ライフサイエンスコーパス: Thr residue

1 he cyano group which interacts with the same Thr residue.

2 yl Lewis x (C2-O-sLe(x)) motif at a specific Thr residue.

3 ent of glycosylation of nearly every Ser and Thr residue.

4 NHERF1 is a phosphoprotein with 40 Ser and Thr residues.

5 tein kinase C isoform phosphorylation of Ser/Thr residues.

6 substrate on Tyr residues and not on Ser or Thr residues.

7 than 180 degrees, particularly noticeable in Thr residues.

8 on modifications of two distinct sets of Ser/Thr residues.

9 nserved catalytic triad of Lys, Tyr, and Ser/Thr residues.

10 ities to the presence of nonglycosylated Ser/Thr residues.

11 ases, which dephosphroylate both Tyr and Ser/Thr residues.

12 oforms are phosphorylated on luminal Ser and Thr residues.

13 lasmic domain of band 3 (CDB3), primarily on Thr residues.

14 hrough the phosphorylation of C-terminal Ser/Thr residues.

15 e installation of the O-GlcNAc moiety to Ser/Thr residues.

16 at GpsB is phosphorylated at several Ser and Thr residues.

17 region C-terminal to the phosphorylated Ser/Thr residues.

18 y GtfA to bind substrate with unmodified Ser/Thr residues.

19 etylglucosamine (GlcNAc) moieties to Ser and Thr residues.

20 d by a cysteine attack on dehydrated Ser and Thr residues.

21 involves glutamyl-tRNA(Glu) to activate Ser/Thr residues.

22 type (HexHexNAc O-structure) attached to Ser/Thr residues.

23 l2 (residues 594-609) that contains four Ser/Thr residues.

24 al approach for the detection of phospho-Ser/Thr residues.

25 onnecting Cys residues 15, 26, and 27 to Ser/Thr residues 10, 12 and 19, respectively, with Thr(25) b

26 phosphorylation at its seven C-terminal Ser/Thr residues: (385)SSLENTVDLHISNSHPLSLTS(405).

27 of the FoxM1B Cdk1/2 phosphorylation site at Thr residue 596 significantly reduced both FoxM1B transc

28 Combined mutation of these Ser/Thr residues along with Ser459 (mutant MT7), resulted in

29 Phosphorylation of a cluster of Ser/Thr residues (amino acids 380-385) on the C-terminal tai

30 ) that phosphorylates target proteins at Ser/Thr residues, an activating gamma subunit (Snf4p), and a

31 PAP is phosphorylated at multiple Ser and Thr residues and is dephosphorylated for in vivo functio

32 ifications, including phosphorylation of Ser/Thr residues and oxidation of cysteine (Cys) residues.

33 formed by the dehydration of select Ser and Thr residues and the intramolecular addition of Cys thio

34 the net dehydration: phosphorylation of Ser/Thr residues and the subsequent phosphate elimination st

35 CylM catalyzes seven dehydrations of Ser and Thr residues and three cyclization reactions during the

36 A to dephosphorylate the NGF receptor on Ser/Thr residues and to potentiate its intrinsic Tyr kinase

37 always featured mutations involving Ser and Thr residues and were characterized by Thr to Ile amino

38 GlcNAc addition to serine and threonine (Ser/Thr) residues and OGA for its removal.

39 orylation occurred principally on threonine (Thr) residues and resulted in elevated ATMPK4 kinase act

40 cts with protons, Ca(2+) and two neighboring Thr residues, and adopts distinct motionally averaged co

41 ation of CDK9 at multiple C-terminal Ser and Thr residues, and full-length CycT1 (amino acids 728) [C

42 the receptor variants that lacked Lys or Ser/Thr residues, and the hD4R mutant that lacked 17 cytopla

43 ty is autophosphorylated on both Ser/Thr and Thr residues, and using both direct kinase assays and SR

44 ed translation, during which untemplated Ala/Thr residues are added C terminally to stalled peptide,

45 The Thr residues are all highly glycosylated within the rang

46 Because not all Ser/Thr residues are glycosylated, rules must exist that sig

47 All the Ser/Thr residues are phosphorylated at significantly greater

48 phorylation state where most Ser2, Ser5, and Thr residues are phosphorylated, expanding on our work o

49 Both Thr residues are preceded by the sequence RRS, and it ha

50 when cytoplasmic serine (Ser) and threonine (Thr) residues are mutated.

51 hich must display a Glu residue at P-3 and a Thr residue at P-2 By means of site-directed mutagenesis

52 are sufficient for this inhibition, and the Thr residue at position 24 and the Phe residue at positi

53 ed with alpha-D-Manp(1-->2)alpha-D-Manp, the Thr residue at position 27 was substituted with a single

54 sidue at position 4 (instead of a Glu) and a Thr residue at position 9 (instead of a charged residue)

55 ize the tetramer, suggesting that the native Thr residue at S4 is important for ultrahigh K+/Na+ sele

56 APP, is related to Abeta42 by an additional Thr residue at the C-terminus.

57 ct with a mutant M(2) mAChR in which the Ser/Thr residues at 307-311 were mutated to alanines.

58 Specifically, the Thr residues at positions 10 and 18 were substituted wit

59 s a hydrogen bond unique to IL-1RAPL between Thr residues at the 8th and 10th positions.

60 RCT domains and conserved phosphorylated Ser/Thr residues at the C-terminus of the nucleolar phosphop

61 terminal phosphorylation of a cluster of Ser/Thr residues, because a mutant with Ser/Thr to Ala subst

62 nd internalization, substitution of four Ser/Thr residues between 328-332 blocks desensitization but

63 Similarly, substitution of four Ser/Thr residues between positions 334 and 339 results in a

64 ound to be phosphorylated by PrkD on Ser and Thr residues but not by PrkG.

65 -glycosylation sites are numerous (59-83 Ser/Thr residues), but only two regions were observed to car

66 All sites were on Ser or Thr residues, but none were on Tyr.

67 Phosphorylation of occludin on Thr residues, but not on Ser residues, was dramatically

68 conjugate Cys, Ala, Trp, Gly, Leu, Asn, and Thr residues, but the basis of peptide substrate and ami

69 reversible phosphorylation of an active-site Thr residue by the PPDK regulatory protein (RP), a most

70 Modification of Ser and Thr residues by attachment of O-linked N-acetylglucos-am

71 at phosphorylates protein targets at Ser and Thr residues by converting ATP to ADP.

72 O-Glycans were released from Ser/Thr residues by mild base/borohydride treatment of purif

73 RF-3) is activated by phosphorylation of Ser/Thr residues clustered in its C-terminal domain.

74 n, which makes identification of P-Ser and P-Thr residues complicated.

75 Site-directed mutagenesis of Ser and Thr residues contained within the extracellular signal-r

76 T328, lacking the Ser/Thr-rich (13 or 12 Ser/Thr residues) cytoplasmic tail of the AT1A-R.

77 nding to a critical MIDAS metal-coordinating Thr residue did not affect ligand binding function, sugg

78 it motions with larger amplitudes than other Thr residues due to solvent interactions.

79 crophages and were phosphorylated on Ser and Thr residues during in vitro kinase assays in the presen

80 that phosphorylation of the newly introduced Thr residue explains the functional change.

81 preference for the phosphorylation of Ser or Thr residues followed by Gln.

82 e, introduced by means of dehydration of Ser/Thr residues followed by reaction of the resulting dehyd

83 bstitutions of larger (Phe) or smaller (Val, Thr) residues for Leu-98.

84 termini of the Gal((13)C(6))-Tn-occupied Ser/Thr residues from immobilized peptides to yield site-con

85 Essentially all of the susceptible Ser or Thr residues had to acquire their GalNAc units before an

86 try of the chiral side chains of the Ile and Thr residues, i.e. containing d-allo-Ile and d-allo-Thr

87 The function of Thr490, another conserved Thr residue in the activation loop of HRI, was also inve

88 hanges affecting a combination of an Arg and Thr residue in the integrin beta3 tail control the bindi

89 docking onto pairs of phosphorylated Ser and Thr residues in a constellation of intracellular targets

90 the pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNA

91 ion of O-acylated and phosphorylated Ser and Thr residues in a variety of derivatives.

92 Phosphorylation of four Thr residues in ABCDE leads to gross structural rearrang

93 the first time that DEPC can modify Ser and Thr residues in addition to His and Tyr residues.

94 /erk2) led to the phosphorylation of Ser and Thr residues in addition to the previously defined sites

95 requires phosphorylation at a cluster of Ser/Thr residues in amino acids 307-311 in the m2 mAChR.

96 rsus high copper, which revealed that 24 Ser/Thr residues in ATP7B could be phosphorylated, and only

97 At least four Ser/Thr residues in HSF1 appeared to be inducibly phosphoryl

98 Occludin is hyperphosphorylated on Ser and Thr residues in intact epithelial tight junction (TJ); h

99 imulated the phosphorylation of both Ser and Thr residues in lipin.

100 roduced by alpha,beta-unsaturation of Ser or Thr residues in peptide substrates by dehydration, follo

101 antitatively determined for 30 of the 31 Ser/Thr residues in the 81-residue porcine submaxillary glan

102 nce of autophosphorylation and the conserved Thr residues in the activation loop.

103 ion results indicated that the Asp, Asn, and Thr residues in the AFP are important in ice binding and

104 cking by using a DOR mutant in which all Ser/Thr residues in the C terminus were mutated to Ala (DTS)

105 Phosphorylation of a cluster of Ser/Thr residues in the C-terminal cytoplasmic region of mel

106 replacement mutagenesis of selected Ser and Thr residues in the C-terminal domain III sequence revea

107 Thus, we have identified a cluster of Ser/Thr residues in the C-terminal domain of Dvl2 that are W

108 We showed that nine of 15 Ser/Thr residues in the C-terminal domain were phosphorylate

109 Whereas substitution of all 11 Ser/Thr residues in the carboxyl terminus prevents both dese

110 demonstrate that phosphorylation of Ser and Thr residues in the carboxyl-tail of CCR2B mediates rece

111 nally, a construct in which multiple Ser and Thr residues in the carboxyl-tail were changed to alanin

112 chanism involving phosphorylation of Ser and Thr residues in the CTE of the receptor in a redundant f

113 Autophosphorylation on specific Ser and/or Thr residues in the cytoplasmic domain is often critical

114 ions that substitute one of the critical Ser/Thr residues in the GSK-3beta region of beta-catenin sta

115 icate that dephosphorylation of specific Ser/Thr residues in the N-terminal domain of p120-catenin me

116 MSP1a appeared to be mainly O-linked to Ser/Thr residues in the N-terminal repeated peptides.

117 d, notably by phosphorylation of several Ser/Thr residues in the N-terminal tail.

118 (GSK-3beta)-dependent phosphorylation of Ser/Thr residues in the N-terminus of the protein, followed

119 on involves enzymatic dehydration of Ser and Thr residues in the precursor peptide to generate unsatu

120 lation site as well as conserved Tyr and Ser/Thr residues in the region corresponding to the P+1 loop

121 , HH induces phosphorylation at multiple Ser/Thr residues in the SMO carboxy-terminal cytoplasmic tai

122 cated N-terminally to the phosphorylated Ser/Thr residues in the substrate and by an acidic patch in

123 termined for 29 of the 31 O-glycosylated Ser/Thr residues in the tandem repeat domains of blood group

124 second intracellular loop and the seven Ser/Thr residues in the third intracellular loop (rFSHR-2L +

125 mutagenesis to identify two clusters of Ser/Thr residues in the third intracellular loop of the m2 m

126 In this series, the four Thr residues in the wild type polypeptide were substitut

127 thetases catalyze the dehydration of Ser and Thr residues in their peptide substrates to dehydroalani

128 Mutation of the putative modified Ser/Thr residues in TSR2, TSR3, and TSR4 led to significantl

129 k1) indeed phosphorylates these p70(s6k) Ser/Thr residues in vitro.

130 ntified four serine (Ser) and one threonine (Thr) residue in the carboxy-terminal region as phosphory

131 are phosphorylated on serine/threonine (Ser/Thr) residues in quiescent cells (basal phosphorylation)

132 ces phosphorylation on serine/threonine (Ser/Thr) residues in the carboxyl termini of beta and gamma

133 Mutation of serine (Ser) and threonine (Thr) residues in the terminal carboxyl-tail of the recep

134 rine (Ser-), threonine (Thr-), or both (Ser-/Thr-) residues in these regions were mutated to alanine.

135 ATR phosphorylates BRCA1 on six Ser/Thr residues, including Ser 1423, in vitro.

136 kingly, hepta-phosphorylation of all Ser and Thr residues increased binding 40- and 80-fold with CH3

137 Phosphorylation of Ser and Thr residues increased the affinity for the p53 TAD.

138 In contrast, mutating only the Thr residues inhibited receptor endocytosis to the same

139 Phosphorylation of this Thr residue is predicted to alter the local charge and c

140 PKA-dependent dephosphorylation of IRS1 Ser/Thr residues is a conserved mechanism by which GPCRs sig

141 O-glycosylation of Ser and Thr residues is an important process in all organisms, w

142 ation, phosphorylation of FA proteins on Ser/Thr residues is far more abundant yet its mechanisms and

143 the N-terminal region adjacent to the paired Thr residues is removed during posttranslational maturat

144 linked N-acetylglucosamine (O-GlcNAc) on Ser/Thr residues is ubiquitous in higher eukaryotes and is a

145 by activation segment phosphorylation of Ser/Thr residues is well understood, relatively little is kn

146 specifically installation of O-GlcNAc on Ser/Thr residues, is a dynamic control element for transcrip

147 lNAc) monosaccharide attached to protein Ser/Thr residues, is found on most cancer yet rarely detecte

148 aminin- and virus-binding occurs on specific Thr residues located at the extreme N terminus of the mu

149 perturbed, however, the dynamics of Lys and Thr residues, located primarily in the imperfect KTKEGV

150 Thus, this conserved Thr residue may be essential for the activities of other

151 Phosphorylation at Ser/Thr residues may regulate the functional assembly of FUS

152 arboxyl-terminal serine (Ser) and threonine (Thr) residues, namely, Ser(346), Ser(351), Thr(362), and

153 diated by phosphorylation of two or more Ser/Thr residues near the C terminus.

154 nt addition of N-acetylglucosamine to Ser or Thr residues (O-GlcNAcylation) as well as to truncation.

155 hylene glycol) methyl ether (aaPEG) onto the Thr residue of colistin.

156 Alteration of either the Met or Thr residue of the HAH1p MTCXXC motif has no observable

157 t an analogous E/DxxT/N motif, the conserved Thr residue of which is critical for transmitter phospha

158 biotics involves the modification of Ser and Thr residues of a precursor peptide.

159 c-T2 attaches GlcNAc in alpha-linkage to the Thr residues of all the synthetic mucin repeats.

160 a nucleotide sugar donor (UDP-GalNAc) to Ser/Thr residues of an acceptor substrate.

161 cetylgalactosamine from UDP-GalNAc to Ser or Thr residues of core proteins to form the Tn antigen (Ga

162 of O-linked GlcNAc (O-GlcNAc) on and off Ser/Thr residues of intracellular proteins, termed O-GlcNAcy

163 Here we show that two distinct sets of Ser/Thr residues of IRF-3, on phosphorylation, synergize fun

164 l post-translational modification of Ser and Thr residues of metazoans.

165 we have systematically analyzed roles of Ser/Thr residues of MuV P in viral RNA synthesis.

166 Modification of specific Ser and Thr residues of nucleocytoplasmic proteins with O-GlcNAc

167 NAc Ts) that add alpha-GalNAc to the Ser and Thr residues of peptides.

168 sfer alpha-GalNAc from UDP-GalNAc to Ser and Thr residues of polypeptide acceptors.

169 ansfer GalNAc from UDP-GalNAc to the Ser and Thr residues of polypeptide acceptors.

170 addition of GlcNAc (O-GlcNAcylation) to Ser/Thr residues of proteins and thereby contributes to diab

171 lcNAc) modification (O-GlcNAcylation) on Ser/Thr residues of proteins was discovered 40 y ago.

172 lglucosamine (GlcNAc) from UDP-GlcNAc to Ser/Thr residues of proteins.

173 tached to a side chain hydroxyl group of Ser/Thr residues of proteoglycan proteins.

174 addition of a fucose moiety to specific Ser/Thr residues of target proteins.

175 mutants was constructed in which the 12 Ser/Thr residues of the COOH-terminal portion of the recepto

176 hosphorylation sites) yet retains the 15 Ser-Thr residues of the Ste3p PEST-like ubiquitination-endoc

177 n all 11 GalNAc residues to selected Ser and Thr residues of the Thr-76-Lys-107 stretch of the mucin

178 h depended on the presence of the N-terminal Thr residue, offer a mechanism to explain altered proper

179 4-3-3s work by docking to phosphorylated Ser/Thr residues on a large network of client proteins and m

180 le posttranslational modification of Ser and Thr residues on cytosolic and nuclear proteins of higher

181 promote dephosphorylation of inhibitory Ser/Thr residues on IRS1, including Ser(789).

182 and Tyr residues and phosphorylates Ser and Thr residues on substrates.

183 O-linkage of beta-N-acetylglucosamine to Ser/Thr residues on target proteins, is increasingly recogni

184 cNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic,

185 tide substrates containing a single GalNAc-O-Thr residue placed near either the N or C terminus of th

186 resonance structure of MA showed that these Thr residues point into the hydrophobic core of the prot

187 The Delta320-413 deletion removes 18 Ser-Thr residues (possible YCK-independent phosphorylation s

188 As the insertion of a Thr residue potentially creates a novel phosphorylation

189 that AAL binds O-linked fucose added to Ser/Thr residues present in or adjacent to Ser-rich domains

190 ced phosphorylation of the rFSHR maps to Ser/Thr residues present in the first and third intracellula

191 Three Ser and seven Thr residues recently proven to be phosphoacceptor sites

192 ellular mutation of either of the identified Thr residues reduces the activation of Vgamma9Vdelta2 T

193 -induced phosphorylation of p22(phox) was on Thr residue(s), in agreement with in vitro results.

194 osphorylate MrpC2 and phosphorylates MrpC at Thr residue(s), thus Thr-21 and/or Thr-22 is (are) the l

195 n the number and position of the substituted Thr residue(s).

196 e phosphorylation sites identified seven Ser/Thr residues scattered throughout PIF1.

197 unidentified kinase that phosphorylates Ser/Thr residues (Ser(411), Ser(418), Ser(424), and Thr(421)

198 ural analysis of mPDE revealed that four Ser/Thr residues (Ser-20, Thr-22, Thr-182, and Thr-240) were

199 Among those 12 Ser/Thr residues, Ser(363), Thr(370), and Ser(375) have been

200 70 S6 kinase (p70(s6k)) has a set of Ser and Thr residues (Ser411, Ser418, Ser424, and Thr421) phosph

201 main is unusual and is rich in Asn, Gln, and Thr residues; similar sequences are found in other devel

202 n that p42(mapk/erk2) phosphorylates Ser and Thr residues (T236, S240, S244, and S270) in the membran

203 most K+ channels contains a highly conserved Thr residue that uniquely forms the S4 binding site for

204 which is in the same position as the Ser and Thr residues that are phosphorylated in many other kinas

205 abilized the phosphorylation of multiple Ser/Thr residues that were located in the transactivation do

206 maximal activation phosphorylation of a Ser/Thr residue (Thr(160) in the case of cdk-2) that is cons

207 was found to predominantly phosphorylate two Thr residues (Thr-14 and Thr-32) that are widely conserv

208 essential SPB component Spc29 at a conserved Thr residue, Thr(240).

209 oups of Thr, particularly of the central two Thr residues, Thr13 and Thr24, play key roles in the ice

210 Da and approximately 2300 GalNAcalpha1-O-Ser/Thr residues (Tn-PSM) has been ascribed to an internal d

211 Mutation of any one of these Ser or Thr residues to Ala caused reductions in the receptor ph

212 Mutation of both clusters of Ser/Thr residues to alanines abolished agonist-dependent pho

213 anthipeptides include dehydration of Ser and Thr residues to dehydroalanine and dehydrobutyrine, a tr

214 out lantibiotic-type dehydrations of Ser and Thr residues to dehydroamino acid side chains, cyclodehy

215 modifications involve dehydration of Ser and Thr residues to generate dehydroalanines and dehydrobuty

216 We mutated key Ser and Thr residues to Glu in two regions of the protein.

217 -type glycans are attached to protein Ser or Thr residues via an O-linked glycosidic bond.

218 tion is catalysed by a conserved Gln, Asn or Thr residue, via a hydrogen bond between the amide or hy

219 The Thr residue was mutated to either alanine or aspartate.

220 When this highly conserved Thr residue was substituted with anything other than ser

221 hat phosphorylation of both BRI1 and BAK1 on Thr residues was BR dependent.

222 ant that lacked 17 cytoplasmic Lys, Ser, and Thr residues was nearly insensitive to bortezomib treatm

223 otein, in which the (11)Ser, (12)Thr and (16)Thr residues were mutated to non-phosphorylable alanine,

224 horylation-deficient mutant in which all Ser/Thr residues were replaced with Ala (DeltaST-PAFR).

225 at PP2A dephosphorylates occludin on phospho-Thr residues, whereas PP1 dephosphorylates it on phospho

226 nvolves phosphorylation on key AANAT Ser and Thr residues which results in 14-3-3zeta recruitment and

227 beta and phosphorylates GSK-3beta at the (43)Thr residue, which primes GSK-3beta for its subsequent p

228 ed tyrosine sulfates (TyrSO3-) adjacent to a Thr residue with a core 2-based O-glycan expressing sial

229 on demonstrated universal O glycosylation of Thr residues with a single alpha-D-Man, mannobiose, or m

230 roducing phosphomimetic substitutions of Ser/Thr residues with negatively charged Asp/Glu residues in

231 hosphorylated on serine (Ser) and threonine (Thr) residues with p-Ser predominating.

232 e, and 58% peptide-linked GalNAcalpha1-O-Ser/Thr residues, with 45% of the peptide-linked alpha-GalNA

233 occurs via phosphorylation of an equivalent Thr residue within the "activation loop" region of both

234 and where the processing sites included Ser/Thr residues within +/- 4 residues that could represent

235 phosphorylation of the proline-directed Ser/Thr residues within the tail domain of NF proteins by in

236 ependent upon the phosphorylation of Ser and Thr residues within their histone acetyltransferase doma

237 remain ambiguous due to multiple Ser and/or Thr residues within these peptides.

238 esizing possible phosphorylations of all Ser/Thr residues without assuming a consensus motif.