Results 91 to 100 of about 223,344 (207)

Small ubiquitin-like modifier protein SUMO enables plants to control growth independently of the phytohormone gibberellin [PDF]

, 2014
Plants survive adverse conditions by modulating their growth in response to a changing environment. Gibberellins (GAs) play a key role in these adaptive responses by stimulating the degradation of growth-repressing DELLA proteins.
Bennett, M., Galbiati, Massimo, Hedden, Peter, Woodcock, A., S. Nelis, Hedden, P., A. Sadanandom, A. Woodcock, Woodcock, Ailidh, R. Swarup, Swarup, Ranjan, Tonelli, Chiara, Bennett, Malcolm J., Bennett, Malcolm, Zhang, Cunjin, C. Tonelli, Sadanandom, Ari, M. Galbiati, Nelis, S., Conti, L., L. Conti, Napier, Richard, Zhang, C., Conti, Lucio, Galbiati, M., Nelis, Stuart, R. Napier, P. Hedden, Sadanandom, A., C. Zhang, Napier, R., Swarup, R., M. Bennett, Tonelli, C.   +33 more
core   +1 more source

The research of AtDWD interacting with DDB1

四川大学学报. 自然科学版, 2017
Ubiquitin-proteasome pathway is a major pathway to regulate cell protein stability in eukaryotes including plants. E3 ubiquitin ligase in the ubiquitin- proteasome pathway is responsible for recruiting specific target proteins for ubiquitination.
WU Ye-Tian, LI De-Kuan, YANG Yi
doaj  

E3 ubiquitin ligase that recognizes sugar chains

Nature, 2002
N-glycosylation of proteins in the endoplasmic reticulum (ER) has a central role in protein quality control. Here we report that N-glycan serves as a signal for degradation by the Skp1-Cullin1-Fbx2-Roc1 (SCF(Fbx2)) ubiquitin ligase complex. The F-box protein Fbx2 (ref. 4) binds specifically to proteins attached to N-linked high-mannose oligosaccharides
Yukiko, Yoshida, Tomoki, Chiba, Fuminori, Tokunaga, Hiroshi, Kawasaki, Kazuhiro, Iwai, Toshiaki, Suzuki, Yukishige, Ito, Koji, Matsuoka, Minoru, Yoshida, Keiji, Tanaka, Tadashi, Tai   +10 more
openaire   +3 more sources

A Tobacco Homolog of DCN1 is Involved in Cellular Reprogramming and in Developmental Transitions [PDF]

, 2011
Plant proteomes show remarkable plasticity in reaction to environmental challenges and during developmental transitions. Some of this adaptability comes from ubiquitin-mediated protein destruction regulated by cullin-RING E3 ubiquitin ligases (CRLs ...
Alexandra Ribarits, Klaus Palme, Marina Baumann, Elisabeth Ankele, Katarzyna Szaszka, Viktor Voronin, Christina Friedmann, Julia Hosp, Alisher Touraev, Yongfeng Jin, Alisher Tashpulatov, Erwin Heberle-Bors, Tatiana Resch   +12 more
core  

Multiple C-terminal Lysine residues target p53 for ubiquitin-proteasome-mediated degradation [PDF]

, 2000
This work was supported by the Medical Research Council, the Biotechnology and Biological Research Council, and the Cancer Research Campaign. D.P.L. is a Gibb fellow of the Cancer Research Campaign.In normal cells, p53 is maintained at a low level by ...
Lain, Sonia, Lane, David P., T. Hay, Ronald, Hay, Ronald Thomas, Rodriguez, Manuel S, Desterro, Joana M P   +6 more
core   +1 more source

Prognostic implications of carboxyl-terminus of Hsc70 interacting protein and lysyl-oxidase expression in human breast cancer [PDF]

, 2010
This article has been made available through the Brunel Open Access Publishing Fund - Copyright @ 2010 Patani.Background: Ubiquitin modification of proteins influences cellular processes relevant to carcinogenesis.
Jiang, W, Newbold, R, Kefah Mokbel, Patani, Neill, Neill Patani, Mokbel, K, Robert Newbold, Jiang, Wen Guo, Newbold, Robert, Patani, N, Wen Jiang, Mokbel, Kefah   +11 more
core   +1 more source

The Human Adenovirus Type 5 E4orf6/E1B55K E3 Ubiquitin Ligase Complex Can Mimic E1A Effects on E2F

mSphere, 2016
The human adenovirus E4orf6/E1B55K E3 ubiquitin ligase is well known to promote viral replication by degrading an increasing number of cellular proteins that inhibit the efficient production of viral progeny.
Frédéric Dallaire, Sabrina Schreiner, G. Eric Blair, Thomas Dobner, Philip E. Branton, Paola Blanchette   +5 more
doaj   +1 more source

Optineurin negatively regulates the induction of IFNβ in response to RNA virus infection [PDF]

, 2010
The innate immune response provides a critical defense against microbial infections, including viruses. These are recognised by pattern recognition receptors including Toll-like receptors (TLRs) and RIG-I like helicases (RLHs).
Harris, M., Macdonald, A., Kohl, A., Richards, KH, Wetherill, L, Kohl, Alain, MacDonald, A, Mankouri, Jamel, Kohl, A, Elliott, Richard M., Elliott, RM, Alain Kohl, Wetherill, L.F., Rennos Fragkoudis, Harris Mark, Andrew Macdonald, Richards Kathryn H., Richards, K.H., Richards, K, Laura F Wetherill, Mankouri, J., Richards, Kathryn H., Mankouri, J, Jamel Mankouri, Elliott, R.M., Wetherill Laura F., Fragkoudis, R., Richard M Elliott, Macdonald, Andrew, Harris, M, Wetherill, Laura F., Kohl Alain, Elliott Richard M., Macdonald Andrew, Wetherill, LF, Elliott, Richard Michael, Mark Harris, Harris, Mark, Fragkoudis, R, Kathryn H Richards, Fragkoudis, Rennos, Mankouri Jamel, Fragkoudis Rennos   +42 more
core   +1 more source

Indirect ubiquitination independent of endogenous ubiquitination machinery for targeted protein degradation

Communications Chemistry
Heterobifunctional small degrader molecules that hijack endogenous E3 ubiquitin ligases have attracted attention for the rapid and irreversible knock-down of target proteins via ubiquitination.
Takafumi Furuhata, Kazuki Yoshida, Ryoka Fujita, Jotaro Miyamoto, Chiharu Moriyama, Tokiha Masuda-Ozawa, Hikaru Tsuchiya, Yasushi Saeki, Akimitsu Okamoto   +8 more
doaj   +1 more source

Structural visualization of HECT-type E3 ligase Ufd4 accepting and transferring ubiquitin to form K29/K48-branched polyubiquitination

Nature Communications
The K29/K48-linked ubiquitination generated by the cooperative catalysis of E3 ligase Ufd4 and Ubr1 is an enhanced protein degradation signal, in which Ufd4 is responsible for introducing K29-linked ubiquitination to K48-linked ubiquitin chains to ...
Xiangwei Wu, Huasong Ai, Junxiong Mao, Hongyi Cai, Lu-Jun Liang, Zebin Tong, Zhiheng Deng, Qingyun Zheng, Lei Liu, Man Pan   +9 more
doaj   +1 more source