<script type="text/javascript">
<!--
document.write('<div id="oa_widget"></div>');
document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=undefined&type=result"></script>');
-->
</script>
pmid: 12083003
Proteasomes are large, multisubunit proteases that are found, in one form or another, in all domains of life and play a critical role in intracellular protein degradation. Although they have substantial structural similarity, the proteasomes of bacteria, archaea, and eukaryotes show many differences in architecture and subunit composition. This article discusses possible paths by which proteasomes may have evolved from simple precursors to the highly complicated and diverse complexes observed today.
Adenosine Triphosphatases, Proteasome Endopeptidase Complex, Molecular Sequence Data, Cell Compartmentation, Evolution, Molecular, Cysteine Endopeptidases, Eukaryotic Cells, Prokaryotic Cells, Multienzyme Complexes, Endopeptidases, Animals, Humans, Amino Acid Sequence, Phylogeny
Adenosine Triphosphatases, Proteasome Endopeptidase Complex, Molecular Sequence Data, Cell Compartmentation, Evolution, Molecular, Cysteine Endopeptidases, Eukaryotic Cells, Prokaryotic Cells, Multienzyme Complexes, Endopeptidases, Animals, Humans, Amino Acid Sequence, Phylogeny
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 54 | |
popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 10% | |
influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 10% |