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1 Plk1 decreased its affinity for IKKgamma in pulldown assay.
2 or PP2A-B) using a glutathione S-transferase-pulldown assay.
3 active state of AIP1 assessed by an in vitro pulldown assay.
4 ation in the glutathione S-transferase (GST) pulldown assay.
5 ction by the glutathione S-transferase (GST) pulldown assay.
6 endogenous ARF6, but not ARF1, using a novel pulldown assay.
7 n vitro by a glutathione S-transferase (GST) pulldown assay.
8 d to form a stable complex with SpoIVFB in a pulldown assay.
9 led-coil domain of MuRF1 was demonstrated by pulldown assay.
10 f apoE, as determined by an in vitro heparin pulldown assay.
11 ently confirmed by glutathione S-transferase pulldown assays.
12 nal domain of RPW8.2, which was confirmed by pulldown assays.
13 oprecipitation and glutathione S-transferase pulldown assays.
14 tion with Akt2 by co-immunoprecipitation and pulldown assays.
15 al 44 amino acids of PDZD11, as shown by GST-pulldown assays.
16 iation of PG with ANX II was demonstrated in pulldown assays.
17 and SHP-2 phosphatase activity, and in vitro pulldown assays.
18 determined by yeast two-hybrid assays and by pulldown assays.
19 n, a result that was confirmed by GST-fusion pulldown assays.
20 ast two-hybrid and glutathione S-transferase pulldown assays.
21 h phosphatase abolishes their association in pulldown assays.
22 and in vitro glutathione S-transferase (GST) pulldown assays.
23 otein complex immunoprecipitation and biotin pulldown assays.
24 ), as shown by yeast two-hybrid and in vitro pulldown assays.
25 by using RNA immunoprecipitation and biotin pulldown assays.
26 cence, flow cytometry, real-time RT-PCR, and pulldown assays.
27 co-immunoprecipitation and in vitro protein pulldown assays.
28 d as the 14-3-3 binding region by GST-14-3-3 pulldown assays.
29 d the TM 4,5-loop was demonstrated using GST pulldown assays.
30 1 for binding to both PP2Acalpha isoforms in pulldown assays.
31 th E2 and interacted only weakly with NS3 in pulldown assays.
32 n protein (amino acids 475-589) on liposomal pulldown assays.
33 s by confocal microscopy and in an in vitro "pulldown" assay.
37 s was confirmed by glutathione S-transferase pulldown assay and co-immunoprecipitation assay in human
38 rabidopsis and Nicotiana benthamiana using a pulldown assay and fluorescence resonance energy transfe
39 em and an in vitro glutathione-S-transferase pulldown assay and observed interactions between cyclin
41 interaction by site-directed mutagenesis and pulldown assay and thereby confirm that the major bindin
43 and NRL-leucine zipper was validated by GST pulldown assays and co-immunoprecipitation from bovine r
44 ee classes of aptamers bound to Smads by GST pulldown assays and co-immunoprecipitation from mammalia
45 using a combination of affinity interaction pulldown assays and co-immunoprecipitations from brain a
49 nteracts physically with Abl and Trio in GST-pulldown assays and in co-immunoprecipitation experiment
50 y impaired both the UL54-UL44 interaction in pulldown assays and long-chain DNA synthesis without aff
52 e in eIF5 interaction with eIF1 and eIF3c in pulldown assays and reduces the eIF5-mediated stimulatio
53 70-binding site in SOD2, we used a series of pulldown assays and showed that hsp70 binds to the amino
54 in two-hybrid and glutathione S-transferase pulldown assays and that interaction with the mutant TFI
55 DM2 required for p21(Waf1) degradation using pulldown assays and Western blotting and then examined t
56 ch as affinity precipitation of protein, GST-pulldown assay, and coimmunoprecipitation of proteins, w
57 ctivity enzyme-linked immunosorbent assay, a pulldown assay, and immunostaining with a monoclonal ant
59 ith MLF1 by yeast two-hybrid analysis and in pulldown assays, and colocalizes with it in both the nuc
60 nity chromatography, co-immunoprecipitation, pulldown assays, and enzyme-linked immunosorbent assay,
61 Here, using size-exclusion chromatography, pulldown assays, and small angle x-ray scattering, we sh
62 brid mating and co-transformation protocols, pulldown assays, and surface plasmon resonance analysis.
63 ient transfection, yeast two-hybrid, and GST pulldown assays are used to show not only that nuclear r
64 s work establishes the single-molecule lipid pulldown assay as a simple and highly sensitive approach
66 ation analysis, immunoprecipitation, and GST pulldown assays based on the theoretical predictions rev
70 n was confirmed by glutathione-S-transferase pulldown assays, by coimmunoprecipitation, and by actin
71 We used L-selectin cytoplasmic tail peptide pulldown assays combined with high sensitivity liquid ch
73 oprecipitation and glutathione S-transferase pulldown assays confirm the complex formation between TB
86 erminal kinase domain combined with in vitro pulldown assays demonstrated that eriodictyol, a flavano
88 and glutathione S-transferase fusion protein pulldown assays demonstrated that Rab8 interacted with t
91 oprecipitation and glutathione S-transferase pulldown assays demonstrated that the N terminus of ClC-
94 biophysical methods, including heterocomplex pulldown assays, far-UV CD spectroscopy, the thioflavin
95 ombination of kindlin knockdown, biochemical pulldown assays, fluorescence microscopy, fluorescence r
96 roteins within platelets and confirmation by pulldown assays followed by immunoblotting, we identifie
97 eract with UL44 by glutathione S-transferase pulldown assays, for basal DNA polymerase activity, and
100 noprecipitation or glutathione S-transferase pulldown assays from detergent-solubilized membrane extr
101 oupled receptor in glutathione S-transferase pulldown assays from rat brain lysates coupled with high
102 oplasmic capping complex was demonstrated by pulldown assays, gel filtration and proximity-dependent
104 trometry and glutathione S-transferase (GST) pulldown assays identified integrin alpha5 as a novel Sc
105 t with pU(L)6 in a glutathione S-transferase pulldown assay in the absence of other viral proteins an
109 , isothermal titration calorimetry data, and pulldown assays indicated that CaM-N and CaM-C both can
111 In this study, glutathione S-transferase pulldown assays indicated that residues 1 to 68 of UL84
112 findings indicate that the streptavidin-bead pulldown assay is valuable for determining the binding o
125 pitation and glutathione S-transferase (GST) pulldown assays revealed that GBP1 interacted with the N
129 hione S-transferase-Ras-binding domain (RBD) pulldown assays revealed that, although high-grade TCR s
141 by absorbance spectroscopy and hemin-agarose pulldown assays showed that Shu1 interacts with hemin, w
147 rectly interacts with importin beta in a GST-pulldown assay, suggesting that the SMN complex might re
148 acted with the helicase domain of BKV Tag in pulldown assays, suggesting that NFI helps recruit Tag t
149 p300 also interacted with Tal1 in protein pulldown assays, suggesting this was a direct interactio
150 sary for PIP3 regulation, and a biochemical "pulldown" assay suggests that PIP3 directly binds this r
151 to embryonic organ explants, with a microRNA pulldown assay that allows direct identification of micr
153 selected biochemical pathways; (c) affinity pulldown assays that, in some cases, confirm and even ex
154 ipt in human T cells and found, using biotin pulldown assay, that HuR specifically interacts with its
160 Rosetta pLysS cells, purified, and used in a pulldown assay to identify interacting proteins from hum
162 al mRNA-binding proteins identified from RNA pulldown assays to determine which of these exhibit bona
163 Here, we used biolayer interferometry and pulldown assays to identify regions of RAG1 necessary fo
164 e interaction with PP2A as demonstrated by a pulldown assay using a fusion of this domain with glutat
171 g luciferase p-miR-Report constructs and RNA pulldown assays, we confirmed that miR-511 bound directl
174 Using EMSA, supershift assays, and promoter pulldown assays, we demonstrated that CREB, ATF-2, and c
178 ce energy transfer experiments, and in vitro pulldown assays, we have now identified the key residues
179 Using the human Cad11 cytoplasmic domain in pulldown assays, we identified human angiomotin (Amot),
180 pitation (co-IP), mass spectrometry, and GST pulldown assays, we identified poly(ADP-ribose) polymera
181 assays, and glutathione S-transferase (GST) pulldown assays, we show that NR2A subunits interact dir
182 depending on its CTD phosphorylation state, pulldown assays were performed using the CTD of the duck
183 tial effect, glutathione S-transferase (GST) pulldown assays were performed, revealing that Y544 is c
185 rmed in vitro by a glutathione S-transferase pulldown assay, which allowed us to detect 2C/2C associa
186 V envelope glycoproteins were also used in a pulldown assay with beads coated with heparin, a close H
191 ed both in vitro by Far-Western and antibody pulldown assays with recombinant proteins and in vivo by
192 say that combines principles of conventional pulldown assays with single-molecule fluorescence micros
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