Results 241 to 250 of about 21,595,561 (335)
Preparation and characterization of renal cell peptides from fetal rats for their antitumor activity
This study aimed to prepare renal cells (RCs) from fetal rats which were digested by enzymes. Candidate peptides RCPs were characterized by capillary HPLC and MS and their bioactivity was predicted using peptideranker. The predicted top 10 bioactive peptides were synthesized.
Zhe Zhang +6 more
wiley +1 more source
1/2 order subharmonic waves of two cavitation bubbles. [PDF]
Tao F, Zhao GY, Chen WZ, Tao D.
europepmc +1 more source
Phenotypic plasticity in a newly established set of EGFR inhibitor‐adapted NSCLC cell lines during adaptation and in established cell lines. Here, we introduce novel sublines of the EGFR‐mutant non‐small cell lung cancer (NSCLC) cell lines HCC827 and HCC4006 adapted to the EGFR kinase inhibitors gefitinib (HCC827rGEFI2μm, HCC4006rGEFI1μm), erlotinib ...
Tharsagini V. Nanthaprakash +6 more
wiley +1 more source
Work Motivation: A Wall That Not Even the COVID-19 Pandemic Could Knock Down: Research Article. [PDF]
Bogdán PM +4 more
europepmc +1 more source
The E3 ubiquitin ligase, RNF219, suppresses CNOT6L expression to exhibit antiproliferative activity
We identified RNF219 as a CCR4‐NOT complex‐interacting E3 ubiquitin ligase that targets the CCR4‐NOT subunit CNOT6L for ubiquitination. RNF219 directly binds to the DUF3819 domain of CNOT1 through its putative α‐helix spanning amino acids 521–542. Our findings also suggest that antiproliferative activity of RNF219 is at least partially mediated by ...
Shou Soeda +9 more
wiley +1 more source
TTT and R2TP chaperone complexes are required for the assembly and activation of mTORC1. WAC directly interacts with components of TTT, R2TP, and mTORC1, and these interactions are affected by the availability of glucose and glutamine, correlating with changes in mTORC1 activity.
Sofía Cabezudo +11 more
wiley +1 more source
Two‐way inhibition of PAX5 transcriptional activity by PAX5::CBFA2T3
PAX5::CBFA2T3 (PAX5‐C) is a fusion protein of the B‐cell transcription factor, PAX5, and is found in B‐cell ALL. We propose a putative model of two‐way inhibition of PAX5 transcriptional activity by PAX5‐C. There are two ways of repression by PAX5‐C: DNA‐binding‐dependent way and HDAC‐dependent way, with either being sufficient for the repression. HDAC
Reina Ueno +12 more
wiley +1 more source

