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1 es a strong T-cell regulator called lymphoid protein tyrosine phosphatase.
2 /mammalian target of rapamycine pathway, and protein tyrosine phosphatase.
3 HP2 is an ubiquitously expressed cytoplasmic protein tyrosine phosphatase.
4 oxidation that underlies redox inhibition of protein tyrosine phosphatases.
5 ype for a novel class of eukaryotic aspartyl protein tyrosine phosphatases.
6 y high conservation of the active site among protein tyrosine phosphatases.
7 phosphatase Src homology 2 domain-containing protein tyrosine phosphatase 1 (Shp1) show increased leu
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 late radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and alpha- and b
11 aling and reduced levels of the phosphatases protein tyrosine phosphatase 1B (PTP1B) and phosphatase
15 at increased NO production via inhibition of protein tyrosine phosphatase 1B (PTP1B) is associated wi
17 e we show how these pillars are connected in Protein Tyrosine Phosphatase 1B (PTP1B), a drug target f
18 tion machinery modulates an interaction with protein tyrosine phosphatase 1B (PTP1B), an ER-associate
19 mally disruptive optical approach to control protein tyrosine phosphatase 1B (PTP1B)-an important reg
23 ory power of these phenolic extracts against Protein Tyrosine Phosphatase 1B enzyme (PTP-1B), overexp
25 we experimentally validate a cryptic site in protein tyrosine phosphatase 1B using a covalent ligand
26 o enzyme inhibition (glycogen phosphorylase, protein tyrosine phosphatase 1B) or by inhibiting renal
29 s zinc transport into hepatocytes to inhibit protein-tyrosine phosphatase 1B (PTP1B) activity, which
30 epatocytes with or without expression of the protein-tyrosine phosphatase 1B (PTP1B) and in wild-type
32 ficiency led to abnormally increased hepatic protein-tyrosine phosphatase 1B (PTP1B) expression and e
33 h as silencer of cell signaling 1 (SOCS1) or protein-tyrosine phosphatase 1B (PTP1B) in this process.
41 o studies have indicated that SH2-containing protein tyrosine phosphatase 2 (SHP-2) is a signaling fa
42 progenitor cells deficient in SH2-containing protein tyrosine phosphatase 2 (Shp2) further enhanced m
43 Shp2 (the Src homology-2 domain containing protein tyrosine phosphatase 2), a ubiquitously expresse
45 eduction of Src homology 2 domain-containing protein-tyrosine phosphatase 2, known to maintain vascul
48 ors trigger Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2) translocation to t
49 two of them, thyrotroph embryonic factor and protein tyrosine phosphatase 4a1, resulted in altered GL
50 ecule inhibitor of the oncogenic phosphatase protein tyrosine phosphatase 4A3 binds to at least one s
52 s an E3 ligase for STEP61 (striatal-enriched protein tyrosine phosphatase), a protein tyrosine phosph
53 These three genes encode a non-receptor type protein tyrosine phosphatase, a serine/threonine protein
54 ling in cells, suggesting inhibition of SHP2 protein tyrosine phosphatase activity by this peptide.
56 mains incompletely understood, receptor type protein tyrosine phosphatase alpha (PTP-alpha encoded by
60 ions of the focal adhesion kinase (FAK) with protein-tyrosine phosphatase-alpha (PTP-alpha) in IL-1 s
62 in its activation through the stimulation of protein tyrosine phosphatases, an effect shared by other
63 Bro1 proteins HD-PTP (His domain-containing protein tyrosine phosphatase) and BROX (Bro1 domain and
64 decreased oxidative stress and oxidation of protein tyrosine phosphatases, and ameliorated activatio
66 e TCR expression and increased expression of protein tyrosine phosphatases as compared with naive T c
75 or type 7 (PTPN7), also called hematopoietic protein tyrosine phosphatase, controls extracellular sig
77 marily with a transsynaptic binding partner, protein tyrosine phosphatase delta (PTPdelta); however,
80 zyme, the interactions between its N-SH2 and protein-tyrosine phosphatase domains are weakened such t
84 st that novel biological pathway such as the protein tyrosine phosphatase family is involved in regul
87 rast, elevated expression of Lar, a receptor protein tyrosine phosphatase found to be necessary for a
88 e PSTPIP2 inhibitory function is mediated by protein tyrosine phosphatases from the proline-, glutami
89 zed that the structural features of receptor protein tyrosine phosphatase-gamma (RPTPgamma) that are
90 everal tumor suppressor genes, including the protein tyrosine phosphatase gene PTPROt, which became s
95 e phosphatases (PTPs) includes hematopoietic protein-tyrosine phosphatase (HePTP), striatal-enriched
96 Here, we show that deletion of Ptpn21, a protein tyrosine phosphatase highly expressed in HSCs, i
97 phatase nonreceptor type 11 Ptpn11 (Shp2), a protein tyrosine phosphatase implicated in multiple cell
98 al-enriched protein tyrosine phosphatase), a protein tyrosine phosphatase implicated in several neuro
100 e temporal regulation of a specific class of protein tyrosine phosphatases in controlling the rate, a
102 nce of the ERK phosphatase striatum-enriched protein-tyrosine phosphatase in hemideletion males.
103 details of reactive oxygen species-catalyzed protein-tyrosine phosphatase inactivation have remained
104 scular permeability via vascular endothelial-protein tyrosine phosphatase inhibition limits mycobacte
105 rotein VAPB interacts with the mitochondrial protein tyrosine phosphatase-interacting protein-51 (PTP
106 ine phosphatase 1B (PTP1B), an ER-associated protein tyrosine phosphatase involved in the negative re
108 yrosine phosphatase, STEP (STriatal-Enriched protein tyrosine Phosphatase) is an important regulator
109 ase 2), a ubiquitously expressed cytoplasmic protein tyrosine phosphatase, is implicated in regulatin
112 ular endothelial cadherin, the transmembrane protein tyrosine phosphatase LAR, and the RAC1 guanidine
113 s with the Ig domains of LAR family receptor protein tyrosine phosphatases (LAR-RPTPs; LAR, PTPdelta,
114 hosphatase that was identified, the receptor protein tyrosine phosphatase leukocyte-antigen-related (
115 res of two catalytically inactive mutants of protein-tyrosine phosphatase-like myo-inositol phosphata
117 sustained in vivo binding and retention of a protein tyrosine phosphatase mu (PTPmu)-targeted, molecu
118 Switching of the substrate specificity of protein tyrosine phosphatase N12 by cyclin-dependent kin
124 x (MHC), interleukin 23 receptor (IL23R) and protein tyrosine phosphatase non-receptor type 22 (PTPN2
128 ng variant (Ala455Thr) was identified in the protein tyrosine phosphatase non-receptor type 6 (PTPN6)
129 ncluded in prior panel testing: a pathogenic protein tyrosine phosphatase, non-receptor type 11 (PTPN
130 was mediated by direct targeting of PTPN14 (protein tyrosine phosphatase, non-receptor type 14) whic
131 have established that the gene encoding the protein tyrosine phosphatase nonreceptor 22 (PTPN22) mak
132 s, are associated with an allelic variant of protein tyrosine phosphatase nonreceptor 22 (PTPN22), wh
134 ephosphorylated, which could be prevented by protein tyrosine phosphatase nonreceptor type 1 inhibiti
137 completely abolish FLNA's interactions with protein tyrosine phosphatase nonreceptor type 12, which
138 mon genetic variant in the gene encoding the protein tyrosine phosphatase nonreceptor type 22 (PTPN22
142 protein encoded by the autoimmune-associated protein tyrosine phosphatase nonreceptor type 22 gene, P
145 stitution of tryptophan with arginine in the protein tyrosine phosphatase, nonreceptor type 22 gene (
146 on the outside of the mitochondria released protein tyrosine phosphatase, nonreceptor type 6 (SHP1,
147 , resulting from increased expression of the protein tyrosine phosphatase, nonreceptor type, 22 (PTPN
149 te increasing evidence for the importance of protein-tyrosine phosphatase oxidation in signal transdu
150 en dephosphorylated by PTP1B, an ER-resident protein tyrosine phosphatase, prior to axonal transport.
151 ree PRL (phosphatases of regenerating liver) protein tyrosine phosphatases (PRL-1, -2 and -3) have be
153 We demonstrate that the activity of the protein tyrosine phosphatase PTP-PEST, which controls pa
155 This paper presents an approach to measure protein tyrosine phosphatase (PTP) activity in individua
156 scribe a novel method for the measurement of protein tyrosine phosphatase (PTP) activity in single hu
161 of IL-4 signaling, we identified reversible protein tyrosine phosphatase (PTP) oxidation as the prim
162 ction mutations in PTPN11, which encodes the protein tyrosine phosphatase (PTP) SHP2, are implicated
164 an adhesion and signaling unit comprised of protein tyrosine phosphatase (PTP)-PEST and the extracel
167 y hidden allosteric sites is demonstrated in protein tyrosine phosphatases (PTP) by creation of singl
172 defines a tumor suppressor function for the protein tyrosine phosphatase PTP1B in myeloid lineage ce
174 sue, Krishnan and colleagues reveal that the protein tyrosine phosphatase PTP1B is upregulated in pat
179 diet (HFD), but that coordinate loss of the protein tyrosine phosphatase Ptpn1 (encoding PTP1B) enab
183 alysis of the dynamics of association of the protein tyrosine phosphatase PTPN22 and lipid phosphatas
186 orylated tyrosine 207 (pTyr207)-CrkL and the protein tyrosine phosphatase PTPRC/CD45; these assays we
190 FR) coupled to dephosphorylating activity of protein tyrosine phosphatases (PTPs) ensures robust yet
191 as long been recognized, the significance of protein tyrosine phosphatases (PTPs) in cellular signali
192 aptic transmission was also prevented by the protein tyrosine phosphatases (PTPs) inhibitor sodium or
193 inhibition by orthovanadate or depletion of protein tyrosine phosphatases (PTPs) resulted in the rec
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
199 s," contribute to proper signal transduction.Protein-tyrosine phosphatases (PTPs) are thought to be m
201 screen to investigate the role of classical protein-tyrosine phosphatases (PTPs) in three-dimensiona
202 The kinase interaction motif (KIM) family of protein-tyrosine phosphatases (PTPs) includes hematopoie
203 been expended to develop inhibitors against protein-tyrosine phosphatases (PTPs), nearly all of it u
204 ting liver (PRLs), the most oncogenic of all protein-tyrosine phosphatases (PTPs), play a critical ro
206 Here, we show that hepatic expression of Protein Tyrosine Phosphatase Receptor Gamma (PTPR-gamma)
207 We report here that homodimerization of protein tyrosine phosphatase receptor J (PTPRJ, also kno
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
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
218 on of the RAS pathway in mice that expressed protein tyrosine phosphatase receptor-zeta (PTPRZ), wher
220 hed protein-tyrosine phosphatase (STEP), and protein-tyrosine phosphatase receptor type R (PTPRR).
223 leukocyte antigen-related (Lar), a receptor protein tyrosine phosphatase (RPTP) and the only known D
228 phogenetic apoptosis, requiring the receptor protein tyrosine phosphatases (RPTPs): LAR and RPTPsigma
229 caused by gain-of-function mutations in the protein tyrosine phosphatase SH2 domain-containing PTP (
231 y activates Src homology domain 2 containing protein tyrosine phosphatase (SHP) 1 and suppresses prod
232 rylation of Src homology domain 2-containing protein tyrosine phosphatase (SHP) 2 and Src homology do
233 cluding the Src homology 2 domain-containing protein-tyrosine phosphatases Shp1 and Shp2, knockout an
237 Here, we have analyzed the function of the protein tyrosine phosphatase Shp2 in mice by deleting it
241 pan-RAS were available, an inhibitor of the protein tyrosine phosphatase SHP2, a critical mediator o
243 ons in Ptpn11, which encodes the nonreceptor protein tyrosine phosphatase Shp2, show hippocampal-depe
244 n of Flt3ITD, we show that inhibition of the protein tyrosine phosphatase SHP2, which is essential fo
246 oplasmic BMP10 interacted with both receptor protein tyrosine phosphatase sigma (PTPRS) and STAT3, wh
247 hat within the human immune system, receptor protein tyrosine phosphatase sigma (PTPRS) is expressed
249 receptor-like protein tyrosine phosphatases, protein tyrosine phosphatase sigma (PTPsigma) and leukoc
255 vatives bound to the axon guidance proteins, protein tyrosine phosphatase sigma (RPTPsigma), and Nogo
256 antigen related (LAR) phosphatase subfamily, protein tyrosine phosphatase sigma and LAR, are function
259 ypoxia-inducible factor/vascular endothelial protein tyrosine phosphatase signaling and reactive oxyg
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
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
268 involved in growth factor signaling, T-cell protein tyrosine phosphatase (TC-PTP), and the E3 ubiqui
269 Here, we report the critical role of T-cell protein tyrosine phosphatase (TC-PTP), encoded by Ptpn2,
273 ntiviral signaling protein (MAVS) and T cell protein tyrosine phosphatase (TCPTP) suggests an avenue
274 ues within ITIMs results in recruitment of a protein tyrosine phosphatase that blocks activation sign
275 domain-containing phosphatase 1 (Shp1) is a protein tyrosine phosphatase that has been identified as
277 encoded by the PTPN11 gene, is a ubiquitous protein tyrosine phosphatase that is a critical regulato
278 selection is followed by the recruitment of protein tyrosine phosphatases that inactivate the RTKs a
279 P1B) is a ubiquitously expressed nonreceptor protein-tyrosine phosphatase that regulates various cell
280 he activity of the receptor and non-receptor protein-tyrosine phosphatases that down-regulate Met pho
284 e HPVs bind to the host cellular nonreceptor protein tyrosine phosphatase type 14 (PTPN14) and direct
285 and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunopr
286 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 ity and determined that vascular endothelial protein tyrosine phosphatase (VE-PTP) is a HIF2alpha tar
290 ompetitive inhibitor of vascular endothelial-protein tyrosine phosphatase (VE-PTP) that promotes Tie2
291 on including claudin-5, vascular endothelial-protein tyrosine phosphatase (VE-PTP), and von Willebran
292 e, we demonstrated that vascular endothelial-protein tyrosine phosphatase (VE-PTP), which negatively
293 in, known to be involved in stabilization of protein-tyrosine phosphatases, were found to be induced
294 s were shown to co-express striatal-enriched protein tyrosine phosphatase, which may have an importan
295 that dephosphorylate STAT3, such as receptor protein tyrosine phosphatases, which are encoded by the
296 ngaged receptor/ligand complex from receptor protein tyrosine phosphatases with large ectodomains, su
298 cultures, we demonstrate a role of receptor protein tyrosine phosphatase zeta (RPTPzeta) in PNN stru
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