oldenlandia affinis asparaginyl endopeptidase, OaAEP1, is promiscuous for in
47 ng the PD-1 signaling pathway and inhibiting asparaginyl endopeptidase, PsA Treg function was signifi
48 d Amphiregulin through a mechanism involving asparaginyl endopeptidase, resulting in FOXP3(+) cells t
49 pecificity of the reaction catalyzed by this asparaginyl endopeptidase, we prepared a series of octap
50 e etiopathogenesis of Alzheimer disease, and asparaginyl endopeptidase-I2(PP2A)-protein phosphatase 2
51 ide-rich cyclic peptides, appears to involve asparaginyl endopeptidase-mediated processing from large
52 st-translationally in storage vacuoles by an asparaginyl endopeptidase.
53  type 1 phenotype and expressed the protease asparaginyl endopeptidase.
54 e a new class of inhibitors specific for the asparaginyl endopeptidases (AE) (legumains).
55  having a similar structural fold with other asparaginyl endopeptidases (AEP).
56                                              Asparaginyl endopeptidases (AEPs) are cysteine proteases
57                                              Asparaginyl endopeptidases (AEPs) have recently been wid
58                In seeds, PawS1 is matured by asparaginyl endopeptidases (AEPs) into the cyclic peptid
59                     Legumains, also known as asparaginyl endopeptidases (AEPs), cleave peptide bonds
60 tively, are shown to be potent inhibitors of asparaginyl endopeptidases (legumains) from the bloodflu
61                                              Asparaginyl endopeptidases are crucial in the final stag
62 ian homologue of the legumain/haemoglobinase asparaginyl endopeptidases found originally in plants an
63 ht into the mechanism of their inhibition of asparaginyl endopeptidases.
64 tidyl-tRNA synthetase (HisRS) or to alanyl-, asparaginyl-, glycyl-, isoleucyl-, or threonyl-tRNA synt
65 hree HIF prolyl hydroxylases (PHD1-3) and an asparaginyl hydroxylase (factor-inhibiting HIF (FIH)).
66 can be enhanced by suppression of prolyl and asparaginyl hydroxylase activity by dimethyloxalylglycin
67                                    FIH is an asparaginyl hydroxylase catalyzing post-translational mo
68 ases, including the hypoxia-inducible factor asparaginyl hydroxylase FIH and histone N(epsilon)-methy
69 oxylation of HIF-1alpha or HIF-2alpha by the asparaginyl hydroxylase FIH-1 blocks coactivator binding
70 ctor-inhibiting HIF-1 (FIH-1), the pertinent asparaginyl hydroxylase involved in hypoxic signaling.
71 f adenosine, both prolyl hydroxylases and an asparaginyl hydroxylase termed factor-inhibiting HIF (FI
72            Factor inhibiting HIF (FIH) is an asparaginyl hydroxylase that regulates HIF function by r
73 roxylases: four prolyl 4-hydroxylases and an asparaginyl hydroxylase.
74   The prolyl-hydroxylases (PHD1/2/3) and the asparaginyl-hydroxylase factor-inhibiting HIF are oxygen
75 evelopment and is a human homolog of the HIF asparaginyl-hydroxylase.
76 nd 2-oxoglutarate (2OG)-dependent prolyl and asparaginyl hydroxylases (PHD1-3 and factor-inhibiting H
77 antial differences in the role of prolyl and asparaginyl hydroxylation in regulating hypoxia-responsi
78      2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible facto
79  studies on the consequences of FIH-mediated asparaginyl hydroxylation of TRPA1.
80 sted severe impairment of HIF prolyl but not asparaginyl hydroxylation which was corrected by provisi
81 een used extensively for peptide ligation at asparaginyl junctions.
82  enzymes such as butelase 1 act as a peptide asparaginyl ligase (PAL) and catalyze Asx-Xaa bond forma
83  equivalent mutation in a consensus-designed asparaginyl ligase facilitates similarly altered substra
84             Here we show that the engineered asparaginyl ligase OaAEP1 catalyzes direct isopeptide li
85            Here, we engineer the widely used asparaginyl ligase OaAEP1 for altered substrate specific
86 r188 residue is a general determinant of the asparaginyl ligase substrate specificity.
87  This review will focus on sortase, peptidyl asparaginyl ligases (PALs) and variants of subtilisin; d
88 nimal tripeptide recognition motif, peptidyl asparaginyl ligases (PALs) are particularly useful tools
89                                      Peptide asparaginyl ligases (PALs) catalyze transpeptidation at
90              The recently discovered peptide asparaginyl ligases (PALs) from cyclotide-producing plan
91                          Hyperactive peptide asparaginyl ligases (PALs), such as butelase-1, belong t
92                                              Asparaginyl ligases are a class of highly efficient tran
93 inants required for ligation activity of the asparaginyl ligases presented here will facilitate genom
94                                   Engineered asparaginyl ligases with orthogonal substrate specificit
95                               PALs (peptidyl asparaginyl ligases) catalyze transpeptidation at the As
96 s resistant to the ligase at the pH used for asparaginyl ligation in the second step.
97         A general method for the analysis of asparaginyl-linked (N-linked) carbohydrate moieties of a
98                               AAG has five N-asparaginyl-linked glycosylation sites, each varying in
99                                          Aza-asparaginyl Michael acceptors react with thiols, which p
100 been designed to replace the quinaldic amide-asparaginyl moiety (P2/P3 ligand) found in several poten
101  MBP-A trimer cross-linked by a high mannose asparaginyl oligosaccharide reveal that monosaccharides
102 s in proteins (which form spontaneously from asparaginyl or aspartyl residues) to normal aspartyl res
103 aa peptide bond through the beta-carbonyl of asparaginyl or aspartyl residues, thereby adding an extr
104 observed oligosaccharides on a non-consensus asparaginyl residue in the C(H)1 constant domain of IgG1
105 at human Bcl-xL undergoes deamidation at two asparaginyl residues and that DNA-damaging antineoplasti
106 ging process from the deamidation of protein asparaginyl residues and the isomerization of protein as
107                  Nonenzymatic deamidation of asparaginyl residues can occur spontaneously under physi
108 ted post-translational hydroxylation of both asparaginyl residues in "VNVN" and related motifs of ank
109 of the specific deamidation rates of 170,014 asparaginyl residues in 13,335 proteins have been carrie
110 lculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 1
111 nce that the beta-hydroxylation of conserved asparaginyl residues in ankyrin repeat domain (ARD) prot
112 ion of beta carbons of specific aspartyl and asparaginyl residues in EGF-like domains of certain prot
113 ational hydroxylation of specific prolyl and asparaginyl residues in HIFalpha subunits and thereby pr
114 ational hydroxylation of specific prolyl and asparaginyl residues in hypoxia-inducible factor (HIF),
115 t of the deamidation rates of glutaminyl and asparaginyl residues in peptides and proteins has been d
116 e(2)-P-P-dolichol (G(3)M(9)Gn(2)-P-P-Dol) to asparaginyl residues of nascent glycoprotein precursor p
117 s nonenzymatic deamidation of glutaminyl and asparaginyl residues of peptides and proteins has been o
118 espect to the hypothesis that glutaminyl and asparaginyl residues serve, through deamidation, as mole
119 tiate the conversion of damaged aspartyl and asparaginyl residues to normal l-aspartyl residues.
120 d peptides is the spontaneous deamidation of asparaginyl residues via a succinimide intermediate to f
121  from the spontaneous deamidation of protein asparaginyl residues.
122 residues to positions previously occupied by asparaginyl residues.
123 n developed; the rates of deamidation of 306 asparaginyl sequences in model peptides at pH 7.4, 37.0
124 nicity island and is inserted into different asparaginyl tRNA genes at different chromosomal location
125                  Many prokaryotes synthesize asparaginyl-tRNA (Asn-tRNA(Asn)) in a similar manner usi
126                                 Synthesis of asparaginyl-tRNA (Asn-tRNA(Asn)) in bacteria can be form
127                                              Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRN
128                                              Asparaginyl-tRNA (Asn-tRNA) is generated in nature via t
129  transamidation pathway for the synthesis of asparaginyl-tRNA and a novel lysyl-tRNA synthetase.
130 he amide aminoacyl-tRNAs glutaminyl-tRNA and asparaginyl-tRNA by tRNA-dependent amidation of the misc
131                                  Conversely, asparaginyl-tRNA promoted a dual slippage event in eithe
132  directly ligating Asn to tRNA(Asn) using an asparaginyl-tRNA synthetase (AsnRS) or by synthesizing A
133    They can be formed by direct acylation by asparaginyl-tRNA synthetase (AsnRS) or glutaminyl-tRNA s
134  direct acylation of tRNA with asparagine by asparaginyl-tRNA synthetase (AsnRS) or in a two-step pat
135 tion was observed, we searched for genes for asparaginyl-tRNA synthetase (AsnRS).
136 ates Asp-tRNA(Asp) and usually coexists with asparaginyl-tRNA synthetase (AsnRS).
137 a-dependent asparagine synthetase (asnA) and asparaginyl-tRNA synthetase (asnS) have been cloned from
138 ovo heterozygous and bi-allelic mutations in asparaginyl-tRNA synthetase (NARS1).
139 ted to the Plasmodium falciparum cytoplasmic asparaginyl-tRNA synthetase (PfAsnRS) as the target, con
140 y the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA syntheta
141  genes for 18 synthetases, whereas those for asparaginyl-tRNA synthetase and glutaminyl-tRNA syntheta
142               Glutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase evolved from glutamyl-tRNA s
143 n is not a major barrier to the retention of asparaginyl-tRNA synthetase in many Archaea.
144                                              Asparaginyl-tRNA synthetase induced migration of lymphoc
145 n as well as the catalytic capacities of the asparaginyl-tRNA synthetase of the parasite in vitro.
146 is in archaea is divergent: some archaea use asparaginyl-tRNA synthetase, whereas others use a hetero
147 n-tRNA(Asn) by direct acylation catalyzed by asparaginyl-tRNA synthetase.
148                                              Asparaginyl-tRNA synthetase1 (NARS1) is a member of the
149 ation of a new antisynthetase, reacting with asparaginyl-tRNA synthetase; the detection of antibodies
150                     Glutaminyl-tRNA(Gln) and asparaginyl-tRNA(Asn) were likely formed in LUCA by amid
151                                              Asparaginyl-tRNA, which decodes the A-site codon AAC, ha
152 stead these organisms derive asparagine from asparaginyl-tRNA, which is made from aspartate in the tR
153 o account for the slipperiness of eukaryotic asparaginyl-tRNA.
154 ococcus, the only route to asparagine is via asparaginyl-tRNA.
155  via the deamidation-linked isomerization of asparaginyl-Xaa bonds or direct isomerization of asparty

 
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