ライフサイエンスコーパス: Ser residue

1 ts trianionic form adjacent to a now neutral Ser residue.

2 otifs and 12 other peptides with one or more Ser residues.

3 -dependent protein kinase at the neighboring Ser residues.

4 ation) cleavage sites to occur before Thr or Ser residues.

5 d by PKA and CK1 phosphorylation at adjacent Ser residues.

6 pancy proportional to the number of modified Ser residues.

7 rabinosylated and with likely galactosylated Ser residues.

8 by PSA (T(1/2) = 12 min) between the Gln and Ser residues.

9 that the proteins are autophosphorylated on Ser residues.

10 ed that these LAST residues, Lys-Arg-Lys-Thr-Ser, residues 110-114, are involved in nucleic acid bind

11 involving serine phosphorylation at serine (Ser) residue 276.

12 duced VP30 phosphorylation in the N-terminal Ser residues 29-46, suggesting a novel mechanism of regu

13 cause phosphorylation of Tyr residue 701 and Ser residue 727 of STAT1, as shown by immunoblotting.

14 ctivity requires only five adjacent serines (Sers) (residues 8-12).

15 Phosphorylation of a conserved Ser residue adjacent to the microtubule-binding exon rel

16 ty, consistent with prior work implicating a Ser residue and a Ser-Asp dyad in patatin's catalytic ac

17 regulate the phosphorylation of neighbouring Ser residues and basal cardiac function, full accelerati

18 conclude that PKA phosphorylates the EGFR on Ser residues and decreases its tyrosine kinase activity

19 hosphorylation at the conserved gate-keeping Ser residues and increased nuclear localization of NFATc

20 residues delimiting the loop substituted by Ser residues) and a control double Cys mutant, C418S/C43

21 bR tag labeling was mapped to the underlined Ser residue, and the ybbR tag was found to have a strong

22 rain as compared to the single mutants, both Ser residues appear to affect stable assembly and functi

23 cesses during the nucleophilic attack by the Ser residue are likely to be more complex for these enzy

24 g of a Lys residue immediately followed by a Ser residue are present in histone tails, our studies re

25 e antibiotic Microcin B17, four Cys and four Ser residues are converted into four thiazoles and four

26 The Ser residues are not involved significantly in MgATP- or

27 r Overhauser effects indicate that the three Ser residues are still packed in the center of the tripl

28 osition of Vbeta11 CDR3 can encode an Arg or Ser residue as a result of somatic rearrangement.

29 g3 processing products defined an acetylated Ser residue as the amino terminus of Gag3/p34, p27, and

30 Here, each of the Ser residues, as well as an intervening Asn residue, was

31 idues, and hairpin-loop of three Pro and one Ser residues, as well as the absence of an N-terminal ER

32 es the inhibition imposed by -5 Leu, while a Ser residue at position -4 or -2 does not restore proces

33 templates, we substituted Lys for the native Ser residue at position 178 on the L polypeptide to make

34 Our data suggest that the Ser residue at position 202 of Gtalpha is critical for t

35 In each case, mode 2 gating depends on a Ser residue at the cytoplasmic end of the S6 helix in do

36 eta 1-3Gal beta 1-4Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of

37 We introduced Gly and/or Ser residues at different positions upstream of the R pe

38 n exon1-like molecules containing phosphoryl-Ser residues at positions 13 and 16 show that they reduc

39 We found that the integrity of two Ser residues at positions 535 and 539 within the specifi

40 We show that the combined mutation of Ser residues at positions 9, 67, 72, and 77 impairs vira

41 alytically inert owing to the insertion of a Ser residue between the Pro-Cys motif found at the activ

42 reduced occludin phosphorylation at Tyr and Ser residues, but not Thr, which in turn led to a redist

43 sible phosphorylation of Drp1 at a conserved Ser residue by an outer mitochondrial kinase (PKA/AKAP1)

44 -S93T:METH revealed that the substitution of Ser residue by Thr caused the expulsion of a water molec

45 ism whereby the phosphorylation of conserved Ser residues, by protein kinases A and C, could induce a

46 We suggest that the Ser residue can form a hydrogen bond with a backbone car

47 egment (residues 375-551) is rich in Asn and Ser residues, carries a net positive charge, and contain

48 Following deletion of this Ser residue, catalytic activity is restored and, using a

49 Three Ser residues clustered in the C-terminal 18 amino acids

50 ccharides are present on one or more of five Ser residues clustered in the carboxyl-terminal region o

51 reflect (along with the absence of a key Thr/Ser residue conserved in oxygen-activating P450s) the ev

52 N-Terminal Ser residues containing an Fmoc carbamate are converted

53 en and carbonyl oxygen of the amino-terminal Ser residue coordinate to a Zn(2+) ion to form a five-me

54 Ala-containing reference channels, the polar Ser residues decrease the analogues' channel-forming pot

55 Mutating only the Ser residues did not inhibit either internalization or d

56 In contrast, the Ser residues display a wide range of glycosylations, ran

57 e addition of the thiol of Cys to dehydrated Ser residues during the biosynthesis of lanthipeptides,

58 Single site mutants at Ser residues embedded in potential PKC consensus sites (

59 a stable triple-helix, and introduction of a Ser residue for Gly at the 901 mutation site led to a 50

60 features, including (i) a high percentage of Ser residues, (ii) an aliphatic amino acid (Ile, Leu, or

61 Although a single Ser residue in a transmembrane helix is unable to mediat

62 Mutation of the Ser residue in HvABI5, which has been shown to be phosph

63 horylates HDAC2 at the same unique conserved Ser residue in its C terminus.

64 hat phosphorylation is at a unique conserved Ser residue in the C terminus of both HDACs.

65 alent attachment of the probes to a specific Ser residue in the carrier proteins or short peptide tag

66 tional modifications (PTMs) can occur at the Ser residue in these linkers.

67 CaM kinase IV are able to phosphorylate this Ser residue in vitro, and mutagenesis studies suggest th

68 the first systematic analysis of the role of Ser residues in c-Mpl signaling.

69 g one or more residues are linked to Thr and Ser residues in gp72 via a phosphodiester linkage (GlcNA

70 long with substitution analyses of candidate Ser residues in mouse DSPP, confirmed that 2 glycosamino

71 was designed to evaluate the roles of these Ser residues in T cell activation.

72 usively on the reversible phosphorylation of Ser residues in the C-terminal RS domain.

73 the fact that PDK exclusively phosphorylates Ser residues in the E1alpha subunit of the PDC.

74 seem to be due to phosphorylation of Thr or Ser residues in the linker regions connecting adjacent z

75 We identify the sites as three Ser residues in the N terminus of TPX2; however, mutatio

76 rg-Glu-Lys-Arg), conserved Asp, His, Asn and Ser residues in the putative catalytic domain, a hydroph

77 Finally, mutation to Ala of the Ser residues in the SerZip motif gave rise to a relative

78 that revealed phosphorylation of key Thr and Ser residues in the short cytoplasmic domain, we introdu

79 t HFR1 is phosphorylated at multiple serine (Ser) residues in the N-terminal regulatory domain of HFR

80 Deletion of the last two Ser residues, including one PKC consensus site in the re

81 amino acid differences, we mutated the nine SER residues individually to the respective residues of

82 with nonpolar (Ala, Pro) or polar (Asp, Arg, Ser) residues inhibited transition to the desensitized s

83 indicated that MA phosphorylation at serine (Ser) residues is important for viral replication.

84 oduct soraphen A and by phosphorylation of a Ser residue just before the BC domain core in mammalian

85 ceptor is modified by glycosaminoglycan at a Ser residue located immediately N terminal to the acidic

86 it is dependent upon the phosphorylation of Ser residues near the C terminus of NS5A, a multifunctio

87 ized within a region containing a cluster of Ser residues near the predicted junction of the helical

88 rsible phosphorylation of a specific serine (Ser) residue near the N terminus.

89 Essential for this interaction is the Ser residue of the beta1-adrenergic receptor carboxyl-te

90 ing phosphoamino acid analysis we found that Ser residues of c-Mpl were constitutively phosphorylated

91 efore, the two conserved ABC signature motif Ser residues of P-glycoprotein cooperatively accelerate

92 function, or mutations in the cleavage site Ser residues of Sst2, did not alter processing.

93 ibose groups onto the hydroxyl oxygen of the Ser residues of target substrates, including both PARP1

94 of the peptide backbone of three Cys and two Ser residues of the prepeptide.

95 Cleavage between the Gly and Ser residues of the reactive site loop and detection of

96 tivated phosphorylation at a terminal region Ser residue plays an important role in regulating their

97 were phosphorylated predominantly on Thr and Ser residues, respectively.

98 me-dependent RelA phosphorylation on serine (Ser) residues Ser-276 and Ser-536 in parallel with enhan

99 nhibited by phosphorylation of an N-terminal Ser residue (Ser(21) in GSK3alpha and Ser(9) in GSK3beta

100 tic group, which is derived from an internal Ser residue (Ser-68).

101 s each with a single Ser --> Cys mutation at Ser residues (Ser(2), Ser(4), and Ser(9)) flanking Cys(6

102 d p90 ribosomal S6 kinases on four conserved Ser residues (Ser-235, Ser-236, Ser-240, and Ser-244) wh

103 icient to dephosphorylate at least four IRS1 Ser residues, Ser(318), Ser(346), Ser(612), and Ser(789)

104 ry identified three phosphorylation sites at Ser residues: Ser(649), Ser(286), and Ser(297).

105 Unusually however, SERA5 possesses a Ser residue (Ser596) at the position of the canonical ca

106 ze CH3OH to model the role of a local Thr or Ser residue shows that an alcohol functionality hydrogen

107 with a bulky, charged Lys residue or with a Ser residue (sometimes found in the same position of oth

108 ced amino acid sequence, and the prospective Ser residue-specific casein kinase I and II phosphorylat

109 ylation occurred only at Ser(16), one of two Ser residues that are the major substrate sites for prot

110 ous NFATc4, which are conserved gate-keeping Ser residues that control NFAT subcellular distribution.

111 emonstrated that both SIBLINGs contained Thr/Ser residues that were preferentially glycosylated by pp

112 horylation of CREB on a conserved cluster of Ser residues (the ATM/CK cluster) by the DNA damage-acti

113 en reported to be phosphorylated at multiple Ser residues, the mechanisms by which phosphorylation at

114 In addition, mutagenesis of the active site Ser residue to Ala (S119A), which renders catalytic inac

115 lin-dependent protein kinase or mutating the Ser residues to Ala prevents the increase in mode 2 gati

116 Importantly, the conversion of these Ser residues to Ala was sufficient to impair the ability

117 otein were studied by mutating the conserved Ser residues to Ala.

118 McbB, C, and D) to cyclize four Cys and four Ser residues to four thiazoles and four oxazoles, respec

119 Mutations changing the same Ser residues to Glu, to mimic the negative charge create

120 all six native Cys residues are replaced by Ser residues, was also evaluated.

121 tion of occludin on Thr residues, but not on Ser residues, was dramatically reduced during the disass

122 phosphorylation sites, in which the Thr and Ser residues were changed to alanine residues, reduced t

123 N-terminal Cys and Ser residues were observed to undergo beta-elimination i

124 T and S1073A/T, affecting conserved Walker A Ser residues, were characterized to elucidate molecular

125 stitution of the C-terminal Cys residue by a Ser residue, which can inhibit wild type Gbetagamma-medi

126 leles contain an Arg in place of a conserved Ser residue, which lies adjacent to the phosphatidylinos

127 In particular, the polar side chains of the Ser residues, which are intimately involved in the solva

128 Replacement of TF's cytoplasmic Ser residues with Asp to mimic phosphorylation enhances

129 observed in vitro on at least two different Ser residues, with the location of two sites being mappe

130 p145-N and Nup145-C), occurs between Phe and Ser residues within a highly conserved domain in a polyp

131 Point mutations affecting conserved Ser residues within the ICD PEST motif prevent hyperphos