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Gurnell, M; Rajanayagam, O; Agostini, M; Clifton-Bligh, R J; Wang, T; Zelissen, P M; van der Horst, F; van de Wiel, A; Macchia, E; Pinchera, A; Schwabe, J W; Chatterjee, V K.

Endocrinology ; 140(12): 5901-6, 1999 Dec.

Artículo en Inglés | MEDLINE | ID: mdl-10579356

13.

St John's wort, a herbal antidepressant, activates the steroid X receptor.

Wentworth, J M; Agostini, M; Love, J; Schwabe, J W; Chatterjee, V K.

J Endocrinol ; 166(3): R11-6, 2000 Sep.

Artículo en Inglés | MEDLINE | ID: mdl-10974665

14.

Distinctly different...or really much the same?

Schwabe, J W.

Curr Biol ; 2(5): 237-9, 1992 May.

Artículo en Inglés | MEDLINE | ID: mdl-15335957

15.

DNA between the sheets.

Schwabe, J W.

Curr Biol ; 2(12): 661-3, 1992 Dec.

Artículo en Inglés | MEDLINE | ID: mdl-15336020

16.

What is evolution playing at?

Schwabe, J W; Travers, A A.

Curr Biol ; 3(9): 628-30, 1993 Sep 01.

Artículo en Inglés | MEDLINE | ID: mdl-15335684

17.

Spurring on transcription?

Travers, A A; Schwabe, J W.

Curr Biol ; 3(12): 898-900, 1993 Dec 01.

Artículo en Inglés | MEDLINE | ID: mdl-15335830

18.

Protein motifs 5. Zinc fingers.

Klug, A; Schwabe, J W.

FASEB J ; 9(8): 597-604, 1995 May.

Artículo en Inglés | MEDLINE | ID: mdl-7768350

19.

All wrapped up.

Choo, Y; Schwabe, J W.

Nat Struct Biol ; 5(4): 253-5, 1998 Apr.

Artículo en Inglés | MEDLINE | ID: mdl-9546210

20.

Towards an understanding of protein-DNA recognition.

Rhodes, D; Schwabe, J W; Chapman, L; Fairall, L.

Philos Trans R Soc Lond B Biol Sci ; 351(1339): 501-9, 1996 Apr 29.

Artículo en Inglés | MEDLINE | ID: mdl-8735272

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Beyond zinc fingers: steroid hormone receptors have a novel structural motif for DNA recognition.

Histone deacetylase (HDAC) 1 and 2 complexes regulate both histone acetylation and crotonylation in vivo.

Transcriptional control: how nuclear receptors get turned on.

Signal transduction: fast lane to transcriptional activation.

Limbs are moving: where are they going?

The role of water in protein-DNA interactions.

Human androgen receptor gene ligand-binding-domain mutations leading to disrupted interaction between the N- and C-terminal domains.

The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation.

DNA recognition by the oestrogen receptor: from solution to the crystal.

A dominant negative human peroxisome proliferator-activated receptor (PPAR){alpha} is a constitutive transcriptional corepressor and inhibits signaling through all PPAR isoforms.

Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet.

Three novel mutations at serine 314 in the thyroid hormone beta receptor differentially impair ligand binding in the syndrome of resistance to thyroid hormone.