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Volume 3 Supplement 6

Proceedings of the 2007 and 2008 Symposia on Protein N-terminal Acetylation


Edited by Thomas Arnesen

NAT 2007 and 2008 Symposia: Protein N-terminal Acetylation and Protein N-terminal Acetyltransferases (NATs).

Bergen, Norway24-25 May 2007 and 11-13 September 2008

  1. Protein N-terminal acetylation is a very common modification, but has during the past decades received relatively little attention. In order to put this neglected field back on the scientific map, we have in M...

    Authors: Thomas Arnesen
    Citation: BMC Proceedings 2009 3(Suppl 6):S1
  2. Protein Nα-terminal acetylation is one of the most common protein modifications in eukaryotic cells, occurring on approximately 80% of soluble human proteins. An increasing number of studies links Nα-terminal ace...

    Authors: Kristian K Starheim, Darina Gromyko, Rolf Velde, Jan Erik Varhaug and Thomas Arnesen
    Citation: BMC Proceedings 2009 3(Suppl 6):S3
  3. Human Nα-acetyltransferase complex B (hNatB) is integrated by hNaa20p (hNAT5/hNAT3) and hNaa25p (hMDM20) proteins. Previous data have shown that this enzymatic complex is implicated in cell cycle progression and ...

    Authors: Amagoia Ametzazurra, Cristina Gázquez, Marta Lasa, Esther Larrea, Jesús Prieto and Rafael Aldabe
    Citation: BMC Proceedings 2009 3(Suppl 6):S4
  4. Protein acetylation is a common modification that plays a central role in several cellular processes. The most widely used methods to study these modifications are either based on the detection of radioactivel...

    Authors: Rune Evjenth, Kristine Hole, Mathias Ziegler and Johan R Lillehaug
    Citation: BMC Proceedings 2009 3(Suppl 6):S5
  5. Acetylation of nascent protein Nα-termini is a common modification among archae and eukaryotes and can influence the structure and function of target proteins. This modification has been studied on an individual ...

    Authors: Petra Van Damme, Jozef Van Damme, Hans Demol, An Staes, Joël Vandekerckhove and Kris Gevaert
    Citation: BMC Proceedings 2009 3(Suppl 6):S6

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    0.790 - SCImago Journal Rank (SJR)

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