Results 91 to 100 of about 105,668 (286)

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

Expanding the arsenal of E3 ubiquitin ligases for proximity-induced protein degradation

, 2022
S.1014-1031Efficacy and selectivity of molecules inducing protein degradation depend on their affinity to the target protein but also on the type of E3 ubiquitin ligase that is recruited to trigger proteasomal degradation.
Dikic, I., Kannt, A.
core   +2 more sources

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

How to Inactivate Human Ubiquitin E3 Ligases by Mutation

Frontiers in Cell and Developmental Biology, 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.
Cristina Garcia-Barcena, Nerea Osinalde, Juanma Ramirez, Ugo Mayor, Ugo Mayor   +4 more
doaj   +1 more source

Role of E3 ubiquitin ligases in lung cancer

, 2013
E3 ubiquitin ligases are a large family of proteins that catalyze the ubiquitination of many protein substrates for targeted degradation by the 26S proteasome.
Jansen, G., Peters, Godefridus J, de Wilt, Leonie Ham, Peters, G.J., Snoek, Barbara C, Snoek, B.C., de Wilt, L.H.A.M., Jansen, Gerrit   +7 more
core   +1 more source

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Spratt, Donald E., Shaw, Gary S., Walden, Helen   +2 more
core   +1 more source

Purification and preparation of Marchantia polymorpha Auxin Response Factor 2 for phase separation studies

FEBS Open Bio, EarlyView.
We describe detailed protocols for the purification and preparation of Marchantia polymorpha Auxin Response Factor 2 (MpARF2). This protein is fused to an MBP solubility tag and an mNG fluorescent tag and is purified from Escherichia coli. The presented procedures make it possible to study MpARF2 assemblies, which could arise from phase separation ...
Bas Janssen, Robin Romein, Willy A. M. van den Berg, Simon Lindhoud, Jan Willem Borst, Carlo P. M. van Mierlo   +5 more
wiley   +1 more source

Expanding the Toolbox of E3 Ligases for Protein Degradation: Targeting the “Undruggable” Fbw7 E3 Ligase [PDF]

The 2nd Molecules Medicinal Chemistry Symposium (MMCS): Facing Novel Challenges in Drug Discovery, 2019
Proteolysis targeting chimera molecules (PROTACS) are heterobifunctional small moleculesdesigned to induce intracellular protein degradation [...]
openaire   +2 more sources

Threonine 348 regulates the subcellular localization of PTEN

FEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source

Role and therapeutic potential of E3s in the tumor microenvironment of hepatocellular carcinoma

Frontiers in Immunology
Hepatocellular carcinoma (HCC) is a high-incidence, poor-prognosis malignancy worldwide, requiring new strategies for treatment. Ubiquitination, especially ubiquitination through E3 ubiquitin ligases, plays an indispensable role in the development and ...
Hailin Wang, Qiang Li, Qinqin Tang, Gang Shi, Guo Wu, Xingbo Mao, Changkang Wu, Lixin Zhang, Jie Liu, Jingdong Li, Bo Li   +10 more
doaj   +1 more source