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  • Artikel  (16)
  • Neueste Artikel (Zeitschrifteninhaltsverzeichnisse / in press)  (16)
  • Protein Conformation
  • Signal Transduction
  • 2000-2004
  • 1980-1984  (16)
  • 1935-1939
  • 1981  (7)
  • 1980  (9)
  • Medizin  (16)
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  • Neueste Artikel (Zeitschrifteninhaltsverzeichnisse / in press)  (16)
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  • 2000-2004
  • 1980-1984  (16)
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  • 1
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    Rational approaches to chemotherapy: antisickling agents (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-08-14
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klotz, I M -- Haney, D N -- King, L C -- New York, N.Y. -- Science. 1981 Aug 14;213(4509):724-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256275" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Anemia, Sickle Cell/*drug therapy ; Aspirin/analogs & derivatives/therapeutic use ; Chemical Phenomena ; Chemistry ; *Hemoglobin, Sickle ; Humans ; Protein Binding/drug effects ; Protein Conformation ; Salicylates/*therapeutic use ; Solubility ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 2
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    Diameter of the cell-to-cell junctional membrane channels as probed with neutral molecules (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-07-31
    Beschreibung: The cell-to-cell channels in the junctions of an insect salivary gland and of insect and mammalian cells in culture were probed with fluorescent molecules-neutral linear oligosaccharides, neutral branched glycopeptides, and charged linear peptides. From the molecular dimensions of the largest permeants and smallest impermeants the permeation-limiting channel diameter was obtained: 16 to 20 angstroms for the mammalian cells and 20 to 30 angstroms for the insect cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarzmann, G -- Wiegandt, H -- Rose, B -- Zimmerman, A -- Ben-Haim, D -- Loewenstein, W R -- CA 14464/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):551-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7244653" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Cell Line ; Chironomidae ; Fluorescent Dyes ; Glycopeptides/*metabolism ; Intercellular Junctions/*ultrastructure ; Mice ; Mice, Inbred BALB C ; Models, Molecular ; Oligosaccharides/*metabolism ; Protein Conformation ; Salivary Glands/*ultrastructure ; Species Specificity
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 3
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    Cross-linked fibrinogen dimers demonstrate a feature of the molecular packing in fibrin fibers (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-01-16
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fowler, W E -- Erickson, H P -- Hantgan, R R -- McDonagh, J -- Hermans, J -- HL 20319/HL/NHLBI NIH HHS/ -- HL 23454/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):287-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6108612" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Factor XIII/metabolism ; *Fibrin/metabolism ; *Fibrinogen/metabolism ; Humans ; Macromolecular Substances ; Microscopy, Electron ; Protein Conformation ; gamma-Glutamyltransferase/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 4
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    A new understanding of sickle cell emerges (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-01-16
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1981 Jan 16;211(4479):265-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7444466" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Anemia, Sickle Cell/*blood ; Erythrocytes, Abnormal/pathology ; *Hemoglobin, Sickle ; Humans ; Protein Binding ; Protein Conformation ; Temperature
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 5
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    Real-time color graphics in studies of molecular interactions (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-02-13
    Beschreibung: Studies of the structures and interactions of large biological molecules require both coordinate data and three-dimensional visualization. Orthodox molecular models often bear a tenuous relationship to the coordinate data. In contrast, computer graphics requires that the display directly and accurately represent the data, and storage of modified configurations and recovery of original structures are simple. Software has been developed that allows real-time display of color line and surface displays of several interacting molecules, while quantitatively monitoring the stereochemistry.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langridge, R -- Ferrin, T E -- Kuntz, I D -- Connolly, M L -- GM 19267/GM/NIGMS NIH HHS/ -- RR-1081-03/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 Feb 13;211(4483):661-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7455704" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Carboxypeptidases/antagonists & inhibitors ; Color ; *Computers ; Macromolecular Substances ; *Models, Molecular ; *Models, Structural ; Nucleic Acid Conformation ; Protein Conformation ; Trypsin ; Trypsin Inhibitors ; Water
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 6
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    Structural changes at the heme induced by freezing hemoglobin (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-08-07
    Beschreibung: A dramatic change occurs in the vibrational properties of the iron-histidine bond, trans to the oxygen binding site, on freezing deoxyhemoglobin. The large, quaternary structure-dependent differences in the shape and frequency of the iron-histidine mode observed in resonance Raman scattering measurements above freezing ae significantly diminished by the freezing event and the scattering intensity increases substantially. On further reduction in temperature to 10 K this broad line becomes narrow and shifts to a higher frequency. These data implicate dynamical processes and protein interaction with water as contributors to the quaternary structure dependence of the iron-histidine bond and thus reflect on the role of that bond in the energetics of cooperative ligand binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ondrias, M R -- Rousseau, D L -- Simon, S R -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):657-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256263" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Allosteric Regulation ; *Freezing ; *Heme ; *Hemoglobin A ; Histidine ; Humans ; Motion ; Protein Conformation ; Spectrum Analysis, Raman ; Water
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 7
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    Cadmium-113 nuclear magnetic resonance studies of bovine insulin: two-zinc insulin hexamer specifically binds calcium (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1981-05-01
    Beschreibung: By use of cadmium-113 nuclear magnetic resonance spectroscopy, a specific calcium ion binding site has been identified in the bovine two-zinc insulin hexamer. This site is composed of six glutamyl carboxylate groups clustered in the center of the hexamer, and is distinct from the normal zinc ion binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudmeier, J L -- Bell, S J -- Storm, M C -- Dunn, M F -- 5S05RR 07010-09/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):560-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010607" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Binding Sites ; Cadmium ; Calcium/*metabolism ; Cattle ; *Insulin/metabolism ; Isotopes ; Ligands ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Zinc/*metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 8
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-11-07
    Beschreibung: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; Structure-Activity Relationship
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 9
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    Collagen: molecular diversity in the body's protein scaffold (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-03-21
    Beschreibung: Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eyre, D R -- New York, N.Y. -- Science. 1980 Mar 21;207(4437):1315-22.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7355290" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Amino Acid Sequence ; Animals ; Calcification, Physiologic ; Cartilage/ultrastructure ; *Collagen/genetics/metabolism ; Epithelium/ultrastructure ; Extracellular Space/ultrastructure ; Humans ; Hydrogen Bonding ; Polymorphism, Genetic ; Protein Biosynthesis ; Protein Conformation ; Vertebrates
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 10
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    Modeling coordination sites in metallobiomolecules (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-07-11
    Beschreibung: Synthetic metal complexes can closely approach the properties of metal ions in proteins and yield useful information concerning biological structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibers, J A -- Holm, R H -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):223-35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384796" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Binding Sites ; Electron Transport ; Humans ; Iron-Sulfur Proteins ; *Metalloproteins ; *Metals ; Molecular Conformation ; Myoglobin ; Oxygen/blood ; Oxyhemoglobins ; Protein Binding ; Protein Conformation
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 11
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    Hormone binding alters the conformation of the insulin receptor (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-12-05
    Beschreibung: Fat cells or fat cell membranes were briefly subjected to mild proteolysis under conditions where insulin receptors were either free or bound to (125)I-labeled insulin. When receptors were then affinity-labeled to visualize the effects of this treatment, it was observed that receptors that had been occupied by ligand during proteolysis exhibited greater rates of degradation than unoccupied receptors. These results demonstrate that insulin-receptor interaction induces a change in receptor structure that may be related to signal transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pilch, P F -- Czech, M P -- AM 06069/AM/NIADDK NIH HHS/ -- AM 17893/AM/NIADDK NIH HHS/ -- HD 11343/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1980 Dec 5;210(4474):1152-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7003712" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adipose Tissue/metabolism ; Animals ; Cell Membrane/metabolism ; Insulin/*metabolism ; Male ; Peptide Fragments/analysis ; Protein Binding ; Protein Conformation ; Rats ; Receptor, Insulin/*metabolism ; Trypsin/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 12
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    Assembly of proteins into membranes (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-11-21
    Beschreibung: Two pathways for protein assembly into biological membranes have been proposed. The "signal hypothesis" emphasizes the role of specific membrane proteins in binding the growing polypeptide and conducting it into the bilayer during its synthesis. The "membrane-triggered folding" hypothesis emphasizes self-assembly and the role of changing protein conformation during transfer from an aqueous compartment into a membrane. These ideas provide a framework for reviewing recent data on the biogenesis of membrane proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wickner, W -- New York, N.Y. -- Science. 1980 Nov 21;210(4472):861-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001628" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Biological Transport ; Membrane Proteins/*metabolism ; Membranes/enzymology/*metabolism ; Protein Conformation ; Protein Precursors/metabolism ; Proteins/secretion ; Solubility ; Viral Proteins/metabolism
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 13
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    Folic acid: crystal structure and implications for enzyme binding (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-10-17
    Beschreibung: The crystal and molecular structure of folic acid dihydrate has been determined by x-ray diffraction. Folic acid is in an extended conformation with the pteridine ring in the keto form. The C(4) oxygen and N(10) atoms are on the same side of the molecule, hydrogen-bonded to the same water. This conformation has the pteridine rotated approximately 180 degrees away from the orientation of the pteridine ring of methotrexate bound to dihydrofolate reductase. The folic acid pteridine and phenyl rings interact in a stacking manner which is suggestive of the type of associations these groups could form in a complex of folate, dihydrofolate reductase, and reduced nicotinamide adenine dinucleotide phosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mastropaolo, D -- Camerman, A -- Camerman, N -- CA-15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):334-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423195" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Binding Sites ; Crystallography ; *Folic Acid ; Molecular Conformation ; Protein Conformation ; Tetrahydrofolate Dehydrogenase ; X-Ray Diffraction
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 14
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    Catecholamine-induced alteration in sedimentation behavior of membrane bound beta-adrenergic receptors (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-10-01
    Beschreibung: Incubation of astrocytoma cells with catecholamines results in a decrease in catecholamine-stimulated adenylate cyclase activity and a concomitant alteration in the sedimentation properties of particulate beta-adrenergic receptors. The altered receptors exhibit agonist binding properties similar to those of receptors that are "uncoupled" from adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Harden, T K -- Cotton, C U -- Waldo, G L -- Lutton, J K -- Perkins, J P -- GM 25163/GM/NIGMS NIH HHS/ -- HL 22490/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct;210(4468):441-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6254143" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Adenylyl Cyclases/metabolism ; Astrocytoma ; Cell Line ; Centrifugation, Density Gradient ; Concanavalin A/pharmacology ; Endocytosis ; Humans ; Isoproterenol/*metabolism ; Protein Conformation ; Receptors, Adrenergic/*metabolism ; Receptors, Adrenergic, beta/*metabolism ; Time Factors
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 15
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    Monte Carlo simulation of water behavior around the dipeptide N-acetylalanyl-N-methylamide (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-05-09
    Beschreibung: Applications of Monte Carlo and molecular dynamics computer simulation techniques indicate that they are potentially powerful tools for understanding biological systems at the molecular level. The Monte Carlo technique can be used to study the solvent structure around a small peptide and the effect of the aqueous environment on the conformational equilibria of the peptide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagler, A T -- Osguthorpe, D J -- Robson, B -- New York, N.Y. -- Science. 1980 May 9;208(4444):599-601.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7367882" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): *Alanine/*analogs & derivatives ; *Dipeptides ; Models, Chemical ; Monte Carlo Method ; Protein Conformation ; Solvents ; *Water
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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  • 16
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    Acetylcholine receptor: complex of homologous subunits (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publikationsdatum: 1980-06-27
    Beschreibung: The acetylcholine receptor from the electric ray Torpedo californica is composed of five subunits; two are identical and the other three are structurally related to them. Microsequence analysis of the four polypeptides demonstrates amino acid homology among the subunits. Further sequence analysis of both membrane-bound and Triton-solubilized, chromatographically purified receptor gave the stoichiometry of the four subunits (40,000:50,000:60,000:65,000 daltons) as 2:1:1:1, indicating that this protein is a pentameric complex with a molecular weight of 255,000 daltons. Genealogical analysis suggests that divergence from a common ancestral gene occurred early in the evolution of the receptor. This shared ancestry argues that each of the four subunits plays a functional role in the receptor's physiological action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raftery, M A -- Hunkapiller, M W -- Strader, C D -- Hood, L E -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1454-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384786" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetylcholine/metabolism ; Amino Acid Sequence ; Animals ; Electric Organ/*analysis ; Fishes ; Macromolecular Substances ; Molecular Weight ; Protein Conformation ; *Receptors, Cholinergic
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    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Publiziert von American Association for the Advancement of Science (AAAS)
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