ライフサイエンスコーパス: Ser residue

1 are unique for MCs with Mdha and an adjacent Ser residue.

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

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

4 ia the concerted action of catalytic Tyr and Ser residues.

5 -dependent protein kinase at the neighboring Ser residues.

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

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

8 rabinosylated and with likely galactosylated Ser residues.

9 pancy proportional to the number of modified Ser residues.

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

11 that the proteins are autophosphorylated on Ser residues.

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

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

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

15 ation, and Kcs1 is phosphorylated in vivo at Ser residues 537 and 646 during pseudohyphal growth.

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

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

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

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

20 reaction occurs between oxygen from adjacent Ser residue and sulfur of the Mdha-bonded thiol or sulfo

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

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

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

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

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

26 that contain both side chain dehydration of Ser residues, and backbone heterocyclization at Ser, Thr

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

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

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

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

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

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

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

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

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

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

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

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

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

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

41 ing an MICU1 contact interface with a nearby Ser residue at the cytoplasmic entrance of the MCU pore.

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

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

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

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

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

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

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

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

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

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

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

53 ments also reveal that phosphorylated Tyr or Ser residues can also promote equivalent levels of APY f

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

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

56 clization removes the carbonyl following the Ser residue, CcaM likely catalyzes dehydration without g

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

72 eviously unidentified functional role of the Ser residue in redox proteins and adds to the expanding

73 TARPs with the Ser residue in the "P-S-Y"-motif of its tail phosphoryla

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

107 in R(ACT), is important: when mutated to the Ser residue present in GL3(ACT), dimerization affinity d

108 er residues to form D-Asp, L/D-isoAsp, and D-Ser residues, respectively.

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

110 osphorylation of an evolutionarily conserved Ser residue (S133) within its intrinsically disordered k

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

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

113 rely on anions interacting with a conserved Ser residue (Ser(cen)) at the center of three anion bind

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

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

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

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

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

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

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

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

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

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

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

125 We demonstrate that CcaM only modifies Ser residues that precede an azole in the core peptide.

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

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

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

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

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

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

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

133 omerization and epimerization of L-Asp and L-Ser residues to form D-Asp, L/D-isoAsp, and D-Ser residu

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

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

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

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

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

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

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

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

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

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

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

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

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

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