| 1. |
- Sodergren, Erica, et al.
(författare)
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The genome of the sea urchin Strongylocentrotus purpuratus.
- 2006
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Ingår i: Science. - : American Association for the Advancement of Science (AAAS). - 1095-9203 .- 0036-8075. ; 314:5801, s. 941-52
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Tidskriftsartikel (refereegranskat)abstract
- We report the sequence and analysis of the 814-megabase genome of the sea urchin Strongylocentrotus purpuratus, a model for developmental and systems biology. The sequencing strategy combined whole-genome shotgun and bacterial artificial chromosome (BAC) sequences. This use of BAC clones, aided by a pooling strategy, overcame difficulties associated with high heterozygosity of the genome. The genome encodes about 23,300 genes, including many previously thought to be vertebrate innovations or known only outside the deuterostomes. This echinoderm genome provides an evolutionary outgroup for the chordates and yields insights into the evolution of deuterostomes.
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| 2. |
- Arbyn, M, et al.
(författare)
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Methods for screening and diagnosis
- 2007
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Ingår i: 2nd edition of the EU Guidelines for cervical cancer screening. - 9789279076985 ; , s. 69-141
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Bokkapitel (övrigt vetenskapligt/konstnärligt)
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| 3. |
- Gilchrist, Annalyn, et al.
(författare)
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Quantitative proteomics analysis of the secretory pathway.
- 2006
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Ingår i: Cell. - : Elsevier BV. - 0092-8674. ; 127:6, s. 1265-81
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Tidskriftsartikel (refereegranskat)abstract
- We report more than 1400 proteins of the secretory-pathway proteome and provide spatial information on the relative presence of each protein in the rough and smooth ER Golgi cisternae and Golgi-derived COPI vesicles. The data support a role for COPI vesicles in recycling and cisternal maturation, showing that Golgi-resident proteins are present at a higher concentration than secretory cargo. Of the 1400 proteins, 345 were identified as previously uncharacterized. Of these, 230 had their subcellular location deduced by proteomics. This study provides a comprehensive catalog of the ER and Golgi proteomes with insight into their identity and function.
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| 4. |
- Au, Catherine E, et al.
(författare)
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Organellar proteomics to create the cell map.
- 2007
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Ingår i: Current opinion in cell biology. - : Elsevier BV. - 0955-0674. ; 19:4, s. 376-85
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Tidskriftsartikel (refereegranskat)abstract
- The elucidation of a complete, accurate, and permanent representation of the proteome of the mammalian cell may be achievable piecemeal by an organellar based approach. The small volume of organelles assures high protein concentrations. Providing isolated organelles are homogenous, this assures reliable protein characterization within the sensitivity and dynamic range limits of current mass spec based analysis. The stochastic aspect of peptide selection by tandem mass spectrometry for sequence determination by fragmentation is dealt with by multiple biological replicates as well as by prior protein separation on 1-D gels. Applications of this methodology to isolated synaptic vesicles, clathrin coated vesicles, endosomes, phagosomes, endoplasmic reticulum, and Golgi apparatus, as well as Golgi-derived COPI vesicles, have led to mechanistic insight into the identity and function of these organelles.
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| 5. |
- Bell, Alexander W, et al.
(författare)
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The protein microscope: incorporating mass spectrometry into cell biology.
- 2007
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Ingår i: Nature methods. - : Springer Science and Business Media LLC. - 1548-7091 .- 1548-7105. ; 4:10, s. 783-4
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Tidskriftsartikel (refereegranskat)abstract
- Mass spectrometry has come into its own as an extremely powerful tool for the study of whole proteomes. So why are not more cell biologists embracing it with open arms?
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| 6. |
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