ライフサイエンスコーパス: threonine residue

1 ly direct phosphorylation of the appropriate threonine residue.

2 membrane when phosphorylated at a conserved threonine residue.

3 orylation of nuclear SREBP-1c at a conserved threonine residue.

4 elated G-proteins have a conserved serine or threonine residue.

5 single O-GlcNAc modification on a serine or threonine residue.

6 functional Ras GAPs, the GRD has a conserved threonine residue.

7 on by these enzymes was found to be only the threonine residue.

8 osphorylation of a conserved activation loop threonine residue.

9 pendent kinase (CDK) 2 at a highly conserved Threonine residue.

10 te (PIP2) and phosphorylation of a conserved threonine residue.

11 tylglucosamine (GlcNAc) residue to serine or threonine residues.

12 carries eight putative regulatory serine and threonine residues.

13 that attach ubiquitin to cysteine or serine/threonine residues.

14 es, including five phosphorylated serine and threonine residues.

15 ed GAG polysaccharides O-linked to serine or threonine residues.

16 horylation and O-GlcNAcylation of serine and threonine residues.

17 y for peptides containing multiple serine or threonine residues.

18 nd is regulated by phosphorylation of serine/threonine residues.

19 1 was phosphorylated on multiple serine and threonine residues.

20 edicted PP2C phosphatase specific for serine/threonine residues.

21 and the side-chain orientation angles of the threonine residues.

22 competes directly with phosphate for serine/threonine residues.

23 ively phosphorylated on serine and weakly on threonine residues.

24 osphorylation of the proline-directed serine/threonine residues.

25 I beta-turns stabilized by the aspartate and threonine residues.

26 phosphorylated endoglin on cytosolic domain threonine residues.

27 three 11-residue repeat units beginning with threonine residues.

28 gh phosphorylation of cytoplasmic serine and threonine residues.

29 dephosphorylation of TRPV1, specifically at threonine residues.

30 phosphorylation of NET occurs on serine and threonine residues.

31 ero-L-manno) and is beta-linked to serine or threonine residues.

32 ne residue that is alpha-linked to serine or threonine residues.

33 with and phosphorylated ATF4 at tyrosine and threonine residues.

34 omain of dense O-glycosylation on serine and threonine residues.

35 of ubiquitin oxyester formation on serine or threonine residues.

36 es with both phosphoacceptor site serine and threonine residues.

37 osphoric acid from phosphorylated serine and threonine residues.

38 osphorylate BIK1 at both tyrosine and serine/threonine residues.

39 ds between proline and phosphorylated serine/threonine residues.

40 lternatively observed on the same serine and threonine residues.

41 he phosphorylation of proteins on serine and threonine residues.

42 tyrosine (Y) residues in addition to serine/threonine residues.

43 orylation of conserved N-terminal serine and threonine residues.

44 peptides involves dehydration of serine and threonine residues.

45 on was clearly identified at both serine and threonine residues.

46 t of glycans to hydroxyl groups of serine or threonine residues.

47 egular outward-projecting parallel arrays of threonine residues.

48 n kinase PknB in vitro on one serine and six threonine residues.

49 rotein receptor-related protein 6 (LRP6), at threonine residue 1479 (Thr1479) and serine residue 1490

50 Remarkably, substitution of the single threonine (residue 15) within the TPXR/H motif caused co

51 vity, as evaluated by its phosphorylation at threonine residue 172 (AMPK-Thr(P)(172)).

52 f Erk correlates with the phosphorylation of threonine residue 184 in RasGRP1.

53 tive activity through autophosphorylation at threonine residue 286 (Thr286) are thought to play a maj

54 lated by cyclin-dependent kinase 1 (CDK1) at threonine residues 345 and 487 in a cell cycle-dependent

55 Inhibitor-1 (I-1) is phosphorylated on threonine residue 35 (Thr35) by the cAMP-dependent prote

56 on was increased phosphorylation of ATF-2 on threonine residue 71 (T71).

57 modification at the physiologically relevant threonine residue 72.

58 X3.1 constructs with AD phosphorylation site threonine residues (89 and 93) mutated to glutamate were

59 eted the hydroxyl group from the neighboring threonine residues abolished amino acid editing activity

60 biochemical evidence that a highly conserved threonine residue acts as a glutamate switch in the repl

61 if, as defined by a phosphorylated serine or threonine residue adjacent to glutamine, [s/t]Q.

62 irect phosphorylation of Cdc14 on serine and threonine residues adjacent to a nuclear localization si

63 2 was also phosphorylated on both serine and threonine residues after PMA treatment.

64 Although threonine residues analogous to Thr(705) of XA21 are pre

65 The serine/histidine juxtaposition to a threonine residue and a carbonyl oxygen atom, along with

66 mitosis, is essential to dephosphorylate the threonine residues and activate the APC/C.

67 The serine/threonine residues and betaTrCP-binding site in the N-te

68 it is phosphorylated on multiple serine and threonine residues and can be a target for phosphorylati

69 onfirmed the role of conserved extracellular threonine residues and demonstrated that FXYD7 protein,

70 We mutated C-terminal serine and threonine residues and examined their role in NOPR traff

71 phosphorylation at the Akt-regulating serine/threonine residues and induced prolonged nuclear accumul

72 catalyze both the dehydration of serine and threonine residues and the Michael-type additions of cys

73 ntly induce Vangl2 phosphorylation of serine/threonine residues and Vangl2 activities depend on its l

74 specifically counteracts phosphorylation on threonine residues, and consequently, we find that threo

75 The results suggest that these threonine residues are cooperatively involved in PAC1 ac

76 The most frequently mutated nonserine/threonine residues are D32 and G34.

77 at in addition to a di-leucine motif, serine/threonine residues are important for internalization and

78 When all the threonine residues are phosphorylated, Cdc20 binding to

79 Mutation of a threonine residue at amino acid (aa) 148 and a serine re

80 Using mass spectrometry analysis, the threonine residue at position 286 of P of parainfluenza

81 strate that alanine substitution of a single threonine residue at position 61 (T61) in CD30v abrogate

82 Instead, these proteins invariably contain a threonine residue at this position.

83 usters identified previously but also at the threonine residues at positions 143 and 146.

84 These effects require critical serine and threonine residues at positions Ser119, Ser130, Thr132,

85 oxygen species and phosphorylation of serine/threonine residues at sites in the C-terminus of the pro

86 phorylation by CKII on the identified serine/threonine residues at the N-terminal unstructured domain

87 itution mutants of the predicted beta-strand threonine residues became antagonists at the PAC1 recept

88 50cin lacks the almost universally conserved threonine residue believed to be involved in dioxygen ac

89 at Env mutants containing an extra serine or threonine residue between the second and third positions

90 Mutation of the four serine/threonine residues between residues 355 and 364 led to t

91 was shown to be phosphorylated at serine and threonine residues, but not tyrosine.

92 DKs that require phosphorylation of a serine/threonine residue by a CDK-activating kinase (CAK) for f

93 clear proteins can be modified on serine and threonine residues by O-linked beta-N-acetylglucosamine

94 s is known about the glycosylation of serine/threonine residues by O-linked N-acetylglucosamine (O-Gl

95 N cofactors in subunits B and C are bound to threonine residues by phosphoester linkages.

96 ctivation and phosphorylation of AQP1 at two threonine residues by protein kinase C.

97 inding, but that the presence of neighboring threonine residues can inhibit these processes.

98 of mouse (m)FFAR4 occurs at five serine and threonine residues clustered in two separable regions of

99 te Parkin, as the mutation of all serine and threonine residues conserved between Drosophila and huma

100 ent, APC-mediated phosphorylation of S1P1 on threonine residues consistent with S1P1 receptor activat

101 riptional oncoproteins at specific serine or threonine residues creates binding sites for the COP1 tu

102 A covalently bound N-acetyl-l-threonine residue demonstrates the geometry of C3b attac

103 Mutation of all seven serine/threonine residues distal to residue 381 did not affect

104 ations include the dehydration of serine and threonine residues followed by the intramolecular additi

105 le-associated protein tau at specific serine/threonine residues found in paired helical filaments (PH

106 horylation of tau protein at specific Serine/Threonine residues found in paired helical filaments, su

107 posttranslational modification of serine and threonine residues functions as a critical regulator of

108 ingle mutations of either of these conserved threonine residues had minimal effects on amino acid edi

109 pathway, p38 MAPK, phosphorylates a critical threonine residue in ATF6 upstream of its DNA binding do

110 ed levels of phosphorylation of a regulatory threonine residue in both isoforms in the mutants.

111 tic subunit and phosphorylate the equivalent threonine residue in its activation loop in vitro.

112 vivo could result in O-glycosylation of the threonine residue in question and that this could boost

113 epends on the phosphorylation of a conserved threonine residue in the actin-binding domain.

114 ilitated by phosphorylation of the conserved threonine residue in the actin-binding domain.

115 nd rate-limiting phosphorylation occurs at a threonine residue in the activation loop (AL), which tri

116 also show that YopJ causes acetylation of a threonine residue in the activation loop of both the alp

117 activated by phosphorylation at a conserved threonine residue in the activation loop of the kinase d

118 A threonine residue in the regulatory segment, which when

119 e A-type gamma-aminobutyric acid receptor, a threonine residue in the second transmembrane domain is

120 actin assembly by AMPylation of a conserved threonine residue in the switch 1 region of Rho GTPases.

121 ragine residue in transmembrane helix 8 or a threonine residue in transmembrane helix 5.

122 OGT transfers O-GlcNAc onto serine and threonine residues in intrinsically disordered domains o

123 obal assessment of phosphorylation of serine/threonine residues in IRS-1 in vivo in humans.

124 The 182 serine and 60 threonine residues in IRS-1 make position-by-position an

125 enin is phosphorylated at defined serine and threonine residues in its amino (N) terminus.

126 ed by phosphorylation on multiple serine and threonine residues in its C terminus.

127 ost-translational modification of serine and threonine residues in nuclear and cytoplasmic proteins,

128 Neither serine nor threonine residues in peptides corresponding to other ph

129 indicate that phosphorylation of serine and threonine residues in proline-rich sequences induces a c

130 ngle N-acetylglucosamine sugar to serine and threonine residues in proteins by the enzyme O-linked be

131 The phosphorylation of threonine residues in proteins regulates diverse process

132 co plants BRI1-FLAG became phosphorylated on threonine residues in response to brassinolide applicati

133 acetylglucosamine (O-GlcNAc) onto serine and threonine residues in response to stimuli or stress anal

134 ic groups attached by a phosphoester bond to threonine residues in subunits NqrB and NqrC.

135 ave evolved to target adjacent and essential threonine residues in switch region I of immunity-relate

136 ds to phosphorylated proline-directed serine/threonine residues in target proteins and isomerizes cis

137 Acetylation of critical serine/threonine residues in the activation loop of Drosophila

138 me A (CoA) to modify the critical serine and threonine residues in the activation loop of MAPKK6 and

139 strate that phosphorylation of two conserved threonine residues in the activation loop of the kinase

140 We identified four serine or threonine residues in the C-terminal domain of Runx2 tha

141 singly or doubly phosphorylated at serine or threonine residues in the C-terminal sequence SSATDHT (a

142 All of the observed mutations altered serine/threonine residues in the GSK3beta binding domain in exo

143 that a poxvirus kinase phosphorylates serine/threonine residues in the human small ribosomal subunit

144 Phosphorylation of serine/threonine residues in the ID induces charge repulsions t

145 ignaling and that the presence of serine and threonine residues in the PAR2 C-tail hinder constitutiv

146 We mutated serine and threonine residues in the putative activation segment of

147 sst2A phosphorylation occurs on serine and threonine residues in the third intracellular loop and c

148 ionally important mutations of glutamine and threonine residues in the TM domain on its structure, pr

149 re activated by phosphorylation of conserved threonine residues in their activation loops.

150 tibiotic synthases that dehydrate serine and threonine residues in their peptide substrates and catal

151 Phosphorylation of threonine residues in this region regulates both the tar

152 dopsis seedlings, whereas phosphorylation of threonine residues increased rapidly and then remained c

153 that catalyzes O-GlcNAcylation of serine or threonine residues, interacts with UBN1, modifies HIRA,

154 after conversion of CXCR7 C-terminal serine/threonine residues into alanines.

155 ent of 566 RND transporters showed that this threonine residue is conserved in about 96% of cases.

156 An evolutionarily conserved N-terminal threonine residue is required for Cyclin-Cdk response an

157 Phosphorylation of the critical PKA threonine residue is stimulated by engagement of TCR/CD2

158 O-GlcNAc modification of serine and threonine residues is a common regulatory post-translati

159 lucosamine (O-GlcNAc) modification of serine/threonine residues is an abundant posttranslational modi

160 tion of peptides at phosphorylated serine or threonine residues is demonstrated.

161 To determine whether any one of these serine/threonine residues is phosphorylated and/or is involved

162 The role of native threonine residues is unclear.

163 ed with N-acetyl-galactosamine on serine and threonine residues, is regulated by the substrate specif

164 of O-linked N-acetylglucosamine to serine or threonine residues, known as O-GlcNAcylation.

165 O-GlcNAc cycles on serine or threonine residues like phosphorylation, is nearly as ab

166 The mutation occurs at a threonine residue located near the cytoplasmic end of th

167 but depends on phosphorylation of the serine/threonine residues located in the C-terminal domain of P

168 ir target proteins via phosphorylated serine/threonine residues located within distinct motifs.

169 ion sites (acidic residue n + 3 to serine or threonine residue) located immediately adjacent to both

170 y phosphorylated, with at least 14 of its 19 threonine residues modified.

171 In addition to disruption of key serine and threonine residues, mutations are frequently reported in

172 ion of casein kinase IIalpha (CK2alpha) on a threonine residue near its N terminus.

173 s a result of phosphorylation on a conserved threonine residue near the C terminus.

174 e kinases is a highly conserved "gatekeeper" threonine residue near the kinase active site.

175 ses the addition of O-GlcNAc onto serine and threonine residues (O-GlcNAcylation) in vivo.

176 f N-Acetylglucosamine (GlcNAc) on serine and threonine residues (O-GlcNAcylation) is an essential pro

177 on by which GlcNAc is attached to the serine/threonine residues of a protein via an O-linked glycosid

178 es the transfer of O-linked GlcNAc to serine/threonine residues of a variety of target proteins, many

179 ylation by transferring GalNAc to serine and threonine residues of acceptor polypeptides.

180 exposes the N-terminal phosphorylated serine/threonine residues of beta-catenin to PP2A.

181 sylation (O-GlcNAcylation) of the serine and threonine residues of cellular proteins is a dynamic pro

182 c) sugar moiety to hydroxyl groups of serine/threonine residues of cytosolic and nuclear proteins.

183 fication on hydroxyl groups of serine and/or threonine residues of cytosolic and nuclear proteins.

184 ynamic and reversible modification of serine/threonine residues of different cellular proteins cataly

185 Ac moiety from UDP-GlcNAc to specific serine/threonine residues of hundreds of nuclear and cytoplasmi

186 a-N-acetylglucosamine (GlcNAc) to serine and threonine residues of intracellular proteins (O-GlcNAc),

187 GlcNAc) modification found on the serine and threonine residues of intracellular proteins is an induc

188 iology through phosphorylation of serine and threonine residues of many proteins in most cell types.

189 inkage of beta-N-acetylglucosamine to serine/threonine residues of membrane, cytosolic, and nuclear p

190 rmal conditions, the proline-directed serine/threonine residues of neurofilament tail-domain repeats

191 n role in adding beta-O-GlcNAc to serine and threonine residues of nuclear and cytoplasmic proteins,

192 tion of an N-acetylglucosamine to serine and threonine residues of nuclear and cytosolic proteins (O-

193 OGTs add a GlcNAc monosaccharide to serine/threonine residues of nuclear and cytosolic proteins.

194 samine (termed O-GlcNAcylation) on serine or threonine residues of nuclear or cytoplasmic proteins se

195 cetylglucosamine beta-O-linked to serine and threonine residues of nucleocytoplasmic proteins (O-GlcN

196 posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by beta

197 dification that cycles on and off serine and threonine residues of nucleocytoplasmic proteins.

198 d N-acetylglucosamine residues to serine and threonine residues of nucleocytoplasmic proteins.

199 onal modification occurring on the serine or threonine residues of nucleocytoplasmic proteins.

200 mes: OGT, which transfers O-GlcNAc to serine/threonine residues of numerous cellular proteins, and TE

201 on of the hydroxyl substituent in serine and threonine residues of peptides.

202 lglucosamine sugar molecule on serine and/or threonine residues of protein chains is referred to as O

203 cleotide sugar donor UDP-GlcNAc to serine or threonine residues of protein substrates.

204 T), which attaches O-GlcNAc to serine and/or threonine residues of proteins and by O-GlcNAcase, which

205 produces the covalent linkage of serine and threonine residues of proteins.

206 the addition of a GlcNAc group to serine and threonine residues of TET proteins and thereby decreases

207 Our results suggest C-terminal serine and threonine residues of the FPR represent a combinatorial

208 phosphatase, selectively dephosphorylates a threonine residue on p38 MAPK and mediates a negative fe

209 S could act to covalently modify a conserved threonine residue on Rho, Rac, and Cdc42 with adenosine

210 The modification of serine/threonine residues on cytoplasmic and nuclear proteins b

211 N-acetylglucosamine (O-GlcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic pro

212 f the gamma phosphate from ATP to serine and threonine residues on protein substrates.

213 pectrometric identification of 17 serine and threonine residues on SHIP1 as being phosphorylated by P

214 Phosphorylation of serine/threonine residues preceding a proline regulates the fat

215 rylation of tau and APP on certain serine or threonine residues preceding proline affects tangle form

216 cMyBP-C (142 kDa) has 81 serine and 73 threonine residues presenting a major challenge for uneq

217 Acetylation of serine and threonine residues prevents them from being phosphorylat

218 nearly all of the triplet repeats contain a threonine residue, providing multiple potential sites fo

219 amine linkage (O-GlcNAcylation) to serine or threonine residues regulates numerous biological process

220 -N-acetylglucosamine (O-GlcNAc) to serine or threonine residues regulates numerous metazoan cellular

221 clear and cytoplasmic proteins at serine and threonine residues, regulates some aspects of mitotic ch

222 ed a surprisingly high substitution rate for threonine residues, resulting in a reduction of threonin

223 MPAK, in turn, phosphorylated MFP2 on threonine residues, resulting in incorporation of MFP2 i

224 Mutational analysis of serine and threonine residues revealed that substitution of threoni

225 the RD kinase, PktA5, autophosphorylated on threonine residue(s) and phosphorylated the artificial s

226 t TGF-beta induces Fli1 phosphorylation on a threonine residue(s).

227 he activated GSK-3beta phosphorylates Fyn at threonine residue(s).

228 phosphorylating highly conserved serine and threonine residues (S359/T360) within the activation loo

229 (rich in proline, glutamic acid, serine, and threonine residues) sequence in NFkappaB stripping, a mu

230 more than 50 phosphorylated IRS1 serine and threonine residues (Ser(P)/Thr(P) residues) in IRS1 from

231 tterns of both mucins (comprising 50+ serine/threonine residues), specific effects of neighboring pep

232 BC membranes reveals 9 phosphorylated serine/threonine residues, suggesting that activation of atNHE1

233 ed by phosphorylation of the most C-terminal threonine residue, switching them from an activated to a

234 A conserved threonine residue (T169) in the PIG-1 activation loop is

235 t casein kinase 2 phosphorylates a conserved threonine residue (T22) in alpha helix-1 of the yeast Hs

236 This phosphorylation occurs at a threonine residue, T226, within the Atg1 activation loop

237 We speculated that four threonine residues (T231, T236, T243, and T247) in the a

238 Phosphorylation of a threonine residue (T308 in Akt1) in the activation loop

239 Using mass spectrometry, we identified a threonine residue, T346, as the main autoacetylation sit

240 ty was observed with a mutant of a conserved threonine residue, T370S, also implicated to participate

241 ls is the phosphorylation status of a single threonine residue (T389) within the extensive ( approxim

242 ence that PKC eta phosphorylates occludin on threonine residues (T403 and T404) and plays a crucial r

243 effect of CaMKII was abolished by mutating a threonine residue (T425) at a consensus CaMKII phosphory

244 sphorylates the Par-1 kinases on a conserved threonine residue (T595) to regulate localization and ki

245 PLK1 phosphorylates NDR1 at three putative threonine residues (T7, T183 and T407) at mitotic entry,

246 P2X7R, a loop insertion (residues 73-79) and threonine residues T90 and T94, are required for high af

247 ce that Akt-mediated phosphorylation of USP8 threonine residue T907 contributes to USP8 stability.

248 with the carbonyl oxygen at C4, a conserved threonine residue that forms hydrogen bonds with N5, and

249 ydrogen bonds with N5, and another conserved threonine residue that forms hydrogen bonds with the car

250 eoformans crystal structure, in particular a threonine residue that may serve as an additional point

251 TNF-alpha induced ERM phosphorylation on the threonine residue that required activation of p38, PKC i

252 IRG, and 2) it alters the orientation of two threonine residues that are targeted by the Toxoplasma S

253 Although the serine and threonine residues that form GPCR kinase phosphorylation

254 ct with proteins phosphorylated on serine or threonine residues that precede prolines (pS/T-P), such

255 ically highly non-random gain of serines and threonines, residues that are potential substrates of po

256 tosolic G6PD6 on an evolutionarily conserved threonine residue, thereby stimulating its activity.

257 (2+)/CaM-bound CaMKIV on its activation loop threonine (residue Thr(200) in human CaMKIV) by Ca(2+)/c

258 Phosphorylation of a threonine residue (Thr(11)) in Cds1 by Rad3 occurs at a

259 n, but phosphorylation of a highly conserved threonine residue (Thr(328)) in the activation loop is t

260 AMP or ADP binding and phosphorylation of a threonine residue (Thr-172) within the activation loop o

261 factor that is phosphorylated on a critical threonine residue (Thr-72) by the Ras/MAPK pathway in th

262 stal structure information, two other nearby threonine residues (Thr(247) and Thr(248)) were hypothes

263 Previously, we identified one of these threonine residues (Thr(252)) as a critical amino acid s

264 he mediator Mrc1 function to phosphorylate a threonine residue, Thr(11), in the SQ/TQ domain of Cds1.

265 comprised of Thr-380 and a second conserved threonine residue, Thr-398.

266 that phosphorylation occurs on two specific threonine residues, Thr-150 and Thr-208.

267 Cdr2 through phosphorylation of a conserved threonine residue (Thr166) in the activation loop of the

268 mutagenesis of Ee;CDKF;1 indicated that two threonine residues (Thr291 and Thr296) were mutually res

269 The specific contributions of a conserved threonine residue (Thr380) to autoprocessing and hydrola

270 Here we study the effect of a threonine residue (Thr62 in hDAT) that is highly conserv

271 proteins are phosphorylated on this critical threonine residue through TNF-alpha-induced activation o

272 Substitution of the threonine residue to alanine uncoupled specificity as in

273 esidue and the PTX molecule, we mutated this threonine residue to serine, valine, and tyrosine to cha

274 Mutation of these threonine residues to alanine (DNA-PKcs(3A)) renders DNA

275 lts in phosphorylation of GAB1 on serine and threonine residues to form GAB1-p85 PI3K complex.

276 s of individual and combinatorial serine and threonine residues to internalization, desensitization,

277 rtance of individual and combined serine and threonine residues to these processes is not well unders

278 tly shown to be phosphorylated on serine and threonine residues upon activation of NADPH oxidase, but

279 ced the wild-type proline residue, whereas a threonine residue was found in RCASBP M2C (797-8).

280 osphorylation, which primarily occurred on a threonine residue, was accompanied by a 50% decrease in

281 some organization, phosphorylated serine and threonine residues were identified and changed to alanin

282 in Ntcp translocation, each of these serine/threonine residues were mutated to alanine.

283 To assess the loop's role in catalysis, two threonine residues were mutated to alanine: QFR Thr-A244

284 94R) induce dephosphorylation of occludin on threonine residues, whereas active PKC eta elevates occl

285 t 2.4-A resolution, reveals a phosphorylated threonine residue, which provides clues about the cataly

286 We propose that these threonine residues, which are also conserved in the homo

287 the phosphorylation of several nearby serine/threonine residues, which constitute a phosphorylation h

288 Unlike phospho-serine and phospho-threonine residues, which in some cases can be mimicked

289 ay facilitate the glycosylation of serine or threonine residues, which occur in sequence contexts tha

290 transmembrane helices contain serine and/or threonine residues whose side chains form intrahelical H

291 ified by O-linked glycosylation of serine or threonine residues with beta-N-acetylglucosamine (O-GlcN

292 tudy the rotational energy profiles of these threonine residues with the use of molecular mechanics (

293 Surprisingly, a highly conserved threonine residue within the bound sorting signal substr

294 riggering Cdk2-mediated phosphorylation of a threonine residue within the flexible C-terminus of p27.

295 ue within the kinase inhibitory domain and a threonine residue within the flexible C-terminus.

296 We investigated the role of a threonine residue within the highly conserved and putati

297 protein kinase that phosphorylates serine or threonine residues within extracellular cadherin domains

298 Subsequently, phosphorylation of serine/threonine residues within five repeating signature PPPSP

299 asmic proteins are glycosylated at serine or threonine residues within the specific three-amino acid

300 sulted in the identification of eight serine/threonine residues within the third cytoplasmic loop of