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Bringing ancient light-sensing proteins back to life

Researchers from The University of Osaka have developed a method to reconstruct ancestral rhodopsins that can be produced and experimentally tested in bacteria. This innovation utilizes an insertions-deletions aware sequence reconstruction approach, enabling scientists to study the evolution of functional proteins.

SourceThe University of Osaka·JournalACS Omega·TypeData/statistical analysis·DateJun 16, 2026
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Tweaking cancer cell response to ultrasound treatment

Increasing the spacing between integrin-ECM binding domains on the extracellular matrix can boost the efficiency of ultrasound treatment applied to kill cancer cells. A new study found that this increased spacing triggers myosin forces, pumps more calcium inside, and promotes cell death.

SourceIndian Institute of Science (IISc)·JournalNano Letters·DateFeb 17, 2025

Images of crucial cell receptors show promising new drug targets

Researchers at UChicago captured complete images of adhesion G protein-coupled receptors, revealing their complex extracellular region's interaction with the transmembrane region. The findings suggest alternative means of activating the receptor without separating the GAIN domain.

SourceUniversity of Chicago·JournalNature Communications·TypeImaging analysis·DateDec 17, 2024

Another building block for personalized medicine for lung cancer is discovered

A new study reveals a link between the removal of the FGFR1 protein's extracellular domain and a significant decrease in tumour volume. This finding offers a potential new avenue of treatment for patients with squamous cell carcinoma of the lungs, who have shown limited success with current therapies.

SourceUniversity of Cologne·JournalJournal of Clinical Investigation·DateNov 7, 2023

A twisted cell-cell adhesion molecule complex structure revealed by single-molecule fluorescence microscopy and high-speed atomic force microscopy

Researchers have elucidated the mechanism of CELSR cadherin dimerization, revealing a twisted cell-cell adhesion molecule complex structure. The extracellular domains of CELSR cadherins exhibited strand- and globule-like portions, which bound through strand-like structures in an antiparallel orientation.

SourceNational Institutes of Natural Sciences·JournalProceedings of the National Academy of Sciences·TypeExperimental study·DateApr 24, 2023
SAMSUNG T9 Portable SSD 2TB

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How oral cancer acquires radioresistance

A recent study has identified a new mechanism by which oral cancer cells acquire radioresistance through the transfer of microRNA, specifically miR-503-3p. This discovery brings hope for the development of new treatments for radiation-resistant oral cancer.

SourceKumamoto University·JournalJournal of Extracellular Vesicles·TypeExperimental study·DateDec 15, 2021

Breakthrough study shows how plants sense the world

Researchers created the first network map for 200 plant sensing proteins, revealing unknown interactions and key proteins that act as master nodes. The map could lead to ways to increase plant resistance to pathogens, heat, drought, salinity, or cold shock.

SourceUniversity of Alabama at Birmingham·JournalNature·DateJan 19, 2018

Gaining a better understanding of the way we taste

A team of Japanese researchers made a groundbreaking discovery about the way we taste by studying the structure changes of taste receptor proteins when they bind to taste substances. This change is thought to transmit information from outside the cell, enabling precise analysis of taste substance binding and related processes.

SourceOsaka University·JournalScientific Reports·DateJul 20, 2016
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