| 1. |
- Ahmadian, Afshin, et al.
(författare)
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Genetic instability in the 9q22.3 region is a late event in the development of squamous cell carcinoma.
- 1998
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Ingår i: Oncogene. - : Springer Science and Business Media LLC. - 0950-9232 .- 1476-5594. ; 17:14
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Tidskriftsartikel (refereegranskat)abstract
- Squamous cell carcinoma (SCC) of the skin represents a group of neoplasms which is associated with exposure to UV light. Recently, we obtained data suggesting that invasive skin cancer and its precursors derive from one original neoplastic clone. Here, the analysis were extended by loss of heterozygosity (LOH) analysis in the chromosome 9q22.3 region. A total of 85 samples, taken from twenty-two sections of sun-exposed sites, corresponding to normal epidermis, morphological normal cells with positive immuno-staining for the p53 protein (p53 patches), dysplasias, cancer in situ (CIS) and squamous cell carcinomas (SCC) of the skin were analysed. Overall, about 70% of p53 patches had mutations in the p53 gene but not LOH in the p53 gene or 9q22.3 region. Approximately 70% of the dysplasias showed p53 mutations of which about 40% had LOH in the p53 region but not in the 9q22.3 region. In contrast, about 65% of SCC and CIS displayed LOH in the 9q22.3 region, as well as frequent (80%) mutations and/or LOH in the p53 gene. These findings strongly suggest that alterations in the p53 gene is an early event in the progression towards SCC, whereas malignant development involves LOH and alterations in at least one (or several) tumor suppressor genes located in chromosome 9q22.3.
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| 3. |
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| 4. |
- Dujon, B, et al.
(författare)
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The nucleotide sequence of Saccharomyces cerevisiae chromosome XV
- 1997
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Ingår i: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 387:6632, s. 98-102
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Tidskriftsartikel (refereegranskat)abstract
- Chromosome XV was one of the last two chromosomes of Saccharomyces cerevisiae to be discovered(1). It is the third-largest yeast chromosome after chromosomes XII and IV, and is very similar in size to chromosome VII. It alone represents 9% of the yeast genome (8% if ribosomal DNA is included). When systematic sequencing of chromosome XV was started, 93 genes or markers were identified, and most of them were mapped(2). However, very little else was known about chromosome XV which, in contrast to shorter chromosomes, had not been the object of comprehensive genetic or molecular analysis. It was therefore decided to start sequencing chromosome XV only in the third phase of the European Yeast Genome Sequencing Programme, after experience was gained on chromosomes III, XI and II (refs 3-5). The sequence of chromosome XV has been determined from a set of partly overlapping cosmid clones derived from a unique yeast strain, and physically mapped at 3.3-kilobase resolution before sequencing. As well as numerous new open reading frames (ORFs) and genes encoding tRNA or small RNA molecules, the sequence of 1,091,283 base pairs confirms the high proportion of orphan genes and reveals a number of ancestral and successive duplications with other yeast chromosomes.
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| 5. |
- Gräslund, Torbjörn, et al.
(författare)
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Production of a Thermostable DNA Polymerase by Site-Specific Cleavage of a Heat-Eluted Affinity Fusion Protein
- 1997
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Ingår i: Protein Expression and Purification. - : Elsevier BV. - 1046-5928 .- 1096-0279. ; 9, s. 125-132
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Tidskriftsartikel (refereegranskat)abstract
- A novel strategy is described for bacterial expression and affinity purification of a recombinant truncated version of the heat-stable DNA polymerase I fromThermus aquaticus.The DNA polymerase ([Delta]Taq) was produced as a fusion to a serum albumin binding affinity handle (ABP) derived from streptococcal protein G. Based on the thermostability of the [Delta]TaqDNA polymerase, affinity-purified ABP-[Delta]Taqcould be heat-eluted from HSA columns by incubation at 85ï¿œC. To produce free [Delta]TaqDNA polymerase, efficient site-specific cleavage of the affinity tag was performed using a recombinant coxsackievirus 3C protease (3Cpro), also produced as an ABP affinity fusion. Thus, an integrated strategy could be devised where both the cleaved ABP affinity tag and the protease fusion could be recovered after site-specific cleavage using HSA-affinity chromatography. The flow-through fraction contained essentially pure [Delta]TaqDNA polymerase with full enzymatic activity.
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| 6. |
- Hober, Sophia, et al.
(författare)
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Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.
- 1999
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Ingår i: FEBS Letters. - 0014-5793 .- 1873-3468. ; 443:3
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Tidskriftsartikel (refereegranskat)abstract
- Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.
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| 7. |
- Ljungqvist, Charlotta, et al.
(författare)
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Derivatives of the B or Z domain from staphylococcal protein A (SPA) interacting with at least one domain of human factor VIII
- 1999
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Patent (populärvet., debatt m.m.)abstract
- The present invention relates to modified polypeptides which are derivatives of the B domain or Z domain from staphylococcal protein A (SPA), wherein between 1 and 20 amino acid residues of the said B or Z domain have been substituted by other amino acid residues, said substitution being made without substantial loss of the basic structure and stability of the said B or Z domain, and said substitution resulting in interaction capacity of the said polypeptide with at least one domain of human Factor VIII protein.
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| 8. |
- Ljungqvist, Charlotta, et al.
(författare)
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Receptor structures
- 1999
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Patent (populärvet., debatt m.m.)abstract
- The present invention relates to modified polypeptide derivatives of the B domain or Z domain of staphylococcal protein A (SPA). The derivatives contain amino acid substitutions that result in the ability of the B domain or Z domain to interact with at least one domain of a human Factor VIII protein, without substantially disrupting the structure and stability of the B domain or Z domain.
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| 10. |
- Lundeberg, Joakim, 1963-, et al.
(författare)
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Method for quantifying nucleic acid using multiple competitor nucleic acids
- 1997
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Patent (populärvet., debatt m.m.)abstract
- A method of determining the amount of target nucleic acid in a sample which comprises the steps of: a) adding to said sample a known amount of at least two different competitor nucleic acids at different concentrations, which have at least a portion of the sequence in common with the target nucleic acid, said common sequence comprising a binding site for a complementary primer sequence, b) co-amplifying the target nucleic acid and competitor nucleic acids in the sample by an in vitro amplification reaction using at least one primer, wherein at least one of said primers comprises a region complementary to said common sequence and the amplification products carry a label or means for attaching a label, c) separation of the amplification products, d) assessing the amount of label associated with the amplification products and e); comparison of the amount of label associated with each of the amplified target nucleic acid and amplified competitor nucleic acids to assess the amount of target nucleic acid in said sample, a method of diagnosis using the assay and kits for performing the same.
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