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  • Binding Sites
  • Models, Molecular
  • Protein Conformation
  • American Association for the Advancement of Science (AAAS)  (29)
  • 1975-1979  (29)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (29)
Years
Year
  • 1
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    Molecular conformation of a halogen-free thyroxine analog: 4-Methoxy-3,5,3-trimethyl-L-thyronine N-acetyl ethyl ester (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-22
    Description: The molecular conformation of the halogen-free thyroxine analog 4-methoxy-3,5,3'-trimethyl-L-thyronine -n-acetyl ethyl ester has been determined by x-ray diffraction techniques. The unsubstituted parent compound, trimethylthyronine, has significant biological activity in rat thymocyte tests when compared with the thyroid hormone 3,5,3'-triiodo-L-thyronine (T3). Although no activity data are available for the analog studied, it is presumed to be inactive because of the 4-methoxy blocking group. The observed conformation of this structure is similar to that found for the natural hormone T(3). The 3'-methyl group is distal, the overall conformation is cisoid, and the diphenyl ether conformation is twist-skewed. The results of this diffraction study show that methyl substituents are capable of maintaining the thyronine conformation required for hormonal activity; they suggest that iodine enhances hormone-protein binding because of the electronic effects it produces either by alteration of molecular charge distributions or by direct charge-transfer interactions with the serum or nuclear binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cody, V -- New York, N.Y. -- Science. 1978 Sep 22;201(4361):1131-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/684433" target="_blank"〉PubMed〈/a〉
    Keywords: Models, Molecular ; Molecular Conformation ; Thyronines/*analogs & derivatives ; 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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  • 2
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    The biology of oxygen radicals (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-08
    Description: The reactive superoxide radical, O2-, formerly of concern only to radiation chemists and radiobiologists, is now understood to be a normal product of the biological reduction of molecular oxygen. An unusual family of enzymes, the superoxide dismutases, protect against the deleterious actions of this radical by catalyzing its dismutation to hydrogen peroxide plus oxygen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fridovich, I -- New York, N.Y. -- Science. 1978 Sep 8;201(4359):875-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/210504" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Catalase/metabolism ; Free Radicals ; Inflammation/metabolism ; Kinetics ; Metals ; Oxidation-Reduction ; Oxygen/*metabolism ; Paraquat/pharmacology ; Peroxidases/metabolism ; Superoxide Dismutase/*metabolism ; Superoxides/*metabolism/toxicity
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  • 3
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    Thrombin-induced platelet aggregation is mediated by a platelet plasma membrane-bound lectin (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-16
    Description: Throbin-activated human platelets cause agglutination of trypsinized, formalinized bovine erythrocytes. This lectin activity of stimulated platelets was blocked by galactosamine, glucosamine, mannosamine, lysine, and arginine, but not by N-acetylated sugars, other neutral sugars, or other amino acids. Inhibitors of the thrombin-induced lectin activity also blocked thrombin-induced platelet aggregation. It appears that a membrane surface component that has lectin activity mediates platelet aggregation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gartner, T K -- Williams, D C -- Minion, F C -- Phillips, D R -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1281-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663608" target="_blank"〉PubMed〈/a〉
    Keywords: *Agglutinins ; Amino Acids/pharmacology ; Amino Sugars/pharmacology ; Animals ; Binding Sites ; Cytochalasin B/pharmacology ; *Hemagglutinins ; Humans ; Membrane Proteins/blood ; Platelet Aggregation/*drug effects ; Prostaglandins E/pharmacology ; Species Specificity ; Thrombin/*pharmacology
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  • 4
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    Synchrotron radiation: new window on metalloprotein structure (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-07-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1978 Jul 21;201(4352):243-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663653" target="_blank"〉PubMed〈/a〉
    Keywords: Ferritins ; Hemoglobins ; Ligands ; *Metalloproteins ; Molybdenum ; Nitrogenase ; Oxyhemoglobins ; *Particle Accelerators ; Protein Conformation ; Spectrophotometry, Atomic/methods
    Print ISSN: 0036-8075
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  • 5
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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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  • 6
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    The hydrophobic effect and the organization of living matter (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-02
    Description: Biological organization may be viewed as consisting of two stages: biosynthesis and assembly. The assembly process is largely under thermodynamic control; that is, as a first approximation it represents a search by each structural molecule for its state of lowest chemical potential. The hydrophobic effect is a unique organizing force, based on repulsion by the solvent instead of attractive forces at the site of organization. It is responsible for assembly of membranes of cells and intracellular compartments, and the absence of strong attractive forces makes the membranes fluid and deformable. The spontaneous folding of proteins, however, involves directed polar bonds, leading to more rigid structures. Intercellular organization probably involves polar bonds between cell surface proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tanford, C -- New York, N.Y. -- Science. 1978 Jun 2;200(4345):1012-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/653353" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Compartmentation ; Cells/*ultrastructure ; Chemistry, Physical ; Membrane Proteins ; Membranes/ultrastructure ; Micelles ; *Models, Biological ; Phospholipids ; Physicochemical Phenomena ; Protein Conformation ; Solubility ; *Thermodynamics ; Water
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  • 7
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    Distribution of transmembrane polypeptides in freeze fracture (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-03-30
    Description: Human erythrocytes have been freeze-fractured, and the polypeptides associated with the separate halves of the membrane bilayer have been analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The transmembrane proteins were differentially separated by the fracture process. Although sialoglycoproteins associated with the outer half of the membrane, the anion transport protein (band 3) mainly remained with the inner half of the membrane. Well-defined fragments of the sialoglycoproteins were produced by the freeze-fracture procedure, indicating that selected covalent bonds of these transmembrane proteins were broken.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Edwards, H H -- Mueller, T J -- Morrison, M -- New York, N.Y. -- Science. 1979 Mar 30;203(4387):1343-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/424755" target="_blank"〉PubMed〈/a〉
    Keywords: Erythrocyte Membrane/*ultrastructure ; Erythrocytes/*ultrastructure ; Freeze Fracturing/methods ; Glycoproteins/blood ; Humans ; Macromolecular Substances ; *Membrane Proteins/blood ; Molecular Weight ; Polylysine ; Protein Binding ; Protein Conformation
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  • 8
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    Time-resolved europium(III) excitation spectroscopy: a luminescence probe of metal ion binding sites (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-12-07
    Description: A laser-induced luminescence technique is introduced for probing the structure and equilibria of lanthanide complexes and lanthanide ion binding to macromolecules. The method involves the excitation of the 7F0 leads to 5D0 transition between nondegenerate levels in the europium(III) ion by means of an intense pulsed dye laser source. Excitation profits obtained by scanning the laser through the transition region reveal distinct peaks characteristic of individual europium(III) ion environments. The technique may be used to characterize the species present in complex equilibria in solution or to study europium(III) binding to macromolecules. Distinct europium(III) binding sites in thermolysin with long and short excited state lifetimes are observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horrocks, W D Jr -- Sudnick, D R -- New York, N.Y. -- Science. 1979 Dec 7;206(4423):1194-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/505007" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Europium ; Luminescence ; Protein Binding ; Spectrum Analysis/methods ; Thermolysin
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  • 9
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    Radioimmunoassay of the insulin receptor: a new probe of receptor structure and function (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-02-09
    Description: A sensitive and specific radioimmunoassay for the insulin receptor has been developed employing receptor autoantibodies from the serum of a patient with insulin-resistant diabetes. The assay detects insulin binding sites at concentrations as low as 0.1 nanomolar; distinguishes between receptors originating from human placental membranes, human lymphoblastoid cells, and mouse liver membranes; and measures the receptor independently of its binding function. Down-regulation, or loss of binding after exposure to insulin, is associated with loss of immunoreactive receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harrison, L C -- Flier, J -- Itin, A -- Kahn, C R -- Roth, J -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):544-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/83675" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Antibody Reactions ; Binding Sites ; Binding Sites, Antibody ; Epitopes ; Female ; Humans ; Liver/analysis ; Lymphocytes/analysis ; Mice ; Placenta/analysis ; Pregnancy ; Radioimmunoassay/methods ; Receptor, Insulin/analysis/*immunology ; Solubility
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  • 10
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    A structural model for the kinetic behavior of hemoglobin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    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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  • 11
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    Fibrinopeptide B and aggregation of fibrinogen (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-13
    Description: Removal of fibrinopeptide B from human fibrinogen by reaction with the procoagulant enzyme from copperhead snake venom below 25 degrees C resulted in tight aggregation of the fibrinogen, which, in turn, progressively blocked a concomitant but sluggish release of fibrinopeptide A by the enzyme. When the clots obtained at less than 25 degrees C were warmed, they dissociated into soluble aggregates and monomers. Release of fibrinopeptide A then resumed, and a secondary coagulation followed. The aggregation induced by release of fibrinopeptide B itself involves a plasmin-susceptible segment located just distal to B in the B beta chain of fibrinogen, a segment previously shown to be of little importance in the aggregation induced by release of fibrinopeptide A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shainoff, J R -- Dardik, B N -- New York, N.Y. -- Science. 1979 Apr 13;204(4389):200-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/155308" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crotalid Venoms/*metabolism ; Fibrinogen/*metabolism ; Fibrinolysin/metabolism ; Fibrinopeptide A/metabolism ; Fibrinopeptide B/*metabolism ; Humans ; Molecular Weight ; Protein Binding ; Temperature
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  • 12
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    Structure of collagen in cartilage of intervertebral disk (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-02-03
    Description: Small-angle x-ray and neutron diffraction patterns have been obtained from the annulus fibrosus of porcine intervertebral disk. These show that the collagen in this tissue is modified compared with that in tendon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berthet, C -- Hulmes, D J -- Miller, A -- Timmins, P A -- New York, N.Y. -- Science. 1978 Feb 3;199(4328):547-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/622556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Collagen ; Glycosaminoglycans ; Intervertebral Disc/*ultrastructure ; Neutrons ; Protein Conformation ; Proteoglycans ; Scattering, Radiation ; Swine ; X-Ray Diffraction
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  • 13
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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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  • 14
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    Rapid changes in brain benzodiazepine receptors after experimental seizures (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-11-24
    Description: Seizures induced in the rat by electroshock or by injections of pentylenetetrazol increase the specific binding of diazepam to putative receptor sites in cerebral cortical membranes. The enhancement of diazepam binding results from a rapid increase in the number of available binding sites rather than a change in receptor affinity. The postictal increase in cortical benzodiazepine receptors suggests that the cerebral cortex might be more sensitive to the anticonvulsant effects of the benzodiazepines after seizures. This observation may be related to the mechanism of action of these drugs in the treatment of recurrent seizures such as status epilepticus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S M -- Skolnick, P -- New York, N.Y. -- Science. 1978 Nov 24;202(4370):892-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/715447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anoxia/metabolism ; Binding Sites ; Brain/*metabolism ; Cerebral Cortex/metabolism ; Diazepam/*metabolism ; Electroshock ; Kinetics ; Male ; Pentylenetetrazole ; Rats ; Receptors, Drug/*metabolism ; Seizures/*metabolism ; Synaptosomes/metabolism
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  • 15
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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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  • 16
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    Prolactin binding sites in the rat brain (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-09-15
    Description: The principles of the competitive-binding assay were used in conjunction with light microscopic radioautography to demonstrate specific prolactin binding sites localized on ependyma of the rat choroid plexus, a previously unknown prolactin target tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walsh, R J -- Posner, B I -- Kopriwa, B M -- Brawer, J R -- New York, N.Y. -- Science. 1978 Sep 15;201(4360):1041-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/684427" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoradiography ; Binding Sites ; Binding, Competitive ; Brain/cytology/*metabolism ; Female ; Iodine Radioisotopes ; Male ; Prolactin/*metabolism ; Rats
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  • 17
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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)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 18
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    Antibodies to purified insulin receptor have insulin-like activity (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-06-16
    Description: Antibodies to insulin receptors purified from rat liver membranes do not complete with [125I]insulin for binding to the insulin receptor but do precipitate solubilized receptors labeled with [125I]insulin. These antibodies have the insulin-like activities of enhancing glucose oxidation and inhibiting epinephrine-induced lipolysis in rat adipocytes. Thus, antibody binds to the receptor at a different site from that to which insulin binds, yet the interaction can initiate an effective biological response. These results indicate that the previously studied insulin-binding sites are the physiological macromolecular receptors for insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobs, S -- Chang, K J -- Cuatrecasas, P -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1283-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663609" target="_blank"〉PubMed〈/a〉
    Keywords: Acanthosis Nigricans/physiopathology ; Adipose Tissue/metabolism ; Animals ; *Antibodies ; Antigen-Antibody Reactions ; Binding Sites ; Binding, Competitive ; Biological Transport ; Epinephrine/pharmacology ; Glucose/metabolism ; Insulin/metabolism ; Lipid Mobilization ; Liver/immunology ; Rats ; Receptor, Insulin/*physiology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 19
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    Covalent immunoglobulin assembly in vitro: reactivity of light chain covalent dimers (L2) and blocked light chain monomers (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-02-10
    Description: Covalent light chain dimers (L2) and cysteine-blocked L chain monomers readily react with partially reduced heavy (H) chains. A rapid disappearance of these blocked L chain species is followed by the appearance of covalent intermediates-HL, H2, and H2L-leading to fully assembled H2L2. The mechanism of initial disulfide bond formation between heavy and light chains is disulfide interchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kazin, A R -- Beychok, S -- New York, N.Y. -- Science. 1978 Feb 10;199(4329):688-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/415360" target="_blank"〉PubMed〈/a〉
    Keywords: Bence Jones Protein/metabolism ; Cysteine/metabolism ; Disulfides ; Humans ; *Immunoglobulin G/biosynthesis ; *Immunoglobulin Heavy Chains/biosynthesis ; *Immunoglobulin Light Chains/biosynthesis ; *Immunoglobulin gamma-Chains/biosynthesis ; *Immunoglobulin kappa-Chains/biosynthesis ; In Vitro Techniques ; Oxidation-Reduction ; Protein Conformation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 20
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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)
    Details
    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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  • 21
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    Space-filling models of kinase clefts and conformation changes (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 22
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    Tumor surveillance: how tumors may resist macrophage-mediated host defense (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-01-12
    Description: Both normal human serum and supernatant from explanted malignant tumors contained a heat-stable low-molecular-weight factor that inhibited monocyte activation in vitro. In contrast, serum from individuals with solid tumors enhanced monocyte activation. It is suggested that the systemic activation of monocytes that occurs in malignant disease may be an appropriate host response but that successful tumors may continue to grow because they subvert the normal physiological signal for inhibition of macrophage activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhodes, J -- Bishop, M -- Benfield, J -- New York, N.Y. -- Science. 1979 Jan 12;203(4376):179-82.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/758686" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carcinoma/*immunology ; Carcinoma, Squamous Cell/immunology ; Chemotaxis ; Colonic Neoplasms/*immunology ; Humans ; Immunity, Cellular ; Immunoglobulin Fc Fragments ; Lung Neoplasms/*immunology ; Macrophages/*immunology ; Monocytes/*immunology ; Rosette Formation
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 23
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    Anomalous amide I infrared absorption of purple membrane (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-04-20
    Description: Infrared absorption of purple membrane reveals an amide I frequency that falls outside the range normally found for alpha helices. This may indicate along with x-ray diffraction the existence of bacteriorhodopsin alpha helices with unusual structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothschild, K J -- Clark, N A -- New York, N.Y. -- Science. 1979 Apr 20;204(4390):311-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432645" target="_blank"〉PubMed〈/a〉
    Keywords: Amides ; *Bacteriorhodopsins ; *Carotenoids ; Deuterium ; Halobacterium/ultrastructure ; Membrane Proteins ; Protein Conformation ; Spectrophotometry, Infrared
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  • 24
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    Crystal structure of [Leu5]enkephalin (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-07-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blundell, T L -- Hearn, L -- Tickle, I J -- Palmer, R A -- Morgan, B A -- Smith, G D -- Griffin, J F -- New York, N.Y. -- Science. 1979 Jul 13;205(4402):220.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/451597" target="_blank"〉PubMed〈/a〉
    Keywords: Crystallography ; *Endorphins ; *Enkephalins ; Protein Conformation
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  • 25
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    Acridine araphanes: a new class of probe molecules for biological systems (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-09-21
    Description: The bis-acridine ring system forms the basis for new biophysical probes of novel stereochemistry. Spectral data indicate that certain alkylene bridged bis-9-aminoacridines have a parallel plane conformation of predictable interplane distance. The parallel plane conformation is independent of solvent and thus is different from nucleic acid systems. This stable conformation allows these compounds to be used as sensitive "rulers" for describing binding site geometry in cholinergic enzymes and in the delineation of the mechanism of allosteric control in acetylcholinesterase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Himel, C M -- Taylor, J L -- Pape, C -- Millar, D B -- Christopher, J -- Kurlansik, L -- New York, N.Y. -- Science. 1979 Sep 21;205(4412):1277-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/472743" target="_blank"〉PubMed〈/a〉
    Keywords: *Acetylcholinesterase/metabolism ; *Acridines ; Binding Sites ; Kinetics ; Molecular Conformation ; Phosphorylation ; Protein Conformation ; Spectrophotometry, Ultraviolet
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  • 26
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    Human and mouse hypoxanthine-guanine phosphoribosyltransferase: dimers and tetramers (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-01-12
    Description: Human and mouse hypoxanthine-guanine phosphoribosyltransferase subunits combine to form an active heteropolymer. Dimers form the basic subunit structure of the enzymes, yet the dimers can readily associate to form tetramers. The equilibrium between dimers and tetramers is significantly influenced by the ionic strength of the enzyme solvent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, G G -- Eisenberg, L R -- Migeon, B R -- New York, N.Y. -- Science. 1979 Jan 12;203(4376):174-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/569362" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Female ; Genetic Linkage ; Humans ; Hybrid Cells/enzymology ; *Hypoxanthine Phosphoribosyltransferase/genetics ; Macromolecular Substances ; Mice ; Molecular Weight ; Protein Conformation ; X Chromosome
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  • 27
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    The major histocompatibility complex of the mouse (1979)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1979-02-09
    Description: Like physicists striving to develop a unified field theory, immunologists are attempting to bring order to the microcosmos of defense reactions. Indications are that one of the most important constants in this microcosmos is the major histocompatibility complex (MHC) of the species. A test of any interpretation of the MHC's role in immunity is how well it explains this system's polymorphism. One of the most crucial questions an MHC hypothesis must answer is: Why are there so many alleles at this complex?〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, J -- New York, N.Y. -- Science. 1979 Feb 9;203(4380):516-21.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/104386" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Blood Proteins/genetics ; Genes ; *Genes, MHC Class II ; Genetic Linkage ; H-2 Antigens/*genetics ; Lymphocytes/immunology ; *Major Histocompatibility Complex ; Mice/*immunology ; Phenotype ; Polymorphism, Genetic
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  • 28
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    Embryonic rodent brain contains estrogen receptors (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-05-04
    Description: Estradiol-binding proteins with the properties of putative estrogen receptors are present in cytosol extracts of embryonic mouse hypothalamus and other brain regions. These embryonic estrogen receptors are adultlike in their high affinity and limited capacity for estradiol, sensitivity to diethylstilbestrol, ability to adhere to DNA, and behavior during DNA-cellulose affinity chromatography. As early as 4 days before birth, mouse hypothalamus has approximately 40 percent of the adult concentration of hypothalamic estrogen receptors with these properties. These observations raise the possibility that embryonic rodent brain has the biochemical potential to respond to sex hormones and that the critical period of brain sexual differentiation could be initiated prenatally.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vito, C C -- Fox, T O -- New York, N.Y. -- Science. 1979 May 4;204(4392):517-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/432656" target="_blank"〉PubMed〈/a〉
    Keywords: Age Factors ; Animals ; Binding Sites ; Brain/*embryology ; Chromatography, Affinity ; Cytosol/metabolism ; Hypothalamus/embryology ; Mice ; Receptors, Estrogen/*metabolism ; Sexual Maturation
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  • 29
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    Water, protein folding, and the genetic code (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-11-02
    Description: The absolute affinities of amino acid side chains for solvent water closely match their relative distributions between the surface and the interior of native proteins and are associated with a remarkable bias in the genetic code.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolfenden, R V -- Cullis, P M -- Southgate, C C -- New York, N.Y. -- Science. 1979 Nov 2;206(4418):575-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/493962" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/*genetics ; *Genetic Code ; Mutation ; Protein Conformation ; Solubility ; Thermodynamics ; Water
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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