ライフサイエンスコーパス: PTPase

1 PTPase activities in subcellular fractions from the nond

2 PTPase activity, in turn, is highly regulated in vivo by

3 PTPase inhibitors, such as pervanadate or phenylarsine o

4 PTPase kinetics are generally interrogated spectrophotom

5 -1 and a mutant protein containing the SHP-1 PTPase domain alone.

6 to insulin, protein-tyrosine phosphatase 1B (PTPase 1B) dephosphorylates 95- and 160-180-kDa tyrosine

7 Human PTP-1B, a PTPase implicated to play an important role in the regul

8 explaining how tyrosine phosphorylation of a PTPase is important in signal transduction.

9 t of Jurkat cells with phenylarsine oxide, a PTPase inhibitor, inhibited ameba-induced dephosphorylat

10 ific activity of immunoprecipitated PTP1B, a PTPase homolog implicated in the regulation of insulin s

11 e phosphatases (PTPases), including PTP1B, a PTPase that has been previously implicated in the regula

12 esent study, we treated adipose cells with a PTPase inhibitor containing the phosphotyrosyl mimetic d

13 tion, synaptic stimulation may also activate PTPase which acts globally to destabilize preexisting AC

14 more, by introducing a constitutively active PTPase into cultured muscle cells, hot spots were disper

15 mic PTPase domain (D1) of CD45 is the active PTPase, which may be regulated by an enzymatically inact

16 of the WPD motif present in standard active PTPases.

17 That suramin is a high affinity PTPase inhibitor is consistent with the observation that

18 -19) which is the signature sequence for all PTPases.

19 tion of protein-tyrosine phosphorylation and PTPase inhibition by several K vitamin analogs.

20 orylation sites within both the receptor and PTPase 1B.

21 es (PTKs), receptors for growth factors, and PTPases.

22 Anti-PTPase 1B antibodies coprecipitated a 95-kDa PY protein

23 A novel ELISA-based PTPase assay was developed to rapidly screen protein fra

24 useful in defining the interactions between PTPases and their targets.

25 f magnitude slower than O-aryl phosphates by PTPases.

26 detailed understanding of the role played by PTPases in various signaling pathways has not yet been a

27 at this Src activity is highly restricted by PTPases.

28 nd of ligand-free and arsenate-ligated C403S PTPase contain a single W3 band which is correlated to t

29 contrast, the ligand-free and ligated C403S PTPase remain in the loop closed configuration over the

30 The lack of WpD loop motion in the C403S PTPase is believed to be due to either a loss of repulsi

31 ase and of both ligation states of the C403S PTPase reveal a single correlation time of 30-48 ns due

32 rted demonstration that PTPH1 is a candidate PTPase capable of interacting with and dephosphorylating

33 lytic cleavage between the SH2 and catalytic PTPase domains.

34 on of the SH2 domains to yield the catalytic PTPase domain.

35 tution of CD45(-) T cells with specific CD45 PTPase mutants allowed demonstration of a critical role

36 Whereas CD45 PTPase activity was absolutely required for the reconsti

37 The activity of purified T cell PTPase was inhibited only by the thioether analogs, but

38 electivity over the highly homologous T-cell PTPase (TCPTP) and high selectivity over other phosphata

39 In addition, inhibition of Jurkat cell PTPases with phenylarsine oxide blocked Jurkat cell apop

40 conclude that SHP-2 is an important cellular PTPase that is mutated in myeloid malignancies.

41 Identification of cellular PTPase substrates will help elucidate the biological fun

42 inhibition of up to 62% of overall cellular PTPase activity, as measured by a novel method using str

43 (2)O(2) substantially reduced total cellular PTPase activity to a degree approximately equivalent to

44 results suggest that inhibition of cellular PTPases by sulfhydryl arylation and subsequent perturbat

45 The inhibition of cellular PTPases by the drug was suggested by its rapid induction

46 2)O(2) as well as the inhibition of cellular PTPases, including PTP1B, and was associated with reduce

47 e WpD loop (previously inferred by comparing PTPase X-ray single-cyrstal diffraction structures in th

48 Suramin is a reversible and competitive PTPase inhibitor with Kis values in the low microM range

49 1) as a general, reversible, and competitive PTPase inhibitor.

50 Consequently, PTPases and DSPases have a central role controlling sign

51 hosphatase 1B (PTP1B), SH2 domain-containing PTPase-2 (SHP-2), leukocyte common antigen-related (LAR)

52 In contrast, PTPase activity in both fractions from the obese subject

53 o studies suggest that the first cytoplasmic PTPase domain (D1) of CD45 is the active PTPase, which m

54 y found in the WPD motifs in all cytoplasmic PTPases and all the D1 domains of receptor-like PTPases,

55 hose observed for the general acid-deficient PTPase D356N.

56 All detectable PTPase activity maps to PTP-D1 in vitro.

57 yr recognition are conserved among different PTPases, it is possible to generate selective inhibitors

58 horylation sites were in the membrane-distal PTPase domain (D2) and the C-terminal tail and none were

59 he "inactive" D2 domains of many dual-domain PTPases, in place of the WPD motif present in standard a

60 he F(2)Pmp analogue showed slightly enhanced PTPase stimulation compared with the Pmp analogue, consi

61 Like eukaryotic PTPases, YopH catalyzes the hydrolysis of the phosphate

62 ghly enriched protein fractions that exhibit PTPase activities toward a tyrosine-phosphorylated TCR z

63 This effect of exogenous PTPase was also blocked by pervanadate.

64 L-1 is a predominantly nuclear, farnesylated PTPase that has been linked to the control of cellular g

65 The generation of ROS is essential for PTPase inactivation, receptor tyrosine kinase activation

66 oughput assay procedure that can be used for PTPase inhibitor screening.

67 suggesting a common catalytic mechanism for PTPases from all eukaryotic systems.

68 The data also suggest a role for PTPases in the PKC action.

69 ne (pTyr) mimic into a peptide substrate for PTPases.

70 ation of the binding affinity of suramin for PTPases and several catalytically impaired mutant PTPase

71 2) domain of PTPalpha by itself is a genuine PTPase, possessing catalytic activity comparable to that

72 To identify PTPase 1B tyrosine (Tyr) residues that are phosphorylate

73 lso suggest roles for Gln-446 and Gln-450 in PTPase catalysis.

74 ts shed light on the role of the WPD loop in PTPase-mediated catalysis, and are useful in structure-b

75 nts to define the role of phosphorylation in PTPase activity and in signaling.

76 e site, it is unclear whether selectivity in PTPase inhibition can be achieved.

77 nsfer from the phosphoenzyme intermediate in PTPases can only occur to water and not to other nucleop

78 (H/V)C(X)5R(S/T) signature motif present in PTPases.

79 ated cells expressing catalytically inactive PTPase 1B (CS) were immunoadsorbed and subsequently immu

80 An E2171D mutation that retains or increases PTPase activity but eliminates PIPase activity, eliminat

81 to determine the functionality of individual PTPases.

82 idate the biological functions of individual PTPases.

83 Cpd 5 inhibited PTPase activity, which was also significantly antagonize

84 In hepatocytes and HuH7 cells, DCA inhibited PTPase activity.

85 evidence that sodium stibogluconate inhibits PTPases and augments cytokine responses.

86 ll death occurs by a mechanism that involves PTPase activation.

87 e-trapping mutants are being used to isolate PTPase substrates.

88 a SHP2 activator but also is a target of its PTPase.

89 ult from its PIPase activity rather than its PTPase activity.

90 ivalent to that of pervanadate, a well known PTPase inhibitor.

91 replacement of CD45 D2 with that of the LAR PTPase to form a CD45/LAR:D2 chimera, abrogates CD45-dep

92 hibitors for individual members of the large PTPase family of enzymes.

93 ases and all the D1 domains of receptor-like PTPases, only increases the kcat for D2 by 4-fold.

94 resolution structure of the second human LMW PTPase isoenzyme provides the opportunity to examine the

95 cular weight phosphotyrosyl phosphatase (LMW PTPase) is reported here at a resolution of 1.6 A.

96 is likely to be similar to that of other LMW PTPases, the hydrogen bonding and electrostatic changes

97 ar weight protein tyrosine phosphatases (LMW PTPases) studied to date contain a conserved, high-pK(a)

98 hich can be observed for other wild-type LMW PTPases.

99 ecombinant catalytic domain of PTPRQ has low PTPase activity against tyrosine-phosphorylated peptide

100 n-446 residue is responsible for maintaining PTPases' strict hydrolytic activity and for preventing t

101 enesis and kinetic analysis in the mammalian PTPase PTP1.

102 ese findings to skeletal muscle, we measured PTPase activity in the skeletal muscle particulate fract

103 ements and the binding proteins that mediate PTPase and neuregulin-dependent gene expression remain u

104 ocking of signaling proteins and to modulate PTPase activity.

105 levels of transgenic CD45RO, or with mutant PTPase null or PTPase-low CD45R0.

106 the general acid deficient Asp to Ala mutant PTPases display an enhanced affinity toward suramin, whi

107 nchers in the wild-type and the C403S mutant PTPases.

108 es and several catalytically impaired mutant PTPases by fluorescence titration techniques.

109 unit in the wild type and all of the mutant PTPases, either in dianionic or in monoanionic form.

110 stic considerations, we seek to create novel PTPase mutants with improved substrate-trapping properti

111 A or BKA prevented DCA-induced inhibition of PTPase activity.

112 kinase activity, separate from inhibition of PTPase.

113 is effect cannot be accounted for by loss of PTPase activity per se.

114 Unfortunately, only a limited number of PTPase substrates have been identified with these two mu

115 e with the kinetic parameters in a number of PTPase variants as predicted by the transition state bin

116 Defective or inappropriate regulation of PTPase activity leads to aberrant tyrosine phosphorylati

117 These results implicate a role of PTPase in AChR cluster dispersal and formation.

118 of cellular proteins and on the activity of PTPases.

119 We have characterized the expression of PTPases in 5-fluorouracil (5-FU)-treated murine bone mar

120 The four families of PTPases, their substrates, structure, function, regulati

121 We report here on the identification of PTPases capable of dephosphorylating the phosphorylated

122 Partial inhibition of PTPases by OVA mimicked TCDD in producing EGF- and Src-d

123 ogs is closely associated with inhibition of PTPases by sulfhydryl arylation and with tyrosine phosph

124 Inhibition of PTPases may be an effective method in the treatment of T

125 Inhibiton of PTPases may be an effective method in the treatment of t

126 t of leishmaniasis, is a potent inhibitor of PTPases Src homology PTPase1 (SHP-1), SHP-2, and PTP1B b

127 A second inhibitor of PTPases, 3,4 dephosphatin, gave very similar effects, in

128 fluxes of a number of specific inhibitors of PTPases have been investigated.

129 e few readily available potent inhibitors of PTPases or DSPases other than vanadate.

130 killing, we investigated the involvement of PTPases during the attachment of E. histolytica to targe

131 rovide clear evidence for the involvement of PTPases in a major signaling network in plants.

132 mutant would be applicable to all members of PTPases for substrate identification.

133 demonstrating differential sensitivities of PTPases to the inhibitor.

134 Suramin binds to the active site of PTPases with a binding stoichiometry of 1:1.

135 when suramin is bound to the active site of PTPases, its fluorescence is enhanced approximately by 1

136 o abolished the inhibitory effects of DCA on PTPase activity.

137 Pmp groups show close to additive effects on PTPase stimulation, suggesting dual SH2 domain occupancy

138 sgenic CD45RO, or with mutant PTPase null or PTPase-low CD45R0.

139 68 was also selective against several other PTPases.

140 terminus could give rise to a 9-fold overall PTPase activation, 30-50% of the value associated with d

141 Protein tyrosine phosphatase (PTPase) 1B (PTP1B) has been implicated as a key negative

142 have increased protein-tyrosine phosphatase (PTPase) activity in adipose tissue that can dephosphoryl

143 y regulated by protein-tyrosine phosphatase (PTPase) activity.

144 n the Yersinia protein-tyrosine phosphatase (PTPase) and its T410A, D356N, W354A, R409K, and D356A mu

145 Using in vitro protein tyrosine phosphatase (PTPase) assays, we found that sodium stibogluconate, a d

146 -Ten acts as a protein tyrosine phosphatase (PTPase) at the nephrin-PI3K binding site and renders PI3

147 The receptor protein tyrosine phosphatase (PTPase) Dlar has an ectodomain consisting of three immun

148 members of the protein tyrosine phosphatase (PTPase) family share a common mechanism of action (hydro

149 ing a putative protein tyrosine phosphatase (PTPase) from Arabidopsis (referred to as AtPTP1).

150 f the Yersinia protein tyrosine phosphatase (PTPase) has been investigated by site-directed mutagenes

151 The CD45 protein tyrosine phosphatase (PTPase) has been shown to regulate the activity of Lck a

152 his study, the role of tyrosine phosphatase (PTPase) in the dispersal of hot spots was examined.

153 Protein tyrosine phosphatase (PTPase) inhibition by orthovanadate (OVA) showed that th

154 for designing protein tyrosine phosphatase (PTPase) inhibitors is to incorporate a nonhydrolyzable p

155 nisms whereby the CD45 tyrosine phosphatase (PTPase) regulates T cell receptor (TCR) signaling respon

156 ulation of the protein tyrosine phosphatase (PTPase) SHP-2 by tyrosine phosphorylation has been diffi

157 regulation of protein tyrosine phosphatase (PTPase) SHP-2 is proposed to involve tyrosine phosphoryl

158 lated cells is protein-tyrosine phosphatase (PTPase) SHP2, which contains tandem SH2 domains.

159 ukaryotic-like protein tyrosine phosphatase (PTPase) termed Yersinia outer protein H (YopH) that is e

160 eptor tyrosine protein tyrosine phosphatase (PTPase) that relays signals from activated growth factor

161 transmembrane protein-tyrosine phosphatase (PTPase), has been proposed to mediate docking of signali

162 dentified as a protein tyrosine phosphatase (PTPase)-like protein that is upregulated in a model of r

163 kinetics of a protein-tyrosine phosphatase (PTPase).

164 with the PRL-1 protein-tyrosine phosphatase (PTPase).

165 y phosphatase (protein tyrosine phosphatase; PTPase), was shown recently to play a broad role in huma

166 The Yersinia protein tyrosine phosphatases (PTPase) contain a single and invariant tryptophan (W354)

167 Protein tyrosine phosphatases (PTPase) play important roles in the intracellular signal

168 lecular weight phosphotyrosine phosphatases (PTPases) constitute a distinctive class of phosphotyrosi

169 activation of protein tyrosine phosphatases (PTPases) and activation of ERBB1 and the extracellular-r

170 e activity of protein-tyrosine phosphatases (PTPases) and induced protein-tyrosine phosphorylation in

171 of host cell protein tyrosine phosphatases (PTPases) and protein dephosphorylation is an important m

172 activation of protein tyrosine phosphatases (PTPases) and that AT2 receptor stimulation is associated

173 Protein tyrosine phosphatases (PTPases) are essential proteins in many cellular process

174 Protein tyrosine phosphatases (PTPases) are important regulators of signal transduction

175 Protein tyrosine phosphatases (PTPases) are important targets for the treatment of insu

176 Protein tyrosine phosphatases (PTPases) are involved in the control of tyrosine phospho

177 nstrated that protein tyrosine phosphatases (PTPases) are required for iNOS transcription, while the

178 subfamily of protein tyrosine phosphatases (PTPases) associated with oncogenic and metastatic phenot

179 Protein-tyrosine phosphatases (PTPases) catalysis involves a cysteinyl phosphate interm

180 Tyrosine phosphatases (PTPases) dephosphorylate phosphotyrosines while dual-spe

181 Protein tyrosine phosphatases (PTPases) exist in plants, but their role in plant signal

182 Protein-tyrosine phosphatases (PTPases) feature an essential nucleophilic thiol group w

183 Protein-tyrosine phosphatases (PTPases) form a large family of enzymes that serve as ke

184 ecular weight protein tyrosine phosphatases (PTPases) found to be ubiquitous in mammalian cells.

185 l cancers, on protein-tyrosine phosphatases (PTPases) has been examined.

186 Several protein tyrosine phosphatases (PTPases) have been implicated as regulatory agents in th

187 Protein tyrosine phosphatases (PTPases) have been shown to be negative regulators of th

188 Protein tyrosine phosphatases (PTPases) have been shown to be negative regulators of th

189 nvolvement of protein tyrosine phosphatases (PTPases) in mediating the dephosphorylation of the focal

190 catalysis in protein tyrosine phosphatases (PTPases) is accomplished by a conserved Asp residue, whi

191 onstrate that protein tyrosine phosphatases (PTPases) negatively regulate yeast MAP kinases.

192 Protein-tyrosine phosphatases (PTPases) play a key role in maintaining the steady-state

193 Protein-tyrosine phosphatases (PTPases) play an integral role in the regulation of cell

194 Protein-tyrosine phosphatases (PTPases) play key roles in regulating tyrosine phosphory

195 Protein tyrosine phosphatases (PTPases) PTP1B and PTPalpha are known to dephosphorylate

196 Protein tyrosine phosphatases (PTPases) share a number of conserved amino acid residues

197 a new clas of protein-tyrosine phosphatases (PTPases) that exhibit dual catalytic activity toward bot

198 rothioates by protein-tyrosine phosphatases (PTPases) was studied with the aim of providing a mechani

199 n of cellular protein-tyrosine phosphatases (PTPases), including PTP1B, a PTPase that has been previo

200 Since protein-tyrosine phosphatases (PTPases), which have pivotal roles in many cellular func

201 pecificity of protein-tyrosine phosphatases (PTPases).

202 ty to inhibit protein-tyrosine phosphatases (PTPases).

203 y mediated by protein tyrosine phosphatases (PTPases).

204 n of specific protein-tyrosine phosphatases (PTPases).

205 ing various combinations of phosphotyrosine, PTPase 1B, and insulin receptor (IR) antibodies.

206 se interest in obtaining specific and potent PTPase inhibitors for biological studies and pharmacolog

207 d that SHP-1 and PTPH1 are the two principal PTPases capable of regulating the phosphorylation state

208 teine in their active site, we have proposed PTPases as likely targets for Cpd 5.

209 tail and none were in the membrane-proximal PTPase domain (D1).

210 i-IR antibodies coprecipitated the 50-kDa PY-PTPase 1B protein from insulin-treated cells.

211 rugs that alter ROS metabolism or reactivate PTPases may antagonize BCR/ABL transformation.

212 located within this 15-bp sequence, reduced PTPase, neuregulin, and Ras-dependent regulation.

213 s of 10 and 35 nM, but do not bind a related PTPase.

214 ucleophile (via Cys to Ser mutation) renders PTPases catalytically inactive.

215 that PTP-alpha and PTP-1B are the respective PTPases in these fractions, we conclude that these PTPas

216 -Tyr and Glu-1779-to-Asp) conferred a robust PTPase activity to the D2 domain.

217 egulated by an enzymatically inactive second PTPase domain (D2).

218 yet been achieved, and potent and selective PTPase inhibitors are essential in the quest to determin

219 Several PTPases were expressed abundantly in the 5-FU-treated bo

220 ar distribution in rat adipocytes of several PTPases thought to be involved in the counterregulation

221 active mutant suggested that Gab1 was a SHP2 PTPase substrate in the cells.

222 When assayed with peptide substrates, SHP2 PTPase was activated by a bisphosphopeptide containing b

223 The SHP2 PTPase activity is required for activation of the extrac

224 ive regulation of insulin action by specific PTPases in the pathogenesis of insulin resistance in hum

225 ssion and regulation of the dual-specificity PTPases CL100, B23, and PAC1.

226 cascade's induction of the dual-specificity PTPases CL100, PAC1, and B23.

227 an expression of all three dual-specificity PTPases in human mesangial cells (HMC), thereby allowing

228 153 significantly reduced insulin-stimulated PTPase 1B phosphotyrosine content, as well as its associ

229 Furthermore, the well studied PTPase inhibitor orthovanadate also induced protein tyro

230 adily modifiable pharmacophore for synthetic PTPase and DSPase inhibitors and illustrate the signific

231 n and the mTORC1 pathway, mediated by C1-Ten PTPase activity.

232 Herein we report that PTPase, neuregulin, and Ras-dependent regulation of the

233 These results suggest that PTPase 1B complexes with the autophosphorylated insulin

234 Kinetic analyses suggest that PTPases utilize the same active site and similar kinetic

235 vanadate moiety is not invariant across the PTPase variants studied, and the average bond order of t

236 th Asp181 and Gln262 are invariant among the PTPase family, it is predicted that this improved substr

237 e in both cases of full length SHP-1 and the PTPase domain; however, glycerol is not acting as a cosu

238 itors of DSPases: Cdc25A, -B, and -C and the PTPase PTP1B.

239 D was identified in exon 5 that contains the PTPase core motif, with 13 of 30 (43%) CD mutations iden

240 not a true transition state analogue for the PTPase reactions.

241 ansfer reaction the transition state for the PTPase-catalyzed thiophosphoryl transfer is highly disso

242 the DSPase catalytic site distinct from the PTPase catalytic site.

243 However, the PTPase(s) that inactivate IR and IRS-1 under physiologic

244 none of these mutations was observed in the PTPase core motif.

245 t that the large thio effect observed in the PTPase reaction is the result of inability to achieve pr

246 Bronsted analyses suggest that like the PTPase-catalyzed phosphoryl transfer reaction the transi

247 We also found proteolytic cleavage of the PTPase 1B (PTP1B) in Jurkat cells after contact with ame

248 , Trp354 serves as an intrinsic probe of the PTPase active site conformation.

249 er, given the highly conserved nature of the PTPase active site, it is unclear whether selectivity in

250 the full length enzyme by 47-fold and of the PTPase domain by 8-fold.

251 is associated with a rapid activation of the PTPase SHP-1 (the cytoplasmic tyrosine phosphatase that

252 Modification of the PTPase's active site cysteine with the alkylating agent

253 H2 domain to relieve basal inhibition of the PTPase, whereas a phosphonate at Tyr-580 stimulates the

254 reas a phosphonate at Tyr-580 stimulates the PTPase activity by interaction with the C-terminal SH2 d

255 Unique to the PTPase family are two invariant Gln residues which are l

256 % stoichiometric burst was observed with the PTPase domain.

257 With the PTPase from Yersinia, we have examined the effect on gen

258 sphorylate Pyk2 in cells pretreated with the PTPase inhibitor orthovanadate.

259 Moreover, it forms a stable complex with the PTPase: in vitro inhibition of SHP-1 by the drug was not

260 on between mutations upstream and within the PTPase core motif, the core motif containing the majorit

261 the affinity of substrate or product for the PTPases.

262 icate that PTPRQ represents a subtype of the PTPases whose biological activities result from its PIPa

263 t hydrolytic activity and for preventing the PTPases from acting as kinases to phosphorylate undesira

264 To characterize these PTPases, we purified enzyme activities directed against

265 osited crystallographic coordinates of these PTPases reveals three atomic positions within the active

266 s in these fractions, we conclude that these PTPases are responsible for the counterregulation of ins

267 ure representing the other isoenzyme in this PTPase class, in each case with a sulfonate inhibitor bo

268 Since the activity of this PTPase is reportedly regulated by phosphorylation at Tyr

269 e inhibitors have been assayed against three PTPases: the Yersinia PTPase, PTP1B, and LAR.

270 and recombinant PTP-1B showed that all three PTPases dephosphorylate IR.

271 drolyzable phosphotyrosine analogues bind to PTPases with high affinity and act as competitive inhibi

272 LAR, a transmembrane PTPase expressed in insulin-sensitive tissues, acts as a

273 s and a cytoplasmic domain consisting of two PTPase domains, membrane-proximal PTP-D1 and C-terminal

274 significantly less stable than the wild-type PTPase and displays a different sensitivity to urea and

275 R spectra of the arsenate-ligated, wild-type PTPase and of ligand-free and arsenate-ligated C403S PTP

276 that in solution the ligand-free, wild-type PTPase exists as an equilibrium mixture of two tryptopha

277 he protein, while the ligand-free, wild-type PTPase is found to have two correlation times of 31 and

278 S mutant is similar to that of the wild-type PTPase, and the C403S mutant and the wild-type enzyme di

279 The structure of human low molecular weight PTPase is compared with a structure representing the oth

280 ic structure of a human low molecular weight PTPase solved by molecular replacement to 2.2 A.

281 two isoenzymes of these low molecular weight PTPases are commonly expressed.

282 ation mechanism for the low-molecular weight PTPases.

283 Moreover, the manner by which PTPase activity and substrate recruitment are regulated,

284 Cdc25 homology) domain conserved among yeast PTPases and mammalian MAP kinase phosphatases and is res

285 t a panel of phosphatases including Yersinia PTPase, SHP1, SHP2, LAR, HePTP, PTPalpha, CD45, VHR, MKP

286 itors has IC(50) values against the Yersinia PTPase and PTP1B of 0.7 and 2.7 microM, respectively.

287 d analyzed for activity against the Yersinia PTPase and PTP1B.

288 good selectivity for PTP1B and the Yersinia PTPase as compared to LAR.

289 nt of the active-site Arg409 in the Yersinia PTPase by a Lys reduces the thio effect by 54-fold, cons

290 e high affinity RNA aptamers to the Yersinia PTPase from two random pools varying in length.

291 assayed against three PTPases: the Yersinia PTPase, PTP1B, and LAR.

292 phosphotransferase activity to the Yersinia PTPase.

293 l and functional alterations in the Yersinia PTPase.

294 nditions, the nonligated, wild-type Yersinia PTPase alternates between an open WpD loop and a closed

295 The wild-type Yersinia PTPase and an active site mutant in which the esential C

296 ents of the ligand-bound, wild-type Yersinia PTPase and of both ligation states of the C403S PTPase r

297 from various segments of wild-type Yersinia PTPase in the presence or absence of 220 microM vanadate

298 f WpD loop closure of the wild-type Yersinia PTPase is thus independent of the presence of ligand, wh

299 s the fluorescence of the wild-type Yersinia PTPase with a Kd of 55 microM, whereas binding of tungst

300 irst time, the crystal structure of the YopH PTPase domain in complex with a nonhydrolyzable substrat