Results 41 to 50 of about 27,627 (205)
E3 ubiquitin ligases: styles, structures and functions
Molecular Biomedicine, 2021 E3 ubiquitin ligases are a large family of enzymes that join in a three-enzyme ubiquitination cascade together with ubiquitin activating enzyme E1 and ubiquitin conjugating enzyme E2.
Quan Yang +3 more
doaj +1 more source
Huntingtin Is Ubiquitinated and Interacts with a Specific Ubiquitin-conjugating Enzyme [PDF]
Journal of Biological Chemistry, 1996 Using the yeast two-hybrid system, we have identified a human ubiquitin-conjugating enzyme (hE2-25K) as a protein that interacts with the gene product for Huntington disease (HD) (Huntingtin). This protein has complete amino acid identity with the bovine E2-25K protein and has striking similarity to the UBC-1, -4 and -5 enzymes of Saccharomyces ...
Gang Xia +9 more
openaire +2 more sources
Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation. [PDF]
PLoS ONE, 2015 The ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) directly targets its substrates for proteasomal degradation by becoming covalently attached via its C-terminal diglycine motif to internal lysine residues of its substrate proteins.
Johanna Bialas +2 more
doaj +1 more source
A Subset of Ubiquitin-Conjugating Enzymes Is Essential for Plant Immunity [PDF]
Plant Physiology, 2016 Of the three classes of enzymes involved in ubiquitination, ubiquitin-conjugating enzymes (E2) have been often incorrectly considered to play merely an auxiliary role in the process, and few E2 enzymes have been investigated in plants. To reveal the role of E2 in plant innate immunity, we identified and cloned 40 tomato genes encoding ubiquitin E2 ...
Lirong Zeng +9 more
openaire +3 more sources
Sequence of a Cloned Tomato Ubiquitin Conjugating Enzyme
Plant Physiology, 1993 Ubiquitin is a small, abundant protein that is seemingly present in a11 eukaryotic cells and that is covalently ligated to specific protein substrates via an ATP-dependent reaction. This ubiquitinous has been demonstrated to target proteins for subsequent cellular degradation.
Sarah Louise Barton +4 more
openaire +4 more sources
Direct Single Molecule Imaging of Enhanced Enzyme Diffusion [PDF]
Phys. Rev. Lett. 123, 128101 (2019), 2018 Recent experimental results have shown that active enzymes can diffuse faster when they are in the presence of their substrates. Fluorescence correlation spectroscopy (FCS), which relies on analyzing the fluctuations in fluorescence intensity signal to measure the diffusion coefficient of particles, has typically been employed in most of the prior ...
arxiv +1 more source
Master curve of boosted diffusion for ten catalytic enzymes [PDF]
, 2020 Molecular agitation more rapid than thermal Brownian motion is reported for cellular environments, motor proteins, synthetic molecular motors, enzymes, and common chemical reactions, yet that chemical activity couples to molecular motion contrasts with generations of accumulated knowledge about diffusion at equilibrium. To test the limits of this idea,
arxiv +1 more source
SUMO modification of the ubiquitin-conjugating enzyme E2-25K
Nature Structural & Molecular Biology, 2005 Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2).
Edith Oberhofer +10 more
openaire +5 more sources
The protein cost of metabolic fluxes: prediction from enzymatic rate laws and cost minimization [PDF]
, 2016 Bacterial growth depends crucially on metabolic fluxes, which are limited by the cell's capacity to maintain metabolic enzymes. The necessary enzyme amount per unit flux is a major determinant of metabolic strategies both in evolution and bioengineering.
arxiv +1 more source
Enzyme-enriched condensates show self-propulsion, positioning, and coexistence [PDF]
, 2023 Enzyme-enriched condensates can organize the spatial distribution of their substrates by catalyzing non-equilibrium reactions. Conversely, an inhomogeneous substrate distribution induces enzyme fluxes through substrate-enzyme interactions. We find that condensates move towards the center of a confining domain when this feedback is weak.
arxiv +1 more source