Signal sequences: the same yet different
Article Abstract:
An increasing number of studies dispel the traditional concept of a similar coding mechanism in signal sequencing, which occurs among procaryotes and eukaryotes alike. More recent reports reveal a signal sequence-dependent specific targeting of proteins. Signal sequences also play varied molecular roles. Most of these findings were discovered with Saccharomyces cerevisiae. Two Walter laboratory studies, for example, provide new information on pathway preferences of signal sequences.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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Are ubiquitination pathways central to Parkinson's disease?
Article Abstract:
This review examines the physiological changes and biochemical pathways governing the etiology of parkinson's disease. Research findings implicate the involvement of alterations or reductions in ubiquitin-mediated proteasome function in the manifestation of some forms of parkinsonism in terms of dopaminergic neuron degeneration.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2003
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Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
Article Abstract:
The crystal structure of a c-Cbl-UbcH7-ZAP70 peptide ternary complex reveals the rigid coupling between the peptide binding and the ubiquitin-conjugating enzyme binding domains. Results further show that RING domain of the c-Cbl proto-oncogene aids in positioning the substrate and the enzyme for ubiquitin transfer.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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- Abstracts: Sequence of the 305 degrees-307 degrees region of the Bacillus subtilis chromosome. A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a putative 12.3 kb operon involved in hexuronate catabolism and a perfectly symmetrical hypothetical catabolite-responsive element
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