Structure of the negative regulatory domain of p53 bound to S100B(ββ)

No abstract is available for this paper.

• Publication year

  2000

• Venue

  Nature Structural Biology

• Publication date

  2000-07-01

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1038/76797PMID 10876243
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
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  1999cited by this paper
• A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.

  1998cited by this paper
• The Ca(2+)-dependent interaction of S100B(beta beta) with a peptide derived from p53.

  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
• S100B(ββ) inhibits the protein kinase C‐dependent phosphorylation of a peptide derived from p53 in a Ca2+‐dependent manner

  1998cited by this paper
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  1998cited by this paper
• A novel mode of target recognition suggested by the 2.0 A structure of holo S100B from bovine brain.

  1998cited by this paper
• Solution structure of calcium-bound rat S100B(betabeta) as determined by nuclear magnetic resonance spectroscopy,.

  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1998cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1997cited by this paper
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  1995cited by this paper
• Refined solution structure of the oligomerization domain of the tumour suppressor p53

  1995cited by this paper
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  1995cited by this paper
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  1995cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1994cited by this paper
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  1993cited by this paper
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  1992cited by this paper
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  1992cited by this paper
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  1988cited by this paper

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• The Yin and Yang of alarmin S100B in the protection of myocardium.

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• Studying the Structures of Relaxed and Fuzzy Interactions: The Diverse World of S100 Complexes

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• Intrinsically disordered protein regions at membrane contact sites.

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• An integrated view of p53 dynamics, function, and reactivation.

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• S100P Interacts with p53 while Pentamidine Inhibits This Interaction

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  2014cites this paper
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