Results 61 to 70 of about 18,290,537 (258)

The ubiquitin-proteasome system in glioma cell cycle control

open access: yesCell Division, 2012
A major determinant of cell fate is regulation of cell cycle. Tight regulation of this process is lost during the course of development and progression of various tumors.
Vlachostergios Panagiotis J   +2 more
doaj   +1 more source

Targeting the EpCAM‐AXL axis to overcome drug resistance in lung cancer

open access: yesMolecular Oncology, EarlyView.
Lung cancer cells often evade therapy by hijacking signaling pathways. We reveal that cleaved EpCAM (sEpCAM) stabilizes the oncogenic protein AXL, driving NF‐κB and STAT3‐mediated chemoresistance. This EpCAM‐AXL axis identifies a high‐risk patient subset with poor prognosis.
Alexa Guerrero‐Alba   +5 more
wiley   +1 more source

Mechanisms of ubiquitin-independent proteasomal degradation and their roles in age-related neurodegenerative disease

open access: yesFrontiers in Cell and Developmental Biology
Neurodegenerative diseases are characterized by the progressive breakdown of neuronal structure and function and the pathological accumulation of misfolded protein aggregates and toxic protein oligomers.
Taylor R. Church   +2 more
doaj   +1 more source

MURF2B, a novel LC3-binding protein, participates with MURF2A in the switch between autophagy and ubiquitin proteasome system during differentiation of C2C12 muscle cells. [PDF]

open access: yesPLoS ONE, 2013
The ubiquitin proteasome system and macroautophagy are proteolytic pathways essential in the maintenance of cellular homeostasis during differentiation and remodelling of skeletal muscle.
Véronique Pizon   +6 more
doaj   +1 more source

Ubistatins inhibit proteasome-dependent degradation by binding the ubiquitin chain [PDF]

open access: yes, 2004
To identify previously unknown small molecules that inhibit cell cycle machinery, we performed a chemical genetic screen in Xenopus extracts. One class of inhibitors, termed ubistatins, blocked cell cycle progression by inhibiting cyclin B proteolysis ...
K. M. Sakamoto   +10 more
core   +1 more source

USP7 inhibits FOXO1 activity in chronic lymphocytic leukaemia cells enhancing cell survival

open access: yesMolecular Oncology, EarlyView.
CLL cells rely on BCR‐mediated signalling for survival and proliferation in part through suppression of FOXO1. FOXO1 activity is regulated by a plethora of post‐translational modifications including phosphorylation and ubiquitination. We demonstrated that dual inhibition of BCR signalling and the deubiquitinase USP7 activates FOXO1, modulating its ...
Hassan N.B. Almuhanna   +8 more
wiley   +1 more source

Viral Takeover of the Host Ubiquitin System

open access: yesFrontiers in Cellular and Infection Microbiology, 2011
Like the other more well-characterized post-translational modifications (phosphorylation, methylation, acetylation, acylation, etc.), the attachment of the 76 amino acid ubiquitin (Ub) protein to substrates has been shown to govern countless cellular ...
Jean K Gustin   +3 more
doaj   +1 more source

How the ubiquitin-proteasome system controls transcription

open access: yes, 2003
Gene transcription and ubiquitin-mediated proteolysis are two processes that have seemingly nothing in common: transcription is the first step in the life of any protein and proteolysis the last. Despite the disparate nature of these processes, a growing
Muratani, Masafumi, Tansey, William P.
core   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

open access: yes, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
Mainak Guharoy   +15 more
core   +1 more source

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

open access: yesFEBS 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   +6 more
wiley   +1 more source

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