Articles with the keyword:
6

Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p

franklin submitted, created time 1 year 3 months (www.pnas.org)

Proteins conjugated by Lys-48-linked polyubiquitin chains are preferred substrates of the eukaryotic proteasome. Polyubiquitination requires an activating enzyme (E1), a conjugating enzyme (E2), and a ligase (E3).

5

New proteomics research promises to revolutionize biomedical discovery

bianjie submitted, created time 1 year 5 months (www.eurekalert.org)

In a research article that will be published in the July 20 issue of the journal Molecular Cell, a research team led by Dr. Benoit Coulombe from the Institut de recherches clniques de Montrl describes a powerful proteomics approach that promises to have a profound impact on our current understanding of the human proteome, and the function of its individual proteins.

5

One man's junk may be a genomic treasure

bianjie submitted, created time 1 year 5 months (www.eurekalert.org)

Scientists have only recently begun to speculate that what referred to as "junk" DNA -- the 96 percent of the human genome that doesn't encode for proteins and previously seemed to have no useful purpose -- is present in the genome for an important reason. But it wasn't clear what the reason was. Now, researchers at the University of California, San Diego School of Medicine have discovered one important function of so-called junk DNA.

5

Researchers use new approach to predict protein function

bianjie submitted, created time 1 year 5 months (www.news.uiuc.edu)

In a paper published online this month in the journal Nature Chemical Biology, researchers report that they have developed a way to determine the function of some of the hundreds of thousands of proteins for which amino acid sequence data are available, but whose structure and function remain unknown.

5

Site-specific protein modification: advances and applications

julie submitted, created time 1 year 9 months (www.sciencedirect.com)

"Although chemical methods to modify proteins in a sequence-specific manner have yet to be developed, site-specific post-translational modification of proteins has recently emerged as a major focus in biological chemistry. Post-translational modification with functionalized substrate analogues opens up several unique avenues to induce selective reactivity into proteins in a sequence-specific manner, and can be applied to protein identification and manipulation in both in vitro and in vivo contexts

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