ライフサイエンスコーパス: protein tyrosine phosphatase

1 HP2 is an ubiquitously expressed cytoplasmic protein tyrosine phosphatase.

2 es a strong T-cell regulator called lymphoid protein tyrosine phosphatase.

3 /mammalian target of rapamycine pathway, and protein tyrosine phosphatase.

4 ype for a novel class of eukaryotic aspartyl protein tyrosine phosphatases.

5 oxidation that underlies redox inhibition of protein tyrosine phosphatases.

6 phosphatase Src homology 2 domain-containing protein tyrosine phosphatase 1 (Shp1) show increased leu

7 bitory signaling at the step of Src homology protein tyrosine phosphatase 1 recruitment and do not go

8 Sorafenib and SC-1 activated Src-homology protein tyrosine phosphatase-1 (SHP-1) and STAT3 inhibit

9 ion between Src homology 2 domain-containing protein tyrosine phosphatase-1 (SHP-1) and VEGF-R2, whic

10 y, we demonstrate that the non-receptor type protein tyrosine phosphatase 14 (PTPN14) functions as a

11 late radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and alpha- and b

12 aling and reduced levels of the phosphatases protein tyrosine phosphatase 1B (PTP1B) and phosphatase

13 We identified protein tyrosine phosphatase 1B (PTP1B) as a major targe

14 Protein tyrosine phosphatase 1B (PTP1B) counteracts lept

15 Protein tyrosine phosphatase 1B (PTP1B) is a ubiquitousl

16 Protein tyrosine phosphatase 1B (PTP1B) is a validated t

17 at increased NO production via inhibition of protein tyrosine phosphatase 1B (PTP1B) is associated wi

18 Protein tyrosine phosphatase 1B (PTP1B) is implicated in

19 e we show how these pillars are connected in Protein Tyrosine Phosphatase 1B (PTP1B), a drug target f

20 tion machinery modulates an interaction with protein tyrosine phosphatase 1B (PTP1B), an ER-associate

21 imarily to transcriptional downregulation of protein tyrosine phosphatase 1B (PTP1B), an inhibitory p

22 of Ca2+/calpain and resulting activation of protein tyrosine phosphatase 1B (PTP1B).

23 Application of this strategy to protein tyrosine phosphatase 1B and a peptidyl-prolyl ci

24 equired functionally active A1AT protein and protein tyrosine phosphatase 1B expression.

25 translocation, which is reversed by reducing protein tyrosine phosphatase 1B expression.

26 we experimentally validate a cryptic site in protein tyrosine phosphatase 1B using a covalent ligand

27 o enzyme inhibition (glycogen phosphorylase, protein tyrosine phosphatase 1B) or by inhibiting renal

28 T receptor activation through recruitment of protein tyrosine phosphatase 1B.

29 cting ligands of an allosteric pocket of the protein tyrosine phosphatase 1B.

30 Here, we report that protein tyrosine phosphatases 1B (PTP1B) directly dephos

31 s zinc transport into hepatocytes to inhibit protein-tyrosine phosphatase 1B (PTP1B) activity, which

32 epatocytes with or without expression of the protein-tyrosine phosphatase 1B (PTP1B) and in wild-type

33 Neuronal protein-tyrosine phosphatase 1B (PTP1B) deficiency in mi

34 h as silencer of cell signaling 1 (SOCS1) or protein-tyrosine phosphatase 1B (PTP1B) in this process.

35 Protein-tyrosine phosphatase 1B (PTP1B) is a physiologic

36 Protein-tyrosine phosphatase 1B (PTP1B) regulates food i

37 We have demonstrated that protein-tyrosine phosphatase 1B (PTP1B) was underexpress

38 colocalization of S-nitrosothiol (S-NO) and protein-tyrosine phosphatase 1B (PTP1B), and Akt phospho

39 tor-kappaB (NF-kappaB)-mediated induction of protein-tyrosine phosphatase 1B (PTP1B).

40 osphotyrosine (pY) under the assistance of a protein tyrosine phosphatase-1B (PTP-1B).

41 Protein tyrosine phosphatase-1B (PTP1B) negatively regul

42 o studies have indicated that SH2-containing protein tyrosine phosphatase 2 (SHP-2) is a signaling fa

43 progenitor cells deficient in SH2-containing protein tyrosine phosphatase 2 (Shp2) further enhanced m

44 ng receptor kinase and SH2 domain-containing protein tyrosine phosphatase 2 (Shp2) phosphatase activi

45 Shp2 (the Src homology-2 domain containing protein tyrosine phosphatase 2), a ubiquitously expresse

46 ze oxidized Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2).

47 eduction of Src homology 2 domain-containing protein-tyrosine phosphatase 2, known to maintain vascul

48 phosphatase Src homology region 2-containing protein tyrosine phosphatase-2 (SHP-2) and its downstrea

49 The Src homology 2 domain containing protein tyrosine phosphatase-2 (SHP2) is an oncogenic ph

50 ors trigger Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2) translocation to t

51 two of them, thyrotroph embryonic factor and protein tyrosine phosphatase 4a1, resulted in altered GL

52 Protein-tyrosine phosphatase 4A3 (PTP4A3) is highly expr

53 s an E3 ligase for STEP61 (striatal-enriched protein tyrosine phosphatase), a protein tyrosine phosph

54 sine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity.

55 mains incompletely understood, receptor type protein tyrosine phosphatase alpha (PTP-alpha encoded by

56 Protein tyrosine phosphatase alpha (PTPalpha) is essenti

57 Protein tyrosine phosphatase alpha (PTPalpha) promotes i

58 Further, we identify a receptor type-protein tyrosine phosphatase alpha-Src family kinase-Rap

59 We investigated the role of protein-tyrosine phosphatase alpha (PTPalpha) in regulat

60 ions of the focal adhesion kinase (FAK) with protein-tyrosine phosphatase-alpha (PTP-alpha) in IL-1 s

61 in its activation through the stimulation of protein tyrosine phosphatases, an effect shared by other

62 ringent substrate specificity than classical protein-tyrosine phosphatases and recognizes two distinc

63 decreased oxidative stress and oxidation of protein tyrosine phosphatases, and ameliorated activatio

64 Protein-tyrosine phosphatases are important reactive oxy

65 e TCR expression and increased expression of protein tyrosine phosphatases as compared with naive T c

66 Mycobacterium tuberculosis (Mtb) protein tyrosine phosphatase B (mPTPB) is a virulence fa

67 Protein-tyrosine phosphatase B (PtpB), a secretory phosp

68 tion of beta(3) at Tyr(773) through receptor protein-tyrosine phosphatase beta/zeta (RPTPbeta/zeta) a

69 The second PDZ domain of the protein tyrosine phosphatase BL (PDZ2) interacts and bin

70 We investigated whether inhibition of protein tyrosine phosphatases by ROS contributed to H-RA

71 Classical protein-tyrosine phosphatases can exhibit substrate spec

72 The receptor-like protein tyrosine phosphatase CD45 positively regulates c

73 receptor was identified as the cell surface protein tyrosine phosphatase CD45.

74 to a group of redox-sensitive phosphatases (protein tyrosine phosphatases) characterized by a low pK

75 The non-receptor isoform of protein-tyrosine phosphatase (cyt-PTPe) supports adhesio

76 marily with a transsynaptic binding partner, protein tyrosine phosphatase delta (PTPdelta); however,

77 n between the N-SH2 domain and the catalytic protein tyrosine phosphatase domain of SHP-1.

78 Antibodies targeting the protein tyrosine phosphatase domains of IA-2 and IA-2bet

79 SHP2 protein-tyrosine phosphatase (encoded by Ptpn11) positiv

80 Female mice lacking protein tyrosine phosphatase epsilon (PTP epsilon) are m

81 PTPN22, a protein tyrosine phosphatase expressed mainly in hematop

82 st that novel biological pathway such as the protein tyrosine phosphatase family is involved in regul

83 ro substrate preference of 16 members of the protein-tyrosine phosphatase family.

84 rast, elevated expression of Lar, a receptor protein tyrosine phosphatase found to be necessary for a

85 e PSTPIP2 inhibitory function is mediated by protein tyrosine phosphatases from the proline-, glutami

86 zed that the structural features of receptor protein tyrosine phosphatase-gamma (RPTPgamma) that are

87 everal tumor suppressor genes, including the protein tyrosine phosphatase gene PTPROt, which became s

88 genome expression array analyses identified protein tyrosine phosphatase genes PTPRR and PPFIA2, whi

89 ors of Rac and Rho proteins and the receptor protein-tyrosine phosphatase genes PTPRM and PTPRE.

90 tes EGFR dephosphorylation via activation of protein-tyrosine phosphatase H1 (PTPH1).

91 receptor-mediated developmental processes by protein tyrosine phosphatases has diverged between chick

92 Recently, protein tyrosine phosphatases have emerged as critical r

93 Protein tyrosine phosphatases have received little atten

94 e phosphatases (PTPs) includes hematopoietic protein-tyrosine phosphatase (HePTP), striatal-enriched

95 phatase nonreceptor type 11 Ptpn11 (Shp2), a protein tyrosine phosphatase implicated in multiple cell

96 al-enriched protein tyrosine phosphatase), a protein tyrosine phosphatase implicated in several neuro

97 This is the first time a protein tyrosine phosphatase, implicated in platelet sig

98 e temporal regulation of a specific class of protein tyrosine phosphatases in controlling the rate, a

99 However, the role of protein tyrosine phosphatases in leukocyte recruitment i

100 nce of the ERK phosphatase striatum-enriched protein-tyrosine phosphatase in hemideletion males.

101 details of reactive oxygen species-catalyzed protein-tyrosine phosphatase inactivation have remained

102 scular permeability via vascular endothelial-protein tyrosine phosphatase inhibition limits mycobacte

103 rotein VAPB interacts with the mitochondrial protein tyrosine phosphatase-interacting protein-51 (PTP

104 Activating mutations in Ptpn11 (Shp2), a protein tyrosine phosphatase involved in diverse cell si

105 ine phosphatase 1B (PTP1B), an ER-associated protein tyrosine phosphatase involved in the negative re

106 STEP (STriatal-Enriched protein tyrosine Phosphatase) is a neuron-specific phosp

107 yrosine phosphatase, STEP (STriatal-Enriched protein tyrosine Phosphatase) is an important regulator

108 ase 2), a ubiquitously expressed cytoplasmic protein tyrosine phosphatase, is implicated in regulatin

109 ted and SH3 domain-containing B (UBASH3B), a protein tyrosine phosphatase, is overexpressed in TNBC,

110 e that genetic inactivation of receptor-like protein tyrosine phosphatase J (Ptprj), which encodes CD

111 Receptor protein tyrosine phosphatase-kappa (PTPRK) specifically

112 PTPRB is a transmembrane protein tyrosine phosphatase known to regulate blood ves

113 ular endothelial cadherin, the transmembrane protein tyrosine phosphatase LAR, and the RAC1 guanidine

114 s with the Ig domains of LAR family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta,

115 hosphatase that was identified, the receptor protein tyrosine phosphatase leukocyte-antigen-related (

116 res of two catalytically inactive mutants of protein-tyrosine phosphatase-like myo-inositol phosphata

117 The low molecular weight protein tyrosine phosphatase (LMW-PTP) is a regulator of

118 In the absence of ligand, the protein tyrosine phosphatase loop is disordered and the

119 sustained in vivo binding and retention of a protein tyrosine phosphatase mu (PTPmu)-targeted, molecu

120 Switching of the substrate specificity of protein tyrosine phosphatase N12 by cyclin-dependent kin

121 tors of Lck, C-terminal Src kinase (Csk) and protein tyrosine phosphatase N22 (PTPN22).

122 Protein Tyrosine Phosphatase N23 (PTPN23) resides in chr

123 We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), v

124 x (MHC), interleukin 23 receptor (IL23R) and protein tyrosine phosphatase non-receptor type 22 (PTPN2

125 The human protein tyrosine phosphatase non-receptor type 4 (PTPN4)

126 The gene locus encoding protein-tyrosine phosphatase non-receptor type 2 (PTPN2)

127 ncluded in prior panel testing: a pathogenic protein tyrosine phosphatase, non-receptor type 11 (PTPN

128 mechanism of action of a polymorphism in the protein tyrosine phosphatase nonreceptor 22 (PTPN22) (LY

129 have established that the gene encoding the protein tyrosine phosphatase nonreceptor 22 (PTPN22) mak

130 s, are associated with an allelic variant of protein tyrosine phosphatase nonreceptor 22 (PTPN22), wh

131 The protein tyrosine phosphatase nonreceptor 22 gene (PTPN22

132 tion variation within the locus that encodes protein tyrosine phosphatase nonreceptor type (PTPN)22 i

133 ephosphorylated, which could be prevented by protein tyrosine phosphatase nonreceptor type 1 inhibiti

134 ogy region 2 domain-containing phosphatase-2/protein tyrosine phosphatase nonreceptor type 11 and its

135 Gain-of-function (GOF) mutations of protein tyrosine phosphatase nonreceptor type 11 Ptpn11

136 The protein tyrosine phosphatase nonreceptor type 12 (PTPN12

137 Protein tyrosine phosphatase nonreceptor type 14 (PTPN14

138 Inheritance of a coding variant of the protein tyrosine phosphatase nonreceptor type 22 (PTPN22

139 A coding polymorphism in the protein tyrosine phosphatase nonreceptor type 22 (PTPN22

140 The 1858T allele of protein tyrosine phosphatase nonreceptor type 22 (PTPN22

141 mon genetic variant in the gene encoding the protein tyrosine phosphatase nonreceptor type 22 (PTPN22

142 An allelic variant of protein tyrosine phosphatase nonreceptor type 22 (PTPN22

143 protein encoded by the autoimmune-associated protein tyrosine phosphatase nonreceptor type 22 gene, P

144 ogy region 2 domain-containing phosphatase 1/protein tyrosine phosphatase nonreceptor type 6 (SHP1/PT

145 on the outside of the mitochondria released protein tyrosine phosphatase, nonreceptor type 6 (SHP1,

146 , resulting from increased expression of the protein tyrosine phosphatase, nonreceptor type, 22 (PTPN

147 y unclear, due to our inability to visualize protein-tyrosine phosphatase oxidation in cells.

148 te increasing evidence for the importance of protein-tyrosine phosphatase oxidation in signal transdu

149 en dephosphorylated by PTP1B, an ER-resident protein tyrosine phosphatase, prior to axonal transport.

150 ree PRL (phosphatases of regenerating liver) protein tyrosine phosphatases (PRL-1, -2 and -3) have be

151 Recently, the receptor-like protein tyrosine phosphatases, protein tyrosine phosphat

152 scribe a novel method for the measurement of protein tyrosine phosphatase (PTP) activity in single hu

153 Mutation of the protein tyrosine phosphatase (PTP) core cysteine (C909)

154 SHP2 is a nonreceptor protein tyrosine phosphatase (PTP) encoded by the PTPN11

155 tyrosine phosphatase (LYP), a member of the protein tyrosine phosphatase (PTP) family of signaling e

156 CD45 is a receptor-like member of the protein tyrosine phosphatase (PTP) family.

157 of IL-4 signaling, we identified reversible protein tyrosine phosphatase (PTP) oxidation as the prim

158 ction mutations in PTPN11, which encodes the protein tyrosine phosphatase (PTP) SHP2, are implicated

159 PTP-PEST is a cytosolic ubiquitous protein tyrosine phosphatase (PTP) that contains, in add

160 an adhesion and signaling unit comprised of protein tyrosine phosphatase (PTP)-PEST and the extracel

161 Protein tyrosine phosphatase (PTP)sigma (PTPRS) was show

162 Protein tyrosine phosphatases (PTP) are exciting and nov

163 y hidden allosteric sites is demonstrated in protein tyrosine phosphatases (PTP) by creation of singl

164 A versatile assay for protein tyrosine phosphatases (PTP) employing 3-nitropho

165 ate was used to measure dephosphorylation by protein tyrosine phosphatases (PTP) in cell lysates and

166 d-independent activation of PTKs and induces protein-tyrosine phosphatase (PTP) inactivation.

167 ing, but it does not affect interaction with protein-tyrosine phosphatase (PTP)-PEST.

168 We identified the protein tyrosine phosphatase PTP1B as a therapeutic cand

169 defines a tumor suppressor function for the protein tyrosine phosphatase PTP1B in myeloid lineage ce

170 Protein tyrosine phosphatase PTP1B is a critical regulat

171 sue, Krishnan and colleagues reveal that the protein tyrosine phosphatase PTP1B is upregulated in pat

172 Recently, the protein tyrosine phosphatase PTP1B was identified as a n

173 with negative regulators of VEGF signaling, protein tyrosine phosphatases PTP1B and TC-PTP, and VE-c

174 Pharmacological inhibition of the protein-tyrosine phosphatase PTP1B increased K8 Tyr-267

175 The protein-tyrosine phosphatase PTP1B is a negative regulat

176 C1-Ten acts as a protein tyrosine phosphatase (PTPase) at the nephrin-PI3

177 serine/threonine phosphatase, and an active protein tyrosine phosphatase, PTPMEG.

178 diet (HFD), but that coordinate loss of the protein tyrosine phosphatase Ptpn1 (encoding PTP1B) enab

179 In addition, deletion of the protein tyrosine phosphatase PTPN2 in tumour cells incre

180 alysis of the dynamics of association of the protein tyrosine phosphatase PTPN22 and lipid phosphatas

181 The protein tyrosine phosphatase PTPN22(C1858T) allelic poly

182 spho-STAT3 were through up-regulation of the protein-tyrosine phosphatase PTPN6.

183 orylated tyrosine 207 (pTyr207)-CrkL and the protein tyrosine phosphatase PTPRC/CD45; these assays we

184 The protein tyrosine phosphatase PTPRJ/DEP-1 has been implic

185 Protein tyrosine phosphatases (PTPs) are enzymes that re

186 Protein tyrosine phosphatases (PTPs) are key signal-tran

187 Receptor protein tyrosine phosphatases (PTPs) counterbalance RTK

188 FR) coupled to dephosphorylating activity of protein tyrosine phosphatases (PTPs) ensures robust yet

189 as long been recognized, the significance of protein tyrosine phosphatases (PTPs) in cellular signali

190 wever, little is known about the role of the protein tyrosine phosphatases (PTPs) in FLS function.

191 aptic transmission was also prevented by the protein tyrosine phosphatases (PTPs) inhibitor sodium or

192 The inhibitory reversible oxidation of protein tyrosine phosphatases (PTPs) is an important reg

193 inhibition by orthovanadate or depletion of protein tyrosine phosphatases (PTPs) resulted in the rec

194 It is well known that protein tyrosine phosphatases (PTPs) that become oxidize

195 ignaling involves reversible inactivation of protein tyrosine phosphatases (PTPs) through the oxidati

196 aling pathways are very tightly regulated by protein tyrosine phosphatases (PTPs) to prevent excessiv

197 by monitoring active-site loop motion in two protein tyrosine phosphatases (PTPs) using nuclear magne

198 Unlike previously characterized protein tyrosine phosphatases (PTPs), the activity and s

199 e to various stimuli is tightly regulated by protein tyrosine phosphatases (PTPs).

200 ities of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs).

201 s," contribute to proper signal transduction.Protein-tyrosine phosphatases (PTPs) are thought to be m

202 screen to investigate the role of classical protein-tyrosine phosphatases (PTPs) in three-dimensiona

203 The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes hematopoie

204 been expended to develop inhibitors against protein-tyrosine phosphatases (PTPs), nearly all of it u

205 ting liver (PRLs), the most oncogenic of all protein-tyrosine phosphatases (PTPs), play a critical ro

206 c terminals by signaling through presynaptic protein tyrosine phosphatase receptor delta.

207 Here, we show that hepatic expression of Protein Tyrosine Phosphatase Receptor Gamma (PTPR-gamma)

208 -/-) inner hair cells were fused by P17, and protein tyrosine phosphatase receptor Q, normally linked

209 thetic reinnervation by binding the neuronal protein tyrosine phosphatase receptor sigma (PTPsigma).

210 that attained chromosome-wise significance, protein tyrosine phosphatase receptor T (PTPRT; P=4.8 x

211 We found a CNV region in protein tyrosine phosphatase receptor type D (PTPRD) wit

212 the top-scoring tumor suppressor candidates, protein tyrosine phosphatase receptor type F (PTPRF).

213 study, we address this issue by focusing on protein tyrosine phosphatase receptor type gamma (PTPRG)

214 e the expression of the tyrosine phosphatase protein tyrosine phosphatase receptor type J (PTPRJ), a

215 Protein tyrosine phosphatase receptor type O (PTPRO), wh

216 PTPRD, which encodes the protein tyrosine phosphatase receptor-delta, is one of t

217 on of the RAS pathway in mice that expressed protein tyrosine phosphatase receptor-zeta (PTPRZ), wher

218 Protein-tyrosine phosphatase receptor type G (RPTPgamma/

219 hed protein-tyrosine phosphatase (STEP), and protein-tyrosine phosphatase receptor type R (PTPRR).

220 In particular, protein tyrosine phosphatase, receptor type, F (PTPRF) m

221 e kinase, WW and PDZ domain containing 2 and protein tyrosine phosphatase, receptor type, O cooperate

222 Mutations of PTPRD, a receptor-type protein tyrosine phosphatase regulating cell growth, wer

223 h reduced phosphorylation of ERK and SHP2, a protein tyrosine phosphatase required for complete ERK a

224 leukocyte antigen-related (Lar), a receptor protein tyrosine phosphatase (RPTP) and the only known D

225 rs in the brain is regulated by the Receptor Protein Tyrosine Phosphatase RPTP69d.

226 Receptor protein tyrosine phosphatases (RPTPs) can play essential

227 phogenetic apoptosis, requiring the receptor protein tyrosine phosphatases (RPTPs): LAR and RPTPsigma

228 caused by gain-of-function mutations in the protein tyrosine phosphatase SH2 domain-containing PTP (

229 Here, we identified a novel role of the protein tyrosine phosphatase SHP-1 in the regulation of

230 Here we show that the protein tyrosine phosphatase SHP-2 is required for leuci

231 known in the PTPN11 gene that codes for the protein tyrosine phosphatase SHP-2.

232 The protein-tyrosine phosphatase SHP-1 has critical roles in

233 y activates Src homology domain 2 containing protein tyrosine phosphatase (SHP) 1 and suppresses prod

234 rylation of Src homology domain 2-containing protein tyrosine phosphatase (SHP) 2 and Src homology do

235 on recruits Src homology 2 domain-containing protein tyrosine phosphatase (SHP)-1 to the vascular end

236 The protein-tyrosine phosphatase Shp1 is expressed ubiquitou

237 The SH2 domain-containing protein-tyrosine phosphatases Shp1 and Shp2 have been im

238 cluding the Src homology 2 domain-containing protein-tyrosine phosphatases Shp1 and Shp2, knockout an

239 Germline activating mutations of the protein tyrosine phosphatase SHP2 (encoded by PTPN11), a

240 The protein tyrosine phosphatase Shp2 (PTPN11) is crucial fo

241 l phosphotyrosines and SH2 domain within the protein tyrosine phosphatase Shp2 can be tuned by an ada

242 ARD syndrome (LS) patients, mutations in the protein tyrosine phosphatase Shp2 cause hypertrophic car

243 Here, we have analyzed the function of the protein tyrosine phosphatase Shp2 in mice by deleting it

244 We investigated the contribution of protein tyrosine phosphatase Shp2 to lipopolysaccharide

245 ons in Ptpn11, which encodes the nonreceptor protein tyrosine phosphatase Shp2, show hippocampal-depe

246 hat within the human immune system, receptor protein tyrosine phosphatase sigma (PTPRS) is expressed

247 Sympathetic ganglia lacking protein tyrosine phosphatase sigma (PTPRS) were not inhi

248 Receptor protein tyrosine phosphatase sigma (PTPsigma) and its su

249 receptor-like protein tyrosine phosphatases, protein tyrosine phosphatase sigma (PTPsigma) and leukoc

250 Protein tyrosine phosphatase sigma (PTPsigma), along wit

251 molecule trans-interacting with presynaptic protein tyrosine phosphatase sigma (PTPsigma).

252 Receptor protein tyrosine phosphatase sigma (RPTPsigma) regulates

253 vatives bound to the axon guidance proteins, protein tyrosine phosphatase sigma (RPTPsigma), and Nogo

254 antigen related (LAR) phosphatase subfamily, protein tyrosine phosphatase sigma and LAR, are function

255 function as a positive modulator of the TrkC-protein tyrosine phosphatase sigma complex.

256 with a role for iron-dependent inhibition of protein tyrosine phosphatases, SLC11A1(+) lymphocytes we

257 ate that the Salmonella Typhimurium-secreted protein tyrosine phosphatase, SptP, suppresses mast cell

258 High levels of striatal-enriched protein tyrosine phosphatase (STEP) activity are observe

259 in-mediated degradation of striatal-enriched protein tyrosine phosphatase (STEP) and neuronal death.

260 d the tyrosine phosphatase striatal-enriched protein tyrosine phosphatase (STEP) are known to target

261 Excessive activity of striatal-enriched protein tyrosine phosphatase (STEP) in the brain has bee

262 Striatal-enriched protein tyrosine phosphatase (STEP) is a brain-specific

263 Herein we show that the striatal-enriched protein tyrosine phosphatase (STEP) is recruited by Galp

264 found that the activity of striatal-enriched protein tyrosine phosphatase (STEP) was upregulated by c

265 osine phosphatase (HePTP), striatal-enriched protein-tyrosine phosphatase (STEP), and protein-tyrosin

266 Analogous Pi binding measurements with a protein tyrosine phosphatase suggest the generality of t

267 Expression of receptor-like protein tyrosine phosphatase T (PTPRT) mutant proteins i

268 Here, we have identified T cell protein tyrosine phosphatase (TC-PTP), also known as PTP

269 involved in growth factor signaling, T-cell protein tyrosine phosphatase (TC-PTP), and the E3 ubiqui

270 Here, we report the critical role of T-cell protein tyrosine phosphatase (TC-PTP), encoded by Ptpn2,

271 Conversely, the T cell protein tyrosine phosphatase (TCPTP) dephosphorylated Tb

272 The T-cell protein tyrosine phosphatase (TCPTP) pathway consists of

273 ntiviral signaling protein (MAVS) and T cell protein tyrosine phosphatase (TCPTP) suggests an avenue

274 Expression of the PTPN2 gene product, T cell protein-tyrosine phosphatase (TCPTP), in intestinal epit

275 ues within ITIMs results in recruitment of a protein tyrosine phosphatase that blocks activation sign

276 Shp2 is a nonreceptor protein tyrosine phosphatase that has been shown to infl

277 osine phosphatase (STEP) is a brain-specific protein tyrosine phosphatase that opposes the developmen

278 SHP-2 is a protein tyrosine phosphatase that positively regulates t

279 tic member of the Ptp4a family of prenylated protein tyrosine phosphatases that are highly expressed

280 selection is followed by the recruitment of protein tyrosine phosphatases that inactivate the RTKs a

281 P1B) is a ubiquitously expressed nonreceptor protein-tyrosine phosphatase that regulates various cell

282 he activity of the receptor and non-receptor protein-tyrosine phosphatases that down-regulate Met pho

283 The induction of protein-tyrosine phosphatases, thioredoxin, SOCS, and Eg

284 port the development of therapies inhibiting protein tyrosine phosphatases to enhance T cell-mediated

285 Protein-tyrosine phosphatase TULA-2 has been shown to re

286 and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunopr

287 the drosophila ortholog of the non-receptor protein tyrosine phosphatase type II (SHP2) to the Pi3k2

288 x with VEC and its phosphatases, EC-specific protein tyrosine phosphatase (VE-PTP) and Src homology p

289 The vascular endothelial (VE) receptor protein tyrosine phosphatase (VE-PTP) associates with VE

290 ity and determined that vascular endothelial protein tyrosine phosphatase (VE-PTP) is a HIF2alpha tar

291 ompetitive inhibitor of vascular endothelial-protein tyrosine phosphatase (VE-PTP) that promotes Tie2

292 on including claudin-5, vascular endothelial-protein tyrosine phosphatase (VE-PTP), and von Willebran

293 e, we demonstrated that vascular endothelial-protein tyrosine phosphatase (VE-PTP), which negatively

294 Striatal-enriched protein tyrosine phosphatase was selectively expressed i

295 in, known to be involved in stabilization of protein-tyrosine phosphatases, were found to be induced

296 s were shown to co-express striatal-enriched protein tyrosine phosphatase, which may have an importan

297 that dephosphorylate STAT3, such as receptor protein tyrosine phosphatases, which are encoded by the

298 ngaged receptor/ligand complex from receptor protein tyrosine phosphatases with large ectodomains, su

299 IL-34, c-FMS, and a second IL-34 receptor, protein-tyrosine phosphatase zeta (PTP-zeta) were upregu

300 Our previous work demonstrated that receptor protein-tyrosine phosphatase zeta (RPTPzeta)/phosphacan