<div><p>(A) Structure of a HAUSP fragment (residues 53–560) that contains both the substrate-binding (green) and the catalytic domains. Binding sites for ubiquitin and substrate are indicated. The linker sequences between these two domains have high-temperature factors and are flexible in the crystals.</p> <p>(B) A structure-based model showing HAUSP bound to an ubiquitylated MDM2. Only one ubiquitin moiety and the MDM2 peptide are shown in this model.</p></div
Ubiquitin specific proteases (USPs) are a class of enzymes involved in myriad cellular processes. On...
<p>(<b>A</b>) A network of hydrogen bonding and hydrophobic interactions formed by the phosphorylate...
The TPM domain constitutes a family of recently characterized protein domains that are present in mo...
<div><p>(A) Overall structure of the HAUSP TRAF-like domain bound to MDM2 peptide is shown in a ribb...
<div><p>(A) The TRAF-like domain of HAUSP is responsible for binding to MDM2. Various HAUSP fragment...
<div><p>(A) MDM2 peptide (red) binds to the same surface groove as the p53 peptide (magenta). Residu...
AbstractThe ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an...
<div><p>(A) Structure of the HAUSP TRAF-like domain in a ribbon diagram (left) and a surface represe...
The ubiquitin-specific protease (USP) structural class represents the largest and most diverse famil...
<p>Both USP2 and USP14 accommodate ubiquitin (green) in a shallow groove, measuring approximately 25...
The ubiquitin-specific protease USP7/HAUSP regulates p53 and MDM2 levels, and cellular localization ...
<p>(A) The ΔhPus1p monomer is shown in a cartoon representation and coloured according to secondary ...
AbstractUSP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP...
AbstractThe mechanisms by which Hsp40 functions as a molecular chaperone to recognize and bind nonna...
<p>A/ HAMP3 wt and mutant peptides. In the last panel I365S (light grey) and I365S M427T (dark grey)...
Ubiquitin specific proteases (USPs) are a class of enzymes involved in myriad cellular processes. On...
<p>(<b>A</b>) A network of hydrogen bonding and hydrophobic interactions formed by the phosphorylate...
The TPM domain constitutes a family of recently characterized protein domains that are present in mo...
<div><p>(A) Overall structure of the HAUSP TRAF-like domain bound to MDM2 peptide is shown in a ribb...
<div><p>(A) The TRAF-like domain of HAUSP is responsible for binding to MDM2. Various HAUSP fragment...
<div><p>(A) MDM2 peptide (red) binds to the same surface groove as the p53 peptide (magenta). Residu...
AbstractThe ubiquitin-specific processing protease (UBP) family of deubiquitinating enzymes plays an...
<div><p>(A) Structure of the HAUSP TRAF-like domain in a ribbon diagram (left) and a surface represe...
The ubiquitin-specific protease (USP) structural class represents the largest and most diverse famil...
<p>Both USP2 and USP14 accommodate ubiquitin (green) in a shallow groove, measuring approximately 25...
The ubiquitin-specific protease USP7/HAUSP regulates p53 and MDM2 levels, and cellular localization ...
<p>(A) The ΔhPus1p monomer is shown in a cartoon representation and coloured according to secondary ...
AbstractUSP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP...
AbstractThe mechanisms by which Hsp40 functions as a molecular chaperone to recognize and bind nonna...
<p>A/ HAMP3 wt and mutant peptides. In the last panel I365S (light grey) and I365S M427T (dark grey)...
Ubiquitin specific proteases (USPs) are a class of enzymes involved in myriad cellular processes. On...
<p>(<b>A</b>) A network of hydrogen bonding and hydrophobic interactions formed by the phosphorylate...
The TPM domain constitutes a family of recently characterized protein domains that are present in mo...