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What web browsers and proteins have in common

Protein add-ons play a crucial role in customizing protein interfaces, allowing proteins to interact specifically with their dedicated partners. The discovery sheds light on how proteins perform specialized functions and enables new avenues for understanding fundamental principles in nature.

SourceOhio State University·JournalProceedings of the National Academy of Sciences·DateSep 19, 2017

Scientists step closer to halting spread of lung cancer

Researchers at the University of York and Texas have identified a protein, PAQR11, in the Golgi apparatus that receives a signal from Zeb1, triggering the transport of membrane sacks and altering the cancer cell's perimeter. This process allows cancer cells to detach from their fixed position and travel to other parts of the body.

SourceUniversity of York·JournalJournal of Clinical Investigation·DateNov 25, 2016

Breakthrough in 'marriage-broker' protein

Scientists at McGill University have made a breakthrough in understanding the role of Netrin1, a protein that brings cells together and maintains their healthy relationships. The study used genetic technology to remove all Netrin1 from mouse embryos, revealing a greater disruption of the nervous system than previously thought.

SourceMcGill University·JournalCell Reports·DateAug 12, 2015

Sensor demonstrates lack of space in living cells

Researchers developed a novel sensor that changes color depending on the confinement of space in cells, demonstrating the effects of lack of space on protein behavior. The study reveals attractive forces inside cells that override compression effects, leading to changes in protein functions under osmotic stress.

SourceRuhr-University Bochum·JournalAngewandte Chemie International Edition·DateJan 5, 2015

New knowledge about muscular dystrophy

Researchers at Aarhus University discovered that enzyme DDX6 regulates toxic RNA aggregates in muscular dystrophy patients. The study found that increasing DDX6 levels reduces RNA aggregates, while decreasing them leads to more aggregates.

SourceAarhus University·JournalNucleic Acids Research·DateMay 5, 2014

Using your loaf to fight brain disease

Researchers analyze baker's yeast to uncover key features in cellular development linked to diseases such as Parkinson's and cancer. The study reveals a precise cellular role for DJ-1 family proteins, which may provide new insight into mechanisms contributing to these conditions.

SourceUniversity of Leicester·JournalProceedings of the National Academy of Sciences·DateMar 31, 2014

Exit discovered in cellular garbage truck

A team of researchers led by Professor Jean Gruenberg has identified an exit in the cellular garbage truck, a structure responsible for sorting molecules and ensuring inter-cell digestion and regulation. The study reveals how Alix protein uses this route to avoid cellular digestion and how vesicular stomatitis uses it to infect cells.

SourceUniversité de Genève·JournalDevelopmental Cell·DateMay 9, 2013

New understanding can lead to srategies for dealing with neurodegenerative diseases

Researchers at Hebrew University of Jerusalem have identified two inclusion bodies, JUNQ and IPOD, with opposing effects on protein aggregation. Aggregation in JUNQ can lead to toxicity, while aggregation in IPOD is protective, suggesting a new potential strategy for designing therapeutics for neurodegenerative diseases.

SourceThe Hebrew University of Jerusalem·JournalProceedings of the National Academy of Sciences·DateDec 6, 2012

Scripps research scientists identify most lethal known species of prion protein

Scientists at Scripps Research Institute have identified a single prion protein that causes neuronal death similar to 'mad cow' disease, with toxic effects up to 10 times more potent than larger prion species. The study opens new avenues for exploring neurodegenerative disorders like Alzheimer's and Parkinson's diseases.

SourceScripps Research Institute·JournalProceedings of the National Academy of Sciences·DateFeb 9, 2012

How cells dispose of their waste

Researchers have elucidated the structure of the 26S proteasome, a key protein degradation machinery, using a combination of structural biology methods. The discovery sheds light on how cells dispose of their waste and could have important implications for understanding neurodegenerative diseases like Alzheimer's and Parkinson's.

SourceMax-Planck-Gesellschaft·JournalProceedings of the National Academy of Sciences·DateJan 23, 2012

Scripps research scientists elevate little-studied cellular mechanism to potential drug target

Scientists have elevated little-studied cellular mechanism sulfenylation to potential drug target by showing its importance in cell signaling and cancer. A new chemical probe allowed detection of minute differences in sulfenylation rates, revealing a key role for hydrogen peroxide in activating epidermal growth factor receptor.

SourceScripps Research Institute·JournalNature Chemical Biology·DateDec 11, 2011

Atomic model of tropomyosin bound to actin

The study provides the first detailed atomic model of tropomyosin bound to actin, significantly advancing our understanding of this key cellular protein. The researchers found that the interaction between tropomyosin and actin is weak enough that it can be readily perturbed by regulatory proteins, acting as a molecular switch.

SourceCell Press·JournalBiophysical Journal·DateFeb 15, 2011

Mutation linked to protein degradation underlies inherited ALS

A new study identifies a previously unrecognized mutation in the valosin-containing protein (VCP) gene, which causes an inherited form of amyotrophic lateral sclerosis (ALS). The research provides new insight into the disease's underlying pathology and validates the exome sequencing technique for identifying genetic causes.

SourceCell Press·JournalNeuron·DateDec 8, 2010

Viruses are sneakier than we thought

Researchers found that Kaposi's sarcoma-associated herpesvirus uses polyadenylation to block normal gene expression in cells. The virus' SOX protein aberrantly lengthens mRNA poly(A) tails, sending a signal to the cell that its messages are wrong and holding them back.

SourcePLOS·JournalPLOS Biology·DateMay 26, 2009

Yale researchers find new piece in Alzheimer's puzzle

Researchers at Yale University have identified a key role for cellular prion proteins in triggering the damage caused by amyloid-beta peptides in Alzheimer's patients. The study suggests that these proteins act as early targets for new therapies, offering promising hope for the treatment of this debilitating disease.

SourceYale University·JournalNature·DateFeb 25, 2009

Unique role of cell death protein TRADD in viral signaling

Researchers found that TRADD is essential for the transformation of B lymphocytes by Epstein-Barr virus, and that it can be targeted for cancer treatment. The study reveals a unique interaction between the viral protein LMP1 and TRADD, which masks its apoptotic activity.

SourcePLOS·JournalPLOS Biology·DateJan 14, 2008

Story ideas from Molecular & Cellular Proteomics

Researchers have identified new proteins in amniotic fluid that could improve pregnancy marker development. Additionally, a study on the Wlds gene has provided insights into preventing neuronal communication deterioration in Alzheimer's disease. A comprehensive analysis of proteins in human Jurkat T cells has also been conducted.

SourceAmerican Society for Biochemistry and Molecular Biology·JournalMolecular & Cellular Proteomics·DateAug 22, 2007

UNC scientists solve mystery of how largest cellular motor protein powers movement

Researchers have discovered a flexible coiled-coil region in dynein that enables rapid conversion of chemical energy into mechanical force, powering cell division and mitochondrial transport. This breakthrough sheds light on the protein's function and may hold implications for understanding neurodegenerative disorders.

SourceUniversity of North Carolina Health Care·JournalProceedings of the National Academy of Sciences·DateNov 27, 2006

One signal elicits thousands of answers

Researchers at the Max Planck Institute developed a technology to identify and quantify specific protein phosphorylation sites in response to stimuli. They discovered 6,600 phosphorylation sites in 2,244 proteins, with 90% being unknown, and created the Phosida database to share their findings.

SourceMax-Planck-Gesellschaft·JournalCell·DateNov 10, 2006