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  • Articles  (74)
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  • Base Sequence  (74)
  • 1985-1989  (74)
  • 1987  (74)
  • Natural Sciences in General  (74)
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  • Articles  (74)
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  • 1985-1989  (74)
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  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-02
    Description: Overall, each of the program packages performed their tasks satisfactorily. For analyses where there was a well-defined answer, such as a search for a restriction site, there were few significant differences between the program sets. However, for tasks in which a degree of flexibility is desirable, such as homology or similarity determinations and database searches, DNASTAR consistently afforded the user more options in conducting the required analysis than did the other two packages. However, for laboratories where sequence analysis is not a major effort and the expense of a full sequence analysis workstation cannot be justified, MicroGenie and IBI-Pustell offer a satisfactory alternative. MicroGenie is a polished program system. Many may find that its user interface is more "user friendly" than the standard menu-driven interfaces. Its system of filing sequences under individual passwords facilitates use by more than one person. MicroGenie uses a hardware device for software protection that occupies a card slot in the computer on which it is used. Although I am sympathetic to the problem of software piracy, I feel that a less drastic solution is in order for a program likely to be sharing limited computer space with other software packages. The IBI-Pustell package performs the required analysis functions as accurately and quickly as MicroGenie but it lacks the clearness and ease of use. The menu system seems disjointed, and new or infrequent users often find themselves at apparent "dead-end menus" where the only clear alternative is to restart the entire program package. It is suggested from published accounts that the user interface is going to be upgraded and perhaps when that version is available, use of the system will be improved. The documentation accompanying each package was relatively clear as to how to run the programs, but all three packages assumed that the user was familiar with the computational techniques employed. MicroGenie and IBI-Pustell further complicated their documentation by mixing instructions for the version based on floppy disk operation with that for the hard disk version.(ABSTRACT TRUNCATED AT 400 WORDS)〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cannon, G C -- New York, N.Y. -- Science. 1987 Oct 2;238(4823):97-103.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659902" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Sequence Homology, Nucleic Acid ; *Software
    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: 1987-03-06
    Description: Ribonuclease mitochondrial RNA processing, a site-specific endoribonuclease involved in primer RNA metabolism in mammalian mitochondria, requires an RNA component for its activity. On the basis of copurification and selective inactivation with complementary oligonucleotides, a 135-nucleotide RNA species, not encoded in the mitochondrial genome, is identified as the RNA moiety of the endoribonuclease. This finding implies transport of a nucleus-encoded RNA, essential for organelle DNA replication, to the mitochondrial matrix.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, D D -- Clayton, D A -- GM-33088-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1178-84.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2434997" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Nucleus/*physiology ; Chemical Phenomena ; Chemistry ; Drug Resistance ; Endonucleases/isolation & purification/metabolism ; Enzyme Activation/drug effects ; *Genetic Code ; Humans ; Mammals/*genetics/metabolism ; Micrococcal Nuclease/pharmacology ; Mitochondria/*metabolism ; Oligonucleotides/pharmacology ; Organoids/physiology ; RNA/*biosynthesis/genetics/isolation & purification/physiology ; Ribonucleases/metabolism ; Subcellular Fractions/metabolism
    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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  • 3
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D R -- Schultz, P G -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1401-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685986" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Single-Stranded/metabolism ; Hydrolysis ; Micrococcal Nuclease/*genetics/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Staphylococcus aureus/enzymology/genetics ; Substrate Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-06-05
    Description: The body plan of Drosophila is determined to a large extent by homeotic genes, which specify the identity and spatial arrangement of the body segments. Homeotic genes share a characteristic DNA segment, the homeo box, which encodes a defined domain of the homeotic proteins. The homeo domain seems to mediate the binding to specific DNA sequences, whereby the homeotic proteins exert a gene regulatory function. By isolating the normal Antennapedia gene, fusing its protein-coding sequences to an inducible promoter, and reintroducing this fusion gene into the germline of flies, it has been possible to transform head structures into thoracic structures and to alter the body plan in a predicted way. Sequence homologies suggest that similar genetic mechanisms may control development in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gehring, W J -- New York, N.Y. -- Science. 1987 Jun 5;236(4806):1245-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2884726" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blastoderm/ultrastructure ; Drosophila/embryology/*genetics ; Embryonic and Fetal Development ; *Genes, Homeobox ; Mutation ; Ovum/ultrastructure
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-03-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉George, D G -- Hunt, L T -- Barker, W C -- New York, N.Y. -- Science. 1987 Mar 27;235(4796):1562.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823903" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Database Management Systems ; *Information Systems ; *Nucleic Acids ; Software
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    Publication Date: 1987-10-09
    Description: An abnormal alpha 2-antiplasmin that is associated with a serious bleeding tendency has been found in a Dutch family and is referred to as alpha 2-antiplasmin Enschede. This abnormal alpha 2-antiplasmin is converted from an inhibitor of plasmin to a substrate. The molecular defect of alpha 2-antiplasmin Enschede, as revealed by sequencing of cloned genomic DNA fragments, consists of an alanine insertion near the active site region of the molecule. Substitution of this fragment into complementary DNA for a wild-type alpha 2-antiplasmin yields a translation product with physical and functional properties typical of the abnormal alpha 2-antiplasmin Enschede. The naturally occurring mutant may serve as a model for investigating the structures that determine the properties of an inhibitor versus those of a substrate in serine protease inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Lijnen, H R -- Nelles, L -- Kluft, C -- Nieuwenhuis, H K -- Rijken, D C -- Collen, D -- New York, N.Y. -- Science. 1987 Oct 9;238(4824):209-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Thrombosis and Vascular Research, University of Leuven, Belgium.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2958938" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/metabolism ; Fibrinolysin/*antagonists & inhibitors ; *Genes ; Humans ; Molecular Sequence Data ; *Mutation ; Protein Biosynthesis ; alpha-2-Antiplasmin/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    Publication Date: 1987-07-17
    Description: The calcium-calmodulin-dependent protein kinase II is a major component of brain synaptic junctions and has been proposed to play a variety of important roles in brain function. A complementary DNA representing a portion of the smaller 50-kilodalton subunit of the rat brain enzyme has been cloned and sequenced. The calmodulin-binding region has been identified and a synthetic analog prepared that binds calmodulin with high affinity in the presence of calcium. Like the 50-kilodalton kinase polypeptide, the concentration of the messenger RNA varies both neuroanatomically and during postnatal development of the brain. The broad tissue and species cross-reactivity of the complementary DNA suggests that the 50-kilodalton subunit found in rat brain is evolutionarily conserved and is the product of a single gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hanley, R M -- Means, A R -- Ono, T -- Kemp, B E -- Burgin, K E -- Waxham, N -- Kelly, P T -- New York, N.Y. -- Science. 1987 Jul 17;237(4812):293-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037704" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Amino Acid Sequence ; Animals ; Base Sequence ; Biological Assay ; Brain/enzymology/growth & development ; Calcium-Calmodulin-Dependent Protein Kinases ; Cloning, Molecular ; DNA/genetics ; Protein Kinases/*genetics ; RNA, Messenger/genetics ; Rats ; Species Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
    Publication Date: 1987-12-18
    Description: Growth factors and their receptors are involved in the regulation of cell proliferation and also play a key role in oncogenesis. In this study, a novel putative kinase receptor gene, termed eph, has been identified and characterized by molecular cloning. Its primary structure is similar to that of tyrosine kinase receptors thus far cloned and includes a cysteine-rich region in the extracellular domain. However, other features of the sequence distinguish the eph gene product from known receptors with tyrosine kinase activity. Thus the eph protein may define a new class of these molecules. The eph gene is overexpressed in several human carcinomas, suggesting that this gene may be involved in the neoplastic process of some tumors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirai, H -- Maru, Y -- Hagiwara, K -- Nishida, J -- Takaku, F -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1717-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2825356" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA Restriction Enzymes ; *Genes ; Humans ; Molecular Sequence Data ; Neoplasms/metabolism ; Oncogenes ; Protein-Tyrosine Kinases/metabolism ; Receptor, Epidermal Growth Factor/*genetics ; Transcription, Genetic
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  • 9
    Publication Date: 1987-10-16
    Description: A portion of the Duchenne muscular dystrophy (DMD) gene transcript from human fetal skeletal muscle and mouse adult heart was sequenced, representing approximately 25 percent of the total, 14-kb DMD transcript. The nucleic acid and predicted amino acid sequences from the two species are nearly 90 percent homologous. The amino acid sequence that is predicted from this portion of the DMD gene indicates that the protein product might serve a structural role in muscle, but the abundance and tissue distribution of the messenger RNA suggests that the DMD protein is not nebulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoffman, E P -- Monaco, A P -- Feener, C C -- Kunkel, L M -- 2T 32 GM07753-07/GM/NIGMS NIH HHS/ -- HD18658/HD/NICHD NIH HHS/ -- R01 NS23740/NS/NINDS NIH HHS/ -- T32 GM007753/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):347-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Genetics, Children's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3659917" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; DNA/*genetics ; DNA, Recombinant ; Exons ; Humans ; Male ; Mice ; Molecular Sequence Data ; Muscle Proteins/genetics ; Muscles/analysis/embryology ; Muscular Dystrophies/*genetics ; Muscular Dystrophy, Animal/*genetics ; Myocardium/analysis ; Nucleic Acid Hybridization ; RNA, Messenger/genetics ; X Chromosome
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-03-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kolata, G -- New York, N.Y. -- Science. 1987 Mar 13;235(4794):1323.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823884" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics ; Eye Neoplasms/*genetics ; *Genes ; Humans ; Retinoblastoma/*genetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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