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1 n ubiquitously expressed cytoplasmic protein tyrosine phosphatase.
2 n substrate, suggesting that in vivo it is a tyrosine phosphatase.
3 ong T-cell regulator called lymphoid protein tyrosine phosphatase.
4 n that underlies redox inhibition of protein tyrosine phosphatases.
5 a novel class of eukaryotic aspartyl protein tyrosine phosphatases.
6 onservation of the active site among protein tyrosine phosphatases.
7 m of Src homology region 2 domain-containing tyrosine phosphatase 1 (SHP-1) along with the T. cruzi T
8 ase Src homology 2 domain-containing protein tyrosine phosphatase 1 (Shp1) show increased leukocyte a
9 enib and SC-1 activated Src-homology protein tyrosine phosphatase-1 (SHP-1) and STAT3 inhibition foll
10 een Src homology 2 domain-containing protein tyrosine phosphatase-1 (SHP-1) and VEGF-R2, which leads
11 ransport into hepatocytes to inhibit protein-tyrosine phosphatase 1B (PTP1B) activity, which acts to
12 ial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and alpha- and beta-cate
13  led to abnormally increased hepatic protein-tyrosine phosphatase 1B (PTP1B) expression and enhanced
14 encer of cell signaling 1 (SOCS1) or protein-tyrosine phosphatase 1B (PTP1B) in this process.
15 ased NO production via inhibition of protein tyrosine phosphatase 1B (PTP1B) is associated with reduc
16                                      Protein tyrosine phosphatase 1B (PTP1B) is implicated in inflamm
17                                      Protein-tyrosine phosphatase 1B (PTP1B) is the canonical enzyme
18 w how these pillars are connected in Protein Tyrosine Phosphatase 1B (PTP1B), a drug target for diabe
19           Inflammation activates the protein-tyrosine phosphatase 1B (PTP1B), and this could suppress
20 sruptive optical approach to control protein tyrosine phosphatase 1B (PTP1B)-an important regulator o
21 ine the catalytic loop in the enzyme protein tyrosine phosphatase 1B (PTP1B).
22 r of these phenolic extracts against Protein Tyrosine Phosphatase 1B enzyme (PTP-1B), overexpressed i
23 imentally validate a cryptic site in protein tyrosine phosphatase 1B using a covalent ligand and NMR
24  inhibition (glycogen phosphorylase, protein tyrosine phosphatase 1B) or by inhibiting renal sodium-d
25                 Here, we report that protein tyrosine phosphatases 1B (PTP1B) directly dephosphorylat
26 osine (pY) under the assistance of a protein tyrosine phosphatase-1B (PTP-1B).
27 zed Src homology 2 domain-containing protein-tyrosine phosphatase 2 (SHP2).
28      Active Src homology 2 domain-containing tyrosine phosphatase 2 impairs the signaling function of
29  docking of Src homology 2 domain-containing tyrosine phosphatase 2 phosphatase to the cytoplasmic ta
30 the Src homology-2 domain containing protein tyrosine phosphatase 2), a ubiquitously expressed cytopl
31  of Src homology 2 domain-containing protein-tyrosine phosphatase 2, known to maintain vascular barri
32 ubiquitously expressed SH2 domain-containing tyrosine phosphatase-2 (SHP2) as a therapeutic target ha
33                       SH2 containing protein tyrosine phosphatase-2 (SHP2) is an oncogenic phosphatas
34 ger Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2) translocation to the mitoc
35 hibitor of the oncogenic phosphatase protein tyrosine phosphatase 4A3 binds to at least one site on h
36 rt that cell-autonomous loss of the receptor tyrosine phosphatase 69D (RPTP69D) and loss of midline-l
37                                   Lymphocyte tyrosine phosphatase, a coding variant within the tyrosi
38 ree genes encode a non-receptor type protein tyrosine phosphatase, a serine/threonine protein kinase,
39 cells, suggesting inhibition of SHP2 protein tyrosine phosphatase activity by this peptide.
40                         Upregulation of CD45 tyrosine phosphatase activity in MDSCs exposed to hypoxi
41       Both in vivo and in vitro, loss of EYA tyrosine phosphatase activity leads to defective assembl
42     Along with our previous results that the tyrosine phosphatase activity of Eya is dispensable for
43 ulmonary arterial hypertension and that EYA3 tyrosine phosphatase activity promotes the survival of t
44       Pharmacological inhibition of the EYA3 tyrosine phosphatase activity substantially reverses vas
45 f EYA1, which has been reported to have only tyrosine phosphatase activity, has dual phosphatase acti
46 alytic cysteine residue, which inhibited the tyrosine-phosphatase activity of SHP-1.
47                        Receptor-type protein tyrosine phosphatase alpha (RPTPalpha) is an important p
48 Further, we identify a receptor type-protein tyrosine phosphatase alpha-Src family kinase-Rap1 pathwa
49                            STEP is a protein tyrosine phosphatase (also known as PTPN5), with several
50 ctivation through the stimulation of protein tyrosine phosphatases, an effect shared by other short-c
51 ta validate a new approach to study receptor tyrosine phosphatases and show that, by targeting JAKs,
52 s controlled by the accessibility of ITIM to tyrosine phosphatases and that KIR binding to HLA-C must
53 oteins HD-PTP (His domain-containing protein tyrosine phosphatase) and BROX (Bro1 domain and CAAX mot
54 ed oxidative stress and oxidation of protein tyrosine phosphatases, and ameliorated activation of per
55                                      Protein-tyrosine phosphatases are important reactive oxygen spec
56                                  Mtb protein tyrosine phosphatase B (mPTPB) is a virulence factor req
57                                      Protein-tyrosine phosphatase B (PtpB), a secretory phosphatase t
58         The second PDZ domain of the protein tyrosine phosphatase BL (PDZ2) interacts and binds the C
59 KIR2DL1 and KIR2DL1-H36A after inhibition of tyrosine phosphatase by pervanadate suggested that KIR2D
60 the expression of 85 tyrosine kinases and 42 tyrosine phosphatases by in situ hybridization 48 human
61                            Classical protein-tyrosine phosphatases can exhibit substrate specificity
62 m was dependent on increased activity of the tyrosine phosphatase CD45 and CD45-dependent activation
63                            The receptor-like tyrosine phosphatase CD45 regulates antigen receptor sig
64                  T cells require the protein tyrosine phosphatase CD45 to detect and respond to antig
65 hat the local segregation of kinases and the tyrosine phosphatase CD45 underpins T cell antigen recep
66                   Because most receptor-type tyrosine phosphatases contain potential phosphorylation
67 7 (PTPN7), also called hematopoietic protein tyrosine phosphatase, controls extracellular signal-regu
68 ith a transsynaptic binding partner, protein tyrosine phosphatase delta (PTPdelta); however, upon BDN
69     We also demonstrated that T-cell protein-tyrosine phosphatase dephosphorylates pTyr(243) The data
70 or a molecular network in which the receptor tyrosine phosphatase Dlar interacts with the WRC to coup
71 rboring an inactivating mutation in the EYA3 tyrosine phosphatase domain are significantly protected
72 e interactions between its N-SH2 and protein-tyrosine phosphatase domains are weakened such that SHP2
73                SHP2 is a nonreceptor protein tyrosine phosphatase encoded by the PTPN11 gene and is i
74 novel biological pathway such as the protein tyrosine phosphatase family is involved in regulation of
75 rate preference of 16 members of the protein-tyrosine phosphatase family.
76 R1) is a member of the atypical DUSP protein tyrosine phosphatase family.
77                 Here we report a novel plant tyrosine phosphatase from Arabidopsis thaliana (AtRLPH2)
78     Activation of SFKs requires depletion of tyrosine phosphatases from the area of particle engageme
79 2 inhibitory function is mediated by protein tyrosine phosphatases from the proline-, glutamic acid-,
80 rates and cellular events regulated by Eya's tyrosine phosphatase function and highlights some of the
81  the structural features of receptor protein tyrosine phosphatase-gamma (RPTPgamma) that are consiste
82 umor suppressor genes, including the protein tyrosine phosphatase gene PTPROt, which became silenced
83 ac and Rho proteins and the receptor protein-tyrosine phosphatase genes PTPRM and PTPRE.
84  dephosphorylation via activation of protein-tyrosine phosphatase H1 (PTPH1).
85                                      Protein tyrosine phosphatases have received little attention in
86 atases (PTPs) includes hematopoietic protein-tyrosine phosphatase (HePTP), striatal-enriched protein-
87 phosphorylation of p38alpha by hematopoietic tyrosine phosphatase (HePTP).
88 , we show that deletion of Ptpn21, a protein tyrosine phosphatase highly expressed in HSCs, induces s
89 nonreceptor type 11 Ptpn11 (Shp2), a protein tyrosine phosphatase implicated in multiple cell signali
90 he ERK phosphatase striatum-enriched protein-tyrosine phosphatase in hemideletion males.
91 d neurotoxicity, a potential contribution of tyrosine phosphatases in this process has not been well
92 estigated the role of PTPRF, a receptor-type tyrosine phosphatase, in regulating Wnt signaling in CRC
93 of reactive oxygen species-catalyzed protein-tyrosine phosphatase inactivation have remained largely
94                                        Thus, tyrosine phosphatases induced by the activation of naive
95 ermeability via vascular endothelial-protein tyrosine phosphatase inhibition limits mycobacterial gro
96 with CFTR and were further stimulated by the tyrosine phosphatase inhibitor dephostatin.
97 cid and microcystin, but is inhibited by the tyrosine phosphatase inhibitor orthovanadate and is part
98 osphorylation, whereas administration of the tyrosine phosphatase inhibitor sodium orthovanadate prio
99 ese data reveal the potential utility of EYA tyrosine phosphatase inhibitors as therapeutic agents in
100                      To date, only one other tyrosine phosphatase is known in plants; thus AtRLPH2 re
101 phosphatase, STEP (STriatal-Enriched protein tyrosine Phosphatase) is an important regulator of synap
102 a ubiquitously expressed cytoplasmic protein tyrosine phosphatase, is implicated in regulating M-CSF
103 ine phosphatase, a coding variant within the tyrosine phosphatases, is known to participate in AgR si
104             PTPRB is a transmembrane protein tyrosine phosphatase known to regulate blood vessel remo
105 show that the cadherin Fat2 and the receptor tyrosine phosphatase Lar function in a planar signaling
106 othelial cadherin, the transmembrane protein tyrosine phosphatase LAR, and the RAC1 guanidine-exchang
107 he Ig domains of LAR family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta, and PTP
108 se that was identified, the receptor protein tyrosine phosphatase leukocyte-antigen-related (LAR), ab
109 slet cell autoantigen 512 (ICA512/IA-2) is a tyrosine phosphatase-like intrinsic membrane protein inv
110 wo catalytically inactive mutants of protein-tyrosine phosphatase-like myo-inositol phosphatases (PTP
111             The low molecular weight protein tyrosine phosphatase (LMW-PTP) is a regulator of a numbe
112 s demonstrated that the meprin A5 antigen-mu tyrosine phosphatase (MAM) domain and the O-glycan-conta
113 d in vivo binding and retention of a protein tyrosine phosphatase mu (PTPmu)-targeted, molecular magn
114 hing of the substrate specificity of protein tyrosine phosphatase N12 by cyclin-dependent kinase 2 ph
115 Lck, C-terminal Src kinase (Csk) and protein tyrosine phosphatase N22 (PTPN22).
116                                      Protein Tyrosine Phosphatase N23 (PTPN23) resides in chromosomal
117                 We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants
118                 Here, we report that protein tyrosine phosphatase non-receptor 3 (PTPN3) profoundly p
119                                      Protein tyrosine phosphatase non-receptor type 2 (PTPN2) protect
120                         A variant in protein tyrosine phosphatase non-receptor type 22 (PTPN22) is as
121  interleukin 23 receptor (IL23R) and protein tyrosine phosphatase non-receptor type 22 (PTPN22) pathw
122                            The human protein tyrosine phosphatase non-receptor type 4 (PTPN4) prevent
123                                      Protein tyrosine phosphatase non-receptor type 5 (PTPN5, STEP) i
124 nt (Ala455Thr) was identified in the protein tyrosine phosphatase non-receptor type 6 (PTPN6) gene, a
125 in prior panel testing: a pathogenic protein tyrosine phosphatase, non-receptor type 11 (PTPN11) vari
126 iated by direct targeting of PTPN14 (protein tyrosine phosphatase, non-receptor type 14) which, in tu
127 tablished that the gene encoding the protein tyrosine phosphatase nonreceptor 22 (PTPN22) makes an im
128                                  The protein tyrosine phosphatase nonreceptor 22 gene (PTPN22) encode
129                               PTP1B (protein-tyrosine phosphatase nonreceptor type 1, also called PTP
130  Gain-of-function (GOF) mutations of protein tyrosine phosphatase nonreceptor type 11 Ptpn11 (Shp2),
131                                  The protein tyrosine phosphatase nonreceptor type 12 (PTPN12) is a m
132 ely abolish FLNA's interactions with protein tyrosine phosphatase nonreceptor type 12, which has been
133 tic variant in the gene encoding the protein tyrosine phosphatase nonreceptor type 22 (PTPN22 C1858T)
134           The hematopoietic-specific protein tyrosine phosphatase nonreceptor type 22 (PTPN22) is enc
135                An allelic variant of protein tyrosine phosphatase nonreceptor type 22 (PTPN22), PTPN2
136 encoded by the autoimmune-associated protein tyrosine phosphatase nonreceptor type 22 gene, PTPN22, h
137                                      Protein tyrosine phosphatase nonreceptor type 7 (PTPN7), also ca
138 n of tryptophan with arginine in the protein tyrosine phosphatase, nonreceptor type 22 gene (PTPN22)
139 outside of the mitochondria released protein tyrosine phosphatase, nonreceptor type 6 (SHP1, or PTPN6
140 ing from increased expression of the protein tyrosine phosphatase, nonreceptor type, 22 (PTPN22) (p <
141 glomerular nephrin (NPHS1) and receptor-type tyrosine-phosphatase O (PTPRO).
142  activation threshold via the recruitment of tyrosine phosphatases, our results suggest a significant
143 r, due to our inability to visualize protein-tyrosine phosphatase oxidation in cells.
144 asing evidence for the importance of protein-tyrosine phosphatase oxidation in signal transduction, t
145 sphorylated by PTP1B, an ER-resident protein tyrosine phosphatase, prior to axonal transport.
146 tides and readily dephosphorylates a classic tyrosine phosphatase protein substrate, suggesting that
147  found to downregulate the expression of the tyrosine phosphatase protein tyrosine phosphatase recept
148 demonstrate that the activity of the protein tyrosine phosphatase PTP-PEST, which controls paxillin p
149                                      Protein tyrosine phosphatase (PTP) 4A3 is frequently overexpress
150 aper presents an approach to measure protein tyrosine phosphatase (PTP) activity in individual cells
151        Here we report that classical protein tyrosine phosphatase (PTP) domains from multiple subfami
152                SHP2 is a nonreceptor protein tyrosine phosphatase (PTP) encoded by the PTPN11 gene in
153 ndent activation of PTKs and induces protein-tyrosine phosphatase (PTP) inactivation.
154            Vascular endothelial (VE) protein tyrosine phosphatase (PTP) is an endothelial-specific ph
155                      The nonreceptor protein-tyrosine phosphatase (PTP) SHP2 is encoded by the proto-
156 tations in PTPN11, which encodes the protein tyrosine phosphatase (PTP) SHP2, are implicated in CHD a
157                     The non-receptor protein tyrosine phosphatase (PTP) SHP2, encoded by PTPN11, play
158 sion and signaling unit comprised of protein tyrosine phosphatase (PTP)-PEST and the extracellular ma
159                                      Protein tyrosine phosphatases (PTP) are exciting and novel targe
160  allosteric sites is demonstrated in protein tyrosine phosphatases (PTP) by creation of single alanin
161              Double mutants lacking receptor tyrosine phosphatases (PTP) Ptp10D and Ptp4E, clear lumi
162  a tumor suppressor function for the protein tyrosine phosphatase PTP1B in myeloid lineage cells, wit
163                                      Protein tyrosine phosphatase PTP1B is a critical regulator of si
164                                  The protein-tyrosine phosphatase PTP1B is a negative regulator of in
165 shnan and colleagues reveal that the protein tyrosine phosphatase PTP1B is upregulated in patients wi
166                        Recently, the protein tyrosine phosphatase PTP1B was identified as a novel reg
167                       Here, we show that the tyrosine phosphatase PTP4A1 is highly expressed in fibro
168                     C1-Ten acts as a protein tyrosine phosphatase (PTPase) at the nephrin-PI3K bindin
169 threonine phosphatase, and an active protein tyrosine phosphatase, PTPMEG.
170 FD), but that coordinate loss of the protein tyrosine phosphatase Ptpn1 (encoding PTP1B) enables a hi
171                             The non-receptor tyrosine phosphatase Ptpn11 (Shp2) is an important trans
172 ast growth factor receptors FGFR2 and FGFR3, tyrosine phosphatase PTPN11, and RAS oncogene homologs H
173                        Here, we identify the tyrosine phosphatase PTPN13 as a key PDZ binding partner
174                            The novel protein tyrosine phosphatase PTPN14 was identified by mass spect
175                       Here, we show that the tyrosine phosphatase PTPN2 attenuates STAT5 (signal tran
176                                          The tyrosine phosphatase PTPN2 attenuates T-cell receptor an
177         In addition, deletion of the protein tyrosine phosphatase PTPN2 in tumour cells increased the
178 AT1 in response to IL-6 was regulated by the tyrosine phosphatases PTPN2 and PTPN22 expressed in resp
179 actions are released upon binding of protein tyrosine phosphatase PTPN21.
180 f the dynamics of association of the protein tyrosine phosphatase PTPN22 and lipid phosphatase SHIP-1
181    We show that CD8(+) T cells that lack the tyrosine phosphatase Ptpn22, a major predisposing gene f
182 he catalytically inactive, non-receptor-type tyrosine phosphatase PTPN23/HD-PTP.
183  tyrosine 207 (pTyr207)-CrkL and the protein tyrosine phosphatase PTPRC/CD45; these assays were devel
184 tail, and are activated by the receptor-type tyrosine phosphatase PTPRJ (CD148, DEP-1), which dephosp
185                                  The protein tyrosine phosphatase PTPRJ/DEP-1 has been implicated in
186               The plasma membrane-associated tyrosine phosphatase PTPRO is frequently transcriptional
187 ctivated in osteoclasts by the receptor-type tyrosine phosphatase PTPROt.
188                                      Protein tyrosine phosphatases (PTPs) are enzymes that remove pho
189 ribute to proper signal transduction.Protein-tyrosine phosphatases (PTPs) are thought to be major tar
190                                      Protein-tyrosine phosphatases (PTPs) counteract protein tyrosine
191                             Receptor protein tyrosine phosphatases (PTPs) counterbalance RTK signalin
192 led to dephosphorylating activity of protein tyrosine phosphatases (PTPs) ensures robust yet diverse
193 been recognized, the significance of protein tyrosine phosphatases (PTPs) in cellular signaling and d
194 to investigate the role of classical protein-tyrosine phosphatases (PTPs) in three-dimensional mammar
195 se interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes hematopoietic prot
196  involves reversible inactivation of protein tyrosine phosphatases (PTPs) through the oxidation and r
197 thways are very tightly regulated by protein tyrosine phosphatases (PTPs) to prevent excessive activa
198 pended to develop inhibitors against protein-tyrosine phosphatases (PTPs), nearly all of it unsuccess
199 er (PRLs), the most oncogenic of all protein-tyrosine phosphatases (PTPs), play a critical role in me
200  protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs).
201 als by signaling through presynaptic protein tyrosine phosphatase receptor delta.
202 , we show that hepatic expression of Protein Tyrosine Phosphatase Receptor Gamma (PTPR-gamma) is stim
203 report here that homodimerization of protein tyrosine phosphatase receptor J (PTPRJ, also known as DE
204  AP-1A, the small GTPase Rab11B, the surface tyrosine phosphatase receptor PTPRF and its adaptor PPFI
205 er hair cells were fused by P17, and protein tyrosine phosphatase receptor Q, normally linked to myos
206                                      Protein-tyrosine phosphatase receptor type G (RPTPgamma/PTPRG) i
207 pression of the tyrosine phosphatase protein tyrosine phosphatase receptor type J (PTPRJ), a known ex
208 ein-tyrosine phosphatase (STEP), and protein-tyrosine phosphatase receptor type R (PTPRR).
209 ion in muscle, such as myostatin and protein tyrosine phosphatase receptor-gamma.
210 ere we identify the tumor suppressor Protein tyrosine phosphatase receptor-type kappa (PTPRK), as a W
211 ls are transduced through the CLR-1 Lar-like tyrosine phosphatase receptor.
212                                      Protein tyrosine phosphatases regulate a myriad of essential sub
213  Mutations of PTPRD, a receptor-type protein tyrosine phosphatase regulating cell growth, were enrich
214 sents one of the missing pieces in the plant tyrosine phosphatase repertoire and supports the concept
215 te antigen-related (Lar), a receptor protein tyrosine phosphatase (RPTP) and the only known Drosophil
216 e brain is regulated by the Receptor Protein Tyrosine Phosphatase RPTP69d.
217                  The receptor-linked protein tyrosine phosphatases (RPTPs) are key regulators of cell
218                             Receptor protein tyrosine phosphatases (RPTPs) play critical regulatory r
219                  The receptor-linked protein tyrosine phosphatases (RPTPs) receive cues from the extr
220 ic apoptosis, requiring the receptor protein tyrosine phosphatases (RPTPs): LAR and RPTPsigma.
221 by gain-of-function mutations in the protein tyrosine phosphatase SH2 domain-containing PTP (SHP2), h
222  inhibitory signaling pathways involving the tyrosine phosphatase SHP-1 and the inositol phosphatase
223 e, we identified a novel role of the protein tyrosine phosphatase SHP-1 in the regulation of murine L
224 ociated with long-lasting recruitment of the tyrosine phosphatase SHP-1 to the CD16 receptor complex.
225  In this study, we observed that loss of the tyrosine phosphatase SHP-1, a negative regulator of TCR
226 rons by PD-L1 induced phosphorylation of the tyrosine phosphatase SHP-1, inhibited sodium channels an
227 nventional T cell proliferation in vitro via tyrosine phosphatase SHP-1-dependent uncoupling of IL-2R
228 ctly regulated the catalytic activity of the tyrosine phosphatase SHP-1.
229 d phosphorylation, as well as recruitment of tyrosine phosphatase SHP-1.
230 nity driven by B cell loss of the regulatory tyrosine phosphatase SHP-1.
231      Here we identify a crucial role for the tyrosine phosphatase SHP-2 in mediating CLR-induced acti
232 itory receptor with the potential to mediate tyrosine phosphatases SHP-1/-2 dependent signaling.
233 tes Src homology domain 2 containing protein tyrosine phosphatase (SHP) 1 and suppresses production o
234                                     The host tyrosine phosphatase SHP1 is known as a brake on immune
235 his study, we demonstrate that expression of tyrosine phosphatase SHP1, a negative regulator that nor
236 1 deficiency led to reduced levels of active tyrosine phosphatase SHP1, which plays a B cell-intrinsi
237 the Src homology 2 domain-containing protein-tyrosine phosphatases Shp1 and Shp2, knockout and transg
238 ion by inducing downstream signaling via the tyrosine phosphatases Shp1 and Shp2.
239 Germline activating mutations of the protein tyrosine phosphatase SHP2 (encoded by PTPN11), a positiv
240                                  The protein tyrosine phosphatase SHP2 binds to phosphorylated signal
241                                          The tyrosine phosphatase SHP2 controls the activity of pivot
242                                  The protein-tyrosine phosphatase SHP2 is an allosteric enzyme critic
243                                      Protein tyrosine phosphatase SHP2 is an oncoprotein associated w
244                                      Protein tyrosine phosphatase SHP2 promotes RAF-to-MAPK signaling
245  We investigated the contribution of protein tyrosine phosphatase Shp2 to lipopolysaccharide (LPS)-in
246  were available, an inhibitor of the protein tyrosine phosphatase SHP2, a critical mediator of RAS si
247                                  The protein tyrosine phosphatase SHP2, encoded by PTPN11, is ubiquit
248 s FGF receptor adaptor protein Frs2alpha and tyrosine phosphatase Shp2, two upstream regulators of Ra
249 3ITD, we show that inhibition of the protein tyrosine phosphatase SHP2, which is essential for cytoki
250 y tyrosine residues that are targets for the tyrosine phosphatase SHP2, which mediates PD-1 inhibitor
251 ssociated binder-1 (Gab1) and SH2-containing tyrosine phosphatase (SHP2) show slower, sustained incre
252  BMP10 interacted with both receptor protein tyrosine phosphatase sigma (PTPRS) and STAT3, which faci
253                             Receptor protein tyrosine phosphatase sigma (PTPsigma) and its subfamily
254                                      Protein tyrosine phosphatase sigma (PTPsigma), along with its si
255 e trans-interacting with presynaptic protein tyrosine phosphatase sigma (PTPsigma).
256                                      Protein tyrosine phosphatase sigma (PTPsigma, PTPRS), a receptor
257                We further found that protein tyrosine phosphatase sigma (PTPsigma, PTPRS), receptor f
258 bound to the axon guidance proteins, protein tyrosine phosphatase sigma (RPTPsigma), and Nogo recepto
259                        Receptor type protein tyrosine phosphatase-sigma (PTPsigma) is primarily expre
260 nducible factor/vascular endothelial protein tyrosine phosphatase signaling and reactive oxygen speci
261 ng tyrosine kinase but contains one encoding tyrosine phosphatase (SP-PTP).
262                        Mice deficient in the tyrosine phosphatase Src homology 2 domain-containing pr
263 nt study, we investigated the effects of the tyrosine phosphatase, SRC-homology 2 domain-containing p
264 rosine phosphatase striatal-enriched protein tyrosine phosphatase (STEP) are known to target the NMDA
265 essive activity of striatal-enriched protein tyrosine phosphatase (STEP) in the brain has been detect
266                    Striatal-enriched protein tyrosine phosphatase (STEP) is a brain-specific protein
267 n we show that the striatal-enriched protein tyrosine phosphatase (STEP) is recruited by Galphaq-coup
268 osphatase (HePTP), striatal-enriched protein-tyrosine phosphatase (STEP), and protein-tyrosine phosph
269                           The brain-specific tyrosine phosphatase, STEP (STriatal-Enriched protein ty
270 in, with an associated downregulation of the tyrosine phosphatase STEP61.
271         Both the tyrosine kinase Fyn and the tyrosine phosphatase striatal-enriched protein tyrosine
272      Here, we have identified T cell protein tyrosine phosphatase (TC-PTP), also known as PTPN2, as a
273                               T-cell protein tyrosine phosphatase (TC-PTP), encoded by Ptpn2, has bee
274 e report the critical role of T-cell protein tyrosine phosphatase (TC-PTP), encoded by Ptpn2, in chem
275                           The T-cell protein tyrosine phosphatase (TCPTP) pathway consists of signali
276 in ITIMs results in recruitment of a protein tyrosine phosphatase that blocks activation signals.
277 containing phosphatase 1 (Shp1) is a protein tyrosine phosphatase that has been identified as a negat
278                Shp2 is a nonreceptor protein tyrosine phosphatase that has been shown to influence ne
279  by the PTPN11 gene, is a ubiquitous protein tyrosine phosphatase that is a critical regulator of sig
280 ity of the receptor and non-receptor protein-tyrosine phosphatases that down-regulate Met phosphoryla
281 on is followed by the recruitment of protein tyrosine phosphatases that inactivate the RTKs and deliv
282 d inhibit inflammation by recruiting protein tyrosine phosphatases to ITIMs.
283 ng ligands and recruit SH2-domain-containing tyrosine phosphatases to their cytoplasmic tails.
284                                      Protein-tyrosine phosphatase TULA-2 has been shown to regulate r
285 ind to the host cellular nonreceptor protein tyrosine phosphatase type 14 (PTPN14) and direct it for
286 (1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitat
287 sophila ortholog of the non-receptor protein tyrosine phosphatase type II (SHP2) to the Pi3k21B (p60)
288   Expression of vascular endothelial protein tyrosine phosphatase VE-PTP (also known as PTPRB), which
289 EC and its phosphatases, EC-specific protein tyrosine phosphatase (VE-PTP) and Src homology phosphata
290 determined that vascular endothelial protein tyrosine phosphatase (VE-PTP) is a HIF2alpha target.
291 ve inhibitor of vascular endothelial-protein tyrosine phosphatase (VE-PTP) that promotes Tie2 activat
292 ding claudin-5, vascular endothelial-protein tyrosine phosphatase (VE-PTP), and von Willebrand factor
293 hermore, we identify an endo-siRNA-regulated tyrosine phosphatase, which limits the longevity of germ
294 hown to co-express striatal-enriched protein tyrosine phosphatase, which may have an important role i
295 ve and novel target is the Eyes absent (EYA) tyrosine phosphatase, which plays a critical role in the
296 eceptor/ligand complex from receptor protein tyrosine phosphatases with large ectodomains, such as CD
297                SHP2 is a nonreceptor protein tyrosine phosphatase within the mitogen-activated protei
298  c-FMS, and a second IL-34 receptor, protein-tyrosine phosphatase zeta (PTP-zeta) were upregulated in
299 s, we demonstrate a role of receptor protein tyrosine phosphatase zeta (RPTPzeta) in PNN structure.
300 ious work demonstrated that receptor protein-tyrosine phosphatase zeta (RPTPzeta)/phosphacan is hypog

 
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