Results 101 to 110 of about 7,268 (227)

Ribosomal proteins RPL37, RPS15 and RPS20 regulate the Mdm2-p53-MdmX network. [PDF]

PLoS ONE, 2013
Changes to the nucleolus, the site of ribosome production, have long been linked to cancer, and mutations in several ribosomal proteins (RPs) have been associated with an increased risk for cancer in human diseases.
Lilyn Daftuar, Yan Zhu, Xavier Jacq, Carol Prives   +3 more
doaj   +1 more source

Targeting Tumor Dormancy and Recurrence: Molecular Mechanisms and Peptide Therapeutic Delivery

MedComm – Oncology, Volume 5, Issue 1, March 2026.
This review summarizes the molecular mechanisms that regulate tumor dormancy and its role in cancer recurrence, with emphasis on immune evasion, extracellular matrix remodeling, metabolic regulation and angiogenic switching. It further discusses emerging peptide–based therapeutic strategies aimed at detecting, modulating, and eliminating dormant tumor ...
Abdur Raheem Aleem, Atif Ali, Wajid Ali, Yuying Cheng, Zhibin Yan, Chaoyi Xia, Chenguang Liu, Caiyun Fu, Yiren Hu, Xi Wang   +9 more
wiley   +1 more source

MDM2, MDMX and p53 in oncogenesis and cancer therapy [PDF]

Nature Reviews Cancer, 2013
The MDM2 and MDMX (also known as HDMX and MDM4) proteins are deregulated in many human cancers and exert their oncogenic activity predominantly by inhibiting the p53 tumour suppressor. However, the MDM proteins modulate and respond to many other signalling networks in which they are embedded.
Mark, Wade, Yao-Cheng, Li, Geoffrey M, Wahl   +2 more
openaire   +2 more sources

Recent Advances of In Situ Anticancer Nanomedicine from Enzyme‐Instructed Self‐Assembly

ChemNanoMat, Volume 11, Issue 12, December 2025.
This review summarizes advances in enzymatic self‐assemblies for generating in situ anticancer nanomedicine over the past five years. It highlights the unique features of enzyme substrates for in situ anticancer nanomedicine by discussing the representative examples.
Linrui Zou, Meihui Yi, Bing Xu
wiley   +1 more source

Elucidating the abilities of MDM2, MDMX and p21 to regulate ferroptosis [PDF]

, 2020
In this thesis, I have explored the role of three genes related to p53, namely p21, MDM2 and MDMX, in regulating ferroptosis, a form of non-apoptotic cell death. Ferroptosis, an iron-dependent mechanism that leads to cell death due to lipid peroxidation,
Venkatesh, Divya
core   +1 more source

Next‐Generation Proteolysis‐Targeting Chimeras in Precision Oncology: Multifunctional Designs, Emerging Modalities, and Translational Prospects in Targeted Protein Degradation

Drug Development Research, Volume 86, Issue 8, December 2025.
ABSTRACT Proteolysis‐targeting chimeras (PROTACs)‐mediated protein degradation has been recently developed as a game‐changing approach in oncology drug development. It represents a paradigm shift from traditional enzyme inhibition to selective protein degradation.
Mohamed S. Nafie, Mohamed K. Diab, Asmaa S. A. Yassen, Amany M. Elshamy, Mohamed R. El Tohamy, Haytham O. Tawfik, Sherif Ashraf Fahmy   +6 more
wiley   +1 more source

Mouse modeling of the MDM2/MDMX−p53 signaling axis [PDF]

, 2017
It is evident that p53 activity is critical for tumour prevention and stress response through its transcriptional activation of genes affecting cellular senescence, apoptosis, cellular metabolism, and DNA repair.
Zhang, Yanping, Tackmann, Nicole R.
core   +1 more source

MDMX regulation of p53 response to ribosomal stress [PDF]

The EMBO Journal, 2006
Ribosomal stress such as disruption of rRNA biogenesis activates p53 by release of ribosomal proteins from the nucleoli, which bind to MDM2 and inhibit p53 degradation. We found that p53 activation by ribosomal stress requires degradation of MDMX in an MDM2-dependent fashion.
Daniele M, Gilkes, Lihong, Chen, Jiandong, Chen   +2 more
openaire   +2 more sources

Human serum albumin and p53-activating peptide fusion protein is able to promote apoptosis and deliver fatty acid-modified molecules. [PDF]

PLoS ONE, 2013
Therapeutic peptides offer a high degree of specificity, potency, and low toxicity; making them promising candidates for cancer therapy. Despite these advantages, a number of hurdles, such as poor serum stability and inefficient cellular penetration ...
Michelle R Joshi, Nianhuan Yao, Kenneth A Myers, Zhiyu Li   +3 more
doaj   +1 more source

E3 Ubiquitin Ligases: Structures, Biological Functions, Diseases, and Therapy

MedComm, Volume 6, Issue 12, December 2025.
E3 ligases function as critical regulators of cellular protein degradation, and their dysregulation is a core pathogenic mechanism in a wide array of human diseases, including cancer, cardiovascular conditions, neurodegenerative disorders, and autoimmune diseases.
Haochen Wang, Junbo Peng, Hongchan Li, Yuzhe Lan, Jing Guo, Qiang Qiu, Xuan Huang   +6 more
wiley   +1 more source