ライフサイエンスコーパス: asparaginyl

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 Many bacteria lack genes encoding asparaginyl- and/or glutaminyl-tRNA synthetase and conse

9 stability with respect to deamidation of the asparaginyl (Asn) residues in proteins is described.

10 art, mediated by a hydrogen bond between the asparaginyl beta-hydroxyl group and the side chain of a

11 ASPH encodes aspartyl/asparaginyl beta-hydroxylase (ASPH), which has been foun

12 poxia-inducible factor (HIF)-1 (FIH-1) is an asparaginyl beta-hydroxylase enzyme that was initially f

13 The S. typhimurium aspartyl/asparaginyl beta-hydroxylase homologue (designated lpxO)

14 ame(s) with similarity to mammalian aspartyl/asparaginyl beta-hydroxylases in bacteria known to make

15 A second asparaginyl beta-hydroxylation causes further stabilizat

16 l techniques are used to study the effect of asparaginyl beta-hydroxylation on the structure and stab

17 hysical insights into the mechanism by which asparaginyl beta-hydroxylation stabilizes the ARD protei

18 The human aspartyl (asparaginyl) beta-hydroxylase (HAAH) is a highly conserv

19 ysis of several residues in bovine aspartyl (asparaginyl) beta-hydroxylase that are located in a regi

20 ed the antigen as the human form of aspartyl(asparaginyl)beta-hydroxylase.

21 Aspartyl-(asparaginyl)-beta-hydroxylase (ASPH) is a cell-surface e

22 ferating cell nuclear antigen, and aspartyl-(asparaginyl)-beta-hydroxylase, a gene associated with in

23 r isoD) via either aspartyl isomerization or asparaginyl deamidation alters protein structure and pot

24 Asparaginyl endopeptidase (AEP or legumain) is a lysosom

25 but not the terminal acyclic TI, depends on asparaginyl endopeptidase (AEP) for maturation.

26 ned competitive peptide inhibitors of B-cell asparaginyl endopeptidase (AEP) that specifically block

27 d approaches identified unique expression of asparaginyl endopeptidase (AEP), intercellular adhesion

28 Asparaginyl endopeptidase (AEP), which is overexpressed

29 An asparaginyl endopeptidase (legumain) also synergized wit

30 with kainic acid or pH 6.0 medium activated asparaginyl endopeptidase and consequently produced the

31 cemia as in diabetes, I2(PP2A) is cleaved by asparaginyl endopeptidase at Asn-175 into the N-terminal

32 he first time that legumain, a member of the asparaginyl endopeptidase family functioning as a stress

33 Asparaginyl endopeptidase from Alzheimer disease brain c

34 Therefore, the asparaginyl endopeptidase is required for hexamer assemb

35 Here we show that the level of activated asparaginyl endopeptidase is significantly increased, an

36 Here, we showed that legumain, the only asparaginyl endopeptidase of the mammalian genome, is hi

37 phosphorylation of Tau, and the knockdown of asparaginyl endopeptidase with siRNA abolished this path

38 Expression of legumain, a novel asparaginyl endopeptidase, in tumors was identified from

39 pecificity of the reaction catalyzed by this asparaginyl endopeptidase, we prepared a series of octap

40 e etiopathogenesis of Alzheimer disease, and asparaginyl endopeptidase-I2(PP2A)-protein phosphatase 2

41 ide-rich cyclic peptides, appears to involve asparaginyl endopeptidase-mediated processing from large

42 st-translationally in storage vacuoles by an asparaginyl endopeptidase.

43 e a new class of inhibitors specific for the asparaginyl endopeptidases (AE) (legumains).

44 having a similar structural fold with other asparaginyl endopeptidases (AEP).

45 In seeds, PawS1 is matured by asparaginyl endopeptidases (AEPs) into the cyclic peptid

46 tively, are shown to be potent inhibitors of asparaginyl endopeptidases (legumains) from the bloodflu

47 ian homologue of the legumain/haemoglobinase asparaginyl endopeptidases found originally in plants an

48 ht into the mechanism of their inhibition of asparaginyl endopeptidases.

49 tidyl-tRNA synthetase (HisRS) or to alanyl-, asparaginyl-, glycyl-, isoleucyl-, or threonyl-tRNA synt

50 hree HIF prolyl hydroxylases (PHD1-3) and an asparaginyl hydroxylase (factor-inhibiting HIF (FIH)).

51 can be enhanced by suppression of prolyl and asparaginyl hydroxylase activity by dimethyloxalylglycin

52 FIH is an asparaginyl hydroxylase catalyzing post-translational mo

53 ases, including the hypoxia-inducible factor asparaginyl hydroxylase FIH and histone N(epsilon)-methy

54 oxylation of HIF-1alpha or HIF-2alpha by the asparaginyl hydroxylase FIH-1 blocks coactivator binding

55 ctor-inhibiting HIF-1 (FIH-1), the pertinent asparaginyl hydroxylase involved in hypoxic signaling.

56 roxylases: four prolyl 4-hydroxylases and an asparaginyl hydroxylase.

57 evelopment and is a human homolog of the HIF asparaginyl-hydroxylase.

58 nd 2-oxoglutarate (2OG)-dependent prolyl and asparaginyl hydroxylases (PHD1-3 and factor-inhibiting H

59 antial differences in the role of prolyl and asparaginyl hydroxylation in regulating hypoxia-responsi

60 2OG oxygenases also catalyze prolyl and asparaginyl hydroxylation of the hypoxia-inducible facto

61 sted severe impairment of HIF prolyl but not asparaginyl hydroxylation which was corrected by provisi

62 A general method for the analysis of asparaginyl-linked (N-linked) carbohydrate moieties of a

63 AAG has five N-asparaginyl-linked glycosylation sites, each varying in

64 Aza-asparaginyl Michael acceptors react with thiols, which p

65 been designed to replace the quinaldic amide-asparaginyl moiety (P2/P3 ligand) found in several poten

66 MBP-A trimer cross-linked by a high mannose asparaginyl oligosaccharide reveal that monosaccharides

67 s in proteins (which form spontaneously from asparaginyl or aspartyl residues) to normal aspartyl res

68 aa peptide bond through the beta-carbonyl of asparaginyl or aspartyl residues, thereby adding an extr

69 observed oligosaccharides on a non-consensus asparaginyl residue in the C(H)1 constant domain of IgG1

70 at human Bcl-xL undergoes deamidation at two asparaginyl residues and that DNA-damaging antineoplasti

71 ging process from the deamidation of protein asparaginyl residues and the isomerization of protein as

72 Nonenzymatic deamidation of asparaginyl residues can occur spontaneously under physi

73 of the specific deamidation rates of 170,014 asparaginyl residues in 13,335 proteins have been carrie

74 lculations of the deamidation rates of 1,371 asparaginyl residues in a representative collection of 1

75 nce that the beta-hydroxylation of conserved asparaginyl residues in ankyrin repeat domain (ARD) prot

76 ion of beta carbons of specific aspartyl and asparaginyl residues in EGF-like domains of certain prot

77 ational hydroxylation of specific prolyl and asparaginyl residues in HIFalpha subunits and thereby pr

78 t of the deamidation rates of glutaminyl and asparaginyl residues in peptides and proteins has been d

79 e(2)-P-P-dolichol (G(3)M(9)Gn(2)-P-P-Dol) to asparaginyl residues of nascent glycoprotein precursor p

80 s nonenzymatic deamidation of glutaminyl and asparaginyl residues of peptides and proteins has been o

81 espect to the hypothesis that glutaminyl and asparaginyl residues serve, through deamidation, as mole

82 tiate the conversion of damaged aspartyl and asparaginyl residues to normal l-aspartyl residues.

83 d peptides is the spontaneous deamidation of asparaginyl residues via a succinimide intermediate to f

84 from the spontaneous deamidation of protein asparaginyl residues.

85 residues to positions previously occupied by asparaginyl residues.

86 n developed; the rates of deamidation of 306 asparaginyl sequences in model peptides at pH 7.4, 37.0

87 nicity island and is inserted into different asparaginyl tRNA genes at different chromosomal location

88 Many prokaryotes synthesize asparaginyl-tRNA (Asn-tRNA(Asn)) in a similar manner usi

89 Synthesis of asparaginyl-tRNA (Asn-tRNA(Asn)) in bacteria can be form

90 Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRN

91 Asparaginyl-tRNA (Asn-tRNA) is generated in nature via t

92 transamidation pathway for the synthesis of asparaginyl-tRNA and a novel lysyl-tRNA synthetase.

93 he amide aminoacyl-tRNAs glutaminyl-tRNA and asparaginyl-tRNA by tRNA-dependent amidation of the misc

94 Conversely, asparaginyl-tRNA promoted a dual slippage event in eithe

95 directly ligating Asn to tRNA(Asn) using an asparaginyl-tRNA synthetase (AsnRS) or by synthesizing A

96 They can be formed by direct acylation by asparaginyl-tRNA synthetase (AsnRS) or glutaminyl-tRNA s

97 direct acylation of tRNA with asparagine by asparaginyl-tRNA synthetase (AsnRS) or in a two-step pat

98 tion was observed, we searched for genes for asparaginyl-tRNA synthetase (AsnRS).

99 ates Asp-tRNA(Asp) and usually coexists with asparaginyl-tRNA synthetase (AsnRS).

100 a-dependent asparagine synthetase (asnA) and asparaginyl-tRNA synthetase (asnS) have been cloned from

101 genes for 18 synthetases, whereas those for asparaginyl-tRNA synthetase and glutaminyl-tRNA syntheta

102 y the direct acylation of tRNA, catalysed by asparaginyl-tRNA synthetase and glutaminyl-tRNA syntheta

103 Glutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase evolved from glutamyl-tRNA s

104 n is not a major barrier to the retention of asparaginyl-tRNA synthetase in many Archaea.

105 Asparaginyl-tRNA synthetase induced migration of lymphoc

106 n as well as the catalytic capacities of the asparaginyl-tRNA synthetase of the parasite in vitro.

107 is in archaea is divergent: some archaea use asparaginyl-tRNA synthetase, whereas others use a hetero

108 n-tRNA(Asn) by direct acylation catalyzed by asparaginyl-tRNA synthetase.

109 ation of a new antisynthetase, reacting with asparaginyl-tRNA synthetase; the detection of antibodies

110 Glutaminyl-tRNA(Gln) and asparaginyl-tRNA(Asn) were likely formed in LUCA by amid

111 Asparaginyl-tRNA, which decodes the A-site codon AAC, ha

112 stead these organisms derive asparagine from asparaginyl-tRNA, which is made from aspartate in the tR

113 ococcus, the only route to asparagine is via asparaginyl-tRNA.

114 o account for the slipperiness of eukaryotic asparaginyl-tRNA.

115 via the deamidation-linked isomerization of asparaginyl-Xaa bonds or direct isomerization of asparty