ライフサイエンスコーパス: NR box

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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

10 DRIP150 contains C- and N-terminal NR boxes (amino acids 1182-1186 and 69-73, respectively)

11 RT contain sequences that are similar to the NR box and are repeated in each of two NR interaction do

12 mechanism involving direct contacts between NR boxes and the receptor's co-activator pocket.

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

18 Tip110 bound to AR in an NR box-dependent manner and inhibited AREs-mediated repo

19 Our findings suggest that a novel NR box enables MET and GCE to interact JH-dependently wi

20 is mediated by a conserved motif, termed the NR box, found in many coregulators.

21 bestrol (DES) and a peptide derived from the NR box II region of the coactivator GRIP1 and the crysta

22 that typically interacts with LXXLL motifs (NR box) in p160 steroid receptor coactivators.

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

25 an SH3 domain-binding motif (SEPPSPS) and an NR box-like sequence (LKTLL).

26 An NR box motif contributes to but is not solely responsibl

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

29 rd the N-terminal region, which includes the NR-box motif.

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

32 ires an intact ligand-binding domain and the NR box of the coactivators.

33 DRIP205 deletion constructs showed that the NR boxes of DRIP205 are not required for this coactivati

34 ter for SRC1a binding to flERE.E2-ER than an NR box peptide from TRAP220.

35 groove by mimicking the interactions of the NR box peptide with the LBD.

36 Increasing amounts of NR box peptides greatly enhanced the rate of dissociatio

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

41 This suggests that whereas the NR box region is a primary site of interaction between S

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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