Results 11 to 20 of about 224 (106)

Dynamic networks connect the USP14 active site region with the proteasome interaction surface. [PDF]

open access: yesProtein Sci
Abstract Ubiquitin‐specific protease 14 (USP14) is a member of the USP family responsible for the catalytic removal of ubiquitin (Ub) from proteins directed to the proteasome, implicated in the pathogenesis of neurodegeneration and cancer. Crystallography and cryo‐EM analysis have identified loop regions crucial for the deubiquitinase activity of USP14,
Salomonsson J   +6 more
europepmc   +2 more sources

A Linear Diubiquitin-Based Probe for Efficient and Selective Detection of the Deubiquitinating Enzyme OTULIN.

open access: yesCell Chem Biol, 2017
The methionine 1 (M1)-specific deubiquitinase (DUB) OTULIN acts as a negative regulator of nuclear factor κB signaling and immune homeostasis. By replacing Gly76 in distal ubiquitin (Ub) by dehydroalanine we designed the diubiquitin (diUb) activity-
Weber A   +7 more
europepmc   +2 more sources

Cezanne (OTUD7B) regulates HIF-1α homeostasis in a proteasome-independent manner [PDF]

open access: yes, 2014
The transcription factor HIF-1α is essential for cells to rapidly adapt to low oxygen levels (hypoxia). HIF-1α is frequently deregulated in cancer and correlates with poor patient prognosis.
Anja Bremm   +9 more
core   +1 more source

Screening of DUB activity and specificity by MALDI-TOF mass spectrometry [PDF]

open access: yes, 2014
Deubiquitylases (DUBs) are key regulators of the ubiquitin system which cleave ubiquitin moieties from proteins and polyubiquitin chains. Several DUBs have been implicated in various diseases and are attractive drug targets. We have developed a sensitive
Virdee, Satpal; id_orcid   +15 more
core   +1 more source

Cocrystallization of ubiquitin–deubiquitinase complexes through disulfide linkage

open access: yesActa Crystallographica Section D, Volume 79, Issue 11, Page 1044-1055, November 2023., 2023
The crystal structures of two disulfide‐linked ubiquitin‐bound bacterial deubiquitinases reveal the mode of ubiquitin binding. These structures show that disulfide linking is an effective strategy for capturing covalent ubiquitin–deubiquitinase complex structures.Structural characterization of the recognition of ubiquitin (Ub) by deubiquitinases (DUBs)
Kristos I. Negron Teron   +1 more
wiley   +1 more source

14-3-3 Proteins Interact with a Hybrid Prenyl-Phosphorylation Motif to Inhibit G Proteins [PDF]

open access: yes, 2013
Signaling through G proteins normally involves conformational switching between GTP- and GDP-bound states. Several Rho GTPases are also regulated by RhoGDI binding and sequestering in the cytosol.
Riou, P   +62 more
core   +1 more source

Polyubiquitin binding to ABIN1 is required to prevent autoimmunity [PDF]

open access: yes, 2011
The protein ABIN1 possesses a polyubiquitin-binding domain homologous to that present in nuclear factor kappa B (NF-kappa B) essential modulator (NEMO), a component of the inhibitor of NF-kappa B (I kappa B) kinase (IKK) complex.
Ordureau, Alban   +23 more
core   +1 more source

Molecular basis of Lys11-polyubiquitin specificity in the deubiquitinase Cezanne [PDF]

open access: yes, 2016
The post-translational modification of proteins with polyubiquitin regulates virtually all aspects of cell biology. Eight distinct chain linkage types co-exist in polyubiquitin and are independently regulated in cells. This â - ubiquitin code' determines
Monique P.C. Mulder   +44 more
core   +1 more source

Host protein phosphorylation during "Shigella flexneri" infection : a phosphoproteomic based systems biology approach [PDF]

open access: yes, 2015
The enteroinvasive bacterium Shigella flexneri triggers its uptake into epithelial cells by injecting several effector proteins via its type three secretion system (TTSS) and interferes with various host cell processes at later stages of infection.
Schmutz, Christoph
core   +1 more source

Mechanistic studies of the phenobarbital-type induction of cytochromes P450 : role of AMP-activated protein kinase [PDF]

open access: yes, 2007
Inside the liver cells there are sophisticated mechanisms that have evolved over millions of years to metabolize toxic substances, many of which are fat-soluble compounds making them difficult for the body to excrete.
Blättler, Sharon
core   +1 more source

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