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  • Cloning, Molecular  (233)
  • Protein Conformation  (228)
  • American Association for the Advancement of Science (AAAS)  (446)
  • American Chemical Society (ACS)
  • American Meteorological Society
  • 1990-1994  (446)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (446)
  • American Chemical Society (ACS)
  • American Meteorological Society
Years
Year
  • 101
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    Crystal structure of domains 3 and 4 of rat CD4: relation to the NH2-terminal domains (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: The CD4 antigen is a membrane glycoprotein of T lymphocytes that interacts with major histocompatibility complex class II antigens and is also a receptor for the human immunodeficiency virus. the extracellular portion of CD4 is predicted to fold into four immunoglobulin-like domains. The crystal structure of the third and fourth domains of rat CD4 was solved at 2.8 angstrom resolution and shows that both domains have immunoglobulin folds. Domain 3, however, lacks the disulfide between the beta sheets; this results in an expansion of the domain. There is a difference of 30 degrees in the orientation between domains 3 and 4 when compared with domains 1 and 2. The two CD4 fragment structures provide a basis from which models of the overall receptor can be proposed. These models suggest an extended structure comprising two rigid portions joined by a short and possibly flexible linker region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brady, R L -- Dodson, E J -- Dodson, G G -- Lange, G -- Davis, S J -- Williams, A F -- Barclay, A N -- New York, N.Y. -- Science. 1993 May 14;260(5110):979-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of York, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493535" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*chemistry ; Crystallization ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Rats ; Sequence Alignment ; X-Ray Diffraction
    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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  • 102
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    Released form of CNTF receptor alpha component as a soluble mediator of CNTF responses (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-19
    Description: The alpha component of the receptor for ciliary neurotrophic factor (CNTF) differs from other known growth factor receptors in that it is anchored to cell membranes by a glycosylphosphatidylinositol linkage. One possible function of this type of linkage is to allow for the regulated release of this receptor component. Cell lines not normally responsive to CNTF responded to treatment with a combination of CNTF and a soluble form of the CNTF alpha receptor component. These findings not only demonstrate that the CNTF receptor alpha chain is a required component of the functional CNTF receptor complex but also reveal that it can function in soluble form as part of a heterodimeric ligand. Potential physiological roles for the soluble CNTF receptor are suggested by its presence in cerebrospinal fluid and by its release from skeletal muscle in response to peripheral nerve injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Aldrich, T H -- Ip, N Y -- Stahl, N -- Scherer, S -- Farruggella, T -- DiStefano, P S -- Curtis, R -- Panayotatos, N -- Gascan, H -- New York, N.Y. -- Science. 1993 Mar 19;259(5102):1736-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Inc., Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681218" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation/drug effects ; Cell Division/drug effects ; Cell Membrane/metabolism ; Ciliary Neurotrophic Factor ; Cloning, Molecular ; Gene Expression ; Glycosylphosphatidylinositols/metabolism ; Growth Inhibitors/pharmacology ; Hematopoietic Stem Cells/cytology/drug effects ; Humans ; Interleukin-6/pharmacology ; Leukemia Inhibitory Factor ; Lymphokines/pharmacology ; Mice ; Muscle Denervation ; Muscles/innervation/metabolism ; Nerve Tissue Proteins/*pharmacology ; Phosphatidylinositol Diacylglycerol-Lyase ; Phosphoric Diester Hydrolases/metabolism ; Phosphotyrosine ; RNA, Messenger/genetics ; Rats ; Receptor, Ciliary Neurotrophic Factor ; Receptors, Cell Surface/chemistry/*physiology ; Signal Transduction/physiology ; Tumor Cells, Cultured ; Tyrosine/analogs & derivatives/metabolism
    Print ISSN: 0036-8075
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  • 103
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    A faster walk along the genome (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aldhous, P -- New York, N.Y. -- Science. 1993 May 21;260(5111):1075.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493549" target="_blank"〉PubMed〈/a〉
    Keywords: *Base Sequence ; Cloning, Molecular ; DNA/*genetics ; Oligodeoxyribonucleotides/*genetics ; Sequence Analysis, DNA/*methods
    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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  • 104
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    Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-24
    Description: Zinc finger proteins, of the type first discovered in transcription factor IIIA (TFIIIA), are one of the largest and most important families of DNA-binding proteins. The crystal structure of a complex containing the five Zn fingers from the human GLI oncogene and a high-affinity DNA binding site has been determined at 2.6 A resolution. Finger one does not contact the DNA. Fingers two through five bind in the major groove and wrap around the DNA, but lack the simple, strictly periodic arrangement observed in the Zif268 complex. Fingers four and five of GLI make extensive base contacts in a conserved nine base-pair region, and this section of the DNA has a conformation intermediate between B-DNA and A-DNA. Analyzing the GLI complex and comparing it with Zif268 offers new perspectives on Zn finger-DNA recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pavletich, N P -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 24;261(5129):1701-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8378770" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Computer Graphics ; DNA/*chemistry/metabolism ; DNA-Binding Proteins/chemistry/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oncogene Proteins/*chemistry/genetics/metabolism ; Oncogenes ; Protein Conformation ; Trans-Activators ; Transcription Factors/*chemistry/genetics/metabolism ; X-Ray Diffraction ; *Zinc Fingers
    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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  • 105
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    Kinetics of folding of the all-beta sheet protein interleukin-1 beta (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: The folding of the all-beta sheet protein, interleukin-1 beta, was studied with nuclear magnetic resonance (NMR) spectroscopy, circular dichroism, and fluorescence. Ninety percent of the beta structure present in the native protein, as monitored by far-ultraviolet circular dichroism, was attained within 25 milliseconds, correlating with the first kinetic phase determined by tryptophan and 1-anilinonaphthalene-8-sulfonate fluorescence. In contrast, formation of stable native secondary structure, as measured by quenched-flow deuterium-hydrogen exchange experiments, began after only 1 second. Results from the NMR experiments indicated the formation of at least two intermediates with half-lives of 0.7 to 1.5 and 15 to 25 seconds. The final stabilization of the secondary structure, however, occurs on a time scale much greater than 25 seconds. These results differ from previous results on mixed alpha helix-beta sheet proteins in which both the alpha helices and beta sheets were stabilized very rapidly (less than 10 to 20 milliseconds).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Varley, P -- Gronenborn, A M -- Christensen, H -- Wingfield, P T -- Pain, R H -- Clore, G M -- New York, N.Y. -- Science. 1993 May 21;260(5111):1110-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health (NIH), Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493553" target="_blank"〉PubMed〈/a〉
    Keywords: Circular Dichroism ; Hydrogen Bonding ; Interleukin-1/*chemistry ; Kinetics ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Spectrometry, Fluorescence
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  • 106
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    DNA sequence determination by hybridization: a strategy for efficient large-scale sequencing (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-11
    Description: The concept of sequencing by hybridization (SBH) makes use of an array of all possible n-nucleotide oligomers (n-mers) to identify n-mers present in an unknown DNA sequence. Computational approaches can then be used to assemble the complete sequence. As a validation of this concept, the sequences of three DNA fragments, 343 base pairs in length, were determined with octamer oligonucleotides. Possible applications of SBH include physical mapping (ordering) of overlapping DNA clones, sequence checking, DNA fingerprinting comparisons of normal and disease-causing genes, and the identification of DNA fragments with particular sequence motifs in complementary DNA and genomic libraries. The SBH techniques may accelerate the mapping and sequencing phases of the human genome project.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drmanac, R -- Drmanac, S -- Strezoska, Z -- Paunesku, T -- Labat, I -- Zeremski, M -- Snoddy, J -- Funkhouser, W K -- Koop, B -- Hood, L -- New York, N.Y. -- Science. 1993 Jun 11;260(5114):1649-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biological and Medical Research Division, Argonne National Laboratory, IL 60439.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8503011" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cloning, Molecular ; Humans ; Macaca mulatta ; Molecular Sequence Data ; *Nucleic Acid Hybridization ; Oligonucleotide Probes ; Sequence Analysis, DNA/*methods
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  • 107
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    Locating the catalytic water molecule in serine proteases (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perona, J J -- Craik, C S -- Fletterick, R J -- DK-39304/DK/NIDDK NIH HHS/ -- GM13818-02/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):620-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342029" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; Crystallization ; Hydrogen Bonding ; Protein Conformation ; Serine Endopeptidases/*chemistry ; Trypsin/chemistry ; Water/*analysis ; X-Ray Diffraction
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  • 108
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    Ixr1, a yeast protein that binds to platinated DNA and confers sensitivity to cisplatin (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-30
    Description: Structure-specific recognition proteins (SSRPs) bind to DNA containing intrastrand cross-links formed by the anticancer drug cisplatin. A yeast gene encoding an SSRP, designated IXR1, was cloned and sequenced. The Ixr1 protein, a member of the high mobility group-box protein family, bound specifically to DNA modified with cisplatin but not inactive platinum compounds. A yeast strain with an inactivated IXR1 gene was half as sensitive to cisplatin and accumulated one-third as many platinum-DNA lesions after treatment with cisplatin as the parental strain. These findings suggest that SSRPs play a role in mediating the cytotoxicity of cisplatin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, S J -- Kellett, P J -- Lippard, S J -- New York, N.Y. -- Science. 1993 Jul 30;261(5121):603-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342024" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cisplatin/*metabolism/*pharmacology ; Cloning, Molecular ; DNA/*metabolism ; *DNA Adducts ; DNA, Fungal/*metabolism ; *DNA-Binding Proteins ; Fungal Proteins/chemistry/genetics/*metabolism ; Genes, Fungal ; High Mobility Group Proteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Saccharomyces cerevisiae/chemistry/drug effects/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins
    Print ISSN: 0036-8075
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  • 109
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    Relation of phenotype evolution of HIV-1 to envelope V2 configuration (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-06-04
    Description: Biological variability of human immunodeficiency virus type-1 (HIV-1) is involved in the pathogenesis of acquired immunodeficiency syndrome (AIDS). Syncytium-inducing (SI) HIV-1 variants emerge in 50 percent of infected individuals during infection, preceding accelerated CD4+ T cell loss and rapid progression to AIDS. The V1 to V2 and V3 region of the viral envelope glycoprotein gp120 contained the major determinants of SI capacity. The configuration of a hypervariable locus in the V2 domain appeared to be predictive for non-SI to SI phenotype conversion. Early prediction of HIV-1 phenotype evolution may be useful for clinical monitoring and treatment of asymptomatic infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Groenink, M -- Fouchier, R A -- Broersen, S -- Baker, C H -- Koot, M -- van't Wout, A B -- Huisman, H G -- Miedema, F -- Tersmette, M -- Schuitemaker, H -- New York, N.Y. -- Science. 1993 Jun 4;260(5113):1513-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Clinical Viro-Immunology, Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8502996" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/microbiology ; Amino Acid Sequence ; Base Sequence ; Biological Evolution ; Consensus Sequence ; Genetic Variation ; Giant Cells/microbiology ; HIV Envelope Protein gp120/*chemistry ; HIV Seropositivity/microbiology ; HIV-1/*chemistry/*genetics/pathogenicity ; Humans ; Male ; Molecular Sequence Data ; Phenotype ; Protein Conformation ; Recombination, Genetic
    Print ISSN: 0036-8075
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  • 110
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    Identification of the SH3 domain of GAP as an essential sequence for Ras-GAP-mediated signaling (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-22
    Description: Guanosine triphosphatase activating protein (GAP) is an essential component of Ras signaling pathways. GAP functions in different cell types as a deactivator and a transmitter of cellular Ras signals. A domain (amino acids 275 to 351) encompassing the Src homology region 3 (SH3) of GAP was found to be essential for GAP signaling. A monoclonal antibody was used to block germinal vesicle breakdown (GVBD) induced by the oncogenic protein Ha-ras Lys12 in Xenopus oocytes. The monoclonal antibody, which was found to recognize the peptide containing amino acids 275 to 351 within the amino-terminal domain of GAP, did not modify the stimulation of the Ha-Ras-GTPase by GAP. Injection of peptides corresponding to amino acids 275 to 351 and 317 to 326 blocked GVBD induced by insulin or by Ha-Ras Lys12 but not that induced by progesterone. These findings confirm that GAP is an effector for Ras in Xenopus oocytes and that the SH3 domain is essential for signal transduction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duchesne, M -- Schweighoffer, F -- Parker, F -- Clerc, F -- Frobert, Y -- Thang, M N -- Tocque, B -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):525-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rhone Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, Vitry Sur Seine, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7678707" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cloning, Molecular ; Epitopes/analysis ; Escherichia coli/genetics ; GTP Phosphohydrolases/metabolism ; GTPase-Activating Proteins ; *Genes, ras ; Genes, src ; Glutathione Transferase/genetics/metabolism ; Oocytes/physiology ; Polymerase Chain Reaction/methods ; Proteins/*genetics/immunology/*metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism ; Sequence Homology, Amino Acid ; *Signal Transduction ; Xenopus ; ras GTPase-Activating Proteins
    Print ISSN: 0036-8075
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  • 111
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    Formation of an Fe(III)-tyrosinate complex during biomineralization of H-subunit ferritin (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-05
    Description: An iron(III)-tyrosinate complex was identified in ferritin by ultraviolet-visible and resonance Raman spectroscopies. Previously, a specific amino acid side chain coordinated to iron in ferritin was not known. Ferritin protein was overexpressed in Escherichia coli from complementary DNA sequences of bullfrog red cell ferritin. The purple iron(III)-tyrosinate intermediate that formed during the first stages of iron uptake was replaced by the amber multinuclear iron(III)-oxo complexes of fully mineralized ferritin. Only the H subunit formed detectable amounts of the iron(III)-tyrosinate complex, which may explain the faster rates of iron biomineralization in H- compared to L-type ferritin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waldo, G S -- Ling, J -- Sanders-Loehr, J -- Theil, E C -- DK-20251/DK/NIDDK NIH HHS/ -- GM-18865/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):796-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, North Carolina State University, Raleigh 27695.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430332" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cloning, Molecular ; Erythrocytes/metabolism ; Escherichia coli/genetics ; Ferritins/chemistry/genetics/*metabolism ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Organometallic Compounds/*analysis ; Rana catesbeiana ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology ; Spectrum Analysis, Raman ; Tyrosine/*analogs & derivatives/analysis
    Print ISSN: 0036-8075
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  • 112
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    Learning how to suppress cancer (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1993 Sep 10;261(5127):1385-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8367721" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; *Genes, Tumor Suppressor ; Genes, p53 ; Genetic Engineering ; Genetic Therapy ; Humans ; Neoplasms/diagnosis/*genetics/therapy
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  • 113
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    Translocation of repetitive RNA sequences with the germ plasm in Xenopus oocytes (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-10
    Description: Xlsirts are a family of interspersed repeat RNAs from Xenopus laevis that contain from 3 to 13 repeat units (each 79 to 81 nucleotides long) flanked by unique sequences. They are homologous to the mammalian Xist gene that is involved in X chromosome inactivation. Xlsirt RNA appears first in the mitochondrial cloud (Balbiani body) in stage 2 oocytes and is then translocated as island-like structures to the vegetal cortex at early stage 3 coincident with the localization of the germ plasm. Exogenous Xlsirt RNA injected into oocytes translocates to the location of the endogenous RNA at that particular stage. The Xlsirt RNA repeat sequences are required for translocation and can cause the translocation of heterologous unique RNAs to the vegetal cortex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kloc, M -- Spohr, G -- Etkin, L D -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1712-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas, M.D. Anderson Cancer Center, Houston 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7505061" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cells, Cultured ; Cloning, Molecular ; DNA, Complementary ; Female ; In Situ Hybridization ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oocytes/*metabolism ; Oogenesis ; RNA/chemistry/*metabolism ; *Repetitive Sequences, Nucleic Acid ; Xenopus laevis
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  • 114
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    A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-26
    Description: Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of these buried hydrophobic residues in determining the structures of coiled coils was investigated by studying mutants of the GCN4 leucine zipper. When sets of buried residues were altered, two-, three-, and four-helix structures were formed. The x-ray crystal structure of the tetramer revealed a parallel, four-stranded coiled coil. In the tetramer conformation, the local packing geometry of the two hydrophobic positions in the heptad repeat is reversed relative to that in the dimer. These studies demonstrate that conserved, buried residues in the GCN4 leucine zipper direct dimer formation. In contrast to proposals that the pattern of hydrophobic and polar amino acids in a protein sequence is sufficient to determine three-dimensional structure, the shapes of buried side chains in coiled coils are essential determinants of the global fold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harbury, P B -- Zhang, T -- Kim, P S -- Alber, T -- GM44162/GM/NIGMS NIH HHS/ -- GM48958/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1401-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248779" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; *DNA-Binding Proteins ; Fungal Proteins/*chemistry/genetics ; Hydrogen Bonding ; *Leucine Zippers ; Molecular Sequence Data ; Mutation ; Protein Conformation ; Protein Kinases/*chemistry/genetics ; Protein Structure, Secondary ; *Saccharomyces cerevisiae Proteins
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    In pursuit of protein folding (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-05
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432308/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3432308/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Englander, S W -- R01 GM031847/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):848-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia 19104-6059.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235606" target="_blank"〉PubMed〈/a〉
    Keywords: Hydrogen-Ion Concentration ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Models, Molecular ; Muramidase/*chemistry ; Myoglobin/*chemistry ; Protein Conformation ; *Protein Folding ; Ribonuclease, Pancreatic/*chemistry
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    U2AF homolog required for splicing in vivo (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-10-22
    Description: Several fission yeast temperature-sensitive mutants defective in pre-mRNA processing (prp- mutants) at the nonpermissive temperature have been identified. Here, the prp2+ gene has been cloned by its ability to complement the temperature-sensitive growth defect of a prp2- mutant. The gene also corrects the pre-mRNA splicing defect of prp2- mutants and encodes a 59-kilodalton polypeptide (PRP2). A molecular characterization indicates that PRP2 is a previously uncharacterized yeast splicing factor with extensive similarity to the mammalian splicing factor U2AF65. Thus, this study provides evidence that a U2AF homolog participates in RNA processing in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potashkin, J -- Naik, K -- Wentz-Hunter, K -- R01GM47487/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):573-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Biology, University of Health Sciences, Chicago Medical School, IL 60064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211184" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; Conserved Sequence ; DEAD-box RNA Helicases ; Fungal Proteins/chemistry/*genetics/metabolism ; Genes, Fungal ; Genetic Complementation Test ; Molecular Sequence Data ; *Nuclear Proteins ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Fungal/metabolism ; Ribonucleoproteins/chemistry/*genetics/metabolism ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/*genetics ; Sequence Homology, Amino Acid
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    Photoactivated conformational changes in rhodopsin: a time-resolved spin label study (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-26
    Description: Rhodopsin has been selectively spin-labeled near the cytoplasmic termini of helices C and G. Photoactivation with a light flash induces an electron paramagnetic resonance spectral change in the millisecond time domain, coincident with the appearance of the active metarhodopsin II intermediate. The spectral change is consistent with a small movement near the cytoplasmic termination of the C helix and reverses upon formation of the MIII state. These results provide an important link between the optical changes associated with the retinal chromophore and protein conformational states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Farahbakhsh, Z T -- Hideg, K -- Hubbell, W L -- EY05216/EY/NEI NIH HHS/ -- EY07026/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1416-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jules Stein Eye Institute, Los Angeles, CA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248781" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Electron Spin Resonance Spectroscopy ; Light ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Secondary ; Rhodopsin/*chemistry ; Spin Labels ; Temperature
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    Regulation of the human hsp70 promoter by p53 (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-01
    Description: The tumor suppressor p53 is a nuclear phosphoprotein with characteristics of a transcription factor. It displays sequence-specific DNA binding, contains a potent transactivation domain, and has been implicated as both a transcriptional activator and a repressor. Transcription of the human hsp70 gene is stimulated by adenovirus E1a protein. This E1a transactivation of the hsp70 promoter is mediated by CCAAT binding factor (CBF). It is demonstrated here that p53 both represses transcription from the human hsp70 promoter and also interacts with CBF. Thus, the repression of the hsp70 promoter by p53 may be mediated by direct protein-protein interaction with CBF. These results suggest that protein-protein interaction between p53 and specific transcription factors may be an additional mechanism by which p53 regulates gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Agoff, S N -- Hou, J -- Linzer, D I -- Wu, B -- New York, N.Y. -- Science. 1993 Jan 1;259(5091):84-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8418500" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus E1A Proteins/metabolism ; Base Sequence ; CCAAT-Enhancer-Binding Proteins ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Cloning, Molecular ; DNA-Binding Proteins/metabolism ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/genetics ; *Gene Expression Regulation ; Heat-Shock Proteins/biosynthesis/*genetics/isolation & purification ; Humans ; *Promoter Regions, Genetic ; Recombinant Fusion Proteins/isolation & purification/metabolism ; TATA Box ; Transcription Factors/metabolism ; *Transcription, Genetic ; Tumor Suppressor Protein p53/genetics/isolation & purification/*metabolism
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    Structure-based design of a cyclophilin-calcineurin bridging ligand (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-10-08
    Description: The affinity of a flexible ligand that adopts a specific conformation when bound to its receptor should be increased with the appropriate use of conformational restraints. By determining the structure of protein-ligand complexes, such restraints can in principle be designed into the bound ligand in a rational way. A tricyclic variant (TCsA) of the immunosuppressant cyclosporin A (CsA), which inhibits the proliferation of T lymphocytes by forming a cyclophilin-CsA-calcineurin complex, was designed with the known three-dimensional structure of a cyclophilin-CsA complex. The conformational restraints in TCsA appear to be responsible for its greater affinity for cyclophilin and calcineurin relative to CsA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alberg, D G -- Schreiber, S L -- GM-38627/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Oct 8;262(5131):248-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/chemistry/*metabolism ; Amino Acid Sequence ; Calcineurin ; Calmodulin-Binding Proteins/chemistry/*metabolism ; Carrier Proteins/chemistry/*metabolism ; Cyclosporins/chemical synthesis/chemistry/*metabolism ; *Drug Design ; Ligands ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Peptidylprolyl Isomerase ; Phosphoprotein Phosphatases/chemistry/*metabolism ; Protein Conformation
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    Database contamination (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gersuk, V H -- Rose, T M -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):605.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480168" target="_blank"〉PubMed〈/a〉
    Keywords: Cloning, Molecular ; DNA, Fungal ; Databases, Factual ; *Gene Library ; *Genome, Human ; Humans ; RNA, Fungal/genetics ; RNA, Transfer/genetics
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    Identification of a mobile endogenous transposon in Arabidopsis thaliana (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-16
    Description: A mobile endogenous transposable element, Tag1, has been identified in the plant Arabidopsis thaliana. Tag1 was found in the nitrate transporter gene, CHL1, of a chlorate-resistant mutant present in a population of plants containing an active maize Ac transposon. Tag1 excises from the chl1 gene producing chlorate-sensitive revertants with Tag1 or Tag1-related elements at different loci. Tag1 and related elements are present in the Landsberg but not Columbia or Wassilewskija ecotypes of Arabidopsis. Thus, Tag1 provides a tool for the insertional mutagenesis of plant genes essential for biological processes of agronomic importance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsay, Y F -- Frank, M J -- Page, T -- Dean, C -- Crawford, N M -- 5T32CA09345-12/CA/NCI NIH HHS/ -- GM 40672/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):342-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla 92093-0116.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8385803" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/drug effects/*genetics/metabolism ; Base Sequence ; Chlorates/pharmacology ; Cloning, Molecular ; DNA/chemistry/genetics ; *DNA Transposable Elements ; Drug Resistance ; *Genes, Plant ; Molecular Sequence Data ; Mutation ; Nitrates/metabolism ; Plants, Genetically Modified
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    Selection of bacterial virulence genes that are specifically induced in host tissues (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: A genetic system was devised that positively selects for bacterial genes that are specifically induced when bacteria infect their host. With the pathogen Salmonella typhimurium, the genes identified by this selection show a marked induction in bacteria recovered from mouse spleen. Mutations in all ivi (in vivo-induced) genes that were tested conferred a defect in virulence. This genetic system was designed to be of general use in a wide variety of bacterial-host systems and has several applications in both vaccine and antimicrobial drug development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahan, M J -- Slauch, J M -- Mekalanos, J J -- AI08245/AI/NIAID NIH HHS/ -- AI26289/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):686-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes, Bacterial ; Cloning, Molecular ; Genes, Bacterial ; Mice ; Mice, Inbred BALB C ; Mutagenesis ; Recombinant Fusion Proteins/metabolism ; Salmonella Infections, Animal/microbiology ; Salmonella typhimurium/*genetics/*pathogenicity ; Virulence/*genetics ; beta-Galactosidase/genetics/metabolism
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    NMR structure of a specific DNA complex of Zn-containing DNA binding domain of GATA-1 (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-07-23
    Description: The three-dimensional solution structure of a complex between the DNA binding domain of the chicken erythroid transcription factor GATA-1 and its cognate DNA site has been determined with multidimensional heteronuclear magnetic resonance spectroscopy. The DNA binding domain consists of a core which contains a zinc coordinated by four cysteines and a carboxyl-terminal tail. The core is composed of two irregular antiparallel beta sheets and an alpha helix, followed by a long loop that leads into the carboxyl-terminal tail. The amino-terminal part of the core, including the helix, is similar in structure, although not in sequence, to the amino-terminal zinc module of the glucocorticoid receptor DNA binding domain. In the other regions, the structures of these two DNA binding domains are entirely different. The DNA target site in contact with the protein spans eight base pairs. The helix and the loop connecting the two antiparallel beta sheets interact with the major groove of the DNA. The carboxyl-terminal tail, which is an essential determinant of specific binding, wraps around into the minor groove. The complex resembles a hand holding a rope with the palm and fingers representing the protein core and the thumb, the carboxyl-terminal tail. The specific interactions between GATA-1 and DNA in the major groove are mainly hydrophobic in nature, which accounts for the preponderance of thymines in the target site. A large number of interactions are observed with the phosphate backbone.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Omichinski, J G -- Clore, G M -- Schaad, O -- Felsenfeld, G -- Trainor, C -- Appella, E -- Stahl, S J -- Gronenborn, A M -- New York, N.Y. -- Science. 1993 Jul 23;261(5120):438-46.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8332909" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Chickens ; DNA-Binding Proteins/*chemistry ; Erythroid-Specific DNA-Binding Factors ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Protein Structure, Tertiary ; Transcription Factors/*chemistry ; Zinc Fingers
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    Crystal structure of neocarzinostatin, an antitumor protein-chromophore complex (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-12
    Description: Structures of the protein-chromophore complex and the apoprotein form of neocarzinostatin were determined at 1.8 angstrom resolution. Neocarzinostatin is composed of a labile chromophore with DNA-cleaving activity and a stabilizing protein. The chromophore displays marked nonlinearity of the triple bonds and is bound noncovalently in a pocket formed by the two protein domains. The chromophore pi-face interacts with the phenyl ring edges of Phe52 and Phe78. The amino sugar and carbonate groups of the chromophore are solvent exposed, whereas the epoxide, acetylene groups, and carbon C-12, the site of nucleophilic thiol addition during chromophore activation, are unexposed. The position of the amino group of the chromophore carbohydrate relative to C-12 supports the idea that the amino group plays a role in thiol activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, K H -- Kwon, B M -- Myers, A G -- Rees, D C -- CA47148/CA/NCI NIH HHS/ -- GM45162/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 12;262(5136):1042-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235619" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/chemistry ; Computer Graphics ; Computer Simulation ; Crystallography, X-Ray ; Hydrogen Bonding ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Zinostatin/*chemistry
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    The nonhelical structure of antifreeze protein type III (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-19
    Description: Antifreeze proteins (AFPs) are present in the blood of some marine fishes and inhibit the growth of ice crystals at subzero temperatures by adsorption to the ice lattice. The solution structure of a Type III AFP was determined by two-dimensional nuclear magnetic resonance spectroscopy. These measurements indicate that this 66-residue protein has an unusual fold in which eight beta strands form two sheets of three antiparallel strands and one sheet of two antiparallel strands, and the triple-stranded sheets are packed orthogonally into a beta sandwich. This structure is completely different from the amphipathic, helical structure observed for Type I AFPs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sonnichsen, F D -- Sykes, B D -- Chao, H -- Davies, P L -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1154-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438165" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antifreeze Proteins ; Cloning, Molecular ; Escherichia coli/genetics ; Fishes ; Freezing ; Genes, Synthetic ; Glycoproteins/*chemistry/genetics ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry
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    Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-05-28
    Description: Transforming growth factor-beta (TGF-beta) affects cellular proliferation, differentiation, and interaction with the extracellular matrix primarily through interaction with the type I and type II TGF-beta receptors. The type II receptors for TGF-beta and activin contain putative serine-threonine kinase domains. A murine serine-threonine kinase receptor, Tsk 7L, was cloned that shared a conserved extracellular domain with the type II TGF-beta receptor. Overexpression of Tsk 7L alone did not increase cell surface binding of TGF-beta, but coexpression with the type II TGF-beta receptor caused TGF-beta to bind to Tsk 7L, which had the size of the type I TGF-beta receptor. Overexpression of Tsk 7L inhibited binding of TGF-beta to the type II receptor in a dominant negative fashion. Combinatorial interactions and stoichiometric ratios between the type I and II receptors may therefore determine the extent of TGF-beta binding and the resulting biological activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebner, R -- Chen, R H -- Shum, L -- Lawler, S -- Zioncheck, T F -- Lee, A -- Lopez, A R -- Derynck, R -- New York, N.Y. -- Science. 1993 May 28;260(5112):1344-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Growth and Development, University of California, San Francisco 94143-0640.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388127" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cercopithecus aethiops ; Cloning, Molecular ; Humans ; Mice ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases ; Quail ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Receptors, Transforming Growth Factor beta ; Transfection ; Transforming Growth Factor beta/*metabolism
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    Release of excess amyloid beta protein from a mutant amyloid beta protein precursor (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-22
    Description: The 4-kilodalton amyloid beta protein (A beta), which forms fibrillar deposits in Alzheimer's disease (AD), is derived from a large protein referred to as the amyloid beta protein precursor (beta APP). Human neuroblastoma (M17) cells transfected with constructs expressing wild-type beta APP or a mutant, beta APP delta NL, recently linked to familial AD were compared. After continuous metabolic labeling for 8 hours, cells expressing beta APP delta NL had five times more of an A beta-bearing, carboxyl terminal, beta APP derivative than cells expressing wild-type beta APP and they released six times more A beta into the medium. Thus this mutant beta APP may cause AD because its processing is altered in a way that releases increased amounts of A beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cai, X D -- Golde, T E -- Younkin, S G -- AG06656/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):514-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8424174" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/genetics/metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides/*biosynthesis/genetics ; Amyloid beta-Protein Precursor/*genetics/metabolism ; Base Sequence ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; *Mutagenesis, Site-Directed ; Neuroblastoma ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Transfection ; Tumor Cells, Cultured
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    "MegaYAC" library (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, G A -- New York, N.Y. -- Science. 1993 May 14;260(5110):877.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493512" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosomes, Fungal ; Cloning, Molecular ; *Gene Library ; *Human Genome Project ; Humans
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    Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-22
    Description: Ethylene behaves as a hormone in plants, regulating such aspects of growth and development as fruit ripening, flower senescence, and abscission. Ethylene insensitivity is conferred by dominant mutations in the ETR1 gene early in the ethylene signal transduction pathway of Arabidopsis thaliana. The ETR1 gene was cloned by the method of chromosome walking. Each of the four known etr1 mutant alleles contains a missense mutation near the amino terminus of the predicted protein. Although the sequence of the amino-terminal half of the deduced ETR1 protein appears to be novel, the carboxyl-terminal half is similar in sequence to both components of the prokaryotic family of signal transducers known as the two-component systems. Thus, an early step in ethylene signal transduction in plants may involve transfer of phosphate as in prokaryotic two-component systems. The dominant etr1-1 mutant gene conferred ethylene insensitivity to wild-type Arabidopsis plants when introduced by transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, C -- Kwok, S F -- Bleecker, A B -- Meyerowitz, E M -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):539-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arabidopsis/*genetics/metabolism ; Bacterial Proteins/chemistry/genetics ; Base Sequence ; Chromosome Walking ; Cloning, Molecular ; Ethylenes/*metabolism/pharmacology ; Genes, Dominant ; *Genes, Plant ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/metabolism ; Protein Kinases/chemistry/genetics ; *Receptors, Cell Surface ; Sequence Alignment ; *Signal Transduction ; Transcription Factors/chemistry/genetics
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    Conformational flexibility of enzyme active sites (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsou, C L -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):380-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211158" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Creatine Kinase/chemistry/metabolism ; Enzyme Inhibitors ; Enzymes/chemistry/*metabolism ; Glyceraldehyde-3-Phosphate Dehydrogenases/chemistry/metabolism ; Guanidine ; Guanidines/pharmacology ; Papain/chemistry/metabolism ; Protein Conformation ; Protein Denaturation ; Protein Folding ; Ribonuclease, Pancreatic/chemistry/metabolism
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    Cyclin-dependent regulation of G1 in mammalian fibroblasts (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-26
    Description: Eukaryotic cells become committed to proliferate during the G1 phase of the cell cycle. In budding yeast, commitment occurs when the catalytic subunit of a protein kinase, encoded by the CDC28 gene (the homolog of the fission yeast cdc2+ gene), binds to a positively acting regulatory subunit, a cyclin. Related kinases are also required for progression through the G1 phase in higher eukaryotes. The role of cyclins in controlling G1 progression in mammalian cells was tested by construction of fibroblasts that constitutively overexpress human cyclin E. This was found to shorten the duration of G1, decrease cell size, and diminish the serum requirement for the transition from G1 to S phase. These observations show that cyclin levels can be rate-limiting for G1 progression in mammalian cells and suggest that cyclin synthesis may be the target of physiological signals that control cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohtsubo, M -- Roberts, J M -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1908-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8384376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/physiology ; Cell Line ; Cloning, Molecular ; Cyclins/genetics/*physiology ; Fibroblasts/*cytology/metabolism ; Flow Cytometry ; G1 Phase/*physiology ; Gene Expression ; Genetic Vectors ; Humans ; Kanamycin Kinase ; Male ; Phosphotransferases/genetics ; Rats ; Recombinant Fusion Proteins/metabolism ; Retroviridae/genetics ; S Phase/physiology ; Time Factors ; Transfection
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    Measuring single protein motors at work (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vale, R D -- New York, N.Y. -- Science. 1993 Apr 9;260(5105):169-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8469971" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/*metabolism ; Dyneins/*metabolism ; Kinesin/*metabolism ; Muscles/*metabolism ; Myosins/metabolism ; Protein Conformation
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    Characterization of a presynaptic glutamate receptor (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-10-15
    Description: Glutamate receptors mediate excitatory neurotransmission in the brain and are important in the formation of memory and in some neurodegenerative disorders. A complementary DNA clone that encoded a 33-kilodalton protein (GR33) was obtained by screening a library with an antibody generated against glutamate binding proteins. The sequence of GR33 is identical to that of the recently reported presynaptic protein syntaxin. When GR33 was expressed in Xenopus oocytes, it formed glutamate-activated ion channels that are pharmacologically similar to those of N-methyl-D-aspartate receptors but with different electrophysiological properties. Mutation of the leucine 278 residue in the single putative transmembrane segment of GR33 affects the properties of the channel. Thus, in vivo GR33 may be a presynaptic glutamate receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smirnova, T -- Stinnakre, J -- Mallet, J -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de genetique moleculaire de la neurotransmission et des processus neurodegeneratifs, Centre National de la Recherche Scientifique (CNRS), Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8105537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Surface/chemistry ; Brain/embryology ; Brain Chemistry ; Calcium/metabolism ; Cells, Cultured ; Cloning, Molecular ; Glutamates/pharmacology ; Glutamic Acid ; Humans ; Membrane Potentials ; Mutagenesis, Site-Directed ; N-Methylaspartate/pharmacology ; Nerve Tissue Proteins/chemistry ; Neurons/chemistry ; Oocytes ; Rats ; Rats, Wistar ; Receptors, Glutamate/chemistry/genetics/*metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Receptors, Presynaptic/chemistry/genetics/*metabolism ; Syntaxin 1 ; Xenopus
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    Structure and functional expression of a member of the low voltage-activated calcium channel family (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-05-21
    Description: Oscillatory firing patterns are an intrinsic property of some neurons and have an important function in information processing. In some cells, low voltage-activated calcium channels have been proposed to underlie a depolarizing potential that regulates bursting. The sequence of a rat brain calcium channel alpha 1 subunit (rbE-II) was deduced. Although it is structurally related to high voltage-activated calcium channels, the rbE-II channel transiently activated at negative membrane potentials, required a strong hyperpolarization to deinactivate, and was highly sensitive to block by nickel. In situ hybridization showed that rbE-II messenger RNA is expressed in regions throughout the central nervous system. The electrophysiological properties of the rbE-II current are consistent with a type of low voltage-activated calcium channel that requires membrane hyperpolarization for maximal activity, which suggests that rbE-II may be involved in the modulation of firing patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soong, T W -- Stea, A -- Hodson, C D -- Dubel, S J -- Vincent, S R -- Snutch, T P -- New York, N.Y. -- Science. 1993 May 21;260(5111):1133-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Laboratory, University of British Columbia, Vancouver, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388125" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Brain Chemistry ; Calcium Channels/*chemistry/genetics/physiology ; Calcium Channels, R-Type ; Cation Transport Proteins ; Cloning, Molecular ; Electric Conductivity ; Hippocampus/chemistry ; In Situ Hybridization ; Membrane Potentials ; Membrane Proteins/*chemistry/genetics/physiology ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/genetics/physiology ; RNA, Messenger/analysis/genetics ; Rats ; Sequence Alignment
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    A first step toward gene therapy for hemophilia B? (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1993 Oct 1;262(5130):29-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Dogs ; Factor IX/biosynthesis/*genetics ; Gene Transfer Techniques ; *Genetic Therapy ; Genetic Vectors ; Hemophilia A/genetics/therapy ; Hemophilia B/genetics/*therapy ; Hepatectomy ; Humans ; Liver/metabolism ; Liver Regeneration ; Retroviridae/genetics
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    Multiple RNA polymerase conformations and GreA: control of the fidelity of transcription (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-05
    Description: Pre-steady state kinetics of misincorporation were used to investigate the addition of single nucleotides to nascent RNA by Escherichia coli RNA polymerase during transcription elongation. The results were fit with a branched kinetic mechanism that permits conformational switching, at each template position, between an activated and an unactivated enzyme complex, both of which can bind nucleotide triphosphates (NTPs) from solution. The complex exists most often in the long-lived activated state, and only becomes unactivated when transcription is slowed. This model permits multiple levels of nucleotide discrimination in transcription, since the complex can be "kinetically trapped" in the unactivated state in the absence of the correct NTP or if the 3' terminal residue is incorrectly matched. The transcription cleavage factor GreA (or an activity enhanced by GreA) increased the fidelity of transcription by preferential cleavage of transcripts containing misincorporated residues in the unactivated state of the elongation complex. This cleavage mechanism by GreA may prevent the formation of "dead-end" transcription complexes in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erie, D A -- Hajiseyedjavadi, O -- Young, M C -- von Hippel, P H -- GM-12915/GM/NIGMS NIH HHS/ -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):867-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235608" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Endoribonucleases/metabolism ; Escherichia coli/enzymology ; *Escherichia coli Proteins ; Kinetics ; Models, Genetic ; Molecular Sequence Data ; Nucleotides/metabolism ; Peptide Elongation Factors/*metabolism ; Protein Conformation ; RNA, Messenger/*biosynthesis/metabolism ; Templates, Genetic ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Uridine Triphosphate/metabolism
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    A role for the transcription factors Mbp1 and Swi4 in progression from G1 to S phase (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-09-17
    Description: In budding yeast genes that encode G1 cyclins and proteins involved in DNA synthesis are transcriptionally activated in late G1. A transcription factor, called SBF, is composed of Swi4 and Swi6 proteins and activates transcription of G1 cyclin genes. A different, but related, complex called MBF binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. MBF contains Swi6 and a 120-kilodalton protein (p120). MBF was purified and the gene encoding p120 (termed MBP1) was cloned. A deletion of MBP1 was not lethal but led to deregulated expression of DNA synthesis genes, indicating a direct regulatory role for MBF in MCB-driven transcription. Mbp1 is related to Swi4. Strains deleted for both MBP1 and SWI4 were inviable, demonstrating that transcriptional activation by MBF and SBF has an important role in the transition from G1 to S phase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, C -- Moll, T -- Neuberg, M -- Ahorn, H -- Nasmyth, K -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1551-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Pathology, Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372350" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; CDC28 Protein Kinase, S cerevisiae/genetics/metabolism ; Cloning, Molecular ; Cyclins/genetics ; DNA, Fungal/biosynthesis ; DNA-Binding Proteins ; Fungal Proteins/chemistry/*genetics/metabolism ; *G1 Phase ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Promoter Regions, Genetic ; *S Phase ; Saccharomyces cerevisiae/cytology/*genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Transcription Factors/chemistry/*genetics/metabolism
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    Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-08-06
    Description: Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ravichandran, K G -- Boddupalli, S S -- Hasermann, C A -- Peterson, J A -- Deisenhofer, J -- GM43479/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Aug 6;261(5122):731-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8342039" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; Binding Sites ; Computer Graphics ; Crystallization ; Cytochrome P-450 Enzyme System/*chemistry ; Heme/chemistry ; Mixed Function Oxygenases/*chemistry ; Models, Molecular ; Molecular Sequence Data ; NADPH-Ferrihemoprotein Reductase ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; X-Ray Diffraction
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    TH1 and TH2 cell antigen receptors in experimental leishmaniasis (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-05
    Description: The complexity and chronicity of parasitic infections have obscured the identification of biologically relevant antigens. Analysis of the T cell receptor repertoire used by mice infected with Leishmania major revealed the expansion of a restricted population of CD4+ cells. These cells expressed the V alpha 8-J alpha TA72, V beta 4 heterodimer in both progressive infection and protective immunity and across several major histocompatibility haplotypes. Thus, the same immunodominant parasite epitope drives the disparate outcomes of this infectious process, suggesting that candidate vaccine antigens selected by screening of immune individuals may be capable of exacerbating disease in genetically susceptible individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reiner, S L -- Wang, Z E -- Hatam, F -- Scott, P -- Locksley, R M -- AI30663/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1457-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8451641" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/analysis ; Base Sequence ; Cloning, Molecular ; *Leishmania tropica ; Leishmaniasis, Cutaneous/*immunology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; RNA, Messenger/genetics/isolation & purification ; Receptors, Antigen, T-Cell/analysis/genetics/*metabolism ; Receptors, Antigen, T-Cell, alpha-beta/analysis/genetics/*metabolism ; Reference Values ; T-Lymphocyte Subsets/immunology
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    Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-26
    Description: To identify the gene or genes associated with insulin resistance in Type II (non-insulin-dependent) diabetes mellitus, subtraction libraries were prepared from skeletal muscle of normal and diabetic humans and screened with subtracted probes. Only one clone out of 4000 was selectively overexpressed in Type II diabetic muscle as compared to muscle of non-diabetic or Type I diabetic individuals. This clone encoded a new 29-kilodalton member of the Ras-guanosine triphosphatase superfamily and was termed Rad (Ras associated with diabetes). Messenger ribonucleic acid of Rad was expressed primarily in skeletal and cardiac muscle and was increased an average of 8.6-fold in the muscle of Type II diabetics as compared to normal individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reynet, C -- Kahn, C R -- DK 36836/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1441-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Division, Joslin Diabetes Center, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248782" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Blotting, Southern ; Chromosome Aberrations ; Cloning, Molecular ; Diabetes Mellitus, Type 2/*genetics/metabolism ; GTP Phosphohydrolases/biosynthesis/chemistry/genetics ; GTP-Binding Proteins/biosynthesis/chemistry/*genetics ; Gene Amplification ; *Genes ; Humans ; Insulin Resistance/*genetics ; Molecular Sequence Data ; Muscles/*metabolism ; RNA, Messenger/analysis/genetics ; *ras Proteins
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    Structural basis of pilus subunit recognition by the PapD chaperone (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-19
    Description: The assembly of different types of virulence-associated surface fibers called pili in Gram-negative bacteria requires periplasmic chaperones. PapD is the prototype member of the periplasmic chaperone family, and the structural basis of its interactions with pilus subunits was investigated. Peptides corresponding to the carboxyl terminus of pilus subunits bound PapD and blocked the ability of PapD to bind to the pilus adhesin PapG in vitro. The crystal structure of PapD complexed to the PapG carboxyl-terminal peptide was determined to 3.0 A resolution. The peptide bound in an extended conformation with its carboxyl terminus anchored in the interdomain cleft of the chaperone via hydrogen bonds to invariant chaperone residues Arg8 and Lys112. Main chain hydrogen bonds and contacts between hydrophobic residues in the peptide and the chaperone stabilized the complex and may play a role in determining binding specificity. Site-directed mutations in Arg8 and Lys112 abolished the ability of PapD to bind pilus subunits and mediate pilus assembly in vivo, an indication that the PapD-peptide crystal structure is a reflection of at least part of the PapD-subunit interaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuehn, M J -- Ogg, D J -- Kihlberg, J -- Slonim, L N -- Flemmer, K -- Bergfors, T -- Hultgren, S J -- AI07172/AI/NIAID NIH HHS/ -- R01AI29549/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 19;262(5137):1234-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7901913" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry/*metabolism ; Base Sequence ; Chaperonins ; Crystallography, X-Ray ; *Escherichia coli Proteins ; Fimbriae, Bacterial/*metabolism ; Hydrogen Bonding ; Models, Molecular ; *Molecular Chaperones ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Peptide Fragments/chemistry/metabolism ; *Periplasmic Proteins ; Protein Conformation ; Protein Structure, Secondary ; Proteins/chemistry/*metabolism
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    Database contamination (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-04-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mistry, A -- Greenlee, R -- Fong, K -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):605-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480169" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; *Dna ; DNA Probes ; Databases, Factual ; *Gene Library ; Quality Control ; RNA, Fungal/genetics ; RNA, Transfer/genetics
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  • 143
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    Phosphatidylinositol 4-kinase: gene structure and requirement for yeast cell viability (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-26
    Description: Phosphatidylinositol (PtdIns) 4-kinase catalyzes the first step in the biosynthesis of PtdIns-4,5-bisphosphate (PtdIns[4,5]P2). Hydrolysis of PtdIns[4,5]P2 in response to extracellular stimuli is thought to initiate intracellular signaling cascades that modulate cell proliferation and differentiation. The PIK1 gene encoding a PtdIns 4-kinase from the yeast Saccharomyces cerevisiae was isolated by polymerase chain reaction (PCR) with oligonucleotides based on the sequence of peptides derived from the purified enzyme. The sequence of the PIK1 gene product bears similarities to that of PtdIns 3-kinases from mammals (p110) and yeast (Vps34p). Expression of PIK1 from a multicopy plasmid elevated PtdIns 4-kinase activity and enhanced the response to mating pheromone. A pik1 null mutant was inviable, indicating that PtdIns4P and presumably PtdIns[4,5]P2 are indispensable phospholipids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flanagan, C A -- Schnieders, E A -- Emerick, A W -- Kunisawa, R -- Admon, A -- Thorner, J -- CA09041/CA/NCI NIH HHS/ -- GM07232/GM/NIGMS NIH HHS/ -- GM21841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1444-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248783" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Phosphatidylinositol 4-Kinase ; Amino Acid Sequence ; Cloning, Molecular ; Gene Expression ; *Genes, Fungal ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositol Phosphates/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/biosynthesis/chemistry/*genetics ; Polymerase Chain Reaction ; Saccharomyces cerevisiae/enzymology/*genetics/growth & development ; *Saccharomyces cerevisiae Proteins
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  • 144
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    The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-26
    Description: The glycosylphosphatidylinositol (GPI) anchor is a membrane attachment structure of many proteins and occurs in a wide variety of eukaryotes from yeasts to mammals. The structure of the core of the GPI anchor is conserved in protozoa and mammals and so is its biosynthetic pathway. A complementary DNA encoding a human protein termed PIG-A (phosphatidylinositol glycan-class A) was cloned. PIG-A was necessary for synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyata, T -- Takeda, J -- Iida, Y -- Yamada, N -- Inoue, N -- Takahashi, M -- Maeda, K -- Kitani, T -- Kinoshita, T -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1318-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunoregulation, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7680492" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/metabolism ; Antigens, CD55 ; Antigens, CD59 ; Antigens, Surface/metabolism ; Antigens, Thy-1 ; Cloning, Molecular ; DNA/genetics ; Genetic Complementation Test ; Glycosylphosphatidylinositols/*biosynthesis ; HeLa Cells ; Humans ; In Vitro Techniques ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Sequence Data ; Solubility ; Species Specificity
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  • 145
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    The role of backbone flexibility in the accommodation of variants that repack the core of T4 lysozyme (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-12-10
    Description: To understand better how the packing of side chains within the core influences protein structure and stability, the crystal structures were determined for eight variants of T4 lysozyme, each of which contains three to five substitutions at adjacent interior sites. Concerted main-chain and side-chain displacements, with movements of helical segments as large as 0.8 angstrom, were observed. In contrast, the angular conformations of the mutated side chains tended to remain unchanged, with torsion angles within 20 degrees of those in the wild-type structure. These observations suggest that not only the rotation of side chains but also movements of the main chain must be considered in the evaluation of which amino acid sequences are compatible with a given protein fold.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baldwin, E P -- Hajiseyedjavadi, O -- Baase, W A -- Matthews, B W -- GM12989/GM/NIGMS NIH HHS/ -- GM21967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Dec 10;262(5140):1715-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Howard Hughes Medical Institute, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8259514" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage T4/*enzymology ; Crystallography, X-Ray ; Muramidase/*chemistry/genetics/metabolism ; Mutagenesis ; Mutation ; Protein Conformation ; Protein Structure, Secondary ; Structure-Activity Relationship
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  • 146
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    Inhibition of an in vivo antigen-specific IgE response by antibodies to CD23 (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-08-20
    Description: Immunoglobulin E (IgE) mediates many allergic responses. CD23 is a 45-kilodalton type II transmembrane glycoprotein expressed in many cell types. It is a low-affinity IgE receptor and interacts specifically with CD21, thereby modulating IgE production by B lymphocytes in vitro. In an in vivo model of an allergen-specific IgE response, administration of a rabbit polyclonal antibody to recombinant human truncated CD23 resulted in up to 90 percent inhibition of ovalbumin-specific IgE synthesis. Both Fabs and intact IgG inhibited IgE production in vitro and in vivo. Thus, CD23 participates in the regulation of IgE synthesis in vivo and so could be important in allergic disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flores-Romo, L -- Shields, J -- Humbert, Y -- Graber, P -- Aubry, J P -- Gauchat, J F -- Ayala, G -- Allet, B -- Chavez, M -- Bazin, H -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1038-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Institute for Molecular Biology, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/*immunology ; B-Lymphocytes/immunology ; Cloning, Molecular ; Humans ; Immunization ; Immunoglobulin E/*biosynthesis ; Molecular Sequence Data ; Ovalbumin/immunology ; Rabbits ; Rats ; Receptors, Complement 3d/immunology ; Receptors, IgE/analysis/*immunology ; Recombinant Proteins/immunology ; Virulence Factors, Bordetella/immunology
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  • 147
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    Reductase activity encoded by the HM1 disease resistance gene in maize (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-06
    Description: The HM1 gene in maize controls both race-specific resistance to the fungus Cochliobolus carbonum race 1 and expression of the NADPH (reduced form of nicotinamide adenine dinucleotide phosphate)-dependent HC toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus to permit infection. Several HM1 alleles were generated and cloned by transposon-induced mutagenesis. The sequence of wild-type HM1 shares homology with dihydroflavonol-4-reductase genes from maize, petunia, and snap-dragon. Sequence homology is greatest in the beta alpha beta-dinucleotide binding fold that is conserved among NADPH- and NADH (reduced form of nicotinamide adenine dinucleotide)-dependent reductases and dehydrogenases. This indicates that HM1 encodes HCTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johal, G S -- Briggs, S P -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):985-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology Research, Pioneer Hi-Bred International, Inc., Johnston, IA 50131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA/chemistry/genetics ; *Genes, Plant ; *Helminthosporium ; Introns ; Molecular Sequence Data ; NADP/pharmacology ; Nucleic Acid Hybridization ; Oxidoreductases/chemistry/*genetics ; Peptides, Cyclic/antagonists & inhibitors ; *Plant Diseases ; *Plant Proteins ; Polymorphism, Restriction Fragment Length ; RNA Splicing ; RNA, Messenger/genetics ; Zea mays/enzymology/*genetics
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    The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-21
    Description: The fms-like tyrosine kinase (Flt) is a transmembrane receptor in the tyrosine kinase family. Expression of flt complementary DNA in COS cells conferred specific, high-affinity binding of vascular endothelial growth factor, also known as vascular permeability factor (VEGF-VPF), a factor that induces vascular permeability when injected in the guinea pig skin and stimulates endothelial cell proliferation. Expression of Flt in Xenopus laevis oocytes caused the oocytes to release calcium in response to VEGF-VPF. These findings show that flt encodes a receptor for VEGF-VPF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vries, C -- Escobedo, J A -- Ueno, H -- Houck, K -- Ferrara, N -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):989-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cross-Linking Reagents ; Endothelial Growth Factors/*physiology ; Enzyme Activation ; Humans ; In Vitro Techniques ; Lymphokines/*physiology ; Proto-Oncogene Proteins/genetics/*physiology ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Transfection ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 ; Vascular Endothelial Growth Factors ; Xenopus laevis
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  • 149
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    Three-dimensional structure of dimeric human recombinant macrophage colony-stimulating factor (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-20
    Description: Macrophage colony-stimulating factor (M-CSF) triggers the development of cells of the monocyte-macrophage lineage and has a variety of stimulatory effects on mature cells of this class. The biologically active form of M-CSF is a disulfide-linked dimer that activates an intrinsic tyrosine kinase activity on the M-CSF receptor by inducing dimerization of the receptor molecules. The structure of a recombinant human M-CSF dimer, determined at 2.5 angstroms by x-ray crystallography, contains two bundles of four alpha helices laid end-to-end, with an interchain disulfide bond. Individual monomers of M-CSF show a close structural similarity to the cytokines granulocyte-macrophage colony-stimulating factor and human growth hormone. Both of these cytokines are monomeric in their active form, and their specific receptors lack intrinsic tyrosine kinase activity. The similarity of these structures suggests that the receptor binding determinants for all three cytokines may be similar.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pandit, J -- Bohm, A -- Jancarik, J -- Halenbeck, R -- Koths, K -- Kim, S H -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1358-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Structural Biology Division, Lawrence Berkeley Laboratory, Berkeley, CA 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455231" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography ; Disulfides ; Granulocyte-Macrophage Colony-Stimulating Factor/ultrastructure ; Growth Hormone/chemistry ; Macrophage Colony-Stimulating Factor/*ultrastructure ; Models, Molecular ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Proteins/ultrastructure ; Sequence Homology, Amino Acid ; X-Ray Diffraction
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  • 150
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    Spatial control of the gap gene knirps in the Drosophila embryo by posterior morphogen system (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-21
    Description: The gap genes of Drosophila are the first zygotic genes to respond to the maternal positional signals and establish the body pattern along the anterior-posterior axis. The gap gene knirps, required for patterning in the posterior region of the embryo, can be activated throughout the wild-type embryo and is normally repressed from the anterior and posterior sides. These results provide direct molecular evidence that the posterior morphogen system interacts in a fundamentally different manner than do hunchback and bicoid, which are responsible for anterior pattern formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pankratz, M J -- Busch, M -- Hoch, M -- Seifert, E -- Jackle, H -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):986-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546296" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Drosophila melanogaster/embryology/*genetics ; Gene Expression Regulation ; Genes ; Molecular Sequence Data ; Morphogenesis ; Regulatory Sequences, Nucleic Acid
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    Nucleotide-iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125 (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-06
    Description: Electron transfer in nitrogenase involves a gating process initiated by MgATP (magnesium adenosine triphosphate) binding to Fe-protein. The redox site, an 4Fe:4S cluster, is structurally separated from the MgATP binding site. For MgATP hydrolysis to be coupled to electron transfer, a signal transduction mechanism is proposed that is similar to that in guanosine triphosphatase proteins. Based on the three-dimensional structure of Fe-protein, Asp125 is likely to be part of a putative transduction path. Altered Fe-protein with Glu replacing Asp has been prepared and retains the ability for the initial nucleotide-dependent conformational change. However, either MgADP or MgATP can induce the shift and Mg binding to the nucleotide is no longer essential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolle, D -- Dean, D R -- Howard, J B -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):992-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Minnesota, Minneapolis 55455.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359643" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/*metabolism ; Aspartic Acid/*metabolism ; Azotobacter vinelandii/enzymology ; Binding Sites ; Crystallization ; Electron Transport ; Glutamates ; Glutamic Acid ; Iron-Sulfur Proteins/*metabolism ; Molecular Structure ; Mutagenesis, Site-Directed ; Nitrogenase/chemistry/genetics/*metabolism ; Protein Conformation ; Signal Transduction/*physiology
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  • 152
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    Predicted structural similarities of the DNA binding domains of c-Myc and endonuclease Eco RI (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-24
    Description: The c-Myc oncoprotein belongs to a family of proteins whose DNA binding domains contain a basic region-helix-loop-helix (bHLH) motif. Systematic mutagenesis of c-Myc revealed that dimerized bHLH motifs formed a parallel four-helix bundle with the amino termini of helices 1 and 2 directed toward the inner and outer nucleotides of the DNA binding site, respectively. Both the basic region and the carboxyl-terminal end of the loop contributed to DNA binding specificity. The DNA binding domain of c-Myc may therefore be structurally similar to that of restriction endonuclease Eco RI.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Halazonetis, T D -- Kandil, A N -- New York, N.Y. -- Science. 1992 Jan 24;255(5043):464-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Research, Merck Sharp and Dohme Research Laboratories, West Point, PA 19486.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1734524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA-Binding Proteins/*chemistry ; Deoxyribonuclease EcoRI/*chemistry ; Humans ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Protein Conformation ; Proto-Oncogene Proteins c-myc/*chemistry ; Sequence Alignment ; Transcription Factors/chemistry
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    Isolation of two genes that encode subunits of the yeast transcription factor IIA (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-28
    Description: The yeast transcription factor IIA (TFIIA), a component of the basal transcription machinery of RNA polymerase II and implicated in vitro in regulation of basal transcription, is composed of two subunits of 32 and 13.5 kilodaltons. The genes that encode these subunits, termed TOA1 and TOA2, respectively, were cloned. Neither gene shares obvious sequence similarity with the other or with any other previously identified genes. The recombinant factor bound to a TATA binding protein-DNA complex and complemented yeast and mammalian in vitro transcription systems depleted of TFIIA. Both the TOA1 and TOA2 genes are essential for growth of yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranish, J A -- Lane, W S -- Hahn, S -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; DNA Mutational Analysis ; DNA-Binding Proteins/genetics ; *Genes, Fungal ; Molecular Sequence Data ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; Transcription Factor TFIIA ; Transcription Factors/*genetics ; Transcription, Genetic
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  • 154
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    Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: A Src homology 3 (SH3) region is a sequence of approximately 50 amino acids found in many nonreceptor tyrosine kinases and other proteins. Deletion of the SH3 region from the protein encoded by the c-abl proto-oncogene activates the protein's transforming capacity, thereby suggesting the participation of the SH3 region in the negative regulation of transformation. A complementary DNA was isolated that encoded a protein, 3BP-1, to which the SH3 region of Abl bound with high specificity and to which SH3 regions from other proteins bound differentially. The sequence of the 3BP-1 protein is similar to that of a COOH-terminal segment of Bcr and to guanosine triphosphatase-activating protein (GAP)-rho, which suggests that it might have GAP activity for Ras-related proteins. The 3BP-1 protein may therefore be a mediator of SH3 function in transformation inhibition and may link tyrosine kinases to Ras-related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cicchetti, P -- Mayer, B J -- Thiel, G -- Baltimore, D -- A107233/PHS HHS/ -- CA 08875/CA/NCI NIH HHS/ -- CA51462/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):803-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1379745" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Binding Sites ; Chimera ; Cloning, Molecular ; GTPase-Activating Proteins ; Gene Library ; *Genes, abl ; *Genes, src ; Glutathione Transferase/genetics/metabolism ; Mice ; Molecular Sequence Data ; Oncogene Proteins/genetics/*metabolism ; Plasmids ; Polymerase Chain Reaction/methods ; Prosencephalon/physiology ; Protein-Tyrosine Kinases/*metabolism ; Proteins/*metabolism ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-abl/genetics/*metabolism ; Proto-Oncogene Proteins c-bcr ; Proto-Oncogene Proteins pp60(c-src)/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Restriction Mapping ; Rho Factor/*metabolism ; Sequence Homology, Nucleic Acid ; ras GTPase-Activating Proteins
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  • 155
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    Converting trypsin to chymotrypsin: the role of surface loops (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-06
    Description: Trypsin (Tr) and chymotrypsin (Ch) have similar tertiary structures, yet Tr cleaves peptides at arginine and lysine residues and Ch prefers large hydrophobic residues. Although replacement of the S1 binding site of Tr with the analogous residues of Ch is sufficient to transfer Ch specificity for ester hydrolysis, specificity for amide hydrolysis is not transferred. Trypsin is converted to a Ch-like protease when the binding pocket alterations are further modified by exchange of the Ch surface loops 185 through 188 and 221 through 225 for the analogous Tr loops. These loops are not structural components of either the S1 binding site or the extended substrate binding sites. This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired. Like Ch, this mutant utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedstrom, L -- Szilagyi, L -- Rutter, W J -- DK21344/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1249-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143-0534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546324" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chymotrypsin/*chemistry/metabolism ; Hydrolysis ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Protein Conformation ; Substrate Specificity ; Trypsin/*chemistry/genetics/metabolism
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  • 156
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    Molecular cloning of the interleukin-1 beta converting enzyme (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-04-03
    Description: Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA encoding a protease that carries out this cleavage has been cloned. Recombinant expression in COS-7 cells enabled the cells to process precursor IL-1 beta to the mature form. Sequence analysis indicated that the enzyme itself may undergo proteolytic processing. The gene encoding the protease was mapped to chromosomal band 11q23, a site frequently involved in rearrangement in human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerretti, D P -- Kozlosky, C J -- Mosley, B -- Nelson, N -- Van Ness, K -- Greenstreet, T A -- March, C J -- Kronheim, S R -- Druck, T -- Cannizzaro, L A -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caspase 1 ; Cell Line ; Chromosome Banding ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Enzyme Precursors/biosynthesis/*genetics/isolation & purification ; Humans ; Metalloendopeptidases/biosynthesis/*genetics/isolation & purification ; Molecular Sequence Data ; Neutrophils/enzymology ; Oligodeoxyribonucleotides ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Recombinant Proteins/biosynthesis/isolation & purification ; Transfection
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  • 157
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    Regulatory elements that control the lineage-specific expression of myoD (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-04
    Description: The molecular basis of skeletal muscle lineage determination was investigated by analyzing DNA control elements that regulate the myogenic determination gene myoD. A distal enhancer was identified that positively regulates expression of the human myoD gene. The myoD enhancer and promoter were active in myogenic and several nonmyogenic cell lines. In transgenic mouse embryos, however, the myoD enhancer and promoter together directed expression of a lacZ transgene specifically to the skeletal muscle lineage. These data suggest that during development myoD is regulated by mechanisms that restrict accessibility of myoD control elements to positive trans-acting factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldhamer, D J -- Faerman, A -- Shani, M -- Emerson, C P Jr -- CA-06927/CA/NCI NIH HHS/ -- HD-07796/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):538-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315077" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Humans ; Mice ; Mice, Transgenic ; Muscle Proteins/*genetics ; Muscles/embryology/metabolism ; MyoD Protein ; Promoter Regions, Genetic ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; beta-Galactosidase/genetics
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  • 158
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    Awakenings ... UV light and HIV gene activation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, B M -- Lasker, J S -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1211-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519057" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/radiation effects ; DNA Damage ; Gene Expression/*radiation effects ; Genes, Viral/*radiation effects ; HIV/*genetics ; HIV Long Terminal Repeat ; Humans ; Mice ; PUVA Therapy/adverse effects ; Sunlight/adverse effects ; Ultraviolet Rays/*adverse effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 159
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    Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-15
    Description: A facile method for isolating genes that encode interacting proteins has been developed with a polypeptide probe that contains an amino-terminal extension with recognition sites for a monoclonal antibody, a specific endopeptidase, and a site-specific protein kinase. This probe, containing the basic region-leucine zipper dimerization motif of c-Fos, was used to screen a complementary DNA library. A complementary DNA that encoded a member of the basic-helix-loop-helix-zipper (bHLH-Zip) family of proteins was isolated. The complementary DNA-encoded polypeptide FIP (Fos interacting protein) bound to oligonucleotide probes that contained DNA binding motifs for other HLH proteins. When cotransfected with c-Fos, FIP stimulated transcription of an AP-1-responsive promoter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blanar, M A -- Rutter, W J -- DK-21344/DK/NIDDK NIH HHS/ -- DK-41822/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 May 15;256(5059):1014-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589769" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Cloning, Molecular ; DNA/isolation & purification ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; *Genes, fos/genetics ; HeLa Cells ; Humans ; Leucine Zippers/*genetics ; Macromolecular Substances ; Molecular Sequence Data ; Oligonucleotide Probes/chemistry/metabolism ; Protein Conformation ; Proto-Oncogene Proteins c-fos/chemistry/metabolism ; Proto-Oncogene Proteins c-jun/chemistry/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 160
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    Electron-tunneling pathways in proteins (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-12-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beratan, D N -- Onuchic, J N -- Winkler, J R -- Gray, H B -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1740-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Pittsburgh, PA 15260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1334572" target="_blank"〉PubMed〈/a〉
    Keywords: Cytochrome c Group/*chemistry/metabolism ; Cytochrome-c Peroxidase/*chemistry/metabolism ; *Electron Transport ; Models, Molecular ; Photosynthesis ; Protein Conformation ; Proteins/*chemistry ; Saccharomyces cerevisiae/metabolism ; X-Ray Diffraction
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  • 161
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    GAP domains responsible for ras p21-dependent inhibition of muscarinic atrial K+ channel currents (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-10
    Description: The interaction between the low molecular weight G protein ras p21 and a guanosine triphosphatase activating protein (GAP) uncouples a heterotrimeric G protein (Gk) from muscarinic receptors. Through the use of isolated atrial cell membranes and genetically engineered GAP deletion mutants, the src homology regions (SH2-SH3) at the amino terminus of GAP have been identified as the domains responsible for this effect. Deletion of the domain required to stimulate the guanosine triphosphatase activity of ras p21 relieves the requirement for ras p21 in this system. A model is presented that suggests that ras p21 induces a conformational change in GAP, which allows the SH2-SH3 regions of GAP to function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, G A -- Yatani, A -- Clark, R -- Conroy, L -- Polakis, P -- Brown, A M -- McCormick, F -- CA51992-01/CA/NCI NIH HHS/ -- HL36930/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):192-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553544" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Baculoviridae ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; GTP-Binding Proteins/*physiology ; GTPase-Activating Proteins ; Genetic Engineering ; Genetic Vectors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Guinea Pigs ; Heart/*physiology ; Heart Atria ; Models, Biological ; Polymerase Chain Reaction ; Potassium Channels/drug effects/*physiology ; Proteins/genetics/*physiology ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Receptors, Muscarinic/drug effects/*physiology ; ras GTPase-Activating Proteins
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  • 162
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    On the other hand (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petsko, G A -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1403-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/chemistry ; Enzymes/*chemistry/metabolism ; *Functional Laterality ; HIV Protease/chemical synthesis/*chemistry ; Humans ; *Isomerism ; Protein Conformation
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  • 163
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    Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-10
    Description: Six "cavity-creating" mutants, Leu46----Ala (L46A), L99A, L118A, L121A, L133A, and Phe153----Ala (F153A), were constructed within the hydrophobic core of phage T4 lysozyme. The substitutions decreased the stability of the protein at pH 3.0 by different amounts, ranging from 2.7 kilocalories per mole (kcal mol-1) for L46A and L121A to 5.0 kcal mol-1 for L99A. The double mutant L99A/F153A was also constructed and decreased in stability by 8.3 kcal mol-1. The x-ray structures of all of the variants were determined at high resolution. In every case, removal of the wild-type side chain allowed some of the surrounding atoms to move toward the vacated space but a cavity always remained, which ranged in volume from 24 cubic angstroms (A3) for L46A to 150 A3 for L99A. No solvent molecules were observed in any of these cavities. The destabilization of the mutant Leu----Ala proteins relative to wild type can be approximated by a constant term (approximately 2.0 kcal mol-1) plus a term that increases in proportion to the size of the cavity. The constant term is approximately equal to the transfer free energy of leucine relative to alanine as determined from partitioning between aqueous and organic solvents. The energy term that increases with the size of the cavity can be expressed either in terms of the cavity volume (24 to 33 cal mol-1 A-3) or in terms of the cavity surface area (20 cal mol-1 A-2). The results suggest how to reconcile a number of conflicting reports concerning the strength of the hydrophobic effect in proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eriksson, A E -- Baase, W A -- Zhang, X J -- Heinz, D W -- Blaber, M -- Baldwin, E P -- Matthews, B W -- GM12989/GM/NIGMS NIH HHS/ -- GM13709/GM/NIGMS NIH HHS/ -- GM21967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):178-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, Howard Hughes Medical Institute, Eugene, OR.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553543" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calorimetry ; Models, Molecular ; Molecular Sequence Data ; Muramidase/*chemistry/*genetics ; Mutagenesis, Site-Directed ; Protein Conformation ; Structure-Activity Relationship ; T-Phages/enzymology/genetics ; Thermodynamics ; X-Ray Diffraction
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  • 164
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    An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-03
    Description: Aldose reductase, which catalyzes the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH)-dependent reduction of a wide variety of aromatic and aliphatic carbonyl compounds, is implicated in the development of diabetic and galactosemic complications involving the lens, retina, nerves, and kidney. A 1.65 angstrom refined structure of a recombinant human placenta aldose reductase reveals that the enzyme contains a parallel beta 8/alpha 8-barrel motif and establishes a new motif for NADP-binding oxidoreductases. The substrate-binding site is located in a large, deep elliptical pocket at the COOH-terminal end of the beta barrel with a bound NADPH in an extended conformation. The highly hydrophobic nature of the active site pocket greatly favors aromatic and apolar substrates over highly polar monosaccharides. The structure should allow for the rational design of specific inhibitors that might provide molecular understanding of the catalytic mechanism, as well as possible therapeutic agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, D K -- Bohren, K M -- Gabbay, K H -- Quiocho, F A -- DK-39,044/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):81-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621098" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde Reductase/*chemistry/metabolism ; Amino Acid Sequence ; Binding Sites ; *Diabetes Complications ; Diabetes Mellitus/*enzymology ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; X-Ray Diffraction/methods
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  • 165
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    How technique is changing science (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, S S -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):344-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/analysis ; Drosophila/genetics ; Fiber Optic Technology ; Microscopy/methods ; Polymerase Chain Reaction ; Radioimmunoassay ; Research/instrumentation ; *Research Design
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  • 166
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    Site-specific incorporation of novel backbone structures into proteins (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-10
    Description: A number of unnatural amino acids and amino acid analogs with modified backbone structures were substituted for alanine-82 in T4 lysozyme. Replacements included alpha,alpha-disubstituted amino acids, N-alkyl amino acids, and lactic acid, an isoelectronic analog of alanine. The effects of these electronic and structural perturbations on the stability of T4 lysozyme were determined. The relatively broad substrate specificity of the Escherichia coli protein biosynthetic machinery suggests that a wide range of backbone and side-chain substitutions can be introduced, allowing a more precise definition of the factors affecting protein stability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ellman, J A -- Mendel, D -- Schultz, P G -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):197-200.〈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/1553546" target="_blank"〉PubMed〈/a〉
    Keywords: *Alanine ; Amino Acid Sequence ; *Amino Acids ; Circular Dichroism ; Codon ; Enzyme Stability ; Escherichia coli/enzymology/genetics ; Muramidase/*biosynthesis/*chemistry/genetics ; *Mutagenesis, Site-Directed ; Protein Conformation ; Structure-Activity Relationship ; Substrate Specificity ; T-Phages/enzymology
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  • 167
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    Interaction of p107 with cyclin A independent of complex formation with viral oncoproteins (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-03
    Description: The p107 protein and the retinoblastoma protein (RB) both bind specifically to two viral oncoproteins, the SV40 T antigen (T) and adenoviral protein E1A (E1A). Like RB, p107 contains a segment (the pocket) that, alone, can bind specifically to T, E1A, and multiple cellular proteins. Cyclin A bound to the p107 pocket, but not the RB pocket. Although both pockets contain two, related collinear subsegments (A and B), the unique sequence in the p107 pocket that occupies the space between A and B is required for the interaction with cyclin A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ewen, M E -- Faha, B -- Harlow, E -- Livingston, D M -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):85-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1532457" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus Early Proteins ; Amino Acid Sequence ; Antigens, Polyomavirus Transforming/*metabolism ; Base Sequence ; Binding Sites ; Cell Line ; Cloning, Molecular ; Cyclins/*metabolism ; Escherichia coli/genetics ; Eye Neoplasms ; Glutathione Transferase/genetics/metabolism ; Humans ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; *Nuclear Proteins ; Oligodeoxyribonucleotides ; Oncogene Proteins, Viral/genetics/*metabolism ; Protein Conformation ; Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoblastoma ; Retinoblastoma Protein/genetics/*metabolism ; Retinoblastoma-Like Protein p107 ; Structure-Activity Relationship
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  • 168
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    Cloning and characterization of inducible nitric oxide synthase from mouse macrophages (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Nitric oxide (NO) conveys a variety of messages between cells, including signals for vasorelaxation, neurotransmission, and cytotoxicity. In some endothelial cells and neurons, a constitutive NO synthase is activated transiently by agonists that elevate intracellular calcium concentrations and promote the binding of calmodulin. In contrast, in macrophages, NO synthase activity appears slowly after exposure of the cells to cytokines and bacterial products, is sustained, and functions independently of calcium and calmodulin. A monospecific antibody was used to clone complementary DNA that encoded two isoforms of NO synthase from immunologically activated mouse macrophages. Liquid chromatography-mass spectrometry was used to confirm most of the amino acid sequence. Macrophage NO synthase differs extensively from cerebellar NO synthase. The macrophage enzyme is immunologically induced at the transcriptional level and closely resembles the enzyme in cytokine-treated tumor cells and inflammatory neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, Q W -- Cho, H J -- Calaycay, J -- Mumford, R A -- Swiderek, K M -- Lee, T D -- Ding, A -- Troso, T -- Nathan, C -- AI30165/AI/NIAID NIH HHS/ -- CA43610/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beatrice and Samuel A. Seaver Laboratory, Department of Medicine, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373522" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/biosynthesis/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Codon ; Enzyme Induction ; Interferon-gamma/pharmacology ; Isoenzymes/biosynthesis/*genetics ; Kinetics ; Lipopolysaccharides ; Macrophages/drug effects/*enzymology ; Mammary Neoplasms, Experimental ; Mice ; Molecular Sequence Data ; Molecular Weight ; Neutrophils/drug effects/enzymology ; Nitric Oxide Synthase ; Oligodeoxyribonucleotides ; Poly A/genetics ; RNA/genetics ; RNA, Messenger ; Rats ; Sequence Homology, Nucleic Acid ; Transcription, Genetic
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    Cloning of a second type of activin receptor and functional characterization in Xenopus embryos (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-27
    Description: A complementary DNA coding for a second type of activin receptor (ActRIIB) has been cloned from Xenopus laevis that fulfills the structural criteria of a transmembrane protein serine kinase. Ectodermal explants from embryos injected with activin receptor RNA show increased sensitivity to activin, as measured by the induction of muscle actin RNA. In addition, injected embryos display developmental defects characterized by inappropriate formation of dorsal mesodermal tissue. These results demonstrate that this receptor is involved in signal transduction and are consistent with the proposed role of activin in the induction and patterning of mesoderm in Xenopus embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathews, L S -- Vale, W W -- Kintner, C R -- DK-26741/DK/NIDDK NIH HHS/ -- HD-07343/HD/NICHD NIH HHS/ -- HD-13275/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 27;255(5052):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1313188" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; Activins ; Amino Acid Sequence ; Animals ; Cloning, Molecular ; DNA/genetics ; Inhibins/*physiology ; Membrane Proteins/genetics ; Molecular Sequence Data ; Protein Kinases/genetics ; Protein-Serine-Threonine Kinases ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Xenopus laevis/embryology/*genetics
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    Vacuolar chitinases of tobacco: a new class of hydroxyproline-containing proteins (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-10
    Description: The fungicidal type I chitinases contribute to the defense response of plants against pathogens. Two tobacco chitinases represent a different class of hydroxyproline-containing proteins. Hydroxyproline-rich proteins are predominantly extracellular, structural glycoproteins proteins that lack enzymatic activity and contain many hydroxyproline residues. In contrast, type I chitinases are vacuolar enzymes. They are not glycosylated and contain a small number of hydroxyproline residues restricted to a single, short peptide sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sticher, L -- Hofsteenge, J -- Milani, A -- Neuhaus, J M -- Meins, F Jr -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):655-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Friedrich Miescher-Institut, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496378" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chitinase/*chemistry/metabolism ; Glycosylation ; Hydroxylation ; Hydroxyproline/*analysis ; Molecular Sequence Data ; Molecular Weight ; *Plants, Toxic ; Protein Conformation ; Tobacco/*enzymology/ultrastructure ; Vacuoles/*enzymology
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  • 171
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    Emerging principles for the recognition of peptide antigens by MHC class I molecules (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-14
    Description: Class I major histocompatibility complex (MHC) molecules interact with self and foreign peptides of diverse amino acid sequences yet exhibit distinct allele-specific selectivity for peptide binding. The structures of the peptide-binding specificity pockets (subsites) in the groove of murine H-2Kb as well as human histocompatibility antigen class I molecules have been analyzed. Deep but highly conserved pockets at each end of the groove bind the amino and carboxyl termini of peptide through extensive hydrogen bonding and, hence, dictate the orientation of peptide binding. A deep polymorphic pocket in the middle of the groove provides the chemical and structural complementarity for one of the peptide's anchor residues, thereby playing a major role in allele-specific peptide binding. Although one or two shallow pockets in the groove may also interact with specific peptide side chains, their role in the selection of peptide is minor. Thus, usage of a limited number of both deep and shallow pockets in multiple combinations appears to allow the binding of a broad range of peptides. This binding occurs with high affinity, primarily because of extensive interactions with the peptide backbone and the conserved hydrogen bonding network at both termini of the peptide. Interactions between the anchor residue (or residues) and the corresponding allele-specific pocket provide sufficient extra binding affinity not only to enhance specificity but also to endure the presentation of the peptide at the cell surface for recognition by T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumura, M -- Fremont, D H -- Peterson, P A -- Wilson, I A -- CA-09523/CA/NCI NIH HHS/ -- CA-97489/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):927-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323878" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens/chemistry/*metabolism ; Binding Sites ; H-2 Antigens/chemistry/*metabolism ; HLA-A2 Antigen/chemistry ; Histocompatibility Antigens Class I/chemistry/*metabolism ; Hydrogen Bonding ; Mice ; Models, Molecular ; Molecular Sequence Data ; Ovalbumin/chemistry/metabolism ; Peptide Fragments/chemistry/metabolism ; Peptides/chemistry/*metabolism ; Protein Conformation ; Solvents ; Vesicular stomatitis Indiana virus/metabolism ; Viral Proteins/chemistry/*metabolism
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  • 172
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    A conformation of cyclosporin A in aqueous environment revealed by the X-ray structure of a cyclosporin-Fab complex (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-04-03
    Description: The conformation of the immunosuppressive drug cyclosporin A (CsA) in a complex with a Fab molecule has been established by crystallographic analysis to 2.65 angstrom resolution. This conformation of CsA is similar to that recently observed in the complex with the rotamase cyclophilin, its binding protein in vivo, and totally different from its conformation in an isolated form as determined from x-ray and nuclear magnetic resonance analysis. Because the surfaces of CsA interacting with cyclophilin or with the Fab are not identical, these results suggest that the conformation of CsA observed in the bound form preexists in aqueous solution and is not produced by interaction with the proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Altschuh, D -- Vix, O -- Rees, B -- Thierry, J C -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):92-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566062" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/chemistry/metabolism ; Amino Acid Sequence ; Carrier Proteins/chemistry/metabolism ; Cyclosporine/*chemistry/immunology/metabolism ; Immunoglobulin Fab Fragments/*chemistry/metabolism ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Molecular Sequence Data ; Peptidylprolyl Isomerase ; Protein Binding ; Protein Conformation ; Solutions ; X-Ray Diffraction/methods
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  • 173
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    Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-12-04
    Description: The SWI1, SWI2, and SWI3 proteins, which are required for regulated transcription of numerous yeast genes, were found also to be essential for rat glucocorticoid receptor function in yeast; the receptor failed to activate transcription in strains with mutations in the SWI1, SWI2, or SWI3 genes. Certain mutations in genes encoding components of chromatin, identified as suppressors of swi mutations, partially relieved the SWI- requirement for receptor function. Immunoprecipitation of glucocorticoid receptor derivatives from wild-type (SWI+) yeast extracts coprecipitated the SWI3 protein; such receptor-SWI3 complexes were not detected in swi1- or swi2- mutant strains, implying that a complex of multiple SWI proteins may associate with the receptor. Prior incubation of a Drosophila embryo transcription extract with the yeast SWI3-specific antibody inhibited receptor function in vitro whereas the antibody had no effect if added after initiation complex formation. Thus, positive regulation by the glucocorticoid receptor in vivo and in vitro appears to require its interaction, at an early step, with one or more SWI proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshinaga, S K -- Peterson, C L -- Herskowitz, I -- Yamamoto, K R -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1598-604.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1360703" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Animals ; Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; DNA-Binding Proteins/genetics/*metabolism ; Fungal Proteins/genetics/*metabolism ; Gene Deletion ; *Gene Expression Regulation, Fungal ; Glucosephosphate Dehydrogenase/genetics/metabolism ; Nuclear Proteins/genetics/*metabolism ; Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Rats ; Receptors, Glucocorticoid/*genetics/metabolism ; Receptors, Steroid/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; TATA Box ; *Trans-Activators ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Tyrosine Transaminase/genetics/metabolism ; beta-Galactosidase/genetics/metabolism
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    Myoglobin in a cyanobacterium (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-19
    Description: Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune. This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa Paramecium caudatum and Tetrahymena pyriformis. Cyanoglobin is encoded by the glbN gene, which is positioned between nifU and nifH-two genes essential for nitrogen fixation-in the genome of Nostoc. Cyanoglobin was detected in Nostoc cells only when they were starved for nitrogen and incubated microaerobically.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potts, M -- Angeloni, S V -- Ebel, R E -- Bassam, D -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1690-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg Va 24061.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1609281" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromosome Mapping ; Cloning, Molecular ; Cyanobacteria/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Myoglobin/*genetics ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid
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    Solution structure of the SH3 domain of Src and identification of its ligand-binding site (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-12-04
    Description: The Src homology 3 (SH3) region is a protein domain of 55 to 75 amino acids found in many cytoplasmic proteins, including those that participate in signal transduction pathways. The solution structure of the SH3 domain of the tyrosine kinase Src was determined by multidimensional nuclear magnetic resonance methods. The molecule is composed of two short three-stranded anti-parallel beta sheets packed together at approximately right angles. Studies of the SH3 domain bound to proline-rich peptide ligands revealed a hydrophobic binding site on the surface of the protein that is lined with the side chains of conserved aromatic amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, H -- Rosen, M K -- Shin, T B -- Seidel-Dugan, C -- Brugge, J S -- Schreiber, S L -- 1-S10-RR04870/RR/NCRR NIH HHS/ -- CA27951/CA/NCI NIH HHS/ -- GM44993/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1280858" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cloning, Molecular ; Escherichia coli/genetics ; Glutathione Transferase/chemistry/genetics/isolation & purification ; Ligands ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Neurons/physiology ; Protein Conformation ; *Protein Structure, Secondary ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins pp60(c-src)/*chemistry ; Recombinant Fusion Proteins/chemistry/isolation & purification ; Solutions ; X-Ray Diffraction
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    Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-01
    Description: A form of learning in the marine mollusk Aplysia, long-term sensitization of the gill- and siphon-withdrawal reflex, results in the formation of new synaptic connections between the presynaptic siphon sensory neurons and their target cells. These structural changes can be mimicked, when the cells are maintained in culture, by application of serotonin, an endogenous facilitating neurotransmitter in Aplysia. A group of cell surface proteins, designated Aplysia cell adhesion molecules (apCAM's) was down-regulated in the sensory neurons in response to serotonin. The deduced amino acid sequence obtained from complementary DNA clones indicated that the apCAM's are a family of proteins that seem to arise from a single gene. The apCAM's are members of the immunoglobulin class of cell adhesion molecules and resemble two neural cell adhesion molecules, NCAM and fasciclin II. In addition to regulating newly synthesized apCAM, serotonin also altered the amount of preexisting apCAM on the cell surface of the presynaptic sensory neurons. By contrast, the apCAM on the surface of the postsynaptic motor neuron was not modulated by serotonin. This rapid, transmitter-mediated down-regulation of a cell adhesion molecule in the sensory neurons may be one of the early molecular changes in long-term synaptic facilitation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayford, M -- Barzilai, A -- Keller, F -- Schacher, S -- Kandel, E R -- New York, N.Y. -- Science. 1992 May 1;256(5057):638-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia/*metabolism ; Blotting, Northern ; Cell Adhesion Molecules, Neuronal/chemistry/genetics/*metabolism ; Cells, Cultured ; Cloning, Molecular ; DNA/chemistry/genetics ; Fluorescent Antibody Technique ; Molecular Sequence Data ; Motor Neurons/drug effects/metabolism ; Neuronal Plasticity/*physiology ; Neurons, Afferent/drug effects/metabolism ; Protein Sorting Signals/chemistry ; Serotonin/pharmacology ; Synapses/*physiology
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    A site on rod G protein alpha subunit that mediates effector activation (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-15
    Description: The heterotrimeric guanine nucleotide binding proteins (G proteins) are activated by sensory or hormone receptors. In turn, the G proteins activate effector proteins such as adenylyl cyclase, cyclic guanosine 3',5'-monophosphate phosphodiesterase (cGMP PDE), phospholipase C, and potassium and calcium ion channels by mechanisms that are poorly understood. A site on the alpha subunit of the G protein transducin (alpha t) has been identified that interacts with and activates cGMP phosphodiesterase, the effector enzyme in rod photoreceptors. A 22-amino acid peptide, corresponding to residues 293 to 314 from the COOH-terminal region of alpha t, fully mimicked alpha t and potently activated PDE. This region is adjacent to the receptor activation domain; thus, the alpha subunit of this G protein has a site for interaction with both its effector and receptor that maps near the COOH-terminus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rarick, H M -- Artemyev, N O -- Hamm, H E -- EY 06062/EY/NEI NIH HHS/ -- T32 HL 07692-02/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 May 15;256(5059):1031-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317058" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-GMP Phosphodiesterases/*metabolism ; Amino Acid Sequence ; Animals ; Binding Sites ; Cattle ; Chromatography, High Pressure Liquid ; Enzyme Activation/drug effects ; GTP-Binding Proteins/*chemistry/*physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Peptide Fragments/chemistry/*pharmacology ; Protein Conformation
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    Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-26
    Description: A 3.5 angstrom resolution electron density map of the HIV-1 reverse transcriptase heterodimer complexed with nevirapine, a drug with potential for treatment of AIDS, reveals an asymmetric dimer. The polymerase (pol) domain of the 66-kilodalton subunit has a large cleft analogous to that of the Klenow fragment of Escherichia coli DNA polymerase I. However, the 51-kilodalton subunit of identical sequence has no such cleft because the four subdomains of the pol domain occupy completely different relative positions. Two of the four pol subdomains appear to be structurally related to subdomains of the Klenow fragment, including one containing the catalytic site. The subdomain that appears likely to bind the template strand at the pol active site has a different structure in the two polymerases. Duplex A-form RNA-DNA hybrid can be model-built into the cleft that runs between the ribonuclease H and pol active sites. Nevirapine is almost completely buried in a pocket near but not overlapping with the pol active site. Residues whose mutation results in drug resistance have been approximately located.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kohlstaedt, L A -- Wang, J -- Friedman, J M -- Rice, P A -- Steitz, T A -- GM 39546/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1783-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1377403" target="_blank"〉PubMed〈/a〉
    Keywords: Azepines/pharmacology ; Binding Sites ; Crystallography ; DNA Polymerase I/chemistry ; Escherichia coli/genetics ; HIV-1/*enzymology ; Models, Molecular ; Molecular Structure ; Nevirapine ; Protein Conformation ; Pyridines/pharmacology ; RNA-Directed DNA Polymerase/*chemistry
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    Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-09-18
    Description: The double-stranded RNA-dependent protein kinase (dsRNA-PK) is thought to be a key mediator of the antiviral and antiproliferative effects of interferons (IFNs). Studies examining the physiological function of the kinase suggest that it participates in cell growth and differentiation by regulating protein synthesis. Autophosphorylation and consequent activation of dsRNA-PK in vitro and in vivo result in phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2) and inhibition of protein synthesis. Expression of a functionally defective mutant of human dsRNA-PK in NIH 3T3 cells resulted in malignant transformation, suggesting that dsRNA-PK may function as a suppressor of cell proliferation and tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koromilas, A E -- Roy, S -- Barber, G N -- Katze, M G -- Sonenberg, N -- AI22646/AI/NIAID NIH HHS/ -- RR00166/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 18;257(5077):1685-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Faculty of Medicine, McGill University, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1382315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Division ; Cell Line ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA/genetics ; Enzyme Induction ; Gene Expression ; Humans ; Immunoblotting ; Interferons/*pharmacology ; Mice ; Molecular Sequence Data ; *Mutation ; Phosphorylation ; Protein Kinases/chemistry/*genetics/physiology ; Transfection ; eIF-2 Kinase
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    Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-08
    Description: Voltage-sensitive sodium channels are responsible for the initiation and propagation of the action potential and therefore are important for neuronal excitability. Complementary DNA clones encoding the beta 1 subunit of the rat brain sodium channel were isolated by a combination of polymerase chain reaction and library screening techniques. The deduced primary structure indicates that the beta 1 subunit is a 22,851-dalton protein that contains a single putative transmembrane domain and four potential extracellular N-linked glycosylation sites, consistent with biochemical data. Northern blot analysis reveals a 1,400-nucleotide messenger RNA in rat brain, heart, skeletal muscle, and spinal cord. Coexpression of beta 1 subunits with alpha subunits increases the size of the peak sodium current, accelerates its inactivation, and shifts the voltage dependence of inactivation to more negative membrane potentials. These results indicate that the beta 1 subunit is crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the rat brain sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isom, L L -- De Jongh, K S -- Patton, D E -- Reber, B F -- Offord, J -- Charbonneau, H -- Walsh, K -- Goldin, A L -- Catterall, W A -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- NS26729/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 8;256(5058):839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Brain/*physiology ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Female ; Kinetics ; Macromolecular Substances ; Membrane Potentials ; Molecular Sequence Data ; Oocytes/physiology ; Polymerase Chain Reaction/methods ; Protein Conformation ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Rats ; Sodium Channels/*genetics/*physiology ; Voltage-Gated Sodium Channel beta-1 Subunit ; Xenopus
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 181
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    Constructing proteins by dovetailing unprotected synthetic peptides: backbone-engineered HIV protease (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Backbone-engineered HIV-1 protease was prepared by a total chemical synthesis approach that combines the act of joining two peptides with the generation of an analog structure. Unprotected synthetic peptide segments corresponding to the two halves of the HIV-1 protease monomer polypeptide chain were joined cleanly and in high yield through unique mutually reactive functional groups, one on each segment. Ligation was performed in 6 molar guanidine hydrochloride, thus circumventing limited solubility of protected peptide segments, the principal problem of the classical approach to the chemical synthesis of proteins. The resulting fully active HIV-1 protease analog contained a thioester replacement for the natural peptide bond between Gly51-Gly52 in each of the two active site flaps, a region known to be highly sensitive to mutational changes of amino acid side chains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schnolzer, M -- Kent, S B -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):221-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566069" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Guanidine ; Guanidines ; HIV Protease/*chemical synthesis/metabolism ; HIV-1/*enzymology ; Indicators and Reagents ; Mass Spectrometry ; Models, Molecular ; Molecular Sequence Data ; Peptides/*chemical synthesis ; Protein Conformation
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  • 182
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    Small-angle synchrotron x-ray scattering reveals distinct shape changes of the myosin head during hydrolysis of ATP (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-16
    Description: In the energy transduction of muscle contraction, it is important to know the nature and extent of conformational changes of the head portion of the myosin molecules. In the presence of magnesium adenosine triphosphate (MgATP), fairly large conformational changes of the myosin head [subfragment-1 (S1)] in solution were observed by small-angle x-ray scattering with the use of synchrotron radiation as an intense and stable x-ray source. The presence of MgATP reduced the radius of gyration of the molecule by about 3 angstrom units and the maximum chord length by about 10 angstroms, showing that the shape of S1 becomes more compact or round during hydrolysis of MgATP. Comparison with various nucleotide-bound S1 complexes that correspond to the known intermediate states during ATP hydrolysis indicates that the shape of S1 in a key intermediate state, S1-bound adenosine diphosphate (ADP) and phosphate [S1**.ADP.P(i)], differs significantly from the shape in the other intermediate states of the S1 adenosine triphosphatase cycle as well as that of nucleotide-free S1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wakabayashi, K -- Tokunaga, M -- Kohno, I -- Sugimoto, Y -- Hamanaka, T -- Takezawa, Y -- Wakabayashi, T -- Amemiya, Y -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):443-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411537" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Animals ; Chickens ; Ligands ; Motion ; *Muscle Contraction ; Myosin Subfragments/*ultrastructure ; Myosins/*chemistry/ultrastructure ; Protein Conformation ; Scattering, Radiation ; X-Rays
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  • 183
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    Molecular code for cooperativity in hemoglobin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-03
    Description: Although tetrameric hemoglobin has been studied extensively as a prototype for understanding mechanisms of allosteric regulation, the functional and structural properties of its eight intermediate ligation forms have remained elusive. Recent experiments on the energetics of cooperativity of these intermediates, along with assignments of their quaternary structures, have revealed that the allosteric mechanism is controlled by a previously unrecognized symmetry feature: quaternary switching from form T to form R occurs whenever heme-site binding creates a tetramer with at least one ligated subunit on each dimeric half-molecule. This "symmetry rule" translates the configurational isomers of heme-site ligation into six observed switchpoints of quaternary transition. Cooperativity arises from both "concerted" quaternary switching and "sequential" modulation of binding within each quaternary form, T and R. Binding affinity is regulated through a hierarchical code of tertiary-quaternary coupling that includes the classical allosteric models as limiting cases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ackers, G K -- Doyle, M L -- Myers, D -- Daugherty, M A -- P01-HL40453/HL/NHLBI NIH HHS/ -- R37-GM24486/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):54-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553532" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Calorimetry ; Circular Dichroism ; Hemoglobins/*chemistry/genetics/metabolism ; Kinetics ; Ligands ; Macromolecular Substances ; Models, Molecular ; Mutation ; Oxyhemoglobins/chemistry/metabolism ; Protein Conformation ; Thermodynamics
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  • 184
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    The skeletal muscle chloride channel in dominant and recessive human myotonia (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-07
    Description: Autosomal recessive generalized myotonia (Becker's disease) (GM) and autosomal dominant myotonia congenita (Thomsen's disease) (MC) are characterized by skeletal muscle stiffness that is a result of muscle membrane hyperexcitability. For both diseases, alterations in muscle chloride or sodium currents or both have been observed. A complementary DNA for a human skeletal muscle chloride channel (CLC-1) was cloned, physically localized on chromosome 7, and linked to the T cell receptor beta (TCRB) locus. Tight linkage of these two loci to GM and MC was found in German families. An unusual restriction site in the CLC-1 locus in two GM families identified a mutation associated with that disease, a phenylalanine-to-cysteine substitution in putative transmembrane domain D8. This suggests that different mutations in CLC-1 may cause dominant or recessive myotonia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, M C -- Steinmeyer, K -- Lorenz, C -- Ricker, K -- Wolf, F -- Otto, M -- Zoll, B -- Lehmann-Horn, F -- Grzeschik, K H -- Jentsch, T J -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):797-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Center for Human Genetics, Marburg University, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1379744" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Southern ; Chloride Channels ; *Chromosomes, Human, Pair 7 ; Cloning, Molecular ; DNA/genetics ; Female ; *Genes, Dominant ; *Genes, Recessive ; Genetic Linkage ; Humans ; Ion Channels/*genetics ; Lod Score ; Male ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Muscular Dystrophies/*genetics ; Myotonia Congenita/*genetics ; Pedigree ; Polymorphism, Restriction Fragment Length ; Receptors, Antigen, T-Cell/genetics ; Recombination, Genetic ; Sequence Homology, Nucleic Acid
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  • 185
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    Activation of a plant gene by T-DNA tagging: auxin-independent growth in vitro (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-20
    Description: A transferred DNA (T-DNA) tagging vector with the potential to produce dominant mutations was used with cocultured Agrobacterium tumefaciens and protoplasts to tag genes involved in the action of the plant growth substance auxin. Transgenic calli were selected for their ability to grow in the absence of auxin in the culture media. From one experiment, 12 calli that displayed this phenotype were recovered, of which 11 were able to regenerate into plants. In one plant studied in detail, protoplast division in the absence of auxin genetically cosegregated with a single T-DNA insert. A messenger RNA encoded by a 6.4-kilobase sequence of plant genomic DNA rescued from the mutant is overexpressed relative to untransformed plants. The genomic DNA, as well as a cognate complementary DNA, once transfected into protoplasts promote growth and cell division in vitro in the absence of exogenously added auxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayashi, H -- Czaja, I -- Lubenow, H -- Schell, J -- Walden, R -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1350-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Agriculture, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455228" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/genetics ; Amino Acid Sequence ; Cloning, Molecular ; *Gene Expression Regulation ; Genes, Plant ; *Genetic Vectors ; In Vitro Techniques ; Indoleacetic Acids/*genetics ; Molecular Sequence Data ; Plants, Genetically Modified/*genetics/growth & development ; Restriction Mapping
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  • 186
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    Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected] (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-05
    Description: The D and L forms of the enzyme HIV-1 protease have been prepared by total chemical synthesis. The two proteins had identical covalent structures. However, the folded protein-enzyme enantiomers showed reciprocal chiral specificity on peptide substrates. That is, each enzyme enantiomer cut only the corresponding substrate enantiomer. Reciprocal chiral specificity was also evident in the effect of enantiomeric inhibitors. These data imply that the folded forms of the chemically synthesized D- and L-enzyme molecules are mirror images of one another in all elements of the three-dimensional structure. Enantiomeric proteins are expected to display reciprocal chiral specificity in all aspects of their biochemical interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milton, R C -- Milton, S C -- Kent, S B -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1445-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604320" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acids ; HIV Protease/chemical synthesis/*chemistry/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Oligopeptides/pharmacology ; Protein Conformation ; Stereoisomerism ; Substrate Specificity ; X-Ray Diffraction
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  • 187
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    Lambda Int protein bridges between higher order complexes at two distant chromosomal loci attL and attR (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: The excisive recombination reaction of bacteriophage lambda involves a specific and efficient juxtaposition of two distant higher order protein-DNA complexes on the chromosome of Escherichia coli. These complexes, which mediate synapsis and strand exchange, consist of two DNA sequences, attL and attR, the bivalent DNA binding protein Int, and the sequence-specific DNA bending proteins, IHF, Xis, and Fis. The protein-protein and protein-DNA interactions within, and between, these complexes were studied by various biochemical techniques and the patterns of synergism among pairs of mutants with marginally impaired recombination function were analyzed. The DNA bending proteins facilitated long-range tethering of high- and low-affinity DNA sites by the bivalent Int protein, and a specific map is proposed for the resulting Int bridges. These structural motifs provide a basis for postulating the mechanism of site-specific recombination and may also be relevant to other pathways in which two distant chromosomal sites become associated.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904348/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904348/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, S -- Landy, A -- AI 13544/AI/NIAID NIH HHS/ -- GM 33928/GM/NIGMS NIH HHS/ -- R01 GM033928/GM/NIGMS NIH HHS/ -- R01 GM062723/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):198-203.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology and Medicine, Brown University, Providence, RI 02912.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1533056" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophage lambda/*enzymology ; Base Sequence ; Chromosome Mapping ; *Chromosomes, Bacterial ; Crosses, Genetic ; DNA Nucleotidyltransferases/*metabolism ; DNA, Bacterial/genetics ; DNA-Binding Proteins/*metabolism ; Escherichia coli/*genetics/metabolism ; Genes, Bacterial ; Genetic Linkage ; Integrases ; Models, Structural ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Nucleic Acid Conformation ; Plasmids ; Protein Conformation ; Recombination, Genetic
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  • 188
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    Evidence that eukaryotes and eocyte prokaryotes are immediate relatives (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-03
    Description: The phylogenetic origin of eukaryotes has been unclear because eukaryotic nuclear genes have diverged substantially from prokaryotic ones. The genes coding for elongation factor EF-1 alpha were compared among various organisms. The EF-1 alpha sequences of eukaryotes contained an 11-amino acid segment that was also found in eocytes (extremely thermophilic, sulfur-metabolizing bacteria) but that was absent in all other bacteria. The related (paralogous) genes encoding elongation factor EF-2 and initiation factor IF-2 also lacked the 11-amino acid insert. These data imply that the eocytes are the closest surviving relatives (sister taxon) of the eukaryotes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rivera, M C -- Lake, J A -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):74-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621096" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteria/*genetics ; Base Sequence ; *Biological Evolution ; DNA, Bacterial/genetics ; Humans ; Models, Molecular ; Molecular Sequence Data ; Peptide Elongation Factor 1 ; Peptide Elongation Factor G ; Peptide Elongation Factor Tu/chemistry/*genetics ; Peptide Elongation Factors/*genetics ; Peptide Initiation Factors/*genetics ; Phylogeny ; Plants/genetics ; Prokaryotic Initiation Factor-2 ; Protein Conformation ; Saccharomyces cerevisiae/genetics ; Sequence Homology, Nucleic Acid
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  • 189
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    The role of solvent viscosity in the dynamics of protein conformational changes (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-06-26
    Description: Nanosecond lasers were used to measure the rate of conformational changes in myoglobin after ligand dissociation at ambient temperatures. At low solvent viscosities the rate is independent of viscosity, but at high viscosities it depends on approximately the inverse first power of the viscosity. Kramers theory for unimolecular rate processes can be used to explain this result if the friction term is modified to include protein as well as solvent friction. The theory and experiment suggest that the dominant factor in markedly reducing the rate of conformational changes in myoglobin at low temperatures (less than 200 K) is the very high viscosity (greater than 10(7) centipoise) of the glycerol-water solvent. That is, at low temperatures conformational substates may not be "frozen" so much as "stuck."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ansari, A -- Jones, C M -- Henry, E R -- Hofrichter, J -- Eaton, W A -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1796-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1615323" target="_blank"〉PubMed〈/a〉
    Keywords: Carbon Monoxide ; Hot Temperature ; Lasers ; Myoglobin/*chemistry ; Protein Conformation ; Solvents/*adverse effects ; Spectrophotometry, Atomic ; Viscosity
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  • 190
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    Acquisition of myogenic specificity by replacement of three amino acid residues from MyoD into E12 (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-15
    Description: The basic helix-loop-helix (bHLH) protein MyoD is a transcription factor that is important for the induction of the myogenic phenotype. The DNA binding basic region (13 amino acids) is necessary for recognition of the consensus MyoD binding site, for transcriptional activation, and for conversion of fibroblasts to muscle. In contrast, the non-tissue-specific bHLH protein E12 can bind to the MyoD binding site but does not induce myogenesis. Here, it is shown that only two amino acids in the MyoD basic region and a single amino acid from the junction, which separates the basic region and helix 1, are sufficient for myogenic specificity when substituted into the corresponding region of E12. These findings suggest that the recognition of particular determinants in the basic region is required for conversion of fibroblasts to muscle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, R L -- Weintraub, H -- New York, N.Y. -- Science. 1992 May 15;256(5059):1027-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratory, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA/metabolism ; DNA Probes ; DNA-Binding Proteins/chemistry/metabolism/pharmacology ; Fibroblasts/cytology ; Fluorescent Antibody Technique ; Molecular Sequence Data ; Muscle Proteins/chemistry/genetics/*physiology ; Muscles/*cytology ; MyoD Protein ; Protein Conformation ; Structure-Activity Relationship ; Transcription Factors/chemistry/metabolism/pharmacology ; Transfection
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  • 191
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    Peptide binding by chaperone SecB: implications for recognition of nonnative structure (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-10
    Description: The molecular basis for recognition of nonnative proteins by the molecular chaperone SecB was investigated with an in vitro assay based on the protection of SecB from proteolysis when a ligand is bound. The SecB tetramer has multiple binding sites for positively charged peptides. When the peptide binding sites are occupied, the complex undergoes a conformational change to expose hydrophobic sites that bind the fluorescent probe 1-anilinonaphthalene-8-sulfonate. A model is proposed for interaction of nonnative polypeptides with both hydrophilic and hydrophobic sites on SecB.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Randall, L L -- GM29798/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):241-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631545" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/*metabolism ; Binding Sites/physiology ; Electrophoresis, Polyacrylamide Gel ; In Vitro Techniques ; Models, Chemical ; Molecular Sequence Data ; Osmolar Concentration ; Peptides/*metabolism ; Protein Conformation
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  • 192
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    Molecular characterization of helix-loop-helix peptides (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-21
    Description: A class of regulators of eukaryotic gene expression contains a conserved amino acid sequence responsible for protein oligomerization and binding to DNA. This structure consists of an arginine- and lysine-rich basic region followed by a helix-loop-helix motif, which together mediate specific binding to DNA. Peptides were prepared that span this motif in the MyoD protein; in solution, they formed alpha-helical dimers and tetramers. They bound to DNA as dimers and their alpha-helical content increased on binding. Parallel and antiparallel four-helix models of the DNA-bound dimer were constructed. Peptides containing disulfide bonds were engineered to test the correctness of the two models. A disulfide that is compatible with the parallel model promotes specific interaction with DNA, whereas a disulfide compatible with the antiparallel model abolishes specific binding. Electron paramagnetic resonance (EPR) measurements of nitroxide-labeled peptides provided intersubunit distance measurements that also supported the parallel model.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anthony-Cahill, S J -- Benfield, P A -- Fairman, R -- Wasserman, Z R -- Brenner, S L -- Stafford, W F 3rd -- Altenbach, C -- Hubbell, W L -- DeGrado, W F -- GM13731/GM/NIGMS NIH HHS/ -- GM14321/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):979-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Department, DuPont Merck Pharmaceutical Co., Wilmington, DE 19880-0328.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312255" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Circular Dichroism ; DNA-Binding Proteins/*chemistry ; Disulfides ; Electron Spin Resonance Spectroscopy ; Enhancer Elements, Genetic ; Gene Expression Regulation ; Humans ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; Regulatory Sequences, Nucleic Acid ; Sequence Alignment ; Transcription Factors/*chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 193
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    Structural evidence for induced fit as a mechanism for antibody-antigen recognition (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-21
    Description: The three-dimensional structure of a specific antibody (Fab 17/9) to a peptide immunogen from influenza virus hemagglutinin [HA1(75-110)] and two independent crystal complexes of this antibody with bound peptide (TyrP100-LeuP108) have been determined by x-ray crystallographic techniques at 2.0 A, 2.9 A, and 3.1 A resolution, respectively. The nonapeptide antigen assumes a type I beta turn in the antibody combining site and interacts primarily with the Fab hypervariable loops L3, H2, and H3. Comparison of the bound and unbound Fab structures shows that a major rearrangement in the H3 loop accompanies antigen binding. This conformational change results in the creation of a binding pocket for the beta turn of the peptide, allowing TyrP105 to be accommodated. The conformation of the peptide bound to the antibody shows similarity to its cognate sequence in the HA1, suggesting a possible mechanism for the cross-reactivity of this Fab with monomeric hemagglutinin. The structures of the free and antigen bound antibodies demonstrate the flexibility of the antibody combining site and provide an example of induced fit as a mechanism for antibody-antigen recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rini, J M -- Schulze-Gahmen, U -- Wilson, I A -- AI-23498/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):959-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546293" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/ultrastructure ; *Antigen-Antibody Reactions ; Hemagglutinins, Viral/*immunology ; Hydrogen Bonding ; Immunoglobulin Fab Fragments/*ultrastructure ; Immunoglobulin G/ultrastructure ; In Vitro Techniques ; Influenza A virus/immunology ; Mice ; Models, Molecular ; Molecular Sequence Data ; Motion ; Peptides/chemistry/immunology ; Protein Binding ; Protein Conformation ; X-Ray Diffraction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 194
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    The human Y chromosome: overlapping DNA clones spanning the euchromatic region (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: The human Y chromosome was physically mapped by assembling 196 recombinant DNA clones, each containing a segment of the chromosome, into a single overlapping array. This array included more than 98 percent of the euchromatic portion of the Y chromosome. First, a library of yeast artificial chromosome (YAC) clones was prepared from the genomic DNA of a human XYYYY male. The library was screened to identify clones containing 160 sequence-tagged sites and the map was then constructed from this information. In all, 207 Y-chromosomal DNA loci were assigned to 127 ordered intervals on the basis of their presence or absence in the YAC's, yielding ordered landmarks at an average spacing of 220 kilobases across the euchromatic region. The map reveals that Y-chromosomal genes are scattered among a patchwork of X-homologous, Y-specific repetitive, and single-copy DNA sequences. This map of overlapping clones and ordered, densely spaced markers should accelerate studies of the chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foote, S -- Vollrath, D -- Hilton, A -- Page, D C -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):60-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Whitehead Institute, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359640" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Centromere ; Cloning, Molecular ; DNA Fingerprinting ; Gene Library ; Genes, Fungal ; *Genome, Human ; Humans ; Male ; Molecular Sequence Data ; Multigene Family ; Polymorphism, Restriction Fragment Length ; Sequence Homology ; Sequence Tagged Sites ; X Chromosome ; *Y Chromosome
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 195
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    Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (A). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (less than 4 A) are formed between CaM and the peptide, with van der Waals contacts comprising approximately 80% of this total.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meador, W E -- Means, A R -- Quiocho, F A -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1251-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519061" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calmodulin/*chemistry ; Crystallography ; Models, Molecular ; Molecular Sequence Data ; Myosin-Light-Chain Kinase/*metabolism ; Protein Conformation
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  • 196
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    Magnetoferritin: in vitro synthesis of a novel magnetic protein (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-24
    Description: The iron storage protein ferritin consists of a spherical polypeptide shell (apoferritin) surrounding a 6-nanometer inorganic core of the hydrated iron oxide ferrihydrite (5Fe2O3.9H2O). Previous studies have shown that the in vitro reconstitution of apoferritin yields mineral cores essentially identical to those of the native proteins. A magnetic mineral was synthesized within the nanodimensional cavity of horse spleen ferritin by the use of controlled reconstitution conditions. Transmission electron microscopy and electron diffraction analysis indicate that the entrapped mineral particles are discrete 6-nanometer spherical single crystals of the ferrimagnetic iron oxide magnetite (Fe3O4). The resulting magnetic protein, "magnetoferritin," could have uses in biomedical imaging, cell labeling, and separation procedures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meldrum, F C -- Heywood, B R -- Mann, S -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):522-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉School of Chemistry, University of Bath, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1636086" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Ferric Compounds ; Ferritins/*chemistry/ultrastructure ; Horses ; *Magnetics ; Microscopy, Electron ; Protein Conformation ; Spleen/metabolism
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  • 197
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    Heteromeric NMDA receptors: molecular and functional distinction of subtypes (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-22
    Description: The N-methyl D-aspartate (NMDA) receptor subtype of glutamate-gated ion channels possesses high calcium permeability and unique voltage-dependent sensitivity to magnesium and is modulated by glycine. Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% identical in sequence. These are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor subunits, including the NMDA receptor subunit NMDAR1 (NR1). Upon expression in cultured cells, the new subunits yielded prominent, typical glutamate- and NMDA-activated currents only when they were in heteromeric configurations with NR1. NR1-NR2A and NR1-NR2C channels differed in gating behavior and magnesium sensitivity. Such heteromeric NMDA receptor subtypes may exist in neurons, since NR1 messenger RNA is synthesized throughout the mature rat brain, while NR2 messenger RNA show a differential distribution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monyer, H -- Sprengel, R -- Schoepfer, R -- Herb, A -- Higuchi, M -- Lomeli, H -- Burnashev, N -- Sakmann, B -- Seeburg, P H -- New York, N.Y. -- Science. 1992 May 22;256(5060):1217-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Glutamates/pharmacology ; Glutamic Acid ; Glycine/pharmacology ; Macromolecular Substances ; Magnesium/pharmacology ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Multigene Family ; N-Methylaspartate/pharmacology ; Oligonucleotide Probes ; Organ Specificity ; Peptides ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*genetics/*metabolism ; Recombinant Proteins/drug effects/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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  • 198
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    Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-31
    Description: Subdomain-size proteolytic fragments of Escherichia coli trp repressor have been produced that assemble in defined order to regenerate fully native dimers. By characterization of the secondary and tertiary structures of isolated and recombined fragments, the structure of assembly intermediates can be correlated with the kinetic folding pathway of the intact repressor deduced from spectroscopic measurement of folding rates. The nativelike structure of these intermediates provides further evidence that protein folding pathways reflect the stabilities of secondary structural units and assemblies found in the native state. The proteolytic method should be generally useful in adding structural detail to spectroscopically determined folding mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tasayco, M L -- Carey, J -- GM43558/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 31;255(5044):594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemistry Department, Princeton University, NJ 08544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1736361" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacterial Proteins/chemistry ; Circular Dichroism ; Escherichia coli/metabolism ; Kinetics ; Macromolecular Substances ; Magnetic Resonance Spectroscopy/methods ; Models, Structural ; Molecular Sequence Data ; Peptide Fragments/chemistry ; Protein Conformation ; Repressor Proteins/*chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 199
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    An unstable triplet repeat in a gene related to myotonic muscular dystrophy (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-16
    Description: Synthetic oligonucleotides containing GC-rich triplet sequences were used in a scanning strategy to identify unstable genetic sequences at the myotonic dystrophy (DM) locus. A highly polymorphic GCT repeat was identified and found to be unstable, with an increased number of repeats occurring in DM patients. In the case of severe congenital DM, the paternal triplet allele was inherited unaltered while the maternal, DM-associated allele was unstable. These studies suggest that the mutational mechanism leading to DM is triplet amplification, similar to that occurring in the fragile X syndrome. The triplet repeat sequence is within a gene (to be referred to as myotonin-protein kinase), which has a sequence similar to protein kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, Y H -- Pizzuti, A -- Fenwick, R G Jr -- King, J -- Rajnarayan, S -- Dunne, P W -- Dubel, J -- Nasser, G A -- Ashizawa, T -- de Jong, P -- 5-M01-RR00350/RR/NCRR NIH HHS/ -- P30-HG00210/HG/NHGRI NIH HHS/ -- P50HL42267-01/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1256-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecular Genetics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546326" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Chromosomes, Human, Pair 19 ; Cloning, Molecular ; DNA/chemistry ; Humans ; Molecular Sequence Data ; Mutation ; Myotonic Dystrophy/*genetics ; Nucleic Acid Hybridization ; Polymerase Chain Reaction ; Polymorphism, Genetic ; *Repetitive Sequences, Nucleic Acid
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  • 200
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    Isolation of a complementary DNA that encodes the mammalian splicing factor SC35 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: The mammalian splicing factor SC35 is required for the first step in the splicing reaction and for spliceosome assembly. The cloning and characterization of a complementary DNA encoding this protein revealed that it is a member of a family of splicing factors that includes mammalian SF2/ASF. This family of proteins is characterized by the presence of a ribonucleoprotein (RNP)-type RNA binding motif and a carboxyl-terminal serine-arginine-rich (SR) domain. A search of the DNA sequence database revealed that the thymus-specific exon (ET) of the c-myb proto-oncogene is encoded on the antisense strand of the SC35 gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, X D -- Maniatis, T -- GM42231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):535-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373910" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Baculoviridae/genetics ; Base Sequence ; Binding Sites ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; Codon ; DNA/chemistry/*isolation & purification ; Exons ; Humans ; Molecular Sequence Data ; *Nuclear Proteins ; Proteins/chemistry/*genetics ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-myb ; RNA/metabolism ; *RNA Splicing ; *Ribonucleoproteins ; Sequence Homology, Nucleic Acid ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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