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  • 1
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    Global efforts in structural genomics (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-06
    Description: A worldwide initiative in structural genomics aims to capitalize on the recent successes of the genome projects. Substantial new investments in structural genomics in the past 2 years indicate the high level of support for these international efforts. Already, enormous progress has been made on high-throughput methodologies and technologies that will speed up macromolecular structure determinations. Recent international meetings have resulted in the formation of an International Structural Genomics Organization to formulate policy and foster cooperation between the public and private efforts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, R C -- Yokoyama, S -- Wilson, I A -- P50 GM62411/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Oct 5;294(5540):89-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joint Center for Structural Genomics, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11588249" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Computational Biology ; Congresses as Topic ; Costs and Cost Analysis ; Crystallography, X-Ray ; Databases, Factual ; *Genomics ; Guidelines as Topic ; Humans ; Information Management ; Information Services ; International Cooperation ; Internet ; Nuclear Magnetic Resonance, Biomolecular ; Patents as Topic ; Private Sector ; *Protein Conformation ; Protein Folding ; Proteins/*chemistry ; *Proteome ; Public Sector ; Publishing ; Technology Transfer
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-13
    Description: Endocytic proteins such as epsin, AP180, and Hip1R (Sla2p) share a conserved modular region termed the epsin NH2-terminal homology (ENTH) domain, which plays a crucial role in clathrin-mediated endocytosis through an unknown target. Here, we demonstrate a strong affinity of the ENTH domain for phosphatidylinositol-4,5-bisphosphate [PtdIns(4,5)P2]. With nuclear magnetic resonance analysis of the epsin ENTH domain, we determined that a cleft formed with positively charged residues contributed to phosphoinositide binding. Overexpression of a mutant, epsin Lys76 --〉 Ala76, with an ENTH domain defective in phosphoinositide binding, blocked epidermal growth factor internalization in COS-7 cells. Thus, interaction between the ENTH domain and PtdIns(4,5)P2 is essential for endocytosis mediated by clathrin-coated pits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Itoh, T -- Koshiba, S -- Kigawa, T -- Kikuchi, A -- Yokoyama, S -- Takenawa, T -- New York, N.Y. -- Science. 2001 Feb 9;291(5506):1047-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11161217" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Vesicular Transport ; Amino Acid Motifs ; Amino Acid Substitution ; Animals ; COS Cells ; Carrier Proteins/*chemistry/*metabolism ; Cercopithecus aethiops ; Clathrin/metabolism ; Coated Pits, Cell-Membrane/metabolism ; DNA-Binding Proteins/metabolism ; *Endocytosis ; Epidermal Growth Factor/metabolism ; Inositol Phosphates/metabolism ; Liposomes/metabolism ; Models, Molecular ; Neuropeptides/*chemistry/*metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/chemistry/metabolism ; Transcription Factors/metabolism ; *Vesicular Transport Proteins ; Zinc Fingers
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Molecular computation by DNA hairpin formation (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-20
    Description: Hairpin formation by single-stranded DNA molecules was exploited in a DNA-based computation in order to explore the feasibility of autonomous molecular computing. An instance of the satisfiability problem, a famous hard combinatorial problem, was solved by using molecular biology techniques. The satisfiability of a given Boolean formula was examined autonomously, on the basis of hairpin formation by the molecules that represent the formula. This computation algorithm can test several clauses in the given formula simultaneously, which could reduce the number of laboratory steps required for computation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sakamoto, K -- Gouzu, H -- Komiya, K -- Kiga, D -- Yokoyama, S -- Yokomori, T -- Hagiya, M -- New York, N.Y. -- Science. 2000 May 19;288(5469):1223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10817993" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Biotinylation ; Computational Biology/*methods ; DNA Ligases/chemistry ; DNA, Single-Stranded/*chemistry ; DNA-Directed DNA Polymerase/chemistry ; Electrophoresis, Agar Gel ; *Nucleic Acid Conformation ; Nucleic Acid Denaturation ; Polymerase Chain Reaction ; Temperature ; Templates, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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