Lab-on-a-Chip Breaks Protein-Expression Bottleneck

The Nucleic Acid Programmable Protein Array (NAPPA) was developed at the Harvard Institute of Proteomics and led to the spin-out of Auguron about a year ago. The firm says this technology enables proteins from any gene in the genome to be generated on microchips from surface printed DNA.
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Scientists report full humanization of yeast glycosylation pathway

For the first time, scientists have engineered yeast cells capable of producing a broad repertoire of recombinant therapeutic proteins with fully human sugar structures (glycosylation). These sugar structures ensure a glycoprotein’s biological activity and half-life and to date, have necessitated the expression of therapeutic glycoproteins in mammalian hosts. The accomplishment reported today has the potential to eliminate the need for mammalian cell culture, while improving control over glycosylation, and improving performance characteristics of many therapeutic proteins. Continue reading “Scientists report full humanization of yeast glycosylation pathway”

Proteome researchers map the entire active protein inventory in cells

Cells are like small cities. They contain all the necessary parts that allow their infrastructure, function, growth, and communication to operate. For over a century scientists have been looking at the structures and organelles in cells using microscopic methods, and then drawing conclusions about their function. Biochemical methods have allowed scientists to examine the inner life of the cell, an organisational unit basic to all life. Now, they are clarifying its structures in detail: from mitochondria, the "factories" of cells, which create energy; to the endoplasmic reticulum, necessary for protein synthesis and metabolic processes; to the Golgi apparatus, responsible for lipid synthesis and producing important energy reserves for cell growth.

Scientists have shown how cutting-edge methods can be used to catalogue the entire inventory of active proteins in cell organelles at a particular moment. Their work sheds considerable light on how cells use proteins. The work is published in the journal Cell.

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Scientists Reveal Most Detailed Map Of Life-forming Instructions

Researchers at the University of Toronto and the Hospital for Sick Children have recorded the most comprehensive and reliable map of protein interactions in a living organism to date, bringing science one step closer to deciphering and correcting disease-causing genetic instructions in humans and animals.

The findings, which will be released in the March 30 issue of Nature, reveal how researchers used sophisticated proteomic techniques to identify close to 4,000 proteins and 550 protein complexes involved in 7,123 protein-protein interactions in yeast cells, about half of which are novel. Many of the same complexes and protein interactions that go awry in human disease are also found in yeast. While living yeast cells have only 6,000 genes compared to a human’s 25,000, the structures of their encoded proteins and interactions among the proteins are virtually identical to ours.

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Study of human protein ‘interaction map’ reveal novel pathways

Discoveries made during the first large-scale analysis of interactions between proteins in our cells hold promise for identifying new genes involved in genetic diseases, according to researchers at Johns Hopkins and the Institute of Bioinformatics (IOB) in Bangalore.

The findings, reported in the March issue of Nature Genetics, were made using a database of more than 25,000 protein-protein interactions compiled by the Hopkins-IOB team. The result is believed to be the most detailed human “interactome” yet describing the interplay of proteins that occur in cells during health and disease.
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First disease-specific (breast cancer) protein library opens new drug paths

In research that could significantly advance the pace of drug discovery in the fight against breast cancer, Harvard Medical School investigators announce in today’s online Journal of Proteome Research that they have created the first publicly available library of reliably expressible proteins of a human disease, in this case for breast cancer.

Perhaps more significantly, these researchers expressed a subset of the 1,300 protein-expressing complementary DNAs in the library into a model system mimicking cells of a human breast, allowing them to study on a broad scale how these proteins might contribute to the development of breast cancer. Through this comprehensive approach, they identified potentially novel functional activities for both well known and lesser-known breast cancer-associated proteins.
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Decoding the cellular machinary

Researchers from Germany announce they have finished the first complete analysis of the “molecular machines” in one of biology’s most important model organisms: S. cerevisiae (baker’s yeast).

The study combined a method of extracting complete protein complexes from cells (tandem affinity purification, developed in 2001 by Bertrand Séraphin at EMBL), mass spectrometry and bioinformatics to investigate the entire protein household of yeast, turning up 257 machines that had never been observed. It also revealed new components of nearly every complex already known.
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