Molecular processes

Articles

• RNA editing
  14 April 2004

  Definition: The most prevalent type of RNA editing is mediated by ADAR (adenosine deaminase acting on RNA) enzymes, which convert adenosines to inosines (a process known as A—>I RNA editing) in double-stranded (ds)RNA substrates.
  A—>I RNA editing was long thought to affect only selected transcripts by altering the proteins they encode. However, genome-wide screening has revealed numerous editing sites within inverted Alu repeats in introns and untranslated regions.
  A—>I RNA editing (...)

• protein carbonylation
  14 April 2004

  See also
  carbonyl group
  References
  Dalle-Donne I, Giustarini D, Colombo R, Rossi R, Milzani A. Protein carbonylation in human diseases. Trends Mol Med. 2003 Apr;9(4):169-76. PMID: #12727143#

• prenylation
  14 April 2004

  protein farnesylation, farnesylation WKP
  Definition: Prenylation consists of the addition of an isoprenoid group to a cysteine residue located near the carboxyl terminal of a protein, or the addition of hydrophobic molecules to a protein or chemical compound.
  It is usually assumed that prenyl groups (3-methyl-but-2-en-1-yl) facilitate attachment to cell membranes, similar to lipid anchors like the GPI anchor, though direct evidence is missing.
  Prenyl groups have been shown to be (...)

• exonic skipping
  14 April 2004

  exon skipping

• extracellular proteolysis
  14 April 2004

  References
  Madani R, Nef S, Vassalli JD. Emotions are building up in the field of extracellular proteolysis. Trends Mol Med. 2003 May;9(5):183-5. PMID: #12763521#

• S-nitrosylation
  14 April 2004

  S-nitrosylation is a ubiquitous redox-related modification of cysteine thiol by nitric oxide (NO), which transduces NO bioactivity. Accumulating evidence suggests that the products of S-nitrosylation, S-nitrosothiols (SNOs), play key roles in human health and disease.
  Feature
  nitric oxide metabolism
  References
  Foster MW, McMahon TJ, Stamler JS. S-nitrosylation in health and disease. Trends Mol Med. 2003 Apr;9(4):160-8. PMID: (...)

• protein glycosylation
  27 January 2005

  proteic glyscosylation

• mutation mechanisms
  26 May 2004

  Exemples
  splice site mutation and exon skipping
  LINE insertion
  retroviral insertion

• protein aggregation
  7 March 2004

  protein aggregates

• unfolded protein response
  14 January 2006

  UPR, unfolded-protein response
  The endoplasmic reticulum (ER) responds to the accumulation of unfolded proteins in its lumen (ER stress) by activating intracellular signal transduction pathways, cumulatively called the unfolded protein response (UPR).
  Together, at least three mechanistically distinct arms of the UPR regulate the expression of numerous genes that function within the secretory pathway but also affect broad aspects of cell fate and the metabolism of proteins, amino acids and (...)

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