Results 21 to 30 of about 39,918 (341)

UBE2C (ubiquitin-conjugating enzyme E2C) [PDF]

open access: yesAtlas of Genetics and Cytogenetics in Oncology and Haematology, 2011
Review on UBE2C (ubiquitin-conjugating enzyme E2C), with data on DNA, on the protein encoded, and where the gene is implicated.
Pallate, P, Berlingieri, MT, Fusco, A
openaire   +2 more sources

NEDD8-conjugating enzyme E2s: critical targets for cancer therapy

open access: yesCell Death Discovery, 2023
NEDD8-conjugating enzymes, E2s, include the well-studied ubiquitin-conjugating enzyme E2 M (UBE2M) and the poorly characterized ubiquitin-conjugating enzyme E2 F (UBE2F).
Lisha Zhou   +7 more
doaj   +1 more source

In vitro Di-ubiquitin Formation Assay and E3 Cooperation Assay

open access: yesBio-Protocol, 2022
Ubiquitination is a post-translational modification conserved across eukaryotic species. It contributes to a variety of regulatory pathways, including proteasomal degradation, DNA repair, and cellular differentiation.
Rebecca Burge   +3 more
doaj   +1 more source

Characterization of a Dominant Negative Mutant of the Cell Cycle Ubiquitin-conjugating Enzyme Cdc34 [PDF]

open access: yes, 1995
The yeast Saccharomyces cerevisiae CDC34 gene encodes a ubiquitin-conjugating enzyme that is required for the cell cycle G(1)/S transition. We show here that a dominant negative Cdc34 protein is generated by simultaneously replacing both Cys and Leu with
Banerjee, Amit   +2 more
core   +2 more sources

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

open access: yes, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S.   +2 more
core   +1 more source

MALDI-TOF Mass Spectrometry for interrogating ubiquitin enzymes

open access: yesFrontiers in Molecular Biosciences, 2023
The attachment of ubiquitin to a substrate (ubiquitination or ubiquitylation) impacts its lifetime and regulates its function within the cell. Several classes of enzymes oversee the attachment of ubiquitin to the substrate: an E1 activating enzyme that ...
Virginia De Cesare
doaj   +1 more source

A Molecular Basis for Stabilization of the von Hippel-Lindau (VHL) Tumor Suppressor Protein by Components of the VHL Ubiquitin Ligase [PDF]

open access: yes, 2002
The multiprotein von Hippel-Lindau (VHL) tumor suppressor (CBCVHL, Cul2-Elongin BC-VHL) and SCF (Skp1-Cul1/Cdc53-F-box protein) complexes are members of structurally related families of E3 ubiquitin ligases that use a heterodimeric module composed of a ...
Brower, Christopher S.   +3 more
core   +2 more sources

The ubiquitin-proteasome pathway in Huntington's disease. [PDF]

open access: yes, 2008
The accumulation of mutant protein is a common feature of neurodegenerative disease. In Huntington's disease, a polyglutamine expansion in the huntingtin protein triggers neuronal toxicity.
Finkbeiner, Steven, Mitra, Siddhartha
core   +2 more sources

Solution Structure of the Ubiquitin-conjugating Enzyme UbcH5B [PDF]

open access: yesJournal of Molecular Biology, 2004
The ubiquitination pathway is the main pathway for protein degradation in eukaryotic cells. The attachment of ubiquitin to a substrate protein is catalyzed by three types of enzymes, namely a ubiquitin activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin ligase (E3). Here, the structure of the human ubiquitin-conjugating enzyme (
Houben, K   +5 more
openaire   +5 more sources

The ubiquitin-proteasome system is required for African swine fever replication. [PDF]

open access: yesPLoS ONE, 2017
Several viruses manipulate the ubiquitin-proteasome system (UPS) to initiate a productive infection. Determined viral proteins are able to change the host's ubiquitin machinery and some viruses even encode their own ubiquitinating or deubiquitinating ...
Lucía Barrado-Gil   +4 more
doaj   +1 more source

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