Speed
40 days from acceptance to publication
Citation Impact
1.80 - Cite Score
0.304 - Source Normalized Impact per Paper (SNIP)
0.347 - SCImago Journal Rank (SJR)
Usage
468,191 downloads
53 Altmetric mentions
Volume 3 Supplement 6
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
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...
Citation: BMC Proceedings 2009 3(Suppl 6):S1
We have introduced a consistent nomenclature for the various subunits of the NatA-NatE N-terminal acetyltransferases from yeast, humans and other eukaryotes.
Citation: BMC Proceedings 2009 3(Suppl 6):S2
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...
Citation: BMC Proceedings 2009 3(Suppl 6):S3
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 ...
Citation: BMC Proceedings 2009 3(Suppl 6):S4
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...
Citation: BMC Proceedings 2009 3(Suppl 6):S5
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 ...
Citation: BMC Proceedings 2009 3(Suppl 6):S6
Speed
40 days from acceptance to publication
Citation Impact
1.80 - Cite Score
0.304 - Source Normalized Impact per Paper (SNIP)
0.347 - SCImago Journal Rank (SJR)
Usage
468,191 downloads
53 Altmetric mentions