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  • 1
    Publication Date: 1999-04-09
    Description: Mature Arabidopsis seeds are enriched in storage proteins and lipids, but lack starch. In the shrunken seed 1 (sse1) mutant, however, starch is favored over proteins and lipids as the major storage compound. SSE1 has 26 percent identity with Pex16p in Yarrowia lipolytica and complements pex16 mutants defective in the formation of peroxisomes and the transportation of plasma membrane- and cell wall-associated proteins. In Arabidopsis maturing seeds, SSE1 is required for protein and oil body biogenesis, both of which are endoplasmic reticulum-dependent. Starch accumulation in sse1 suggests that starch formation is a default storage deposition pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Y -- Sun, L -- Nguyen, L V -- Rachubinski, R A -- Goodman, H M -- New York, N.Y. -- Science. 1999 Apr 9;284(5412):328-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10195899" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/genetics/*metabolism/ultrastructure ; *Arabidopsis Proteins ; *Fungal Proteins ; Gene Expression ; Genetic Complementation Test ; Membrane Proteins/chemistry/genetics ; Microbodies/metabolism/ultrastructure ; Microscopy, Electron ; Molecular Sequence Data ; Mutation ; Organelles/*metabolism/ultrastructure ; Phenotype ; Plant Oils/metabolism ; Plant Proteins/chemistry/genetics/metabolism/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Saccharomycetales/chemistry/genetics/metabolism ; Seeds/*metabolism/ultrastructure ; Starch/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 2004-11-06
    Description: One of the important roles of microRNA (miRNA) is to direct the cleavage of messenger RNA (mRNA). However, the mechanisms of decay of the cleaved mRNA products is not well understood. We show that miRNA-directed cleavage products in organisms as diverse as Arabidopsis, mouse, and Epstein-Barr virus have at their 3' ends a stretch (1 to 24 nucleotides) of oligouridine posttranscriptionally added downstream of the cleavage site. This 3' uridine addition, as shown for Arabidopsis, is correlated with decapping and 5' shortening of the cleaved products, suggesting a mechanistic step in the miRNA-directed mRNA decay mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shen, Binzhang -- Goodman, Howard M -- New York, N.Y. -- Science. 2004 Nov 5;306(5698):997.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, and Department of Molecular Biology, Massachusetts General Hospital, 50 Blossom Street, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528436" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arabidopsis ; Cells, Cultured ; Cloning, Molecular ; Herpesvirus 4, Human/metabolism ; Humans ; Mice ; MicroRNAs/*metabolism ; Poly U/metabolism ; RNA, Messenger/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Uridine/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1988-11-25
    Description: Nucleotide sequences for the nuclear genes encoding chloroplast (GapA and GapB) and cytosolic (GapC) glyceraldehyde-3-phosphate dehydrogenases (GAPDHs) from Arabidopsis thaliana were determined. Comparison of nucleotide sequences indicates that the divergence of chloroplast and cytosolic GAPDH genes preceded the divergence of prokaryotes and eukaryotes. In addition, some intron-exon junctions are conserved among GapB, GapC, and chicken GAPDH genes. These results provide evidence at the molecular level to support the idea that introns existed before the divergence of prokaryotes and eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shih, M C -- Heinrich, P -- Goodman, H M -- New York, N.Y. -- Science. 1988 Nov 25;242(4882):1164-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Harvard Medical School, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3055302" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; *Cells ; Chickens/genetics ; Chloroplasts/enzymology ; Cytosol/enzymology ; Escherichia coli/genetics ; *Eukaryotic Cells ; Exons ; Glyceraldehyde-3-Phosphate Dehydrogenases/*genetics/metabolism ; *Introns ; Molecular Sequence Data ; NAD/metabolism ; NADP/metabolism ; Plants/genetics ; *Prokaryotic Cells
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 1992-11-20
    Description: A gene from the flowering plant Arabidopsis thaliana that encodes an omega-3 desaturase was cloned on the basis of the genetic map position of a mutation affecting membrane and storage lipid fatty acid composition. Yeast artificial chromosomes covering the genetic locus were identified and used to probe a seed complementary DNA library. A complementary DNA clone for the desaturase was identified and introduced into roots of both wild-type and mutant plants by Ti plasmid-mediated transformation. Transgenic tissues of both mutant and wild-type plants had significantly increased amounts of the fatty acid produced by this desaturase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Arondel, V -- Lemieux, B -- Hwang, I -- Gibson, S -- Goodman, H M -- Somerville, C R -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1353-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing 48824-1312.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455229" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*genetics ; Chromosome Mapping ; Cloning, Molecular ; Fatty Acid Desaturases/*genetics ; *Genes, Plant ; Genetic Complementation Test ; Molecular Sequence Data ; Plant Proteins/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 1981-09-04
    Description: The arrangement of the human insulin gene in DNA from 87 individuals was analyzed by the Southern blot hybridization technique with a cloned genomic human insulin probe. Insertions of 1.5 to 3.4 kilobase pairs in the 5'-flanking region of the gene were found in DNA from 38 individuals. These insertions occurred within 1.3 kilobase pairs of the transcription initiation site. In contrast, no insertions were observed in the region 3' to the coding sequence. The prevalence of these insertions in type 2 diabetes was significantly greater than in the other groups (P less than .001). The limitation of this striking length polymorphism to a potential promoter region suggests that these insertions may play a role in insulin gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rotwein, P -- Chyn, R -- Chirgwin, J -- Cordell, B -- Goodman, H M -- Permut, M A -- AM-00033/AM/NIADDK NIH HHS/ -- AM-07120/AM/NIADDK NIH HHS/ -- AM-16724/AM/NIADDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1981 Sep 4;213(4512):1117-20.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6267694" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA Restriction Enzymes ; Diabetes Mellitus/*genetics ; Gene Expression Regulation ; Genes ; Genetic Linkage ; Humans ; Insulin/*genetics ; Leukocytes ; Operon ; Polymorphism, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1979-08-10
    Description: The nucleotide sequence of a DNA complementary to human growth hormone messenger RNA was cloned; it contains 29 nucleotides in its 5' untranslated region, the 651 nucleotides coding for the prehormone, and the entire 3' untranslated region (108 nucleotides). The data reported predict the previously unknown sequence of the signal peptide of human growth hormone and, by comparison with the previously determined sequences of rat growth hormone and human chorionic somatomammotropin, strengthens the hypothesis that these genes evolved by gene duplication from a common ancestral sequence. The human growth hormone gene sequences have been linked in phase to a fragment of the trp D gene of Escherichia coli in a plasmid vehicle, and a fusion protein is synthesized at high level (approximately 3 percent of bacterial protein) under the control of the regulatory region of the trp operon. This fusion protein (70 percent of whose amino acids are coded for by the human growth hormone gene) reacts specifically with antibodies to human growth hormone and is stable in E. coli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martial, J A -- Hallewell, R A -- Baxter, J D -- Goodman, H M -- New York, N.Y. -- Science. 1979 Aug 10;205(4406):602-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/377496" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cattle ; DNA, Recombinant/*metabolism ; Escherichia coli/*metabolism ; Growth Hormone/*biosynthesis ; Humans ; Pituitary Gland/metabolism ; Pituitary Neoplasms/metabolism ; *Plasmids ; Poly A/metabolism ; Prolactin/biosynthesis ; *Protein Biosynthesis ; RNA, Messenger/metabolism ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1980-09-19
    Description: Crown gall tumors are induced in plants by infection with the soil bacterium Agrobacterium tumefaciens. Because the tumor induction involves transfer of a portion of the tumor-inducing (Ti) plasmid DNA from the bacterium to the plant cells, this system is of interest for the study of genetic exchange as well as tumor induction. The boundaries of the transferred DNA (T-DNA) have been cloned from transformed plant cells of tobacco. Detailed mapping with restriction enzymes and nucleotide sequence analysis of two independent clones were used to study the molecular structure of the ends of the T-DNA. One clone contains the two ends of the T-DNA joined together; the other contains one end of the T-DNA joined to repetitive plant DNA sequences. These studies provide direct evidence that the T-DNA can be integrated into the plant genome. In addition, the data suggest that in the plant, T-DNA can be tandemly repeated. Sequence analysis of the junction of crown gall clone 1 reveals several direct repeats as well as an inverted repeat; these structures may be involved in the transfer of the DNA from Agrobacterium to plant cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zambryski, P -- Holsters, M -- Kruger, K -- Depicker, A -- Schell, J -- Van Montagu, M -- Goodman, H M -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1385-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251546" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular/methods ; DNA Restriction Enzymes/metabolism ; DNA, Neoplasm/*genetics ; DNA, Recombinant ; Plant Tumors/*microbiology ; Plants, Toxic ; *Plasmids ; Recombination, Genetic ; Rhizobium/*genetics ; Tobacco ; Transformation, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1986-06-06
    Description: A glutamine synthetase gene from alfalfa (Medicago sativa) has been expressed in Escherichia coli after fusion of bacterial transcription and translation signals to a complete alfalfa glutamine synthetase coding sequence. Synthesis of the alfalfa glutamine synthetase enzyme in Escherichia coli was demonstrated by functional genetic complementation of a glutamine synthetase-deficient mutant and by immunoblotting analysis. These results should facilitate protein engineering and structure-function analysis of the plant enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DasSarma, S -- Tischer, E -- Goodman, H M -- New York, N.Y. -- Science. 1986 Jun 6;232(4755):1242-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2871626" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *DNA, Recombinant ; Escherichia coli/*genetics ; Genes ; Genetic Complementation Test ; Glutamate-Ammonia Ligase/*genetics ; Medicago sativa/*genetics ; Molecular Weight ; Plasmids ; Promoter Regions, Genetic
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Publication Date: 1987-10-23
    Description: Transcriptional regulation by cyclic adenosine monophosphate (cAMP) in mammalian cells could be mediated by a phosphoprotein substrate of the cAMP-dependent protein kinase or, as in prokaryotes, by a cAMP-binding protein. Two synthetic genes that code for an active fragment of the protein inhibitor of this kinase and a mutant inactive fragment were constructed and used to distinguish these alternatives. Transient expression of the active peptide product specifically inhibited the cAMP-stimulated expression of a cotransfected reporter gene by more than 90 percent, whereas the expression of the inactive peptide did not alter cAMP-stimulated gene expression. The results indicate that an active kinase catalytic subunit is a necessary intermediate in the cAMP stimulation of gene transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grove, J R -- Price, D J -- Goodman, H M -- Avruch, J -- New York, N.Y. -- Science. 1987 Oct 23;238(4826):530-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2821622" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Carrier Proteins/*pharmacology ; Chloramphenicol O-Acetyltransferase ; Cyanogen Bromide ; Cyclic AMP/*pharmacology ; DNA, Recombinant ; Escherichia coli/genetics ; *Intracellular Signaling Peptides and Proteins ; Nucleic Acid Hybridization ; Peptide Fragments/*pharmacology ; Phosphorylation ; Plasmids ; Protein Kinase Inhibitors ; Protein Kinases/metabolism ; RNA, Messenger/genetics ; Recombinant Proteins/*pharmacology ; Transcription, Genetic/*drug effects ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
    Publication Date: 1987-05-08
    Description: In a variety of human genetic diseases, replacement of the absent or defective protein provides significant therapeutic benefits. As a model for a somatic cell gene therapy system, cultured murine fibroblasts were transfected with a human growth hormone (hGH) fusion gene and cells from one of the resulting clonal lines were subsequently implanted into various locations in mice. Such implants synthesized and secreted hGH, which was detectable in the serum. The function of the implants depended on their location and size, and on the histocompatibility of the donor cells with their recipients. The expression of hGH could be modified by addition of regulatory effectors, and, with appropriate immunosuppression, the implants survived for more than 3 months. This approach to gene therapy, here termed "transkaryotic implantation," is potentially applicable to many genetic diseases in that the transfected cell line can be extensively characterized prior to implantation, several anatomical sites are suitable for implantation, and regulated expression of the gene of therapeutic interest can be obtained.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selden, R F -- Skoskiewicz, M J -- Howie, K B -- Russell, P S -- Goodman, H M -- AM-07055/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1987 May 8;236(4802):714-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3472348" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; DNA, Recombinant ; Fibroblasts/immunology/*transplantation ; *Genetic Engineering ; Graft Survival ; Growth Hormone/biosynthesis/*genetics ; Humans ; Immunosuppression ; Kidney ; Kinetics ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Plasmids ; Therapeutics ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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