<p><b>A.</b> Sequence alignment of human UbcH6 (UBE2E1) and UbcH8 (UBE2E2). Secondary structures and E3-interface regions (H1, L1 and L2) are indicated. Arrows indicate E2-specific residues; asterisks indicate conserved residues involved in bridging. N-terminal extensions are indicated as shaded. <b>B.</b> E3-interaction profiles of <i>wt</i> UbcH6, UbcH8 and UbcH8 D113E (see <a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1002754#s4" target="_blank">Materials and Methods</a> section for details).</p
<p>Fully- and partially-conserved residues are in red and yellow, respectively. The secondary struct...
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cas...
AbstractUbcH2 encodes a human ubiquitin conjugating enzyme (E2) able to conjugate ubiquitin to histo...
Highly selective interactions between ubiquitin-conjugating enzymes and RING-type E3 ligases are cru...
Ubiquitin-mediated proteolysis utilizes a series of three key enzymes (E1, E2, and E3) to transfer a...
Thesis (Master's)--University of Washington, 2019The human proteome contains over forty ubiquitin-co...
Protein ubiquitination is a post-translational modification that controls essential biological proce...
<p><b>A</b>) The 3D structure of the E2 UBC domain is shown, along with the conserved residues in th...
<p>(<b>A</b>) Sequence alignment of full length human EB1 (accession number AAC09471) and EB3 (acces...
Ubiquitination is crucial for many cellular processes such as protein degradation, DNA repair, trans...
SummaryThe combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essentia...
Protein modification by ubiquitin conjugation (ubiquitination) is responsible for degradation of mos...
In a recent issue of Molecular Cell, Das et al. (2009) show that the G2BR domain of gp78, a RING-fam...
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for u...
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for u...
<p>Fully- and partially-conserved residues are in red and yellow, respectively. The secondary struct...
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cas...
AbstractUbcH2 encodes a human ubiquitin conjugating enzyme (E2) able to conjugate ubiquitin to histo...
Highly selective interactions between ubiquitin-conjugating enzymes and RING-type E3 ligases are cru...
Ubiquitin-mediated proteolysis utilizes a series of three key enzymes (E1, E2, and E3) to transfer a...
Thesis (Master's)--University of Washington, 2019The human proteome contains over forty ubiquitin-co...
Protein ubiquitination is a post-translational modification that controls essential biological proce...
<p><b>A</b>) The 3D structure of the E2 UBC domain is shown, along with the conserved residues in th...
<p>(<b>A</b>) Sequence alignment of full length human EB1 (accession number AAC09471) and EB3 (acces...
Ubiquitination is crucial for many cellular processes such as protein degradation, DNA repair, trans...
SummaryThe combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essentia...
Protein modification by ubiquitin conjugation (ubiquitination) is responsible for degradation of mos...
In a recent issue of Molecular Cell, Das et al. (2009) show that the G2BR domain of gp78, a RING-fam...
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for u...
The combination of an E2 ubiquitin-conjugating enzyme with an E3 ubiquitin-ligase is essential for u...
<p>Fully- and partially-conserved residues are in red and yellow, respectively. The secondary struct...
Protein ubiquitination is a fundamental regulatory component in eukaryotic cell biology, where a cas...
AbstractUbcH2 encodes a human ubiquitin conjugating enzyme (E2) able to conjugate ubiquitin to histo...