Revolutionizing HER2-Positive Breast Cancer Treatment: Insights from the 47th San Antonio Breast Cancer Symposium on Trastuzumab Deruxtecan. [PDF]
Negahi A +5 more
europepmc +1 more source
Phosphorylation of Optineurin by TBK1 induces the formation of filaments that condensate upon binding to linear polyubiquitin. Membrane‐anchored LC3 partitions into these condensates, suggesting that phase separation of filamentous Optineurin with ubiquitylated cargo promotes the sequestration of cargo and its subsequent alignment with LC3‐positive ...
Maria G. Herrera +10 more
wiley +1 more source
Impact of Anti-HER2 Therapies on Overall Survival in Patients with HER2-Positive Metastatic Breast Cancer: Focusing on Intracranial Efficacy of Emerging Treatments. [PDF]
Drittone D +4 more
europepmc +1 more source
This study revealed how the osteoblastic microenvironment determines the fate of cancer cells disseminated in bone, with a focus on whether they colonize, reside in quiescence, or reactivate from dormancy. Targeting integrin signaling may offer promising strategies for preventing quiescent cancer cells reactivation and bone colonization.
Hong‐Li Wang +7 more
wiley +1 more source
Reply to "Critical Evaluation of HER2 PET Imaging in Metastatic Breast Cancer: Addressing Key Challenges and Future Directions" and "The Role of HER2 PET in Treatment of Breast Cancer". [PDF]
Yeh R.
europepmc +1 more source
This research deciphers the m6A transcriptome by profiling its sites and functional readout effects: from mRNA stability, translation to alternative splicing, across five different cell types. Machine learning model identifies novel m6A‐binding proteins DDX6 and FXR2 and novel m6A reader proteins FUBP3 and L1TD1.
Zhou Huang +11 more
wiley +1 more source
Trastuzumab deruxtecan in HER2-low metastatic breast cancer: long-term survival analysis of the randomized, phase 3 DESTINY-Breast04 trial. [PDF]
Modi S +24 more
europepmc +1 more source
The Unwisdom of Allowing City Growth to Work Out Its Own Destiny [PDF]
Power, Garrett
core +1 more source
Lactylation‐Driven YTHDC1 Alleviates MASLD by Suppressing PTPN22‐Mediated Dephosphorylation of NLRP3
In MASLD, YTHDC1 undergoes increased lactylation and ubiquitination, reducing its expression. AARS1 mediates lactylation at lysine 565, while disrupted binding to LDHA further promotes lactylation, suppressing YTHDC1. This downregulation enhances PTPN22 mRNA stability, leading to NLRP3 dephosphorylation and activation, which exacerbates inflammation ...
Feng Zhang +16 more
wiley +1 more source

