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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
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
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
21 tors by virtue of the distinct preference of phosphotyrosyl-containing sequences for SH2 domains.
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
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
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
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
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
65 cells with a PTPase inhibitor containing the phosphotyrosyl mimetic difluorophosphonomethyl phenylala
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
74 determined by Stat3's ability to bind to its phosphotyrosyl-peptide ligand, an interaction critical f
77 human isoenzyme of the low molecular weight phosphotyrosyl phosphatase (LMW PTPase) is reported here
80 n with significant similarity to a mammalian phosphotyrosyl phosphatase activator (PTPA) regulatory s
83 n that possesses an ability to stimulate the phosphotyrosyl phosphatase activity of PP2A in vitro.
87 ly immunodepleted the CrkL-associated 120kDa phosphotyrosyl polypeptide, suggesting that the recently
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
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
103 of a retroviral LTR, the reduced binding of phosphotyrosyl-proteins is compatible with wild-type tra
107 hosphonophenylalanine ((alpha-Me)Ppp) in the phosphotyrosyl (pTyr) C-proximal position (pY + 1 residu
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
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-
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
126 otected phosphotyrosine into proteins from a phosphotyrosyl-tRNACUA by UAG codon suppression during i
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