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  • 1
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    Acetogenesis from H2 plus CO2 by spirochetes from termite guts (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-01-29
    Description: Pure cultures of termite gut spirochetes were obtained and were shown to catalyze the synthesis of acetate from H2 plus CO2. The 16S ribosomal DNA sequences of two strains were 98 percent similar and were affiliated with those of the genus Treponema. However, neither was closely related to any known treponeme. These findings imply an important role for spirochetes in termite nutrition, help to reconcile the dominance of acetogenesis over methanogenesis as an H2 sink in termite hindguts, suggest that the motility of termite gut protozoa by means of attached spirochetes may be based on interspecies H2 transfer, and underscore the importance of termites as a rich reservoir of novel microbial diversity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leadbetter, J R -- Schmidt, T M -- Graber, J R -- Breznak, J A -- New York, N.Y. -- Science. 1999 Jan 29;283(5402):686-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Center for Microbial Ecology, Michigan State University, East Lansing, MI 48824-1101, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9924028" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/*metabolism ; Anaerobiosis ; Animals ; Carbon Dioxide/metabolism ; Culture Media ; DNA, Bacterial/chemistry/genetics ; DNA, Ribosomal/chemistry/genetics ; Digestive System/microbiology ; Hydrogen/metabolism ; Isoptera/*microbiology ; Molecular Sequence Data ; Oxidation-Reduction ; RNA, Ribosomal, 16S/genetics ; Spirochaetaceae/classification/isolation & purification/metabolism/physiology ; Treponema/classification/isolation & purification/*metabolism/physiology
    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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    Discrete determinants in transfer RNA for editing and aminoacylation (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-05-23
    Description: During translation errors of aminoacylation are corrected in editing reactions which ensure that an amino acid is stably attached to its corresponding transfer RNA (tRNA). Previous studies have not shown whether the tRNA nucleotides needed for effecting translational editing are the same as or distinct from those required for aminoacylation, but several considerations have suggested that they are the same. Here, designed tRNAs that are highly active for aminoacylation but are not active in translational editing are presented. The editing reaction can be controlled by manipulation of nucleotides at the corner of the L-shaped tRNA. In contrast, these manipulations do not affect aminoacylation. These results demonstrate the segregation of nucleotide determinants for the editing and aminoacylation functions of tRNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hale, S P -- Auld, D S -- Schmidt, E -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1997 May 23;276(5316):1250-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9157882" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Escherichia coli ; Molecular Sequence Data ; Nucleic Acid Conformation ; *RNA Editing ; RNA, Transfer/*metabolism ; RNA, Transfer, Ile/chemistry/metabolism ; RNA, Transfer, Val/chemistry/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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    Metal ion chaperone function of the soluble Cu(I) receptor Atx1 (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-11-05
    Description: Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pufahl, R A -- Singer, C P -- Peariso, K L -- Lin, S J -- Schmidt, P J -- Fahrni, C J -- Culotta, V C -- Penner-Hahn, J E -- O'Halloran, T V -- GM-38047/GM/NIGMS NIH HHS/ -- GM-50016/GM/NIGMS NIH HHS/ -- GM-54111/GM/NIGMS NIH HHS/ -- R01 GM054111/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1997 Oct 31;278(5339):853-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9346482" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Carrier Proteins ; *Cation Transport Proteins ; Copper/*metabolism ; Escherichia coli ; Fungal Proteins/metabolism/*physiology ; Humans ; Molecular Chaperones/*physiology ; Molecular Sequence Data ; Recombinant Proteins ; Saccharomyces cerevisiae/metabolism/*physiology ; *Saccharomyces cerevisiae Proteins ; Sequence Homology, Amino Acid
    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
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    Candidate gene for the chromosome 1 familial Alzheimer's disease locus (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-18
    Description: A candidate gene for the chromosome 1 Alzheimer's disease (AD) locus was identified (STM2). The predicted amino acid sequence for STM2 is homologous to that of the recently cloned chromosome 14 AD gene (S182). A point mutation in STM2, resulting in the substitution of an isoleucine for an asparagine (N141l), was identified in affected people from Volga German AD kindreds. This N141l mutation occurs at an amino acid residue that is conserved in human S182 and in the mouse S182 homolog. The presence of missense mutations in AD subjects in two highly similar genes strongly supports the hypothesis that mutations in both are pathogenic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy-Lahad, E -- Wasco, W -- Poorkaj, P -- Romano, D M -- Oshima, J -- Pettingell, W H -- Yu, C E -- Jondro, P D -- Schmidt, S D -- Wang, K -- AG0513C/AG/NIA NIH HHS/ -- R01-AG11762/AG/NIA NIH HHS/ -- R01-AG11899/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geriatric Research Education, and Clinical Center (182B), Veterans Affairs Medical Center, Seattle, WA 98108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638622" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/ethnology/*genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Cloning, Molecular ; DNA, Complementary/genetics ; Female ; Gene Expression ; Germany/ethnology ; Humans ; Lod Score ; Male ; Membrane Proteins/chemistry/*genetics ; Middle Aged ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Presenilin-2
    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
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    Diversification of C-function activity in maize flower development (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-11-29
    Description: The Arabidopsis gene AGAMOUS is required for male and female reproductive organ development and for floral determinacy. Reverse genetics allowed the isolation of a transposon-induced mutation in ZAG1, the maize homolog of AGAMOUS. ZAG1 mutants exhibited a loss of determinacy, but the identity of reproductive organs was largely unaffected. This suggested a redundancy in maize sex organ specification that led to the identification and cloning of a second AGAMOUS homolog, ZMM2, that has a pattern of expression distinct from that of ZAG1. C-function organ identity in maize (as defined by the A, B, C model of floral organ development) may therefore be orchestrated by two closely related genes, ZAG1 and ZMM2, with overlapping but nonidentical activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mena, M -- Ambrose, B A -- Meeley, R B -- Briggs, S P -- Yanofsky, M F -- Schmidt, R J -- New York, N.Y. -- Science. 1996 Nov 29;274(5292):1537-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology and Center for Molecular Genetics, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA. rschmidt@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8929416" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; DNA Transposable Elements ; DNA-Binding Proteins/chemistry/*genetics ; Gene Expression ; *Genes, Plant ; MADS Domain Proteins ; Microscopy, Electron, Scanning ; Molecular Sequence Data ; Morphogenesis ; Mutation ; Phenotype ; Plant Proteins/chemistry/*genetics ; RNA, Messenger/genetics/metabolism ; RNA, Plant/genetics/metabolism ; Transcription Factors/*genetics ; Zea mays/*genetics/*growth & development/ultrastructure
    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
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    Modification of phytohormone response by a peptide encoded by ENOD40 of legumes and a nonlegume (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-07-19
    Description: The gene ENOD40 is expressed during early stages of legume nodule development. A homolog was isolated from tobacco, which, as does ENOD40 from legumes, encodes an oligopeptide of about 10 amino acids. In tobacco protoplasts, these peptides change the response to auxin at concentrations as low as 10(-12) to 10(-16)M. The peptides encoded by ENOD40 appear to act as plant growth regulators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉van de Sande, K -- Pawlowski, K -- Czaja, I -- Wieneke, U -- Schell, J -- Schmidt, J -- Walden, R -- Matvienko, M -- Wellink, J -- van Kammen, A -- Franssen, H -- Bisseling, T -- New York, N.Y. -- Science. 1996 Jul 19;273(5273):370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur Zuchtungsforschung, Koln, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8662527" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cell Division ; Fabaceae/chemistry/*genetics/growth & development ; *Genes, Plant ; Green Fluorescent Proteins ; Indoleacetic Acids/*pharmacology ; Luminescent Proteins/biosynthesis ; Molecular Sequence Data ; Naphthaleneacetic Acids/pharmacology ; Open Reading Frames ; Plant Growth Regulators ; Plant Proteins/biosynthesis/*genetics/*physiology ; Plant Roots/growth & development/metabolism ; *Plants, Medicinal ; *Plants, Toxic ; Protoplasts/cytology ; RNA, Long Noncoding ; RNA, Untranslated/*physiology ; Recombinant Fusion Proteins ; Tobacco/chemistry/*genetics/growth & development ; 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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