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  • Structure-Activity Relationship
  • American Association for the Advancement of Science (AAAS)  (48)
  • MDPI Publishing
  • 2000-2004  (13)
  • 1975-1979  (35)
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Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (48)
  • MDPI Publishing
Years
Year
  • 1
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    Generation of an LFA-1 antagonist by the transfer of the ICAM-1 immunoregulatory epitope to a small molecule (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: The protein-protein interaction between leukocyte functional antigen-1 (LFA-1) and intercellular adhesion molecule-1 (ICAM-1) is critical to lymphocyte and immune system function. Here, we report on the transfer of the contiguous, nonlinear epitope of ICAM-1, responsible for its association with LFA-1, to a small-molecule framework. These LFA-1 antagonists bound LFA-1, blocked binding of ICAM-1, and inhibited a mixed lymphocyte reaction (MLR) with potency significantly greater than that of cyclosporine A. Furthermore, in comparison to an antibody to LFA-1, they exhibited significant anti-inflammatory effects in vivo. These results demonstrate the utility of small-molecule mimics of nonlinear protein epitopes and the protein epitopes themselves as leads in the identification of novel pharmaceutical agents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gadek, T R -- Burdick, D J -- McDowell, R S -- Stanley, M S -- Marsters, J C Jr -- Paris, K J -- Oare, D A -- Reynolds, M E -- Ladner, C -- Zioncheck, K A -- Lee, W P -- Gribling, P -- Dennis, M S -- Skelton, N J -- Tumas, D B -- Clark, K R -- Keating, S M -- Beresini, M H -- Tilley, J W -- Presta, L G -- Bodary, S C -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1086-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Bioorganic Chemistry, Genentech, One DNA Way, South San Francisco, CA 94080, USA. trg@gene.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834839" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Anti-Inflammatory Agents, Non-Steroidal/chemical ; synthesis/chemistry/metabolism/pharmacology ; Cyclosporine/pharmacology ; Dermatitis, Irritant/drug therapy ; Dinitrofluorobenzene ; Drug Design ; Enzyme-Linked Immunosorbent Assay ; Epitopes ; Female ; Humans ; Immunoglobulin Fab Fragments/immunology/pharmacology ; Immunosuppressive Agents/chemical synthesis/chemistry/metabolism/*pharmacology ; Intercellular Adhesion Molecule-1/chemistry/*immunology/*metabolism ; Lymphocyte Culture Test, Mixed ; Lymphocyte Function-Associated Antigen-1/immunology/*metabolism ; Mice ; Mice, Inbred BALB C ; Molecular Mimicry ; Mutagenesis ; Protein Structure, Secondary ; Structure-Activity Relationship ; Thiophenes/*chemical synthesis/chemistry/metabolism/*pharmacology ; beta-Alanine/analogs & derivatives/*chemical ; synthesis/chemistry/metabolism/*pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Structural mechanism for STI-571 inhibition of abelson tyrosine kinase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-16
    Description: The inadvertent activation of the Abelson tyrosine kinase (Abl) causes chronic myelogenous leukemia (CML). A small-molecule inhibitor of Abl (STI-571) is effective in the treatment of CML. We report the crystal structure of the catalytic domain of Abl, complexed to a variant of STI-571. Critical to the binding of STI-571 is the adoption by the kinase of an inactive conformation, in which a centrally located "activation loop" is not phosphorylated. The conformation of this loop is distinct from that in active protein kinases, as well as in the inactive form of the closely related Src kinases. These results suggest that compounds that exploit the distinctive inactivation mechanisms of individual protein kinases can achieve both high affinity and high specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schindler, T -- Bornmann, W -- Pellicena, P -- Miller, W T -- Clarkson, B -- Kuriyan, J -- GM29362/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1938-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988075" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/chemistry/*pharmacology ; Benzamides ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Activation ; Enzyme Inhibitors/chemistry/*pharmacology ; Humans ; Imatinib Mesylate ; Mice ; Models, Molecular ; Phosphorylation ; *Piperazines ; Protein Conformation ; Proto-Oncogene Proteins c-abl/*antagonists & inhibitors/chemistry/metabolism ; Pyrimidines/chemistry/*pharmacology ; Recombinant Fusion Proteins ; Structure-Activity Relationship
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  • 3
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    Structure of MsbA from E. coli: a homolog of the multidrug resistance ATP binding cassette (ABC) transporters (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-08
    Description: Multidrug resistance (MDR) is a serious medical problem and presents a major challenge to the treatment of disease and the development of novel therapeutics. ABC transporters that are associated with multidrug resistance (MDR-ABC transporters) translocate hydrophobic drugs and lipids from the inner to the outer leaflet of the cell membrane. To better elucidate the structural basis for the "flip-flop" mechanism of substrate movement across the lipid bilayer, we have determined the structure of the lipid flippase MsbA from Escherichia coli by x-ray crystallography to a resolution of 4.5 angstroms. MsbA is organized as a homodimer with each subunit containing six transmembrane alpha-helices and a nucleotide-binding domain. The asymmetric distribution of charged residues lining a central chamber suggests a general mechanism for the translocation of substrate by MsbA and other MDR-ABC transporters. The structure of MsbA can serve as a model for the MDR-ABC transporters that confer multidrug resistance to cancer cells and infectious microorganisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, G -- Roth, C B -- GM61905-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1793-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, MB-9, The Scripps Research Institute, La Jolla, CA 92037, USA. gchang@scripps.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546864" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Bacterial Proteins/*chemistry/genetics/metabolism ; Binding Sites ; Biological Transport ; Crystallography, X-Ray ; Dimerization ; *Drug Resistance, Microbial ; *Drug Resistance, Multiple ; Escherichia coli/*enzymology ; Lipid A/metabolism ; Membrane Proteins/*chemistry/genetics/metabolism ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Sequence Alignment ; Static Electricity ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Designing small-molecule switches for protein-protein interactions (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-17
    Description: Mutations introduced into human growth hormone (hGH) (Thr175 --〉 Gly-hGH) and the extracellular domain of the hGH receptor (Trp104 --〉 Gly-hGHbp) created a cavity at the protein-protein interface that resulted in binding affinity being reduced by a factor of 10(6). A small library of indole analogs was screened for small molecules that bind the cavity created by the mutations and restore binding affinity. The ligand 5-chloro-2-trichloromethylimidazole was found to increase the affinity of the mutant hormone for its receptor more than 1000-fold. Cell proliferation and JAK2 phosphorylation assays showed that the mutant hGH activates growth hormone signaling in the presence of added ligand. This approach may allow other protein-protein and protein-nucleic acid interactions to be switched on or off by the addition or depletion of exogenous small molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, Z -- Zhou, D -- Schultz, P G -- New York, N.Y. -- Science. 2000 Jun 16;288(5473):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10856217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Division ; Cell Line ; Human Growth Hormone/chemistry/genetics/*metabolism ; Imidazoles/*chemistry/metabolism ; Janus Kinase 2 ; Ligands ; Mice ; Molecular Sequence Data ; Peptide Library ; Phosphorylation ; Protein Binding ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; Receptors, Somatotropin/chemistry/genetics/*metabolism ; Signal Transduction ; Structure-Activity Relationship ; Transfection
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  • 5
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    Cell biology. Integrin crystal structure solved (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Couzin, J -- New York, N.Y. -- Science. 2001 Sep 7;293(5536):1743-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11546844" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallization ; Crystallography, X-Ray/*methods ; Drug Design ; Models, Molecular ; Protein Structure, Tertiary ; Protein Subunits ; Receptors, Vitronectin/*chemistry/metabolism ; Solubility ; Structure-Activity Relationship
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  • 6
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    Location, location, location: membrane targeting directed by PX domains (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-01
    Description: Phosphoinositide (PI)-binding domains play critical roles in the intracellular localization of a variety of cell-signaling proteins. The 120-amino acid Phox homology (PX) domain targets proteins to organelle membranes through interactions between two conserved basic motifs within the PX domain and specific PIs. The combination of protein-lipid and protein-protein interactions ensures the proper localization and regulation of PX domain-containing proteins. Upon proper localization, PX domain-containing proteins can then bind to additional proteins and execute their functions in a diverse set of biological pathways, including intracellular protein transport, cell growth and survival, cytoskeletal organization, and neutrophil defense.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sato, T K -- Overduin, M -- Emr, S D -- New York, N.Y. -- Science. 2001 Nov 30;294(5548):1881-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Medicine and Howard Hughes Medical Institute, University of California at San Diego School of Medicine, La Jolla, CA 92093-0668, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11729306" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Animals ; Carrier Proteins/chemistry/metabolism ; Humans ; Intracellular Membranes/*metabolism ; Models, Molecular ; NADPH Oxidase ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphatidylinositols/*metabolism ; Phosphoproteins/*chemistry/*metabolism ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Protein Transport ; Signal Transduction ; Structure-Activity Relationship ; src Homology Domains
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  • 7
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    Structural basis of transcription activation: the CAP-alpha CTD-DNA complex (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-31
    Description: The Escherichia coli catabolite activator protein (CAP) activates transcription at P(lac), P(gal), and other promoters through interactions with the RNA polymerase alpha subunit carboxyl-terminal domain (alphaCTD). We determined the crystal structure of the CAP-alphaCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with alphaCTD, and alphaCTD makes direct protein-DNA interactions with the DNA segment adjacent to the DNA site for CAP. There are no large-scale conformational changes in CAP and alphaCTD, and the interface between CAP and alphaCTD is small. These findings are consistent with the proposal that activation involves a simple "recruitment" mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benoff, Brian -- Yang, Huanwang -- Lawson, Catherine L -- Parkinson, Gary -- Liu, Jinsong -- Blatter, Erich -- Ebright, Yon W -- Berman, Helen M -- Ebright, Richard H -- GM21589/GM/NIGMS NIH HHS/ -- GM41376/GM/NIGMS NIH HHS/ -- GM64375/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 30;297(5586):1562-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute and Department of Chemistry, Howard Hughes Medical Institute, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12202833" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography, X-Ray ; Cyclic AMP Receptor Protein/*chemistry/metabolism/physiology ; DNA/*chemistry/metabolism ; DNA-Directed RNA Polymerases/*chemistry/metabolism/physiology ; Macromolecular Substances ; Models, Molecular ; Nucleic Acid Conformation ; Protein Binding ; Protein Conformation ; Structure-Activity Relationship ; *Transcription, Genetic ; Transcriptional Activation
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  • 8
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    Bypassing a kinase activity with an ATP-competitive drug (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-10-18
    Description: Unfolded proteins in the endoplasmic reticulum cause trans-autophosphorylation of the bifunctional transmembrane kinase Ire1, which induces its endoribonuclease activity. The endoribonuclease initiates nonconventional splicing of HAC1 messenger RNA to trigger the unfolded-protein response (UPR). We explored the role of Ire1's kinase domain by sensitizing it through site-directed mutagenesis to the ATP-competitive inhibitor 1NM-PP1. Paradoxically, rather than being inhibited by 1NM-PP1, drug-sensitized Ire1 mutants required 1NM-PP1 as a cofactor for activation. In the presence of 1NM-PP1, drug-sensitized Ire1 bypassed mutations that inactivate its kinase activity and induced a full UPR. Thus, rather than through phosphorylation per se, a conformational change in the kinase domain triggered by occupancy of the active site with a ligand leads to activation of all known downstream functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papa, Feroz R -- Zhang, Chao -- Shokat, Kevan -- Walter, Peter -- AI44009/AI/NIAID NIH HHS/ -- GM32384/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Nov 28;302(5650):1533-7. Epub 2003 Oct 16.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco, CA 94143-2200, USA. frpapa@medicine.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14564015" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate/pharmacology ; Adenosine Triphosphate/analogs & derivatives/chemistry/*metabolism/pharmacology ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Binding, Competitive ; Cytosol/metabolism ; Dithiothreitol/pharmacology ; Endoplasmic Reticulum/*metabolism ; Endoribonucleases/metabolism ; Enzyme Activation ; Ligands ; Membrane Glycoproteins/antagonists & inhibitors/*chemistry/genetics/*metabolism ; Models, Biological ; Mutagenesis, Site-Directed ; Phosphorylation ; Protein Conformation ; *Protein Folding ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/antagonists & ; inhibitors/*chemistry/genetics/*metabolism ; Pyrazoles/chemistry/*metabolism/*pharmacology ; Pyrimidines/chemistry/*metabolism/*pharmacology ; RNA Splicing ; RNA, Messenger/genetics/metabolism ; Repressor Proteins/genetics/metabolism ; Saccharomyces cerevisiae Proteins/antagonists & ; inhibitors/*chemistry/genetics/*metabolism ; Signal Transduction ; Structure-Activity Relationship ; Substrate Specificity ; Transcription Factors/genetics/metabolism ; Up-Regulation
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  • 9
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    Derivatives of erythropoietin that are tissue protective but not erythropoietic (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-13
    Description: Erythropoietin (EPO) is both hematopoietic and tissue protective, putatively through interaction with different receptors. We generated receptor subtype-selective ligands allowing the separation of EPO's bioactivities at the cellular level and in animals. Carbamylated EPO (CEPO) or certain EPO mutants did not bind to the classical EPO receptor (EPOR) and did not show any hematopoietic activity in human cell signaling assays or upon chronic dosing in different animal species. Nevertheless, CEPO and various nonhematopoietic mutants were cytoprotective in vitro and conferred neuroprotection against stroke, spinal cord compression, diabetic neuropathy, and experimental autoimmune encephalomyelitis at a potency and efficacy comparable to EPO.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leist, Marcel -- Ghezzi, Pietro -- Grasso, Giovanni -- Bianchi, Roberto -- Villa, Pia -- Fratelli, Maddalena -- Savino, Costanza -- Bianchi, Marina -- Nielsen, Jacob -- Gerwien, Jens -- Kallunki, Pekka -- Larsen, Anna Kirstine -- Helboe, Lone -- Christensen, Soren -- Pedersen, Lars O -- Nielsen, Mette -- Torup, Lars -- Sager, Thomas -- Sfacteria, Alessandra -- Erbayraktar, Serhat -- Erbayraktar, Zubeyde -- Gokmen, Necati -- Yilmaz, Osman -- Cerami-Hand, Carla -- Xie, Qiao-Wen -- Coleman, Thomas -- Cerami, Anthony -- Brines, Michael -- New York, N.Y. -- Science. 2004 Jul 9;305(5681):239-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉H. Lundbeck A/S, 2500 Valby, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15247477" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Binding Sites ; Cells, Cultured ; Diabetic Neuropathies/drug therapy ; Drug Design ; Encephalomyelitis, Autoimmune, Experimental/drug therapy ; Erythropoiesis ; Erythropoietin/*analogs & ; derivatives/chemistry/genetics/metabolism/pharmacology/*therapeutic use ; Female ; Hematocrit ; Humans ; Ligands ; Mice ; Mice, Inbred C3H ; Mutagenesis ; Nervous System Diseases/*drug therapy ; Neurons/metabolism ; Neuroprotective Agents/chemistry/metabolism/pharmacology/*therapeutic use ; Rats ; Rats, Sprague-Dawley ; Receptors, Erythropoietin/metabolism ; Recombinant Proteins ; Signal Transduction ; Spinal Cord Compression/drug therapy ; Stroke/drug therapy ; Structure-Activity Relationship
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  • 10
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    Resistance to enediyne antitumor antibiotics by CalC self-sacrifice (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-09-13
    Description: Antibiotic self-resistance mechanisms, which include drug elimination, drug modification, target modification, and drug sequestration, contribute substantially to the growing problem of antibiotic resistance among pathogenic bacteria. Enediynes are among the most potent naturally occurring antibiotics, yet the mechanism of resistance to these toxins has remained a mystery. We characterize an enediyne self-resistance protein that reveals a self-sacrificing paradigm for resistance to highly reactive antibiotics, and thus another opportunity for nonpathogenic or pathogenic bacteria to evade extremely potent small molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Biggins, John B -- Onwueme, Kenolisa C -- Thorson, Jon S -- AI52218/AI/NIAID NIH HHS/ -- CA84374/CA/NCI NIH HHS/ -- GM58196/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2003 Sep 12;301(5639):1537-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Biosynthetic Chemistry, Pharmaceutical Sciences Division, School of Pharmacy, University of Wisconsin-Madison, 777 Highland Avenue, Madison, WI 53705, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12970566" target="_blank"〉PubMed〈/a〉
    Keywords: *Aminoglycosides ; Anti-Bacterial Agents/biosynthesis/chemistry/*pharmacology ; Antibiotics, Antineoplastic/biosynthesis/*pharmacology ; Bacterial Proteins/chemistry/genetics/*metabolism ; DNA/metabolism ; Drug Resistance, Bacterial ; Enediynes ; Escherichia coli/drug effects/genetics ; Metalloproteins/chemistry/*metabolism ; Structure-Activity Relationship
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  • 11
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    Organic chemistry in drug discovery (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-03-20
    Description: The role played by organic chemistry in the pharmaceutical industry continues to be one of the main drivers in the drug discovery process. However, the precise nature of that role is undergoing a visible change, not only because of the new synthetic methods and technologies now available to the synthetic and medicinal chemist, but also in several key areas, particularly in drug metabolism and chemical toxicology, as chemists deal with the ever more rapid turnaround of testing data that influences their day-to-day decisions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacCoss, Malcolm -- Baillie, Thomas A -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1810-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Chemistry, Merck Research Laboratories, 126 East Lincoln Avenue, Rahway, NJ 07065, USA. malcolm_maccoss@merck.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15031494" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Chemistry, Organic ; *Chemistry, Pharmaceutical ; Chemistry, Physical ; Combinatorial Chemistry Techniques ; *Drug Design ; *Drug Evaluation, Preclinical ; *Drug Industry ; Drug-Related Side Effects and Adverse Reactions ; Humans ; Organic Chemistry Phenomena ; *Pharmaceutical Preparations/chemistry/metabolism ; Pharmacokinetics ; Pharmacology ; Physicochemical Phenomena ; Structure-Activity Relationship ; Technology, Pharmaceutical
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  • 12
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    The binding mode of epothilone A on alpha,beta-tubulin by electron crystallography (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-07
    Description: The structure of epothilone A, bound to alpha,beta-tubulin in zinc-stabilized sheets, was determined by a combination of electron crystallography at 2.89 angstrom resolution and nuclear magnetic resonance-based conformational analysis. The complex explains both the broad-based epothilone structure-activity relationship and the known mutational resistance profile. Comparison with Taxol shows that the longstanding expectation of a common pharmacophore is not met, because each ligand exploits the tubulin-binding pocket in a unique and independent manner.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nettles, James H -- Li, Huilin -- Cornett, Ben -- Krahn, Joseph M -- Snyder, James P -- Downing, Kenneth H -- New York, N.Y. -- Science. 2004 Aug 6;305(5685):866-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular and Systems Pharmacology, Emory University, Atlanta, GA 30322, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15297674" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography ; Crystallography, X-Ray ; Epothilones/chemistry/*metabolism/pharmacology ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Ligands ; Models, Molecular ; Molecular Conformation ; Molecular Structure ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; Paclitaxel/metabolism ; Protein Conformation ; Stereoisomerism ; Structure-Activity Relationship ; Tubulin/chemistry/genetics/*metabolism
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  • 13
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    Protein kinase inhibitors: insights into drug design from structure (2004)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2004-03-20
    Description: Protein kinases are targets for treatment of a number of diseases. This review focuses on kinase inhibitors that are in the clinic or in clinical trials and for which structural information is available. Structures have informed drug design and have illuminated the mechanism of inhibition. We review progress with the receptor tyrosine kinases (growth factor receptors EGFR, VEGFR, and FGFR) and nonreceptor tyrosine kinases (Bcr-Abl), where advances have been made with cancer therapeutic agents such as Herceptin and Gleevec. Among the serine-threonine kinases, p38, Rho-kinase, cyclin-dependent kinases, and Chk1 have been targeted with productive results for inflammation and cancer. Structures have provided insights into targeting the inactive or active form of the kinase, for targeting the global constellation of residues at the ATP site or less conserved additional pockets or single residues, and into targeting noncatalytic domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noble, Martin E M -- Endicott, Jane A -- Johnson, Louise N -- New York, N.Y. -- Science. 2004 Mar 19;303(5665):1800-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Biophysics, Department of Biochemistry, Rex Richards Building, University of Oxford, Oxford 3X2 3QU, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15031492" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Antineoplastic Agents/chemistry/pharmacology/therapeutic use ; Binding Sites ; Catalytic Domain ; Clinical Trials as Topic ; *Drug Design ; Enzyme Inhibitors/*chemistry/metabolism/pharmacology/therapeutic use ; Humans ; Models, Molecular ; Molecular Structure ; Protein Conformation ; *Protein Kinase Inhibitors ; Protein Kinases/*chemistry/metabolism ; Protein Structure, Tertiary ; Signal Transduction/drug effects ; Structure-Activity Relationship
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  • 14
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    Dual actions of substance P on nociception: possible role of endogenous opioids (1978)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1978-03-24
    Description: Substance P produces analgesia when administered to mice in very small doses by the intraventricular route (1.25 to 5 nanograms per mouse). The analgesic effect can be blocked by naloxone. At higher doses (greater than 50 nanograms per mouse), this activity is lost. At these higher doses, however, substance P produced hyperalgesia when combined with naloxone and analgesia when combined with baclofen [beta-(4-chlorophenyl)-gamma-aminobutyric acid]. Substance P may have dual actions in brain, releasing endorphins at very low doses and directly exciting neuronal activity in nociceptive pathways at higher doses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frederickson, R C -- Burgis, V -- Harrell, C E -- Edwards, J D -- New York, N.Y. -- Science. 1978 Mar 24;199(4335):1359-62.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/204012" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Baclofen/pharmacology ; Dose-Response Relationship, Drug ; Endorphins/*pharmacology ; Enkephalins/antagonists & inhibitors/*pharmacology ; Mice ; Naloxone/pharmacology ; Nociceptors/*drug effects ; Receptors, Opioid/*drug effects ; Structure-Activity Relationship ; Substance P/analogs & derivatives/antagonists & inhibitors/*pharmacology
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  • 15
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    Peptides in the brain: the new endocrinology of the neuron (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guillemin, R -- New York, N.Y. -- Science. 1978 Oct 27;202(4366):390-402.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/212832" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Endorphins/*history/isolation & purification/pharmacology ; Gonadotropin-Releasing Hormone/isolation & purification ; Growth Hormone-Releasing Hormone/isolation & purification ; History, 20th Century ; Hypothalamic Hormones/*history/pharmacology ; Hypothalamo-Hypophyseal System/*physiology ; *Neurosecretion ; Sheep ; Species Specificity ; Structure-Activity Relationship ; Synaptic Transmission ; Thyrotropin-Releasing Hormone/isolation & purification/physiology
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  • 16
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    Enhancement of bovine pancreatic ribonuclease activity by mercaptoethanol (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-10
    Description: Incubation of ribonuclease with 0.1M mercaptoethanol at pH 8.5 can increase the enzyme's hydrolytic activity toward cytidine 2',3'-monophosphate (cyclic CMP) under standard assay conditions. Cation-exchange chromatography of the ribonuclease-thiol reaction mixture revealed seven fractions. The fraction with the highest activity had an approximate tenfold decrease in the apparent Michaelis constant for cyclic CMP with respect to native ribonuclease. The enhanced activity is a metastable property since this fraction reverts back to the control activity and chromatographic behavior of native ribonuclease on standing in solution at room temperature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watkins, J B -- Benz, F W -- New York, N.Y. -- Science. 1978 Mar 10;199(4333):1084-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/564548" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Disulfides/pharmacology ; Enzyme Activation/drug effects ; Glutathione/pharmacology ; Kinetics ; Mercaptoethanol/*pharmacology ; Oxidation-Reduction ; Pancreas/enzymology ; Protein Conformation ; Ribonucleases/*metabolism ; Structure-Activity Relationship
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  • 17
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    Comparative biochemistry and drug design for infectious disease (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-09-07
    Description: In the past two decades, biochemistry and molecular biology have demonstrated the existence of potentially exploitable biochemical differences between etiologic agents of disease and their hosts. Known differences between organism and host with respect to metabolism and polymer structure point to the detailed characterization of key proteins as the focus for the development of potential inhibitors. In the last decade, the methodology of the isolation, characterization, and inactivation of proteins and enzymes has been advanced. The present scientific and technological base suggests that new efforts toward the development of selective chemotherapeutic agents for infections caused by bacteria, viruses, protozoa, and higher eukaryotes should exploit the known differences in proteins or other specific biopolymers serving crucial structural or metabolic roles in the economy of the parasite.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, S S -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):964-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/382357" target="_blank"〉PubMed〈/a〉
    Keywords: *Anti-Bacterial Agents ; *Antiviral Agents ; Communicable Diseases/*drug therapy ; Humans ; Mycobacterium leprae/metabolism ; Polysaccharides, Bacterial/metabolism ; Species Specificity ; Structure-Activity Relationship ; Trypanosomiasis/drug therapy ; Vidarabine/pharmacology ; Viral Proteins/biosynthesis ; Virus Replication/drug effects
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  • 18
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    Amino acid sequence homology between histone H5 and murine leukemia virus phosphoprotein p12 (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-03-30
    Description: The amino terminal acid sequences of several mouse leukemia virus phosphoproteins (p12) show definite homology with the amino terminal conserved region of H5 histones, the phosphorylated nuclear proteins of nucleated erythrocytes. Differences in the amino acid compositions of the two groups of proteins seem to rule out the possibility that they evolved from a single common ancestral gene. The finding of sequence homology between viral p12's and cellular histones, however, is consistent with evolution of retrovirus structural proteins by a process of differentiation from preexisting cellular genes. The conserved primary and secondary structure at the amino terminal region, common to both groups of proteins, may be related to their common function of nucleic acid binding modulated by phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Henderson, L E -- Gilden, R V -- Oroszlan, S -- New York, N.Y. -- Science. 1979 Mar 30;203(4387):1346-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/218289" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins ; Cell Nucleus/analysis ; Chickens/blood ; Erythrocytes/analysis ; Geese/blood ; *Histones ; Leukemia Virus, Murine/*analysis ; Nucleic Acids/metabolism ; *Phosphoproteins ; Structure-Activity Relationship ; *Viral Proteins
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  • 19
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    Thiourea reverses cross-links and restores biological activity in DNA treated with dichlorodiaminoplatinum (II) (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-04-13
    Description: Cis and trans dichlorodiaminoplatinum (II) compounds bind to DNA and form DNA cross-links, which are usually considered to be irreversible. Thiourea can reverse these cross-links without any apparent breakdown of the DNA. In addition, cis- and trans-Pt (II) treatment of lambda decreases its transfectivity. After suitable incubation with thiourea, full transfectivity of Pt(II)-treated lambda DNA can be restored.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Filipski, J -- Kohn, K W -- Prather, R -- Bonner, W M -- New York, N.Y. -- Science. 1979 Apr 13;204(4389):181-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/571145" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Coliphages ; DNA/*metabolism ; DNA, Neoplasm/metabolism ; DNA, Viral/metabolism ; Leukemia L1210 ; Organoplatinum Compounds/*antagonists & inhibitors ; Structure-Activity Relationship ; Thiourea/*pharmacology
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  • 20
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    Digitalis genin activity: side-group carbonyl oxygen position is a major determinant (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-08-31
    Description: The Na+,k+-adenosine triphosphatase-inhibiting activity of digitalis genins and their analogs is a function of side-group carbonyl (C = O) oxygen position. For each 2.2 angstroms that this oxygen is displaced from its position in digitoxigenin, activity drops by one order of magnitude. This quantitative relation resolves previously proposed models which have attempted to describe the molecular basis of genin activity. A multidisciplinary (crystallographic, conformational energy, synthetic, biological) approach to structure-activity relations is described.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fullerton, D S -- Yoshioka, K -- Rohrer, D C -- From, A H -- Ahmed, K -- New York, N.Y. -- Science. 1979 Aug 31;205(4409):917-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/enzymology ; Digitalis Glycosides/*pharmacology ; Molecular Conformation ; Rats ; Sodium-Potassium-Exchanging ATPase/*antagonists & inhibitors ; Structure-Activity Relationship
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  • 21
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    Specific nonopiate receptors for beta-endorphin (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-09-07
    Description: Iodinated beta H-[2-D-alanine]endorphin exhibits specific binding to cultured human lymphocytes. The binding is inhibited by low concentrations of beta-endorphin and its D-alanine derivative, but is not affected by opiate agonists and antagonists, or by enkephalin analogs, beta-lipotropin, adrenocorticotrophic hormone, or alpha-melanocyte-stimulating hormone; this suggests the existence of a specific, non-opiate binding site (receptor) for beta-endorphin. The carboxy-terminal region of beta-endorphin is essential for this binding activity, since alpha-endorphin is not active. beta-Endorphin may be a circulating hormone with peripheral physiological effects that are not primarily mediated through interactions with opiate or enkephalin receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hazum, E -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):1033-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224457" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cells, Cultured ; Endorphins/blood/*metabolism ; Humans ; Lymphocyte Activation ; Lymphocytes/*metabolism ; Receptors, Drug/*metabolism ; Receptors, Opioid/metabolism ; Stress, Physiological/metabolism ; Structure-Activity Relationship
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  • 22
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    Heterogeneity of vertebrate luteinizing hormone-releasing hormone (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-10-05
    Description: Radioimmunoassay and chromatography analyses of hypothalamic luteinizing hormone-releasing hormone (LHRH) have demonstrated the presence of LHRH-like immunoreactive peptides in a wide range of vertebrates. Contrary to previous reports, the molecule differs in various vertebrates. Avian, reptilian, and teleostean LHRH's are chemically distinct from the mammalian peptide but are in themselves indistinguishable. However, amphibian LHRH appears to be identical to the mammalian peptide. These findings have interesting evolutionary implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉King, J A -- Millar, R P -- New York, N.Y. -- Science. 1979 Oct 5;206(4414):67-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/384514" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Chromatography ; Gonadotropin-Releasing Hormone/*analysis/immunology ; Hypothalamus/analysis ; Radioimmunoassay ; Species Specificity ; Structure-Activity Relationship
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  • 23
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    A structural model for the kinetic behavior of hemoglobin (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-11-30
    Description: The tertiary structures of all liganded hemoglobins in the R state differ in detail. Steric hindrance arising from nonbonded ligand-globin interactions affects the binding of ligands such as CO and cyanide which preferentially form linear axial complexes to heme; these ligands bind in a strained off-axis configuration. Ligands such as O2 and NO, which preferentially form bent complexes, encounter less steric hindrance and can bind in their (preferred) unstrained configuration. Linear complexes distort the ligand pockets in the R state (and by inference, in the T state) more than bent complexes. These structural differences between linear and bent complexes are reflected in the kinetic behavior of hemoglobin. Structural interpretation of this kinetic behavior indicates that the relative contributions of nonbonded ligand-globin interactions and nonbonded heme interactions to transition state free energies differ for linear and bent ligands. The relative contributions of these interactions to the free energy of cooperativity may also differ for linear and bent ligands. Thus the detailed molecular mechanism by which the affinity of heme is regulated differs for different ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moffat, K -- Deatherage, J F -- Seybert, D W -- New York, N.Y. -- Science. 1979 Nov 30;206(4422):1035-42.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493990" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Heme/*metabolism ; Hemoglobins/metabolism ; Horses ; Kinetics ; Ligands ; Oxygen/*metabolism ; Oxyhemoglobins/*metabolism ; Protein Conformation ; Stereoisomerism ; Structure-Activity Relationship
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  • 24
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    Octopamine receptors, adenosine 3',5'-monophosphate, and neural control of firefly flashing (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-01-05
    Description: An adenylate cyclase activated as much as 25-fold by low concentrations of octopamine has been identified in the firefly lantern. The relative potency of octopamine and various other amines in stimulating this enzyme, and effects of antagonists in blocking octopamine activation, correlate well with the known effects of these agents in affecting light production. In addition to suggesting a role for adenosine 3',5'-monophosphate (or pyrophosphate) in the neural control of firefly flashing, identification of this potent enzyme should facilitate the characterization of phenylethylamine receptors in excitable tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nathanson, J A -- New York, N.Y. -- Science. 1979 Jan 5;203(4375):65-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/214856" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*metabolism ; Animals ; Beetles/*physiology ; Catecholamines/pharmacology ; Cyclic AMP/*biosynthesis ; Dose-Response Relationship, Drug ; Enzyme Activation/drug effects ; Kinetics ; Octopamine/*pharmacology ; Phentolamine/pharmacology ; Propranolol/pharmacology ; Receptors, Cell Surface/*drug effects ; Receptors, Neurotransmitter/*drug effects ; Structure-Activity Relationship
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  • 25
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    N-acetyl gramicidin: single-channel properties and implications for channel structure (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-01-05
    Description: Substitution of a methyl group for the N-terminal hydrogen of gramicidin greatly increased the rate of dissociation of conductive channels in lipid bilayer membranes. The finding of short lifetimes for conductive channels, comparable to those seen for the neuromuscular junction, lends support to the head-to-head dimer structure for the conductive channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Szabo, G -- Urry, D W -- New York, N.Y. -- Science. 1979 Jan 5;203(4375):55-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/83000" target="_blank"〉PubMed〈/a〉
    Keywords: Cations, Monovalent ; Electric Conductivity ; *Gramicidin ; *Ion Channels ; Membranes, Artificial ; Models, Biological ; Structure-Activity Relationship
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  • 26
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    Elimination of metabolic cooperation in Chinese hamster cells by a tumor promoter (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-11-30
    Description: Wild-type Chinese hamster V79 cells (6-thioguanine-sensitive) reduce the recovery of 6-thioguanine-resistant cells when they are cultured together at high densities, through a form of intercellular communication (metabolic cooperation). Cooperation is inhibited by 12-O-tetradecanoyl phorbol-13-acetate, rescuing the 6-thioguanine-resistant cells. These results may be useful in the study of an aspect of the mechanism of tumor promotion and in assaying for promoters.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yotti, L P -- Chang, C C -- Trosko, J E -- New York, N.Y. -- Science. 1979 Nov 30;206(4422):1089-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493994" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Communication/*drug effects ; Cell Membrane/drug effects ; Cricetinae ; Dose-Response Relationship, Drug ; Drug Resistance ; Phorbol Esters/*pharmacology ; Phorbols/*pharmacology ; Structure-Activity Relationship ; Tetradecanoylphorbol Acetate/pharmacology ; Thioguanine/pharmacology
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  • 27
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    Photoejection of electrons from flavins in polar media (1978)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1978-08-18
    Description: Riboflavin and 12 of its derivatives have been shown to form solvated electrons under ultraviolet irradiation (253.7 nanometers) in various water-methanol solvent mixtures. The highest quantum yield of solvated electrons (about 0.03) was obtained for flavins containing tyrosine on a side chain in the isoalloxazine N-3 or N-10 position. The splitting of hydrogen atoms from excited flavin molecules was also observed. From the results presented here, it can be determined that the semiquinone transients are formed not only by way of the flavin triplet, as usually suggested, but also by the attack of the electrons and hydrogen atoms on flavin molecules in the ground state. This is important, because the flavin radicals remaining after the electron-ejection or hydrogen-splitting processes must also be considered in the subsequent reaction mechanisms. The electron-ejection process from electronically excited flavins has important implications in the photobiology of these compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Getoff, N -- Solar, S -- New York, N.Y. -- Science. 1978 Aug 18;201(4356):616-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/675244" target="_blank"〉PubMed〈/a〉
    Keywords: Electrons ; Methanol ; Oxidation-Reduction ; Photochemistry ; Riboflavin/*analogs & derivatives/*radiation effects ; Solvents ; Structure-Activity Relationship ; *Ultraviolet Rays ; Water
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  • 28
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    Another flame retardant, tris-(1,3-dichloro-2-propyl)-phosphate, and its expected metabolites are mutagens (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-05-19
    Description: A flame retardant used in children's sleepwear, tris-(1,3-dichloro-2-propyl)phosphate (Fyrol FR2) is a mutagen in the Salmonella-mammalian tissue homogenate test after it has been activated by mouse or rat liver homogenate. The expected enzymatic hydrolysis product, 1,3-dichloro-2-propanol, is similarly a mutagen after activation by liver homogenate. A proposed metabolite of the flame retardant, 1,3-dichloro-2-propanone, is a potent mutagen in the absence of such activation. A flame retardant with similar structure, tris-(2,3-dibromopropyl)phosphate (tris-BP), was shown previously to be a mutagen, to cause sterility in animals, to be a carcinogen, and to be absorbed through human skin. These and other flame retardants have characteristic nuclear magnetic resonance spectra that can be used to determine which flame retardant is present in commercially purchased sleepwear. Sleepwear treated with tris-BP, Fyrol FR2, and other chemical additives was being sold in late 1977.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gold, M D -- Blum, A -- Ames, B N -- New York, N.Y. -- Science. 1978 May 19;200(4343):785-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/347576" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biotransformation ; Flame Retardants/*toxicity ; Hydrocarbons, Chlorinated/toxicity ; Liver/metabolism ; Mice ; *Mutagens ; Organophosphorus Compounds/*toxicity ; Salmonella typhimurium/drug effects ; Structure-Activity Relationship
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    Channel structures of gramicidin: characterization of succinyl derivatives (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-04-28
    Description: Succinyl derivatives of gramicidin were tested for their ability to form channels in planar artificial lipid bilayers. Both N-succinyldeformylgramicidin methyl ester and charged O-succinylgramicidin formed channels, but the channels had markedly different sizes and lifetimes. This implies that gramicidin forms channels by end-to-end association. However, the doubly charged N,O-bissuccinyldeformylgramicidin was inactive, which suggests that only end-to-end association of gramicidin may result in channel formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradley, R J -- Urry, D W -- Okamoto, K -- Rapaka, R -- New York, N.Y. -- Science. 1978 Apr 28;200(4340):435-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/77040" target="_blank"〉PubMed〈/a〉
    Keywords: Electric Conductivity ; *Gramicidin ; Hydrogen Bonding ; Ionophores ; Membranes, Artificial ; Protein Conformation ; Structure-Activity Relationship
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    Electrostatic effects in proteins (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-29
    Description: Electrostatic effects dominate many aspects of protein behavior. When polypeptide chains fold up, most polar side chains seek the exterior, where they can be solvated. Water bound in the interior has been found between the domains of enzymes of the chymotrypsin family, and between the subunits of hemoglobin and tobacco mosaic virus protein. Assembly of this protein from disk to virus is triggered by electrostatic interactions between neighboring subunits. Lysozyme stabilizes the constellation of charges involved in the transition state of its substrate by both permanent and induced dipoles. All factors that lower the oxygen affinity of hemoglobin act by strengthening the salt bridges that constrain its quaternary deoxy (T) structure. Enzymes of thermophile bacteria owe their extra stability mostly to additional salt bridges. The rate of denaturation of hemoglobins by alkali is determined by the ionization of internal side chains with pK's of about 12.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Perutz, M F -- New York, N.Y. -- Science. 1978 Sep 29;201(4362):1187-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/694508" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Catalysis ; Ions ; Macromolecular Substances ; Protein Conformation ; Protein Denaturation ; *Proteins ; Salts ; Structure-Activity Relationship ; Temperature ; Viruses/ultrastructure ; Water
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  • 31
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    Tricyclic antidepressants: therapeutic properties and affinity for alpha-noradrenergic receptor binding sites in the brain (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-01-13
    Description: Tricyclic antidepressants vary in their capacity to cause psychomotor activation, to relieve agitated depressive states, and to cause sedation and hypotension. We have quantified relative potencies of tricyclic antidepressants in competing for the binding of 3H-labeled WB-4101 to alpha-noradrenergic receptor sites in rat brain membranes. Affinities of tricyclic drugs for alpha-noradrenergic receptor sites in the brain correlate well with the capacity of these agents to relieve psychomotor agitation and to induce sedation and hypotension; these affinities also correlate inversely with tendencies to elicit psychomotor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉U'Prichard, D C -- Greenberg, D A -- Sheehan, P P -- Snyder, S H -- New York, N.Y. -- Science. 1978 Jan 13;199(4325):197-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/202024" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antidepressive Agents, Tricyclic/*metabolism/therapeutic use ; Binding, Competitive ; Brain/*metabolism ; Humans ; Hypotension/chemically induced ; Psychomotor Agitation/*drug therapy ; Rats ; Receptors, Adrenergic/*metabolism ; Receptors, Adrenergic, alpha/*metabolism ; Structure-Activity Relationship
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  • 32
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    Sporozoite-induced malaria: therapeutic effects of glycolipids in liposomes (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-09-14
    Description: Liposomes containing neutral glycolipids with a terminal glucose or galactose, when injected intravenously, prevented the appearance of erythrocytic forms of malaria (Plasmodium berghei) in mice previously injected with sporozoites. Inhibitory glycolipids included glucosyl, galactosyl, or lactosyl ceramide. Inhibition was not observed with liposomes containing ceramide, phosphocholine ceramide, sulfogalactosyl ceramide (sulfatide), or ganglioside GM1. Liposomes containing glycolipids did not inhibit infection transmitted by injecting blood containing erythrocytic stages of malaria. These results may have therapeutic implications in the treatment of malaria. Analysis of the mechanism of interference with the life cycle of malaria by liposomal glycolipids may yield information about the interactions of parasites with cellular membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alving, C R -- Schneider, I -- Swartz, G M Jr -- Steck, E A -- New York, N.Y. -- Science. 1979 Sep 14;205(4411):1142-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/382358" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ceramides/therapeutic use ; Erythrocytes/parasitology ; Glycolipids/*therapeutic use ; Liposomes/therapeutic use ; Liver/parasitology ; Malaria/parasitology/*therapy ; Mice ; Plasmodium berghei ; Structure-Activity Relationship
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  • 33
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    Vasopressin analog with extraordinarily high antidiuretic potency: a study of conformation and activity (1978)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1978-01-20
    Description: Application of information derived from a three-dimensional model of vasopressin bound to its antidiuretic receptor has resulted in the design and synthesis of a potent analog, [1-deamino, 2-phenylalanine, 7-(3,4-dehydroproline)]-arginine vasopressin; this analog has a specific antidiuretic activity of 13,000 +/- 1,250 units per milligram; noteworthy at these doses is the absence of any detectable pressor activity. Three modifications based on conformational considerations were introduced into the vasopressin molecule in preparing the analog: (i) to enhance binding, a double bond was introduced into the side chain of an amino acid residue occupying a corner position of a beta turn in the vasopressin conformation, (ii) the hydroxyl moiety was deleted from Tyr2, and (iii) to tighten the backbone structure and to enhance the enzymatic resistance of the analog, the NH2-terminal amino group was deleted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C W -- Walter, R -- New York, N.Y. -- Science. 1978 Jan 20;199(4326):297-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/619455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Deamino Arginine Vasopressin/analogs & derivatives ; Diuresis/drug effects ; Heart Rate/drug effects ; Protein Conformation ; Structure-Activity Relationship ; Vasopressins/*analogs & derivatives/pharmacology
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  • 34
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    Physical factors affecting the mutagenicity of fly ash from a coal-fired power plant (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-05-25
    Description: The two finest, most respirable coal fly ash fractions collected from the smokestack of a power plant were more mutagenic than two coarser fractions. Mutagenicity was evaluated in the histidine-requiring bacterial strains TA 1538, TA 98, and TA 100 of Salmonella typhimurium. Ash samples collected from the hoppers of an electrostatic precipitator in the plant were not mutagenic. The mutagens in coal fly ash were resistant to x-ray or ultraviolet irradiation, possibly as a result of stabilization by fly ash surfaces. All mutagenic activity is lost with heating to 350 degrees C.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fisher, G L -- Chrisp, C E -- Raabe, O G -- New York, N.Y. -- Science. 1979 May 25;204(4395):879-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/375394" target="_blank"〉PubMed〈/a〉
    Keywords: Air Pollutants/*toxicity ; Carcinogens ; Coal ; Hot Temperature ; Industry ; *Mutagens ; *Power Plants ; Radiation Effects ; Salmonella typhimurium/drug effects ; Structure-Activity Relationship
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  • 35
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    Cyclic polyether-protonated organic amine binding: significance in enzymatic and ion transport processes (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-03-03
    Description: The cyclic polyether, 18-crown-6, reacts with protonated amines in methanol to form complexes whose formation constants (log K) decrease in the order NH4+, RNH3+ greater than R2NH2+ greater than R3NH+. In the case of the organic amines, this stability order is identical to the earlier observed permeability sequence for protonated organic amines in glyceryl dioleate bilayers treated with valinomycin, nonactin, or gramicidin, and in bullfrog and rabbit gallbladder membranes. The decrease in log K values in the above series is primarily a result of decreased enthalpy change (deltaH) values, the entropy change (TdeltaS) term being essentially constant for the systems studied.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Izatt, R M -- Izatt, N E -- Rossiter, B E -- Christensen, J J -- Haymore, B L -- New York, N.Y. -- Science. 1978 Mar 3;199(4332):994-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/622582" target="_blank"〉PubMed〈/a〉
    Keywords: Amines/*metabolism ; Biological Transport ; Enzymes/metabolism ; Ethers, Cyclic/*metabolism ; Hydrogen Bonding ; Membranes/metabolism ; Permeability ; Protons ; Structure-Activity Relationship ; Thermodynamics
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  • 36
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    Aspects of hypothalamic regulation of the pituitary gland (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schally, A V -- New York, N.Y. -- Science. 1978 Oct 6;202(4363):18-28.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/99816" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Awards and Prizes ; Gonadotropin-Releasing Hormone/isolation & purification/physiology ; Hormones/pharmacology ; Hypothalamic Hormones/*physiology ; Hypothalamus/*physiology ; Pituitary Gland, Anterior/*physiology ; Somatostatin/isolation & purification/physiology ; Structure-Activity Relationship ; Thyrotropin-Releasing Hormone/isolation & purification
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  • 37
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    The glycosylation of hemoglobin: relevance to diabetes mellitus (1978)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1978-04-07
    Description: Glucose reacts nonenzymatically with the NH2-terminal amino acid of the beta chain of human hemoglobin by way of a ketoamine linkage, resulting in the formation of hemoglobin AIc. Other minor components appear to be adducts of glucose 6-phosphate and fructose 1,6-diphosphate. These hemoglobins are formed slowly and continuously throughout the 120-day life-span of the red cell. There is a two- to threefold increase in hemoglobin AIc in the red cells of patients with diabetes mellitus. By providing an integrated measurement of blood glucose, hemoglobin AIc is useful in assessing the degree of diabetic control. Furthermore, this hemoglobin is a useful model of nonenzymatic glycosylation of other proteins that may be involved in the long-term complications of the disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bunn, H F -- Gabbay, K H -- Gallop, P M -- New York, N.Y. -- Science. 1978 Apr 7;200(4337):21-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/635569" target="_blank"〉PubMed〈/a〉
    Keywords: Blood Glucose/metabolism ; Chemical Phenomena ; Chemistry ; Diabetes Complications ; Diabetes Mellitus/*blood/diagnosis ; Diphosphoglyceric Acids/blood ; Glycosides/blood ; Glycosuria/etiology ; Hemoglobin A/*metabolism ; Hemoglobins/*analysis/*metabolism ; Humans ; Kinetics ; Oxygen/blood ; Structure-Activity Relationship
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  • 38
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    Conformation of [Leu5]enkephalin from X-ray diffraction: features important for recognition at opiate receptor (1978)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1978-03-17
    Description: The conformation of [Leu5]enkephalin is produced by a Tyr-Gly-Gly-Phe beta bend stabilized by antiparallel hydrogen bonding between tyrosine and phenylalanine. On the basis of a comparison of the observed structure with the structure of known opiate agonists, three hydrophilic and two hydrophobic regions have been identified as contributing to the recognition of the molecule at the opiate receptor site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, D -- Griffin, J F -- New York, N.Y. -- Science. 1978 Mar 17;199(4334):1214-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/204006" target="_blank"〉PubMed〈/a〉
    Keywords: *Endorphins/metabolism ; *Enkephalins/metabolism ; Hydrogen Bonding ; Models, Molecular ; Morphine ; Protein Conformation ; Receptors, Opioid/metabolism ; Structure-Activity Relationship ; X-Ray Diffraction
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  • 39
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    Space-filling models of kinase clefts and conformation changes (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-04-27
    Description: Space-filling models of yeast hexokinase, adenylate kinase, and phosphoglycerate kinase drawn by computer clearly portray the bilobal character of these phosphoryl transfer enzymes, and the deep cleft which is formed between the lobes. A dramatic conformational change occurs in hexokinase as glucose binds to the bottom of the cleft, which causes the two lobes of hexokinase to come together. A substrate-induced closing of the active site cleft is postulated to occur in other kinases as well. This change may provide a mechanism by which some of these enzymes reduce their inherent adenosine triphosphatase activity and could be a general requirement of the kinase reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Anderson, C M -- Zucker, F H -- Steitz, T A -- New York, N.Y. -- Science. 1979 Apr 27;204(4391):375-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/220706" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylate Kinase ; Binding Sites ; Catalysis ; Hexokinase ; Models, Molecular ; Phosphoglycerate Kinase ; *Phosphotransferases ; Protein Conformation ; Saccharomyces cerevisiae/enzymology ; Structure-Activity Relationship
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  • 40
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    Selective phospholipid adsorption and atherosclerosis (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-05-04
    Description: Disaturated (fully saturated) lecithins adsorb onto solid surfaces more readily than lecithins in which one or both fatty acids are unsaturated. If saturated lecithins adsorb to arterial walls as they do to glass and polystyrene surfaces, there may be increased probability of atherosclerosis when the disaturated lecithin content of plasma is elevated. Analyses of lecithins in plasma samples from patients with myocardial infarction, and from patients with premature atherosclerosis but with low concentrations of plasma cholesterol and triglycerides, are consistent with the hypothesis that a high concentration of disaturated lecithin in plasma may be a significant risk factor for atherosclerosis, independent of triglyceride and cholesterol concentrations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gershfeld, N L -- New York, N.Y. -- Science. 1979 May 4;204(4392):506-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/581915" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Adult ; Aged ; Arteriosclerosis/blood/*etiology ; Coronary Disease/*blood ; Fatty Acids, Unsaturated ; Female ; Humans ; Male ; Middle Aged ; Myocardial Infarction/blood ; *Phosphatidylcholines/blood ; Pulmonary Surfactants/blood ; Structure-Activity Relationship ; Temperature
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  • 41
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    A synthetic pentapeptide with biological activity characteristic of the thymic hormone thymopoietin (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-06-22
    Description: The pentapeptide arginyl-lysyl-aspartyl-valyl-tyrosine, corresponding to amino acid residues 32--36 in thymopoietin, was synthesized. In vitro, this pentapeptide induced the differentiation of murine prothymocytes to thymocytes and inhibited differentiative induction of cells of the B lineage. This combination of actions is presently unique to the parent molecule thymopoietin. In vivo, the pentapeptide reduced the high numbers of autologous rosette-forming cells normally present in the spleens of athymic mice; this also is a property of thymopoietin. These results suggest that this readily synthesized pentapeptide corresponds to an active site of thymopoietin and might serve as a therapeutic substitute for thymopoietin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldstein, G -- Scheid, M P -- Boyse, E A -- Schlesinger, D H -- Van Wauwe, J -- New York, N.Y. -- Science. 1979 Jun 22;204(4399):1309-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, Surface/analysis ; Cell Differentiation/drug effects ; Complement System Proteins ; Isoantigens/analysis ; Lymphocytes/cytology/*immunology ; Mice ; Mice, Nude/immunology ; Oligopeptides/chemical synthesis/*pharmacology ; Receptors, Drug/analysis ; Structure-Activity Relationship ; Thymopoietins/*pharmacology ; Thymus Hormones/*pharmacology
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  • 42
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    Genetic effects of impure and pure saccharin in yeast (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-09-07
    Description: Yeast cells were grown in media containing impure or purified saccharin preparations. Dose-dependent increases in frequencies of cells possessing aberrant cell morphologies were revealed by light microscopy. At each test dose, cells grown in impure saccharin exhibited up to sevenfold higher frequencies of mitotic crossing-over or gene conversion in three of four assays for genetic recombination than cells grown in purified saccharin from the same lot. With one exception, the sweetener produced by the Maumee process caused larger increases in recombination and gene reversion than the sweetener produced by the Remsen-Fahlberg process. The several test markers did not respond equally to any test saccharin. Cells grown in liquid media containing no saccharin or two of three test concentrations of saccharin produced cell titers that were approximately equivalent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, C W -- Schmick, A -- New York, N.Y. -- Science. 1979 Sep 7;205(4410):1007-10.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/382356" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Division/drug effects ; Crossing Over, Genetic/drug effects ; Dose-Response Relationship, Drug ; Mitosis/drug effects ; *Mutagens ; Recombination, Genetic/drug effects ; Saccharin/chemical synthesis/*pharmacology ; Saccharomyces cerevisiae/*drug effects ; Structure-Activity Relationship
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  • 43
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    Differential competition with cytotoxic agents: an approach to selectivity in cancer chemotherapy (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-11-30
    Description: An approach to increasing the selectivity of cancer chemotherapeutic agents is presented in which noncytotoxic competitive substrates are used to discern the differences in structural requirements for transport of cytotoxic agents between tumor cells and a sensitive host tissue, the hematopoietic precursor cells of the bone marrow. Examples are given for two such systems, one responsible for the transport of nucleosides and another for the transport of amino acids. Cytidine is twice as effective in reducing the toxicity of showdomycin for murine bone marrow cells in culture as it is for murine L1210 leukemia cella. Conversely, homoleucine is twice as effective in reducing the toxicity of melphalan for L1210 cells as it is for bone marrow cells. These observations can serve as a basis for the development of bone marrow protective agents and for the design of cytotoxic agents that may be preferentially transported into tumor cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rabinowitz, M -- Uehara, Y -- Vistica, D T -- New York, N.Y. -- Science. 1979 Nov 30;206(4422):1085-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493993" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibiotics, Antineoplastic/*metabolism ; Biological Transport ; Bone Marrow/drug effects ; Leukemia L1210/drug therapy ; Melphalan/metabolism/therapeutic use ; Mice ; Neoplasms/*drug therapy ; Showdomycin/*metabolism/therapeutic use ; Structure-Activity Relationship
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  • 44
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    Effect of fluorine substitution on the agonist specificity of norepinephrine (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-06-15
    Description: Substitution of fluorine for hydrogen in position 2, 5, or 6 of the aromatic ring of norepinephrine markedly alters the alpha- and beta-adrenergic agonist properties of norephinephrine. The 6-fluoro isomer is an beta-adrenergic agonist with virtually no beta agonist activity, while the 2-fluoro isomer is a beta-adrenergic agonist with little alpha activity. The 5-fluoro isomer is equipotent with norepinephrine as an alpha agonist and significantly more potent as a beta agonist. The possible physiochemical basis for these differences is discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cantacuzene, D -- Kirk, K L -- McCulloh, D H -- Creveling, C R -- New York, N.Y. -- Science. 1979 Jun 15;204(4398):1217-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/221978" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aorta ; Fluorine ; Guinea Pigs ; Hydrogen Bonding ; In Vitro Techniques ; Norepinephrine/*analogs & derivatives/chemical synthesis/pharmacology ; Receptors, Adrenergic/*drug effects ; Receptors, Adrenergic, alpha/*drug effects ; Receptors, Adrenergic, beta/*drug effects ; Structure-Activity Relationship
    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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  • 45
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    Partially modified retro-inverso-enkephalinamides: topochemical long-acting analogs in vitro and in vivo (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-06-15
    Description: The synthesis of four enkephalinamide analogs is described in which the peptide bond between residues 4 and 5 is reversed with or without simultaneous reversal of the carboxyl-terminal amide bond. These so-called partially modified retro-inverso-isomers are new, potent, topochemical analogs of the enkephalins. Tests, both in vitro and in vivo, have shown that these analogs are considerably longer acting than any previously studied enkephalins. Thus, partial reversal of the peptide bonds of the backbone can result in peptides with enhanced activity compared to a parent compound, provide that the structural complementarity of both the side chains and end groups are conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chorev, M -- Shavitz, R -- Goodman, M -- Minick, S -- Guillemin, R -- New York, N.Y. -- Science. 1979 Jun 15;204(4398):1210-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451565" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/drug effects ; Brain/drug effects ; Endorphins/*pharmacology ; Enkephalins/chemical synthesis/metabolism/*pharmacology ; Rats ; Structure-Activity Relationship
    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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  • 46
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    Heparin: an old drug with a new paradigm (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-11-02
    Description: Recent studies have shown that heparin is a biochemical representative of a distinct class of compounds known as linear anionic polyelectrolytes. Members of this class are mixtures of individual highly negatively charged chains that show a wide spectrum of specific reactions with biologically active proteins. Upon administration, heparin chains enter a cellular pool and effectively prevent thrombosis by increasing the electronegative potential of the vessel wall. Anticoagulant activity is an unusual feature of a few heparin chains and appears to play a minor role in many clinical uses and in physiological and pathological responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacques, L B -- New York, N.Y. -- Science. 1979 Nov 2;206(4418):528-33.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/386509" target="_blank"〉PubMed〈/a〉
    Keywords: Antithrombin III/metabolism ; Blood Coagulation/drug effects ; Heparin/adverse effects/*pharmacology/therapeutic use ; Humans ; Ions ; Mast Cells/physiology ; Structure-Activity Relationship ; Sulfates/metabolism ; Thrombosis/prevention & control
    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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  • 47
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    Inhibition of mast cell histamine secretion by N-substituteed derivatives of phosphatidylserine (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-11
    Description: The structural basis for the highly specific action of phosphatidylserine in enhancing mast cell histamine secretion induced by concanavalin A was investigated by studying the activities of three N-substituted derivatives: N-acetyl phosphatidylserine, N-1-dimethylaminonaphthalene-5-sulfonly phosphatidylserine, and N-4-nitrobenzo-2-oxa-1,3-diazole phosphatidylserine. None of the derivatives was capable of activating concanavalin A-induced histamine secretion at concentrations two to three times that required for maximal activation by phosphatidylserine. Instead, the derivatives were found to inhibit the secretory response of mast cells to the calcium ionophore A23187 as well as to concanavalin A. The inhibition was noncytotoxic, partially reversible by washing, and associated with binding of N-substituted phosphatidylserine to the mast cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, T W -- Lagunoff, D -- New York, N.Y. -- Science. 1979 May 11;204(4393):631-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/86210" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/drug effects ; Exocytosis/drug effects ; Histamine Release/*drug effects ; Mast Cells/*drug effects ; Phosphatidylserines/*pharmacology ; Rats ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 48
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    Liposomes and local hyperthermia: selective delivery of methotrexate to heated tumors (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-13
    Description: Liposomes with phase transitions a few degrees above physiological temperature delivered more than four times as much methotrexate to murine tumors heated to 42 degrees C as to unheated control tumors. Most of the accumulated drug appeared to be intracellular and bound to dihydrofolate reductase, the enzyme blocked by methotrexate in its role as an antineoplastic agent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weinstein, J N -- Magin, R L -- Yatvin, M B -- Zaharko, D S -- New York, N.Y. -- Science. 1979 Apr 13;204(4389):188-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432641" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Hot Temperature ; Liposomes/*therapeutic use ; Male ; Metabolic Clearance Rate ; Methotrexate/*administration & dosage/metabolism ; Mice ; Neoplasms, Experimental/*drug therapy ; Phospholipids ; Structure-Activity Relationship
    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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