Results 41 to 50 of about 49,812 (243)

Image_2_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.jpg [PDF]

, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331), Cristina Garcia-Barcena (8395278), Nerea Osinalde (2989329), Juanma Ramirez (812674)   +3 more
core   +1 more source

Structure-guided design and optimization of small molecules targeting the protein-protein interaction between the von hippel-lindau (VHL) E3 ubiquitin ligase and the hypoxia inducible factor (HIF) alpha subunit with in vitro nanomolar affinities [PDF]

, 2014
E3 ubiquitin ligases are attractive targets in the ubiquitin-proteasome system, however, the development of small-molecule ligands has been rewarded with limited success.
Dias, David M, Carles Galdeano (1305135), Galdeano, Carles, Dias, David M., David M. Dias (1340694), Van Molle, Inge, Gadd, Morgan Stuart, Ciulli, Alessio, Sarah Hewitt (1340700), Soares, Pedro, Galdeano , Carles, Pedro Soares (393566), Gadd, Morgan S., Salvatore Scaffidi (1340703), Inge Van Molle (1284120), Morgan S. Gadd (149371), Scaffidi, Salvatore, Ipek Birced (1340697), Alessio Ciulli (762789), Hewitt, Sarah, Birced, Ipek   +20 more
core   +1 more source

Ubiquitination, Biotech Startups, and the Future of TRIM Family Proteins: A TRIM-Endous Opportunity

Cells, 2021
Ubiquitination is a post-translational modification that has pivotal roles in protein degradation and diversified cellular processes, and for more than two decades it has been a subject of interest in the biotech or biopharmaceutical industry. Tripartite
Utsa Bhaduri, Giuseppe Merla
doaj   +1 more source

Image_1_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.jpg [PDF]

, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331), Cristina Garcia-Barcena (8395278), Nerea Osinalde (2989329), Juanma Ramirez (812674)   +3 more
core   +1 more source

MAGE-A cancer/testis antigens inhibit MDM2 ubiquitylation function and promote increased levels of MDM4 [PDF]

, 2015
Melanoma antigen A (MAGE-A) proteins comprise a structurally and biochemically similar sub-family of Cancer/Testis antigens that are expressed in many cancer types and are thought to contribute actively to malignancy.
Susan E. Bray (264528), Thompson, Alastair M., Hourihan John, Quinlan Philip R., Philip R. Quinlan (743773), Thompson Alastair M., Meek, David W., Alastair M. Thompson (743775), Meek, David W, Marcar Lynnette, Lee B. Jordan (743774), Ihrig Bianca, David W Meek, Ted R. Hupp (141798), Hupp Ted R., Ihrig, Bianca, Hourihan, John, Meek David W., Bray Susan E., Thompson, Alastair M, Quinlan, Philip R., Susan E Bray, Lynnette Marcar (743770), Hupp, Ted R., John Hourihan, Philip R Quinlan, Jordan, Lee B., Bray, Susan E, Ted R Hupp, Lynnette Marcar, Quinlan, Philip R, David W. Meek (743776), Jordan Lee B., Alastair M Thompson, Marcar, Lynnette, Bianca Ihrig, John Hourihan (743772), Hupp, Ted R, Bray, Susan E., Lee B Jordan, Bianca Ihrig (743771), Jordan, Lee B   +41 more
core   +1 more source

A capsid-encoded PPxY-motif facilitates adenovirus entry. [PDF]

, 2010
Viruses use cellular machinery to enter and infect cells. In this study we address the cell entry mechanisms of nonenveloped adenoviruses (Ads). We show that protein VI, an internal capsid protein, is rapidly exposed after cell surface attachment and ...
Segura-Morales, Carolina, Ruzsics, Zsolt, Kremer, Eric J, Wiethoff, Christopher M, Kremer Eric J., Baptist Jammart, Wodrich, Harald, Jammart, Baptist, Seelmeir Sigrid, Jammart Baptist, Christopher M Wiethoff, Wiethoff, Christopher M., Ruzsics Zsolt, Segura-Morales Carolina, Seelmeir, Sigrid, Carolina Segura-Morales, Henaff, Daniel, Zsolt Ruzsics, Kremer, Eric J., Coux, Olivier, Harald Wodrich, Henaff Daniel, Sigrid Seelmeir, Coux Olivier, Wodrich Harald, Eric J Kremer, Daniel Henaff, Olivier Coux, Wiethoff Christopher M.   +28 more
core   +1 more source

The Role of E3 Ubiquitin Ligases in Chloroplast Function [PDF]

, 2022
Chloroplasts are ancient organelles responsible for photosynthesis and various biosynthetic functions essential to most life on Earth. Many of these functions require tightly controlled regulatory processes to maintain homeostasis at the protein level ...
Hand, Katherine A,; Shabek, Nitzan,, Hand, Katherine A., Nitzan Shabek, Shabek, Nitzan, Katherine A. Hand, Hand, Katherine A   +5 more
core   +4 more sources

A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence [PDF]

, 2011
Intrinsic antiviral resistance represents the first line of intracellular defence against virus infection. During herpes simplex virus type-1 (HSV-1) infection this response can lead to the repression of viral gene expression but is counteracted by the ...
Delphine Cuchet-Lourenço, Roger D Everett, Roger D. Everett, Boutell Chris, McFarlane Steven, Cuchet, D., Mandy Glass, Steven McFarlane, Cuchet-Lourenço Delphine, Chris Boutell, Glass, M., Vanni, E., Orr Anne, Everett Roger D., McFarlane, S., Everett, R.D., Glass Mandy, Vanni Emilia, Boutell, C., Emilia Vanni, Anne Orr, Orr, A.   +21 more
core   +1 more source

E3 Ubiquitin Ligases: Potential Therapeutic Targets for Skeletal Pathology and Degeneration

Stem Cells International, 2022
The ubiquitination-proteasome system (UPS) is crucial in regulating a variety of cellular processes including proliferation, differentiation, and survival. Ubiquitin protein ligase E3 is the most critical molecule in the UPS system.
Ruiyin Zeng, Yuan Xiong, Ze Lin, Adriana C. Panayi, Yun Sun, Faqi Cao, Guohui Liu   +6 more
doaj   +1 more source

Generation and physiological roles of linear ubiquitin chains [PDF]

, 2012
Ubiquitination now ranks with phosphorylation as one of the best-studied post-translational modifications of proteins with broad regulatory roles across all of biology.
Iwai Kazuhiro, Walczak, H, Walczak, Henning, Kazuhiro Iwai, Walczak Henning, Đikić, Ivan, Ivan Dikic, Iwai, Kazuhiro, Iwai, K, Dikic, I, Dikic Ivan, Henning Walczak   +11 more
core   +1 more source