Publications by authors named "L J Penn"
ClpXP is a two-component mitochondrial matrix protease. The caseinolytic mitochondrial matrix peptidase chaperone subunit X (ClpX) recognizes and translocates protein substrates into the degradation chamber of the caseinolytic protease P (ClpP) for proteolysis. ClpXP degrades damaged respiratory chain proteins and is necessary for cancer cell survival.
View Article and Find Full Text PDFIntroduction: While observational studies suggest favorable associations between statin use and prostate cancer (CaP) outcomes, data from randomized-controlled trials remain inconclusive. Our study explores the relationship between statin use and survival outcomes in the context of the phase III ARAMIS study, a trial of darolutamide in the treatment of nonmetastatic castration-resistant prostate cancer.
Methods: We reviewed all 1,509 patients in the ARAMIS trial.
Article Synopsis
- Sinonasal neoplasms encompass a wide variety of tumor types, ranging from benign lesions to aggressive cancers, reflecting the diverse tissue types in the nasal cavities and sinuses.
- Recent advancements in understanding the genetic and molecular factors influencing sinonasal tumor behavior have led to the identification of new tumor types and an updated classification in the World Health Organization's fifth edition for head and neck tumors.
- It's essential for radiologists to be familiar with this new classification to accurately assess tumor behavior and effectively participate in patient care decisions alongside a multidisciplinary cancer team.
Objective: To evaluate for the first time, comparative serum and prostate tissue concentrations of lipophilic and hydrophilic statins.
Methods: After reviewing all patients who underwent radical prostatectomy between 1993 and 2019, we selected 80 patients taking atorvastatin (lipophilic) or rosuvastatin (hydrophilic) for cholesterol control and with available banked fresh-frozen tissue from the prostatectomy. Primary endpoint was serum and prostate statin concentration measured by HPLC-mass spectrometry analysis.
Targeted protein degradation (TPD) is an emerging therapeutic strategy that would benefit from new chemical entities with which to recruit a wider variety of ubiquitin E3 ligases to target proteins for proteasomal degradation. Here we describe a TPD strategy involving the recruitment of FBXO22 to induce degradation of the histone methyltransferase and oncogene NSD2. UNC8732 facilitates FBXO22-mediated degradation of NSD2 in acute lymphoblastic leukemia cells harboring the NSD2 gain-of-function mutation p.
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