Results 91 to 100 of about 3,429,300 (308)

Mechanisms and therapeutic opportunities of the ribotoxic stress response in cancer

Molecular Oncology, EarlyView.
Cancer cells' high translational demand creates opportunities to therapeutically target ribosome function. Ribosome stalling and collisions activate ZAKα and the ribotoxic stress response (RSR), which can trigger rapid, p53‐independent apoptosis in cancer.
Anastassiya Kim, Maryam Aslam, Elouise Torruella, Alphons Sony, Asif Rahman, Simira Smith, Columba de la Parra, Moira Sauane   +7 more
wiley   +1 more source

Immune regulation by protein ubiquitination: roles of the E3 ligases VHL and Itch

Protein & Cell, 2018
Protein ubiquitination is an important means of post-translational modification which plays an essential role in the regulation of various aspects of leukocyte development and function.
Daisuke Aki, Qian Li, Hui Li, Yun-Cai Liu, Jee Ho Lee   +4 more
doaj   +1 more source

Distinct ubiquitin binding modes exhibited by SH3 domains: Molecular determinants and functional implications [PDF]

, 2013
SH3 domains constitute a new type of ubiquitin-binding domains. We previously showed that the third SH3 domain (SH3-C) of CD2AP binds ubiquitin in an alternative orientation.
Jerónimo Bravo (22727), Jose L Ortega Roldan, Jerónimo Bravo, Ana I. Azuaga, Casares Atienza, Salvador, Ringkjøbing Jensen, M, van Nuland, Nico A. J., Azuaga, AI, Malene Ringkjøbing Jensen, Buday, Laszlo, Azuaga, Ana I., Ortega Roldan, Jose L., Martin Blackledge, van Nuland, Nico a J, Martin Blackledge (204261), Cárdenes, N, Nuland, Nico A. J. van, Blackledge, M, Ringkjøbing Jensen, Malene, Azuaga, Ana I, Casares, S, Salvador Casares (69741), Jensen, Malene Ringkjøbing, Ortega-Roldán, José Luis, Casares, Salvador, Nico A. J. van Nuland (116707), Bravo, J, Ortega Roldan, Jose L, Van Nuland, NAJ, Bravo, Jerónimo, Jose L. Ortega Roldan (457421), Azuaga Fortes, Ana Isabel, Ana I. Azuaga (121437), Ortega-Roldan, Jose L., Nico A J van Nuland, Jose L. Ortega Roldan, Malene Ringkjøbing Jensen (204257), Nayra Cárdenes (457422), Cárdenes, Nayra, Nico A. J. Van Nul, Ana I Azuaga, Salvador Casares, Ortega Roldan, JL, Nayra Cárdenes, Blackledge, Martin   +44 more
core   +1 more source

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

Molecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad, Silvio Carlo Ermanno Tosatto, Emanuela Leonardi   +2 more
wiley   +1 more source

Trim17, novel E3 ubiquitin-ligase, initiates neuronal apoptosis [PDF]

, 2010
Accumulating data indicate that the ubiquitin-proteasome system controls apoptosis by regulating the level and the function of key regulatory proteins. In this study, we identified Trim17, a member of the TRIM/RBCC protein family, as one of the critical ...
Rahmeh, R, Magiera, M, Ham, Jonathan, M Kristiansen, Kristiansen, Mark, Ham, J, Desagher, Solange, Lipkin, A, Desagher, S., Rahmeh, Rita, Mora, Stéphan, M M Magiera, Vanhille, Laurent, Pettmann, B, Lipkin, Alexey, Mora, S, Lipkin, A., Kristiansen, M, Robbins, Ian, S Mora, Ham, J., R Rahmeh, Rahmeh, R., A Lipkin, Pettmann, Brigitte, Robbins, I., Mora, S., Lassot, I., Desagher, S, Lassot, I, Magiera, Maria Magdalena, Magiera, M. M., L Vanhille, Jaudon, F, I Lassot, Vanhille, L., Jaudon, F., S Desagher, Jaudon, Fanny, Lassot, Irina, Kristiansen, M., F Jaudon, Pettmann, B., Vanhille, L, Robbins, I, J Ham, I Robbins, B Pettmann   +47 more
core   +1 more source

Loss of AMBRA1 activates MAPK and angiogenesis signaling pathways in melanoma cells

FEBS Open Bio, EarlyView.
Loss of AMBRA1 in melanoma cells activates multiple oncogenic pathways associated with tumor progression. Transcriptomic and protein network analyses revealed that AMBRA1 depletion enhances MAPK/ERK signaling, angiogenesis, TGF‐β/EMT signaling, and Wnt/axon guidance pathways.
Milad Ibrahim, Marco Corazzari, Iman Osman, Jane Armstrong, Noel Carter   +4 more
wiley   +1 more source

Regulation of human papillomavirus E6 oncoprotein function via a novel ubiquitin ligase FBXO4

mBio
Previous studies have shown that E6 interacts with the E6-associated protein (E6AP) ubiquitin-protein ligase and directs its ubiquitylation activity toward several specific cellular proteins, one of the most important of which is p53. Interestingly, E6AP
Arushi Vats, Luca Braga, Nezka Kavcic, Paola Massimi, Edoardo Schneider, Mauro Giacca, Laimonis A. Laimins, Lawrence Banks   +7 more
doaj   +1 more source

Effects of IGFBP4 deficiency on human preadipocyte proliferation and differentiation through the IGF1R/AKT pathway

FEBS Open Bio, EarlyView.
IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo, Sandy Richter, Christoph Bach, Wieland Kiess, Anna Kirstein, Diana Le Duc, Antje Garten   +6 more
wiley   +1 more source

The APC/C Ubiquitin Ligase: from Cell Biology to Tumorigenesis

Frontiers in Oncology, 2012
The ubiquitin proteasome system (UPS) is required for normal cell proliferation, vertebrate development, and cancer cell transformation. The UPS consists of multiple proteins that work in concert to target a protein for degradation via the 26S proteasome.
Clara ePenas, Vimal eRamachandran, Nagi George Ayad   +2 more
doaj   +1 more source

Crystal structure of UBA2ufd-Ubc9: insights into E1-E2 interactions in sumo pathways [PDF]

, 2010
Canonical ubiquitin-like proteins (UBLs) such as ubiquitin, Sumo, NEDD8, and ISG15 are ligated to targets by E1-E2-E3 multienzyme cascades. The Sumo cascade, conserved among all eukaryotes, regulates numerous biological processes including protein ...
Miller, D.J., Asad M Taherbhoy, Schulman, B.A., Darcie J Miller, Steven N Seyedin, Huang Danny T., Wang, J., Kobe, B., Steven N. Seyedin, Seyedin Steven N., David W. Miller, Miller David W., Darcie J. Miller, Hunt Harold W., Miller, D.W., Taherbhoy, A.M., Danny T. Huang, Brenda A. Schulman, Miller Darcie J., Danny T Huang, Wang Jing, Harold W. Hunt, Harold W Hunt, Asad M. Taherbhoy, Schulman Brenda A., Jing Wang, Huang, D.T., Taherbhoy Asad M., David W Miller, Hunt, H.W., Seyedin, S.N., Brenda A Schulman   +31 more
core   +2 more sources