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1 rough its coactivator motifs (LXXLL motifs, "NR boxes").
2 ns containing an Leu-x-x-Leu-Leu motif (the 'NR box').
3 ory effects were abolished by removal of the NR box.
4 raction domain that resembles the eukaryotic NR box.
5 interaction is intact and occurs through the NR-box.
6 XL that represents a novel nuclear receptor (NR) box.
7 205 coactivation of ERalpha does not require NR boxes.
8 to very subtle differences between CoRNR and NR boxes.
9 GCE heterodimer formation involves a typical NR box-AF2 interaction but does not require the canonica
11 RT contain sequences that are similar to the NR box and are repeated in each of two NR interaction do
13 ation of ERalpha by DRIP205 does not require NR boxes, and variants with deletion of N-terminal (amin
14 hese results indicate that both EXXP and the NR box are important for the Mfa-SspB interaction and th
15 g this homogenous method several coregulator NR boxes capable of associating with thyroid receptor at
16 with mutations in either or both of the two NR boxes confirmed a critical role for them in in vitro
17 markedly impaired response to GRIP1, whereas NR box-defective GRIP1 proteins lost part of their Tat c
21 bestrol (DES) and a peptide derived from the NR box II region of the coactivator GRIP1 and the crysta
23 tion of ERalpha by DRIP150 in ZR-75 cells is NR box-independent and requires a novel sequence with pu
24 0 association can be competed by coactivator NR boxes, indicating ERAP140 binds ER alpha on a surface
27 o acid region containing a nuclear receptor (NR)-box motif (-LRILL-) mediates binding of MTA1s with E
28 ison studies showed similarities between the NR-box motif of MTA1s and a similar motif of coregulator
30 main (NID) of p160 proteins containing three NR box motifs (LXXLL) for the interaction with the hormo
31 scence assay shows that a peptide within the NR box of PGC-1 is efficiently recruited by a ligand-bou
33 DRIP205 deletion constructs showed that the NR boxes of DRIP205 are not required for this coactivati
37 imately 40-250-fold molar excess of the P160 NR box peptides was required to inhibit SRC1a binding by
38 Short LXXLL-containing nuclear receptor (NR) box peptides from P160 coactivators competed much be
39 ignated BAR) resembles the nuclear receptor (NR) box protein-protein interacting domain and potently
40 lix resemble the consensus nuclear receptor (NR) box protein-protein interacting domain sequence (LXX
42 on in transfected cells requires both of the NR boxes that contain the LXXLL motif implicated in nucl
43 amino acid), the so-called nuclear receptor (NR) box, through which binding of these regulatory prote
44 lta587-636 is a DRIP205 mutant in which both NR boxes within amino acids 587-636 have been deleted an
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