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1                LAR dephosphorylated EphA2 at phosphotyrosyl 930, uncoupling Nck1 from EphA2 and there
2 sequence 5'-(C/T)CCTT, forming a covalent 3'-phosphotyrosyl adduct.
3 se catalytic mechanism of Tdp1 to resolve 3' phosphotyrosyl and 3' phosphoamide linkages.
4 a 55-kDa enzyme that hydrolyzes both protein phosphotyrosyl and 3-phosphorylated inositol phospholipi
5  of p-nitrophenyl phosphate, dephosphorylate phosphotyrosyl, and phosphothreonyl residues in syntheti
6  a single Mg(2+)-ion mechanism assisted by a phosphotyrosyl-arginine cation-pi interface.
7 whose cytoplasmic tail is known to include a phosphotyrosyl-based motif that inhibits a variety of im
8 the enzyme to the DNA termini by a 3'- or 5'-phosphotyrosyl bond and are implicated in hereditary hum
9 rase I (Top1) activity by hydrolyzing the 3'-phosphotyrosyl bond that links Top1 to a DNA strand brea
10 transferase reaction were linked to HP via a phosphotyrosyl bond, and replacement of the Y63 residue
11 re-cleaved" type I substrate containing a 3'-phosphotyrosyl bond, the Flp-RNase I activity can be eli
12 a complementary human enzyme that cleaves 5'-phosphotyrosyl bonds has not been reported, despite the
13 cesses 3'-blocking lesions, predominantly 3'-phosphotyrosyl bonds resulting from the trapping of topo
14                           Tdp1 hydrolyzes 3'-phosphotyrosyl bonds to generate 3'-phosphate DNA and fr
15 LD) superfamily of enzymes and hydrolyzes 3'-phosphotyrosyl bonds to generate 3'-phosphate DNA and fr
16 DNA phosphodiesterase I (Tdp1) hydrolyzes 3'-phosphotyrosyl bonds to generate 3'-phosphate DNA and ty
17 ), a newly discovered enzyme that cleaves 5'-phosphotyrosyl bonds, is a potential target for chemothe
18 esterase 1 (TDP1), an enzyme that cleaves 3'-phosphotyrosyl bonds.
19 n enzyme that catalyzes the hydrolysis of 3'-phosphotyrosyl bonds.
20                                       The 3'-phosphotyrosyl cleavage activity maps to the MRE11 activ
21 tors by virtue of the distinct preference of phosphotyrosyl-containing sequences for SH2 domains.
22 uman Tdp1 (hTdp1) to identify appropriate 3'-phosphotyrosyl DNA substrates.
23 how that MRE11-RAD50 cleaves the covalent 3'-phosphotyrosyl-DNA bonds that join topoisomerase 1 (Top1
24 eries inhibited recombinant human PTP1B with phosphotyrosyl dodecapeptide TRDI(P)YETD(P)Y(P)YRK as th
25 a DNA topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a pentapyrimidine
26 cinia topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a pentapyrimidine
27 cinia topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a pentapyrimidine
28 a DNA topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a specific target
29 a DNA topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a specific target
30 a DNA topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a specific target
31      Vaccinia TopIB forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at a target site 5'-
32 cinia topoisomerase forms a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate at sites containing
33  re-joining of DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate formed at a specific
34 rand transferase that acts through a DNA-(3'-phosphotyrosyl)-enzyme intermediate, resulting in relaxa
35 and rejoining DNA strands through a DNA- (3'-phosphotyrosyl)-enzyme intermediate.
36 d rejoining of DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate.
37  by forming and resealing a covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate.
38 e strand of duplex DNA via a covalent DNA-(3-phosphotyrosyl)-enzyme intermediate.
39 NA strands through a stable covalent DNA-(3'-phosphotyrosyl)-enzyme intermediate.
40 ases cleave and rejoin DNA through a DNA-(3'-phosphotyrosyl)-enzyme intermediate.
41 ia topoisomerase is unable to form a DNA-(2'-phosphotyrosyl)-enzyme intermediate.
42 d rejoining of DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate.
43 ks and rejoins DNA strands through a DNA-(3'-phosphotyrosyl)-enzyme intermediate.
44 strand transferases that act through DNA-(3'-phosphotyrosyl)-enzyme intermediates.
45 an active site tyrosine to generate a DNA-3'-phosphotyrosyl-enzyme adduct and a free 5'-hydroxyl (5'-
46 merization, suggest that a single SH2 domain-phosphotyrosyl interaction is sufficient for dimerizatio
47                            Although many SH2-phosphotyrosyl interactions have been defined in vitro,
48 ndonuclease activity (type I) towards the 3'-phosphotyrosyl intermediate resulting from strand cleava
49 es (3'-pNP DNAs), which mimic the natural 3'-phosphotyrosyl intermediate, and demonstrate that such p
50 pplies the nucleophile to form a covalent 3'-phosphotyrosyl intermediate.
51 e cleavage reaction, and forms a covalent 3'-phosphotyrosyl intermediate.
52 d upon N-SH2 domain engagement by a specific phosphotyrosyl ligand or upon deletion of the SH2 domain
53     5'-Phosphodiesterase activity requires a phosphotyrosyl linkage and tolerates an extended group a
54 asured in a gel-based assay using 3'- and 5'-phosphotyrosyl linkage at the 3' and 5' ends of an oligo
55 re catalyzed by the formation of a transient phosphotyrosyl linkage between the active-site Tyr-723 a
56 eavage and religation by forming a transient phosphotyrosyl linkage between the DNA and Tyr-274, resu
57 ersial ability of yeast Tdp1 to hydrolyze 5'-phosphotyrosyl linkage between topoisomerase II (Top2) a
58 the repair of 3'-DNA adducts, such as the 3'-phosphotyrosyl linkage of DNA topoisomerase I to DNA.
59 virus (vTopo) forms a reversible covalent 3'-phosphotyrosyl linkage with a single strand of duplex DN
60                     Because Top2p forms a 5' phosphotyrosyl linkage with DNA, previous work predicted
61 Top2 that is covalently bound to DNA by a 5' phosphotyrosyl linkage.
62 nd to the 5' end of the cleaved strand via a phosphotyrosyl linkage.
63 ntly bound to a 5' DNA strand terminus via a phosphotyrosyl linker.
64                                        A new phosphotyrosyl mimetic 4-(alpha-hydroxymalonyl)phenylala
65 cells with a PTPase inhibitor containing the phosphotyrosyl mimetic difluorophosphonomethyl phenylala
66 odiesterase (Tdp1) is an enzyme that removes phosphotyrosyl moieties bound to the 3' end of DNA.
67      Moreover, these data identify the novel phosphotyrosyl motif pYEDP as mediating high affinity as
68  at 1.8 A resolution of the complex with the phosphotyrosyl peptide Ac-pTyr-Glu-Glu-Gly (pYEEG peptid
69 in of human p56lck in complex with the short phosphotyrosyl peptide Ac-pTyr-Glu-Glu-Ile (pYEEI peptid
70 rough reciprocal Src homology 2 domain (SH2)-phosphotyrosyl peptide interactions.
71 L directly inhibited binding of Stat3 to its phosphotyrosyl peptide ligand.
72                     Furthermore, a synthetic phosphotyrosyl peptide that binds to the CRKL SH2 domain
73 mic D1D2 segment of human CD45 in native and phosphotyrosyl peptide-bound forms.
74 determined by Stat3's ability to bind to its phosphotyrosyl-peptide ligand, an interaction critical f
75                                              Phosphotyrosyl peptides corresponding to the p58 tail bo
76      Incubation of p110alpha/p85 dimers with phosphotyrosyl peptides restored activity, but only to t
77  human isoenzyme of the low molecular weight phosphotyrosyl phosphatase (LMW PTPase) is reported here
78                           The Src homology 2 phosphotyrosyl phosphatase (SHP2) is a nonreceptor-type
79                             The Src homology phosphotyrosyl phosphatase 2 (SHP2) plays a positive rol
80 n with significant similarity to a mammalian phosphotyrosyl phosphatase activator (PTPA) regulatory s
81                                              Phosphotyrosyl phosphatase activator (PTPA), also known
82                                              Phosphotyrosyl phosphatase activator PTPA is a type 2A p
83 n that possesses an ability to stimulate the phosphotyrosyl phosphatase activity of PP2A in vitro.
84 ctivation, including Fyn activation, require phosphotyrosyl phosphatase activity.
85                                            A phosphotyrosyl phosphatase was found to be tightly assoc
86 rates by protein tyrosine kinases (PTKs) and phosphotyrosyl phosphatases, respectively.
87 ly immunodepleted the CrkL-associated 120kDa phosphotyrosyl polypeptide, suggesting that the recently
88 ts SH2 domains, with an unidentified 130-kDa phosphotyrosyl protein (P130).
89 h tyrosine-phosphorylated Shc and an unknown phosphotyrosyl protein (pp80).
90             In that study, we had detected a phosphotyrosyl protein of approximately 100 KDa (p100) i
91 n of specific inhibitors of this and related phosphotyrosyl protein phosphatases.
92 ble qualitative changes were observed in the phosphotyrosyl protein profile between c-src and v-src t
93 TPase-activating protein (rasGAP)-associated phosphotyrosyl protein, is thought to act as a multiple
94 istent with a role for Tdp1 in processing 3' phosphotyrosyl protein-DNA covalent complexes.
95 inds duplex DNA and forms a covalent DNA-(3'-phosphotyrosyl) protein adduct at the sequence 5'-CCCTT
96  through the formation of a covalent DNA-(3'-phosphotyrosyl)protein intermediate at sites containing
97 der 1, and three other, as yet unidentified, phosphotyrosyl proteins as candidate physiological subst
98  ability to decrease the cellular content of phosphotyrosyl proteins in these Philadelphia-positive l
99 ndogenous Fes in control BAC1.2F5 cells, the phosphotyrosyl proteins that were recognized were the sa
100  mDab1 can also form complexes with cellular phosphotyrosyl proteins through a domain that is related
101 ntial interaction with proliferation-related phosphotyrosyl proteins.
102                The SH2 domain of v-Src binds phosphotyrosyl-proteins in vivo and in vitro.
103  of a retroviral LTR, the reduced binding of phosphotyrosyl-proteins is compatible with wild-type tra
104 reduced but did not eliminate the binding of phosphotyrosyl-proteins to the v-Src SH2 domain.
105 her than arginine can support the binding of phosphotyrosyl-proteins, albeit at reduced levels.
106 the interaction of the v-Src SH2 domain with phosphotyrosyl-proteins.
107 hosphonophenylalanine ((alpha-Me)Ppp) in the phosphotyrosyl (pTyr) C-proximal position (pY + 1 residu
108                  While most SH2 domains bind phosphotyrosyl (pTyr) containing peptides in extended fa
109                    Macrocyclization from the phosphotyrosyl (pTyr) mimetic's beta-position has previo
110 ll peptide bearing the hydrolytically stable phosphotyrosyl (pTyr) mimetic, (difluorophosphonomethyl)
111 inhibitory potency of an extensive series of phosphotyrosyl (pTyr) mimetics (Xxx) expressed in the EG
112                              Nonhydrolyzable phosphotyrosyl (pTyr) mimetics serve as important compon
113                               Development of phosphotyrosyl (pTyr) mimetics which are stable to prote
114 nded to the beta-methylene of amino-terminal phosphotyrosyl (pTyr) mimetics.
115  Src homology 2 (SH2) domain, which binds to phosphotyrosyl (pTyr) residues generated by the activati
116 ion of this method and a previously reported phosphotyrosyl (pY) library screening technique to dual-
117                                            A phosphotyrosyl (pY) peptide library containing completel
118                                            A phosphotyrosyl (pY) peptide library was screened against
119                              A combinatorial phosphotyrosyl (pY) peptide library was screened to dete
120  binding assay for evaluating the binding of phosphotyrosyl (pY) peptides to the recombinant SH2 doma
121  homology-2 (SH2) domains recognize specific phosphotyrosyl (pY) proteins and promote protein-protein
122 osphatases (PTPs) catalyze the hydrolysis of phosphotyrosyl (pY) proteins to produce tyrosyl proteins
123 rolytic removal of the phosphoryl group from phosphotyrosyl (pY) proteins.
124 odiester-carrying amino acid could mimic the phosphotyrosyl residue.
125 eryl and phosphothreonyl residues as well as phosphotyrosyl residues.
126 otected phosphotyrosine into proteins from a phosphotyrosyl-tRNACUA by UAG codon suppression during i
127 est that TULA-2 is sequence-selective toward phosphotyrosyl (Tyr(P)) peptides.

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