Results 251 to 260 of about 68,518 (300)
Cystine (Cys2) deprivation in pancreatic cancer cells induces oxidative stress that destabilizes cytosolic iron–sulfur cluster (ISC) proteins, triggering an iron‐regulatory protein (IRP)‐mediated iron‐starvation response (ISR). This leads to increased iron uptake (via TFRC), an expanded labile iron pool, and ferroptosis.
Mingjun Tan +8 more
wiley +1 more source
Lock, relax, load, and shoot: a molecular perspective on Nedd4 regulation
Structural basis of inactive and active states of the Nedd4 HECT E3 ligase subfamily, following a ‘lock, relax, load, and shoot’ mechanism. In the locked, autoinhibited state, intramolecular domain interactions restrain the HECT domain. Relaxation releases these restraints, allowing loading of ubiquitin onto the catalytic cysteine, followed by the ...
Masa Janosev +2 more
wiley +1 more source
Rethinking the role of HIF in hepatocellular carcinoma
Tumor hypoxia is a hallmark of cancer driving disease, in part through activation of hypoxia‐inducible factors (HIFs). While HIF‐1α is classically understood as a hypoxia‐responsive transcription factor, its role under normoxic conditions in cells is less clear.
Niall S. Kenneth +2 more
wiley +1 more source
Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinases. [PDF]
Bolhuis DL, Emanuele MJ, Brown NG.
europepmc +1 more source
MARCH family E3 ubiquitin ligases selectively target and degrade cadherin family proteins. [PDF]
Seo T +6 more
europepmc +1 more source
Deciphering the mechanism of E3 ubiquitin ligases in plant responses to abiotic and biotic stresses and perspectives on PROTACs for crop resistance. [PDF]
Su Y +7 more
europepmc +1 more source
Regulation of the water channel aquaporin-2 by cullin E3 ubiquitin ligases.
Murali SK, McCormick JA, Fenton RA.
europepmc +1 more source
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Essays in Biochemistry, 2005
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
openaire +2 more sources
The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds).
Helen C, Ardley, Philip A, Robinson
openaire +2 more sources

