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Disorder-function relationships for the cell cycle regulatory proteins p21 and p27

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Published/Copyright: April 1, 2012
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Biological Chemistry
From the journal Volume 393 Issue 4

Received: 2011-11-8
Accepted: 2011-12-21
Published Online: 2012-04-01
Published in Print: 2012-04-01

©2012 by Walter de Gruyter Berlin Boston

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  1. Editorial
  2. Highlight: GBM Meeting ‘Molecular Life Sciences 2011’
  3. Highlight: GBM Meeting ‘Molecular Life Sciences 2011’
  4. Structural models of the human copper P-type ATPases ATP7A and ATP7B
  5. The proteasome: molecular machinery and pathophysiological roles
  6. At the cutting edge: applications and perspectives of laser nanosurgery in cell biology
  7. N-glycoproteomics: mass spectrometry-based glycosylation site annotation
  8. Disorder-function relationships for the cell cycle regulatory proteins p21 and p27
  9. Regional susceptibilities to mitochondrial dysfunctions in the CNS
  10. Molecular mechanisms of glycine transporter GlyT2 mutations in startle disease
  11. N-terminal acetylation and other functions of Nα-acetyltransferases
  12. Masthead
  13. Masthead
https://doi.org/10.1515/hsz-2011-0254
Keywords for this article
cell cycle regulator; disorder-function; intrinsically disordered proteins; p21; p27; signaling conduit

Articles in the same Issue

  1. Editorial
  2. Highlight: GBM Meeting ‘Molecular Life Sciences 2011’
  3. Highlight: GBM Meeting ‘Molecular Life Sciences 2011’
  4. Structural models of the human copper P-type ATPases ATP7A and ATP7B
  5. The proteasome: molecular machinery and pathophysiological roles
  6. At the cutting edge: applications and perspectives of laser nanosurgery in cell biology
  7. N-glycoproteomics: mass spectrometry-based glycosylation site annotation
  8. Disorder-function relationships for the cell cycle regulatory proteins p21 and p27
  9. Regional susceptibilities to mitochondrial dysfunctions in the CNS
  10. Molecular mechanisms of glycine transporter GlyT2 mutations in startle disease
  11. N-terminal acetylation and other functions of Nα-acetyltransferases
  12. Masthead
  13. Masthead
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