Results 71 to 80 of about 33,702 (335)

Structure and Ubiquitin Binding of the Ubiquitin-interacting Motif [PDF]

Journal of Biological Chemistry, 2003
Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules.
Daniel S. Higginson, Steven L. Alam, Christopher P. Hill, Bin Wang, Howard Robinson, Wesley I. Sundquist, Robert D. Fisher   +6 more
openaire   +3 more sources

A cellular system to study responses to a collision between the transcription complex and a protein‐bound nick in the DNA template

FEBS Letters, EarlyView.
We present the cellular transcription‐coupled Flp‐nick system allowing the introduction of a Top1‐mimicking cleavage complex (Flpcc) at a Flp recognition target site within a controllable LacZ gene. LacZ transcription leads to the collision of RNA polymerase II (RNAPII) with Flpcc, and this causes RNAPII stalling, ubiquitination, and degradation.
Petra Herring, Morten Roedgaard, Camilla Myrup Holst, Helene Christensen, Birgitta R. Knudsen, Lotte Bjergbaek, Anni Hangaard Andersen   +6 more
wiley   +1 more source

Protein folding in a force-clamp [PDF]

, 2006
Kinetics of folding of a protein held in a force-clamp are compared to an unconstrained folding. The comparison is made within a simple topology-based dynamical model of ubiquitin. We demonstrate that the experimentally observed variations in the end-to-end distance reflect microscopic events during folding. However, the folding scenarios in and out of
arxiv   +1 more source

Autophagy in cancer and protein conformational disorders

FEBS Letters, EarlyView.
Autophagy plays a crucial role in numerous biological processes, including protein and organelle quality control, development, immunity, and metabolism. Hence, dysregulation or mutations in autophagy‐related genes have been implicated in a wide range of human diseases.
Sergio Attanasio
wiley   +1 more source

Influence of Hydrodynamic Interactions on Mechanical Unfolding of Proteins [PDF]

, 2007
We incorporate hydrodynamic interactions in a structure-based model of ubiquitin and demonstrate that the hydrodynamic coupling may reduce the peak force when stretching the protein at constant speed, especially at larger speeds. Hydrodynamic interactions are also shown to facilitate unfolding at constant force and inhibit stretching by fluid flows.
arxiv   +1 more source

Protein unfolding and refolding as transitions through virtual states [PDF]

EPL, 108 (2014) 28002, 2014
Single-molecule atomic force spectroscopy probes elastic properties of titin, ubiquitin and other relevant proteins. We explain bioprotein folding dynamics under both length- and force-clamp by modeling polyprotein modules as particles in a bistable potential, weakly connected by harmonic spring linkers.
arxiv   +1 more source

Ubiquitin in the immune system [PDF]

EMBO reports, 2013
Ubiquitination is a post-translational modification process that has been implicated in the regulation of innate and adaptive immune responses. There is increasing evidence that both ubiquitination and its reversal, deubiquitination, play crucial roles not only during the development of the immune system but also in the orchestration of an immune ...
Zinngrebe Julia, Montinaro Antonella, Peltzer Nieves, Walczak Henning   +3 more
openaire   +5 more sources

Stochastic variation in the FOXM1 transcription program mediates replication stress tolerance

Molecular Oncology, EarlyView.
Cellular heterogeneity is a major cause of drug resistance in cancer. Segeren et al. used single‐cell transcriptomics to investigate gene expression events that correlate with sensitivity to the DNA‐damaging drugs gemcitabine and prexasertib. They show that dampened expression of transcription factor FOXM1 and its target genes protected cells against ...
Hendrika A. Segeren, Kathryn A. Wierenga, Frank M. Riemers, Elsbeth A. van Liere, Bart Westendorp   +4 more
wiley   +1 more source

Optineurin functions for optimal immunity [PDF]

, 2018
Optineurin (OPTN) was identified 20 years ago in a yeast-two-hybrid screen with a viral protein known to inhibit the cytolytic effects of tumor necrosis factor.
Slowicka, Karolina, van Loo, Geert
core   +1 more source

Chemical Synthesis of Ubiquitin, Ubiquitin‐Based Probes, and Diubiquitin [PDF]

Angewandte Chemie International Edition, 2010
Post-translational modification of proteins with ubiquitin (Ub) and Ub chains controls protein breakdown by the proteasome, cellular localization of proteins, transcriptional activity, and DNA repair.[1] Ubiquitin is a highly conserved 76 amino acid protein that can be linked to target proteins through an isopeptide bond between the C-terminal ...
Farid El Oualid, Remco Merkx, Reggy Ekkebus, Dharjath S. Hameed, Judith J. Smit, Annemieke de Jong, Henk Hilkmann, Titia K. Sixma, Huib Ovaa   +8 more
openaire   +4 more sources