Literature DB >> 8605622

Comparison of two different DNA-binding modes of the NF-kappa B p50 homodimer.

C W Müller, F A Rey, S C Harrison.   

Abstract

Analysis of the NF-kappa B p50 homodimer bound to different DNA sequences shows that the protein can recognize half-site spacings of either three or four base pairs. The protein can maintain most of its DNA contacts by a relative reorientation of its two domains.

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Year:  1996        PMID： 8605622     DOI： 10.1038/nsb0396-224

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN： 1072-8368


  4 in total

Review 1.  A structural guide to proteins of the NF-kappaB signaling module.

Authors:  Tom Huxford; Gourisankar Ghosh
Journal:  Cold Spring Harb Perspect Biol       Date:  2009-09       Impact factor: 10.005

2.  Oxidative stress and inflammation modulate Rev-erbα signaling in the neonatal lung and affect circadian rhythmicity.

Authors:  Guang Yang; Clyde J Wright; Maurice D Hinson; Amal P Fernando; Shaon Sengupta; Chhanda Biswas; Ping La; Phyllis A Dennery
Journal:  Antioxid Redox Signal       Date:  2014-03-14       Impact factor: 8.401

3.  Structure of the human NF-kappaB p52 homodimer-DNA complex at 2.1 A resolution.

Authors:  P Cramer; C J Larson; G L Verdine; C W Müller
Journal:  EMBO J       Date:  1997-12-01       Impact factor: 11.598

4.  Nuclear factor kappa B activation in human cord blood mononuclear cells.

Authors:  Christian H Schroeter; Bianca Schaub; Diane R Gold; Paola J Contreras; Oscar Manrique; Matthew W Gillman; Scott Weiss; Lyle J Palmer; David Perkins; Patricia W Finn
Journal:  Pediatr Res       Date:  2004-06-04       Impact factor: 3.756
  4 in total

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