ライフサイエンスコーパス: Asn residue

1 ed phage had at least one susceptible Asp or Asn residue.

2 ludes water molecules, a Glu residue, and an Asn residue.

3 hiol group to the beta-carbon of an upstream Asn residue.

4 ecificity to promote cleavage following a -1 Asn residue.

5 cted Asp(84), which had been converted to an Asn residue.

6 ino acid sequencing to identify the specific Asn residue.

7 ts, defined by regularly spaced Ser, Gln and Asn residues.

8 sociated with the spontaneous deamidation of Asn residues.

9 eceptor juxtamembrane region lacking Tyr and Asn residues.

10 odynamic cost than burial of two interacting Asn residues.

11 can undergo nonenzymatic deamidation on two Asn residues.

12 oligosaccharides was observed at individual Asn residues.

13 y preferred for binding to conserved Gly:Asp:Asn residues.

14 se (AspH), catalyze C3 hydroxylations of Asp/Asn-residues.

15 has five potential N-glycosylation sites at Asn residues 210, 222, 286, 313, and 443.

16 Instead, an Asn residue and water molecules are found within H-bondi

17 er interactions among side chains of Gln and Asn residues and explains the tolerance of [URE3] to scr

18 s form between the side-chains of the buried Asn residues and these contribute to the conformational

19 y, suggesting the hypothesis that downstream Asn residues are important for beta-sheet formation.

20 ogether, the results suggested that (a) both Asn residues (Asn-101 and Asn-123) are required for the

21 However, attention was called to a conserved Asn residue (Asn128) that could play a catalytic role by

22 positions 79, 141 and 187 and one deamidated Asn residue at position 176, were detected at low level.

23 f a signal peptide, and a Ser rather than an Asn residue at the penultimate position.

24 determined the energetics of placing Ile or Asn residues at four buried positions in a two-stranded

25 nded coiled coils is the use of buried polar Asn residues at position a, which imparts dimerization a

26 scan mutagenesis screen showed that Gln and Asn residues at positions 49, 54, 139 and 144 were criti

27 Substitution of these buried Asn residues by Leu residues results in a loss of struct

28 To elucidate a role of the Asn residue for RGS GAP function, we have investigated e

29 e stacking with the G-tetrads, while Tyr and Asn residues form essential hydrogen bonds and electrost

30 hobic Leu residues, with the exception of an Asn residue from each strand that is positioned to engag

31 proteins in which 31 unstable and 167 stable Asn residues have been reported and for 7 unstable and 6

32 ency of N-linked glycosylation at individual Asn residues have not been fully defined.

33 of the three-dimensional environment of each Asn residue in the protein and a calculation that includ

34 We replaced the Asn residue in the sixth position of the first or sixth

35 fic mutation that changed a highly conserved Asn residue in the V1 loop of Env to an Asp residue (N-1

36 l group can be added to the side chains of D-Asn residues in a peptide substrate and show how flankin

37 N-Linked glycosylation usually occurs at Asn residues in Asn-X-Ser/Thr sequons where X not equal

38 e residues, instead of the canonical His and Asn residues in calpains.

39 post-translational hydroxylation of Asp and Asn residues in epidermal growth factor-like domains (EG

40 9)GlcNAc(2) from dolichol (Dol) to consensus Asn residues in nascent proteins in the endoplasmic reti

41 Mutation of each of the three Asn residues in Par-4 abrogated binding to all three SPS

42 Here, we alter the positions of the Asn residues in the Acid and Base peptides such that a b

43 d interhelical polar interaction between two Asn residues in the Acid-a1-Base-a1 heterodimer is known

44 s that non-consensus glycosylation occurs on Asn residues in the context of a reverse consensus motif

45 lves the attachment a high mannose glycan to Asn residues in the context of Asn-X-Ser/Thr/Cys, a moti

46 constant distance from conserved Pro and Tyr/Asn residues in the fifth transmembrane domain (TM V).

47 The Asn residues in the five consensus sites for N-linked gl

48 Here, we studied the role of conserved Asn residues in the leucine-rich repeats of GP Ib alpha,

49 The Asn residues in the middle of the helices show the most

50 ng the gating currents, we demonstrated that Asn residues in the S6s of DIII and DIV are important fo

51 hythmic drug, to probe the role of conserved Asn residues in the S6s of DIII and DIV in NaV1.5 and Na

52 cation of aspartic acid (Asp) or asparagine (Asn) residue in proteins.

53 h respect to deamidation of the asparaginyl (Asn) residues in proteins is described.

54 se (AspH) catalyses the hydroxylation of Asp/Asn-residues in epidermal growth factor-like domains (EG

55 regions rather than catalytic action of the Asn residue is a key component for the RGS GAP action.

56 An Asn residue is required in position 2.50(87) for express

57 The deamidation of asparagine (Asn) residues is the most common type of spontaneous pos

58 We identified a key Asn residue, N1285, that when glycosylated reduced album

59 We also investigated another Asn residue (N140) that is catalytically essential and s

60 An Asn residue (N191) that is critical for caC excision is

61 Mutation of the conserved Asn residue (N890A) in the MARCH6 CTE stabilized the nor

62 ly larger driving force for association than Asn residues near the apolar/polar interface.

63 nd to be due to deamidation of either of two Asn residues near the C-terminus of the proteins, in a r

64 ases (PALs) catalyze transpeptidation at the Asn residue of a short Asn-Xaa(1)-Xaa(2) tripeptide moti

65 showed that linking glycans directly to the Asn residue of tyrocidine A diminished its antibacterial

66 primary TCR contact site mimics that of the Asn residue present in the antigenic ligand.

67 by mutating RDH-S to remove an "additional" Asn residue relative to RDH1 in its center, to convert t

68 In MeTr, the Asn residue swings from a distant position to within H-b

69 es cleaved at sites other than the conserved Asn residues targeted by VPE.

70 tion of glycosylation and of substitution of Asn residues that are potential glycosylation sites.

71 en reported and for 7 unstable and 63 stable Asn residues that have been reported in 61 human hemoglo

72 ts of this peptide were prepared in which an Asn residue was introduced at one or more of the "a" pos

73 The position of one of these buried Asn residues was randomized, and bZip heterodimers conta

74 the Ser residues, as well as an intervening Asn residue, was converted to a small, nonhydroxy amino

75 Ten Asn residues were identified as potential glycosylation

76 Asn residues were placed singly and in pairs at three po

77 A mutant hCTR3 in which all three Asn residues were substituted with Ala exhibited no high

78 The Phe, Ala, and Dap/Asn residues were successively removed to generate a 14-

79 f the Mn2 site upon mutation of His141 to an Asn residue, which lacks a potential acid/base residue,

80 Legumain cannot cleave after glycosylated Asn residues, which enabled the robust identification an

81 Moreover, we mapped two Asn residues within CRD4 that are N-linked glycosylated

82 Substitution of Ala for Asn residues within each of three consensus N-linked gly

83 ositions 49 and 139 could not be replaced by Asn residues without interfering with curli assembly, su