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Researchers at EMBL identified a new Polycomb group complex, PR-DUB, which surprisingly removes the same gene-silencing tag as another complex. This unexpected behavior may be a case of fine-tuning to maintain optimal levels of chemical tagging.

Mussels -- material artists with grip

Researchers have discovered that the byssal cuticle of mussels is a protein-based polymeric scaffold stabilized by dopa-iron complexes, enabling its unique hardness and extensibility. The cuticle's mechanical behavior allows it to dissipate energy from crashing waves while resisting abrasive damage.

SourceMax-Planck-Gesellschaft·JournalScience·DateMar 4, 2010

Silence of the genes

Berkeley researchers have imaged the human RISC-loading complex for the first time, proposing a model of how small RNA molecules target specific messenger RNAs for silencing and/or destruction. This work provides new insights into RNA interference mechanisms and has significant implications for gene regulation in humans.

SourceDOE/Lawrence Berkeley National Laboratory·JournalNature Structural & Molecular Biology·DateOct 12, 2009

NIH grant will boost electron microscopy at Brandeis

A $2.2 million NIH grant will enhance the lab's ability to rapidly detect protein clumps in Alzheimer's and other neurodegenerative diseases using a new high-resolution electron microscope. This technology will also enable researchers to study molecular motors in flagella, leading to a better understanding of these diseases.

Researchers study signaling networks that set up genetic code

Researchers at the University of Illinois have identified and visualized signaling pathways in protein-RNA complexes to understand how the genetic code is set in all organisms. The study uses molecular dynamics simulations and visualization software to analyze the optimal communication pathways, revealing modules and local communities ...

SourceUniversity of Illinois at Urbana-Champaign, News Bureau·JournalProceedings of the National Academy of Sciences·DateApr 14, 2009

Protein complex shown to play pivotal role in stem cell development in 2 Stanford studies

Scientists at Stanford University School of Medicine have identified a protein complex that plays a pivotal role in controlling the ability of embryonic stem cells to become any cell type. The finding is an important advance in harnessing the unique abilities of embryonic stem cells to treat disease and generate replacement tissue.

SourceStanford Medicine·JournalProceedings of the National Academy of Sciences·DateMar 2, 2009

How actin networks are actin'

A study published in PLOS Biology reveals that multiple Arp2/3 regulatory proteins play distinct roles in regulating actin networks, which are crucial for cellular processes such as cell migration and intracellular transport. The research provides new insights into the coordination of protein activities to generate complex actin networks.

SourcePLOS·JournalPLOS Biology·DateJan 2, 2008

Certain diseases, birth defects may be linked to failure of protein recycling system

A study at Cincinnati Children's Hospital Medical Center reveals that a protein recycling system failure may be linked to the development of certain diseases, such as cancer and heart disease, as well as birth defects. The Retromer Complex plays a critical role in delivering signaling proteins to tissue-building sites.

SourceCincinnati Children's Hospital Medical Center·JournalDevelopmental Cell·DateDec 20, 2007

Pairing nanoparticles with proteins

Researchers demonstrate ability to attach gold nanoparticles to proteins, forming protein-gold arrays for deciphering protein structures, identifying functional parts, and targeted drug delivery. Applications include catalysts for biomass energy conversion and precision vehicles for tumor targeting.

SourceDOE/Brookhaven National Laboratory·JournalAngewandte Chemie·DateJun 27, 2007

DNA ends: Common tool, different job

Researchers at the Salk Institute have discovered a novel RPA-like complex that specifically targets the short single-stranded DNA tail end of yeast chromosomes. This complex helps maintain telomere integrity and prevent premature senescence or cancer development.

SourceSalk Institute·JournalNature Structural & Molecular Biology·DateFeb 13, 2007

Brown scientists map structure of DNA-doctoring protein complex

Researchers at Brown University have solved the structure of a DNA-protein complex that aids in site-specific recombination, a process that allows mobile DNA to cut into chromosomes. The discovery provides new insights into how this process shapes species over time and its role in spreading antibiotic resistance and certain diseases.

SourceBrown University·JournalMolecular Cell·DateDec 6, 2006

A protein complex that untangles DNA

Researchers have discovered a protein complex called Smc5/6 that plays a crucial role in repairing damaged DNA and untangling chromosomes before cell division. The complex is involved in two distinct pathways, one for repair and the other for untangling, and its function has significant implications for understanding genetic stability.

SourceKarolinska Institutet·JournalMolecular Cell·DateJul 15, 2006

A catalogue of proteins

Researchers have identified over 1400 proteins in liver cells of mice, mapping their locations in ten different compartments. The study's findings show that around 40% of these proteins also appear in other cell organs, suggesting a high degree of conservation across species.

SourceMax-Planck-Gesellschaft·JournalCell·DateMay 29, 2006

The molecular post office inside the cell

The signal recognition particle (SRP) complex plays a crucial role in sorting secretory and membrane proteins, determining their final destination within or outside the cell. By understanding its structure, researchers can uncover key events during protein sorting, essential for expressing these proteins correctly.

SourceMax-Planck-Gesellschaft·JournalScience·DateMay 12, 2006

Mitochondrial biology gets a new chaperone

A study has identified a new molecular chaperone involved in assembling the enzyme complex I of mitochondria. The research found that B17.2L is a key protein required for this process and that it is mutated in patients with progressive encephalopathy.

SourceJCI Journals·JournalJournal of Clinical Investigation·DateOct 3, 2005

Catching a sneak

Researchers at the Weizmann Institute of Science have determined the structure of a protein complex on retroviruses that enables them to infect cells. The complex undergoes a radical change in shape as it attaches to cells, and its arrangement is unlike other known viral envelope protein structures.

SourceAmerican Committee for the Weizmann Institute of Science·JournalProceedings of the National Academy of Sciences·DateApr 13, 2005

Plants, animals share molecular growth mechanisms

Researchers at Purdue University have identified a plant protein complex that triggers cellular growth and development, similar to animal development. The discovery opens new avenues for understanding plant growth and potentially designing plants with enhanced protection against insects and disease.

SourcePurdue University·JournalThe Plant Cell·DateFeb 23, 2005

Biology in four dimensions

Scientists at EMBL have developed a new model for protein-complex interactions in yeast, revealing that key components are produced ahead of time and assembled as needed. This discovery sheds light on the dynamic behavior of cellular machines and offers potential applications in studying human and animal biological systems.

Actin muscles in on DNA transcription

Researchers have discovered that actin acts as a binding protein in the nucleus, recruiting other proteins to facilitate DNA transcription. This process is crucial for cellular activity and understanding its dysregulation is essential for developing new treatments for diseases like cancer.

SourceUniversity of Illinois Chicago·JournalNature Cell Biology·DateOct 29, 2004

In groundbreaking research, Yale and Salk Institute scientists reveal the structure of a key component that makes cells move

Researchers have determined the atomic structure of the Arp2/3 complex, a protein responsible for initiating actin filament growth in moving cells. This discovery provides insights into cellular movement mechanisms and has implications for understanding various biological processes, including immune responses and neural development.

SourceYale University·JournalScience·DateNov 22, 2001