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  • *Biological Evolution
  • Models, Molecular
  • American Association for the Advancement of Science (AAAS)  (49)
  • American Meteorological Society
  • MDPI Publishing
  • 1995-1999
  • 1985-1989  (49)
  • 1989  (25)
  • 1987  (24)
Collection
Publisher
  • American Association for the Advancement of Science (AAAS)  (49)
  • American Meteorological Society
  • MDPI Publishing
Years
  • 1995-1999
  • 1985-1989  (49)
Year
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-03-31
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1989 Mar 31;243(4899):1666-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2928802" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Biological Evolution ; Europe ; *Fossils ; Hominidae/*anatomy & histology ; Humans ; *Paleontology
    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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1989 Jun 30;244(4912):1544.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2740901" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Brain/*anatomy & histology ; Ecology ; Genetics
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  • 3
    Publication Date: 1989-01-06
    Description: The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, P C -- Ohlendorf, D H -- Wendoloski, J J -- Salemme, F R -- New York, N.Y. -- Science. 1989 Jan 6;243(4887):85-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research & Development Department, E. I. du Pont de Neumours and Company, Inc., Wilmington, DE 19880-0228.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911722" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Binding Sites ; Biotin/*metabolism ; Macromolecular Substances ; Models, Molecular ; Protein Conformation ; Streptavidin ; X-Ray Diffraction
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  • 4
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-06-30
    Description: Theories for the evolution of brain weight in mammals suggest that closely related species have diverged largely as a result of selection for differences in body weight, but that differences among more distantly related species have arisen due to greater net directional selection on brain weight. This pattern of changing selection causes brain weight to evolve more slowly than body weight among closely related species, such as those in the same genus, than among more distantly related species, such as those from different families or orders; a phenomenon known as the "taxon-level effect." Thus, brain weight differs more for a given difference in body weight as the species compared are more distantly related. An alternative explanation for the taxon-level effect is proposed. Distantly related species are more likely to inhabit different ecological conditions than are more closely related species. Where the taxon-level effect occurs, brain weight appears to have evolved in response to the demands of these different ecological conditions. As a consequence, brain weight differs more among distantly related species, for any given difference in body weight, than among closely related species. This effect, rather than a progressive pattern of changing selection pressures, may account for the taxon-level effect in mammals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pagel, M D -- Harvey, P H -- New York, N.Y. -- Science. 1989 Jun 30;244(4912):1589-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Zoology, University of Oxford, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2740904" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Artiodactyla/anatomy & histology ; *Biological Evolution ; *Body Weight ; Brain/*anatomy & histology ; Carnivora/anatomy & histology ; Chiroptera/anatomy & histology ; Ecology ; Mammals/*anatomy & histology/classification ; Models, Biological ; Organ Size ; Primates/anatomy & histology ; Regression Analysis ; Rodentia/anatomy & histology ; Selection, Genetic ; Species Specificity ; Statistics as Topic
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  • 5
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-09-01
    Description: Four correlates of fitness were measured in three stocks of the endangered Sonoran topminnow, Poeciliopsis occidentalis, from Arizona. Survival, growth, early fecundity, and developmental stability were greatest in laboratory-reared fish from the most heterozygous natural population studied. Conversely, all four traits were poorest in fish from a population with no electrophoretically detectable genetic variation. These results emphasize the need for genetic as well as demographic information for the development of comprehensive species recovery programs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Quattro, J M -- Vrijenhoek, R C -- New York, N.Y. -- Science. 1989 Sep 1;245(4921):976-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Theoretical and Applied Genetics, Cook College, Rutgers University, New Brunswick, NJ 08903.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2772650" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arizona ; *Biological Evolution ; Cyprinodontiformes/*genetics ; Female ; Fertility ; Genetic Variation ; Male ; Poecilia/anatomy & histology/*genetics ; Species Specificity
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  • 6
    Publication Date: 1989-03-10
    Description: An analysis of the aminoacylation kinetics of unmodified yeast tRNAPhe mutants revealed that five single-stranded nucleotides are important for its recognition by yeast phenylalanyl-tRNA synthetase, provided they were positioned correctly in a properly folded tRNA structure. When four other tRNAs were changed to have these five nucleotides, they became near-normal substrates for the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sampson, J R -- DiRenzo, A B -- Behlen, L S -- Uhlenbeck, O C -- GM 37552/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1363-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2646717" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acyl-tRNA Synthetases/*metabolism ; Base Sequence ; Escherichia coli/genetics ; Models, Molecular ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Phenylalanine-tRNA Ligase/*metabolism ; Plants/genetics ; RNA, Transfer, Amino Acid-Specific/*genetics ; RNA, Transfer, Phe/*genetics/metabolism ; Schizosaccharomyces/genetics ; Transcription, Genetic ; Triticum/genetics
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  • 7
    Publication Date: 1989-05-19
    Description: Chemical probing methods have been used to "footprint" 16S ribosomal RNA (rRNA) at each step during the in vitro assembly of twenty 30S subunit ribosomal proteins. These experiments yield information about the location of each protein relative to the structure of 16S rRNA and provide the basis for derivation of a detailed model for the three-dimensional folding of 16S rRNA. Several lines of evidence suggest that protein-dependent conformational changes in 16S rRNA play an important part in the cooperativity of ribosome assembly and in fine-tuning of the conformation and dynamics of 16S rRNA in the 30S subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stern, S -- Powers, T -- Changchien, L M -- Noller, H F -- GM-17129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 May 19;244(4906):783-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Thimann Laboratories, University of California, Santa Cruz 95064.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2658053" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Escherichia coli ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; RNA, Ribosomal/*metabolism ; RNA, Ribosomal, 16S/*metabolism ; Ribosomal Proteins/*metabolism ; Ribosomes/physiology
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  • 8
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-06-16
    Description: Information relevant to the folding and unfolding of alpha helices has been extracted from an analysis of protein structures. The alpha helices in protein crystal structures have been found to be hydrated, either externally by a water molecule hydrogen bonding to the backbone carbonyl oxygen atom, or internally by inserting into the helix hydrogen bond and forming a hydrogen-bonded bridge between the backbone carbonyl oxygen and the amide nitrogen atoms. The water-inserted alpha-helical segments display a variety of reverse-turn conformations, such as type III, type II, type I, and opened out, that can be considered as folding intermediates that are trapped in the folding-unfolding process of alpha helices. Since the alpha helix, most turns, and the extended beta strand occupy contiguous regions in the conformational space of phi, psi dihedral angles, a plausible pathway can be proposed for the folding-unfolding process of alpha helices in aqueous solution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sundaralingam, M -- Sekharudu, Y C -- AR-34139/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 16;244(4910):1333-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Wisconsin-Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2734612" target="_blank"〉PubMed〈/a〉
    Keywords: Hydrogen Bonding ; Models, Molecular ; *Protein Conformation ; *Water
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  • 9
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-11-17
    Description: The proposal that the absorption maximum of the visual pigments is governed by interaction of the 11-cis-retinal chromophore with charged carboxylic acid side chains in the membrane-embedded regions of the proteins has been tested by mutating five Asp and Glu residues thought to be buried in rhodopsin. Changing Glu113 to Gln causes a dramatic shift in the absorption maximum from 500 nanometers to 380 nanometers, a decrease in the pKa (acidity constant) of the protonated Schiff base of the chromophore to about 6, and a greatly increased reactivity with hydroxylamine. Thus Glu113 appears to be the counterion to the protonated Schiff base. Wavelength modulation in visual pigments apparently is not governed by electrostatic interaction with carboxylate residues, other than the counterion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhukovsky, E A -- Oprian, D D -- 5T32 GM07596-11/GM/NIGMS NIH HHS/ -- EY07965/EY/NEI NIH HHS/ -- R01 EY007965/EY/NEI NIH HHS/ -- S07 RR07044/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):928-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2573154" target="_blank"〉PubMed〈/a〉
    Keywords: *Aspartic Acid ; Glutamates ; Glutamic Acid ; Hydrogen-Ion Concentration ; Hydroxylamine ; Hydroxylamines/pharmacology ; Models, Molecular ; Mutation ; Protein Conformation ; Retinal Pigments/*metabolism ; Retinaldehyde/*metabolism ; Retinoids/*metabolism ; Rhodopsin/genetics/*metabolism ; Schiff Bases ; Spectrophotometry
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  • 10
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-02-17
    Description: Changes in social behavior were a key aspect of human evolution, and yet it is notoriously difficult for paleobiologists to determine patterns of social evolution. By defining the limited number of distributional strategies available to members of each sex of any species and investigating the conditions under which they may occur and change, the social behavior of different hominid taxa may be reconstructed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foley, R A -- Lee, P C -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):901-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2493158" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Behavior ; *Biological Evolution ; Female ; Haplorhini/genetics ; Hominidae/*genetics ; Humans ; Male ; Models, Genetic ; *Social Behavior
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  • 11
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-02-10
    Description: A novel approach to the control of enzyme catalysis is presented in which a disulfide bond engineered into the active-site cleft of bacteriophage T4 lysozyme is capable of switching the activity on and off. Two cysteines (Thr21----Cys and Thr142----Cys) were introduced by oligonucleotide-directed mutagenesis into the active-site cleft. These cysteines spontaneously formed a disulfide bond under oxidative conditions in vitro, and the catalytic activity of the oxidized (cross-linked) T4 lysozyme was completely lost. On exposure to reducing agent, however, the disulfide bond was rapidly broken, and the reduced (non-cross-linked) lysozyme was restored to full activity. Thus an enzyme has been engineered such that redox potential can be used to control catalytic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumura, M -- Matthews, B W -- GM21967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 10;243(4892):792-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2916125" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chromatography, High Pressure Liquid ; DNA Mutational Analysis ; *Disulfides ; Models, Molecular ; Muramidase/*physiology ; *Protein Engineering ; Recombinant Proteins ; Structure-Activity Relationship ; T-Phages/enzymology
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  • 12
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-01-06
    Description: Elasmobranch fishes, the coelacanth, estivating lungfish, amphibians, and mammals synthesize urea by the ornithine-urea cycle; by comparison, urea synthetic activity is generally insignificant in teleostean fishes. It is reported here that isolated liver cells of two teleost toadfishes, Opsanus beta and Opsansus tau, synthesize urea by the ornithine-urea cycle at substantial rates. Because toadfish excrete ammonia, do not use urea as an osmolyte, and have substantial levels of urease in their digestive systems, urea may serve as a transient nitrogen store, forming the basis of a nitrogen conservation shuttle system between liver and gut as in ruminants and hibernators. Toadfish synthesize urea using enzymes and subcellular distributions similar to those of elasmobranchs: glutamine-dependent carbamoyl phosphate synthethase (CPS III) and mitochondrial arginase. In contrast, mammals have CPS I (ammonia-dependent) and cytosolic arginase. Data on CPS and arginases in other fishes, including lungfishes and the coelacanth, support the hypothesis that the ornithine-urea cycle, a monophyletic trait in the vertebrates, underwent two key changes before the evolution of the extant lungfishes: a switch from CPS III to CPS I and replacement of mitochondrial arginase by a cytosolic equivalent.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mommsen, T P -- Walsh, P J -- New York, N.Y. -- Science. 1989 Jan 6;243(4887):72-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology and Living Resources, Rosenstiel School of Marine and Atmospheric Sciences, University of Miami, FL 33149.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2563172" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginase/metabolism ; *Biological Evolution ; Carbamoyl-Phosphate Synthase (Ammonia)/metabolism ; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/metabolism ; Fishes/*metabolism ; Glutamate-Ammonia Ligase/metabolism ; Liver/metabolism ; Species Specificity ; Urea/*biosynthesis ; Vertebrates/*metabolism
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  • 13
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-07-07
    Description: Protein interiors contain many tightly packed apolar atoms in a nearly crystalline state. Both shielding of apolar atoms from solvent and efficient interior packing arrangements affect protein stability, but their relative importance is unclear. To separate these effects, the stabilities of wild-type and mutant gene V proteins from bacteriophage fl were studied by measuring resistance to denaturation. The effects of subtle interior packing changes, both separate from and combined with changes in buried side chain hydrophobicity, were measured. For the interior apolar-to-apolar substitutions studied, the two effects were of the same magnitude and alteration of packing without accompanying hydrophobicity changes substantially destabilized the protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sandberg, W S -- Terwilliger, T C -- 5732 GM07281/GM/NIGMS NIH HHS/ -- GM38714/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Jul 7;245(4913):54-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2787053" target="_blank"〉PubMed〈/a〉
    Keywords: Calorimetry ; Coliphages/genetics ; Drug Stability ; Guanidine ; Guanidines ; Models, Molecular ; Mutation ; *Protein Conformation ; Protein Denaturation ; *Viral Proteins/genetics
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  • 14
    Publication Date: 1989-11-10
    Description: The basal rate of DNA sequence evolution in enterobacteria, as seen in the extent of divergence between Escherichia coli and Salmonella typhimurium, varies greatly among genes, even when only "silent" sites are considered. The degree of divergence is clearly related to the level of gene expression, reflecting constraints on synonymous codon choice. However, where this constraint is weak, among genes not expressed at high levels, divergence is also related to the chromosomal location of the gene; it appears that genes furthest away from oriC, the origin of replication, have a mutation rate approximately two times that of genes near oriC.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharp, P M -- Shields, D C -- Wolfe, K H -- Li, W H -- New York, N.Y. -- Science. 1989 Nov 10;246(4931):808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Trinity College, Dublin, Ireland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2683084" target="_blank"〉PubMed〈/a〉
    Keywords: Bias (Epidemiology) ; *Biological Evolution ; *Chromosomes, Bacterial ; Codon/genetics ; DNA Repair ; DNA Replication ; DNA, Bacterial/genetics ; Enterobacteriaceae/*genetics/ultrastructure ; Escherichia coli/genetics/ultrastructure ; Gene Expression Regulation, Bacterial ; Genes, Bacterial ; *Mutation ; Regression Analysis ; Salmonella typhimurium/genetics/ultrastructure
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  • 15
    Publication Date: 1989-03-10
    Description: The x-ray crystal structure of recombinant human renin has been determined. Molecular dynamics techniques that included crystallographic data as a restraint were used to improve an initial model based on porcine pepsinogen. The present agreement factor for data from 8.0 to 2.5 angstroms (A) is 0.236. Some of the surface loops are poorly determined, and these disordered regions border a 30 A wide solvent channel. Comparison of renin with other aspartyl proteinases shows that, although the structural cores and active sites are highly conserved, surface residues, some of which are critical for specificity, vary greatly (up to 10A). Knowledge of the actual structure, as opposed to the use of models based on related enzymes, should facilitate the design of renin inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sielecki, A R -- Hayakawa, K -- Fujinaga, M -- Murphy, M E -- Fraser, M -- Muir, A K -- Carilli, C T -- Lewicki, J A -- Baxter, J D -- James, M N -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1346-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2493678" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid Endopeptidases ; Cardiovascular Agents/pharmacology ; Endopeptidases/metabolism ; Humans ; Models, Molecular ; Pepsin A/metabolism ; Protein Conformation ; *Recombinant Proteins/metabolism ; *Renin/metabolism
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  • 16
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-09-22
    Description: New discoveries combine to indicate that all the major steps in human evolution took place in Africa. Skeletal analysis of oldest human forbears around 3 million years ago reveal many anatomical similarities to African Great Apes. These and biochemical resemblances indicate a common ancestry for humans and apes, perhaps only a few million years earlier. Enlarged knowledge through recent recovery of skeletons of several successive stages in the line leading to modern peoples shows that many attributes or skills by which we define humanity arose much more recently in time than heretofore believed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simons, E L -- New York, N.Y. -- Science. 1989 Sep 22;245(4924):1343-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Duke University Center, Durham, NC 27705.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2506640" target="_blank"〉PubMed〈/a〉
    Keywords: Africa ; Animals ; *Biological Evolution ; *Haplorhini/anatomy & histology
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  • 17
    Publication Date: 1989-05-12
    Description: Calicheamicin gamma 1I is a recently discovered diyne-ene-containing antitumor antibiotic that cleaves DNA in a double-stranded fashion, a rarity among drugs, at specific sequences. It is proposed that the cutting specificity is due to a combination of the complementarity of the diyne-ene portion of the aglycone with DNA secondary structures and stabilization by association of the thiobenzoate-carbohydrate tail with the minor groove.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zein, N -- Poncin, M -- Nilakantan, R -- Ellestad, G A -- New York, N.Y. -- Science. 1989 May 12;244(4905):697-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cyanamid Company, Medical Research Division, Lederle Laboratories, Pearl River, NY 10965.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2717946" target="_blank"〉PubMed〈/a〉
    Keywords: *Aminoglycosides ; Animals ; Anti-Bacterial Agents/*metabolism ; Antibiotics, Antineoplastic ; Base Sequence ; Benzoates ; Binding Sites ; Carbohydrates ; Cattle ; Computer Simulation ; DNA/*metabolism ; Enediynes ; Models, Molecular ; Molecular Structure ; Nucleic Acid Conformation ; Structure-Activity Relationship
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  • 18
    Publication Date: 1989-02-17
    Description: The human immunodeficiency virus (HIV-1) encodes a protease that is essential for viral replication and is a member of the aspartic protease family. The recently determined three-dimensional structure of the related protease from Rous sarcoma virus has been used to model the smaller HIV-1 dimer. The active site has been analyzed by comparison to the structure of the aspartic protease, rhizopuspepsin, complexed with a peptide inhibitor. The HIV-1 protease is predicted to interact with seven residues of the protein substrate. This information can be used to design protease inhibitors and possible antiviral drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weber, I T -- Miller, M -- Jaskolski, M -- Leis, J -- Skalka, A M -- Wlodawer, A -- CA-06927/CA/NCI NIH HHS/ -- CA38046/CA/NCI NIH HHS/ -- N01-CO-74101/CO/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):928-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crystallography Laboratory, NCI-Frederick Cancer Research Facility, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2537531" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Avian Sarcoma Viruses/enzymology ; Binding Sites ; HIV-1/*enzymology ; Hydrogen Bonding ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Peptide Hydrolases/*metabolism ; Protein Conformation
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  • 19
    Publication Date: 1989-08-11
    Description: The rational design of drugs that can inhibit the action of viral proteases depends on obtaining accurate structures of these enzymes. The crystal structure of chemically synthesized HIV-1 protease has been determined at 2.8 angstrom resolution (R factor of 0.184) with the use of a model based on the Rous sarcoma virus protease structure. In this enzymatically active protein, the cysteines were replaced by alpha-amino-n-butyric acid, a nongenetically coded amino acid. This structure, in which all 99 amino acids were located, differs in several important details from that reported previously by others. The interface between the identical subunits forming the active protease dimer is composed of four well-ordered beta strands from both the amino and carboxyl termini and residues 86 to 94 have a helical conformation. The observed arrangement of the dimer interface suggests possible designs for dimerization inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wlodawer, A -- Miller, M -- Jaskolski, M -- Sathyanarayana, B K -- Baldwin, E -- Weber, I T -- Selk, L M -- Clawson, L -- Schneider, J -- Kent, S B -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1989 Aug 11;245(4918):616-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Crystallography Laboratory, NCI-Frederick Cancer Research Facility, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2548279" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aspartic Acid Endopeptidases ; Avian Sarcoma Viruses/enzymology ; Binding Sites ; Crystallization ; *Endopeptidases/chemical synthesis ; HIV Protease ; HIV-1/*enzymology ; Hydrogen Bonding ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Protein Conformation ; Solutions ; X-Ray Diffraction
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  • 20
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-01-06
    Description: Knowledge of three-dimensional protein structures is one of the foundations of protein design and protein engineering. Nuclear magnetic resonance spectroscopy was recently introduced as a second method for protein structure determination, in addition to the well-established diffraction techniques with protein single crystals. This new approach enables one to carry out detailed structural studies of proteins in solution and other noncrystalline states, which may be similar or identical to the physiological environment, and promises new insights into the dynamics of protein molecules and the protein-folding problem.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wuthrich, K -- New York, N.Y. -- Science. 1989 Jan 6;243(4887):45-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Eidgenossiche Technische Hochschule, Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911719" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Graphics ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; *Protein Conformation ; *Proteins ; Software
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  • 21
    Publication Date: 1989-05-12
    Description: The age of the molecular organization of life as expressed in the genetic code can be estimated from experimental data. Comparative sequence analysis of transfer RNA by the method of statistical geometry in sequence space suggests that about one-third of the present transfer RNA sequence divergence was present at the urkingdom level about the time when archaebacteria separated from eubacteria. It is concluded that the genetic code is not older than, but almost as old as our planet. While this result may not be unexpected, it was not clear until now that interpretable data exist that permit inferences about such early stages of life as the establishment of the genetic code.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eigen, M -- Lindemann, B F -- Tietze, M -- Winkler-Oswatitsch, R -- Dress, A -- von Haeseler, A -- New York, N.Y. -- Science. 1989 May 12;244(4905):673-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck-Institut fur biophysikalische Chemie, Gottingen, Federal Republic of Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2497522" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Archaea/genetics ; Base Sequence ; *Biological Evolution ; Codon ; Computer Simulation ; Eubacterium/genetics ; *Genetic Code ; Mutation ; Nucleic Acid Conformation ; Phylogeny ; *RNA, Transfer ; Statistics as Topic ; Time Factors
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  • 22
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-02-03
    Description: The question of how the amino acid sequence of a protein specifies its three-dimensional structure remains to be answered. Proteins are so large and complex that it is difficult to discern the features in their sequences that contribute to their structural stability and function. One approach to this problem is de novo design of model proteins, much simpler than their natural counterparts, yet containing sufficient information in their sequences to specify a given function (for example, folding in aqueous solution, folding in membranes, or formation of ion channels). Designed proteins provide simple model systems for understanding protein structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉DeGrado, W F -- Wasserman, Z R -- Lear, J D -- New York, N.Y. -- Science. 1989 Feb 3;243(4891):622-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉E. I. du Pont de Nemours & Company, Central Research and Development Department, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2464850" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Ion Channels ; Macromolecular Substances ; Models, Molecular ; Protein Conformation ; *Proteins ; Solubility ; Structure-Activity Relationship ; Tropomyosin ; Water
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  • 23
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-11-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Barinaga, M -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):880.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814509" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; California ; *Curriculum ; *Education
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  • 24
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-01-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉New York, N.Y. -- Science. 1989 Jan 27;243(4890):462-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2911752" target="_blank"〉PubMed〈/a〉
    Keywords: Adoption ; *Biological Evolution ; *Family ; *Homicide ; Humans
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  • 25
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1989-06-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cavalli-Sforza, L -- Piazza, A -- Menozzi, P -- Mountain, J -- New York, N.Y. -- Science. 1989 Jun 9;244(4909):1128-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2727697" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; *Genetics, Medical ; Humans ; *Language ; Models, Genetic
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  • 26
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-04
    Description: The relatively nonspecific single-stranded deoxyribonuclease, staphylococcal nuclease, was selectively fused to an oligonucleotide binding site of defined sequence to generate a hybrid enzyme. A cysteine was substituted for Lys116 in the enzyme by oligonucleotide-directed mutagenesis and coupled to an oligonucleotide that contained a 3'-thiol. The resulting hybrid enzyme cleaved single-stranded DNA at sites adjacent to the oligonucleotide binding site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corey, D R -- Schultz, P G -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1401-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3685986" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA, Single-Stranded/metabolism ; Hydrolysis ; Micrococcal Nuclease/*genetics/metabolism ; Models, Molecular ; Mutation ; Protein Conformation ; Staphylococcus aureus/enzymology/genetics ; Substrate Specificity
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  • 27
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Oct 16;238(4825):273-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3116670" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *Biological Evolution ; DNA/genetics ; Dental Enamel/anatomy & histology ; Gait ; Haplorhini/anatomy & histology/*genetics ; Humans ; Metacarpophalangeal Joint/anatomy & histology ; Molar ; Nucleic Acid Hybridization ; Pan troglodytes/anatomy & histology/*genetics ; Sequence Homology, Nucleic Acid
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  • 28
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-02-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Feb 27;235(4792):969-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3823869" target="_blank"〉PubMed〈/a〉
    Keywords: Anthropology ; *Biological Evolution ; Foot ; Gait ; Humans ; *Locomotion
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  • 29
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-02
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Oct 2;238(4823):24-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3116666" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; DNA, Mitochondrial/*genetics ; Haplorhini/*genetics
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  • 30
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):611-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3672114" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; *Chemistry ; Models, Molecular ; *Nobel Prize
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  • 31
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1987 Oct 30;238(4827):613-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3313727" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens ; Binding Sites ; *HLA Antigens ; Humans ; Models, Molecular ; Protein Conformation
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  • 32
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-20
    Description: The repertoire of antibody variable (V) regions has been subject to evolutionary selection, affecting both the diversity of V region genes in the germline and their expression in the B lymphocyte population and its subsets. In ontogeny, contact with an antigen leads to the expansion of B cells expressing antibodies complementary to it. In a defined phase of B cell differentiation, new sets of V regions are generated from the existing repertoire through somatic hypermutation. Cells carrying advantageous antibody mutants are selected into the memory compartment and produce a stable secondary response upon reexposure to the antigen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rajewsky, K -- Forster, I -- Cumano, A -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1088-94.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Genetics, University of Cologne, Koln, FRG.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317826" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies/*genetics ; *Antibody Diversity ; B-Lymphocytes/*physiology ; *Biological Evolution ; *Genes, Immunoglobulin ; Genes, Switch ; Immunity ; Immunoglobulin Isotypes/genetics ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Selection, Genetic
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  • 33
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-11-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sharp, P A -- Eisenberg, D -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):729-30, 807.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Cancer Research, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2445035" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Catalysis ; Escherichia coli/genetics ; Proteins/genetics ; RNA/*genetics ; Viruses/genetics
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  • 34
    Publication Date: 1987-11-20
    Description: A synthetic 52-residue peptide based on the sequence-specific DNA-binding domain of Hin recombinase (139-190) has been equipped with ethylenediaminetetraacetic acid (EDTA) at the amino terminus. In the presence of Fe(II), this synthetic EDTA-peptide cleaves DNA at Hin recombination sites. The cleavage data reveal that the amino terminus of Hin(139-190) is bound in the minor groove of DNA near the symmetry axis of Hin recombination sites. This work demonstrates the construction of a hybrid peptide combining two functional domains: sequence-specific DNA binding and DNA cleavage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sluka, J P -- Horvath, S J -- Bruist, M F -- Simon, M I -- Dervan, P B -- GM-09534-02/GM/NIGMS NIH HHS/ -- T32GM07616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Nov 20;238(4830):1129-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120311" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; DNA/*metabolism ; DNA Nucleotidyltransferases/*metabolism ; DNA-Binding Proteins/*chemical synthesis ; Edetic Acid ; Ferrous Compounds ; Models, Molecular ; Nucleic Acid Conformation ; Oxidation-Reduction ; Peptide Fragments ; Protein Binding ; Structure-Activity Relationship
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  • 35
    Publication Date: 1987-07-31
    Description: Complementary DNAs for three different muscarinic acetylcholine receptors were isolated from a rat cerebral cortex library, and the cloned receptors were expressed in mammalian cells. Analysis of human and rat genomic clones indicates that there are at least four functional muscarinic receptor genes and that these genes lack introns in the coding sequence. This gene family provides a new basis for evaluating the diversity of muscarinic mechanisms in the nervous system.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bonner, T I -- Buckley, N J -- Young, A C -- Brann, M R -- New York, N.Y. -- Science. 1987 Jul 31;237(4814):527-32.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3037705" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/metabolism ; Cloning, Molecular ; Codon ; Dna ; DNA Restriction Enzymes ; *Genes ; Genetic Code ; Humans ; Models, Molecular ; Nucleic Acid Hybridization ; Rats ; Receptors, Muscarinic/classification/*genetics ; Swine ; Transfection
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  • 36
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-18
    Description: Interleukin-2 is an effector protein that participates in modulating the immune response; it has become a focal point for the study of lymphokine structure and function. The three-dimensional structure of the interleukin molecule has been solved to 3.0 angstrom resolution. Interleukin-2 has a novel alpha-helical tertiary structure that suggests one portion of the molecule forms a structural scaffold, which underlies the receptor binding facets of the molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brandhuber, B J -- Boone, T -- Kenney, W C -- McKay, D B -- A1-00631/PHS HHS/ -- A1-19762/PHS HHS/ -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1707-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3500515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Interleukin-2/isolation & purification ; Mice ; Models, Molecular ; Protein Conformation ; Solvents ; X-Ray Diffraction
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  • 37
    Publication Date: 1987-05-08
    Description: beta-lactamases are enzymes that protect bacteria from the lethal effects of beta-lactam antibiotics, and are therefore of considerable clinical importance. The crystal structure of beta-lactamase from the Gram-positive bacterium Staphylococcus aureus PC1 has been determined at 2.5 angstrom resolution. It reveals a molecule of novel topology, made up of two closely associated domains. The active site is located at the interface between the domains, with the key catalytic residue Ser70 at the amino terminus of a buried helix. Examination of the disposition of the functionally important residues within the active site depression leads to a model for the binding of a substrate and a functional analogy to the serine proteases. The unusual topology of the secondary structure units is relevant to questions concerning the evolutionary relation to the beta-lactam target enzymes of the bacterial cell wall.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Herzberg, O -- Moult, J -- New York, N.Y. -- Science. 1987 May 8;236(4802):694-701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3107125" target="_blank"〉PubMed〈/a〉
    Keywords: *Anti-Bacterial Agents/metabolism ; Binding Sites ; Biological Evolution ; Catalysis ; Crystallization ; Drug Resistance, Microbial ; Endopeptidases ; Models, Molecular ; Polyethylene Glycols ; Protein Conformation ; Serine ; Serine Endopeptidases ; Solvents ; Staphylococcus aureus/*enzymology ; *beta-Lactamases/metabolism ; beta-Lactams
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  • 38
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-02
    Description: Extinction intensities calculated from 505 Paleozoic marine assemblages divided among six environmental zones and 40 stratigraphic intervals indicate that whole communities exhibit increasing extinction offshore but that genera within individual taxonomic classes tend to have their highest extinction onshore. The offshore trend at the community level results from a concentration of genera in classes with low characteristic extinction rates in nearshore environments. This finding is consistent with the ecologic expectation that organisms inhabiting unpredictably fluctuating environments should suffer more extinction than counterparts living under more predictably equitable conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sepkoski, J J Jr -- DEB 81-08890/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 2;235:64-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of the Geophysical Sciences, University of Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11539724" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Classification ; Ecosystem ; *Environment ; *Fossils ; Invertebrates ; *Marine Biology ; Mollusca ; North America ; *Paleontology
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  • 39
    Publication Date: 1987-02-13
    Description: A monoclonal antibody bound to a protein antigen slows the rate of chemical modification of amino acid residues located at the epitope. By comparing the degree of acetylation of 18 lysine and 7 threonine residues in free and antibody-bound horse cytochrome c, a discontiguous, conformational epitope was characterized on this protein antigen. The new approach is particularly suitable to probe discontiguous and conformational epitopes, which are difficult to analyze by other procedures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnens, A -- Demotz, S -- Corradin, G -- Binz, H -- Bosshard, H R -- New York, N.Y. -- Science. 1987 Feb 13;235(4790):780-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2433768" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/*immunology ; *Antigen-Antibody Complex ; Cytochrome c Group/*immunology ; Epitopes/*immunology ; Horses ; Humans ; Models, Molecular ; Protein Conformation ; Species Specificity
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  • 40
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, D L -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1633-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3120316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; *Carcinogens ; *Diet ; *Haplorhini ; Humans ; *Paleontology
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  • 41
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-09-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 Sep 25;237(4822):1570.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3629257" target="_blank"〉PubMed〈/a〉
    Keywords: *Base Sequence ; *Biological Evolution ; *Sequence Homology, Nucleic Acid ; Terminology as Topic
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  • 42
    Publication Date: 1987-03-06
    Description: A DNA cross-link adduct of the antitumor agent mitomycin C (MC) to DNA has been isolated and characterized; the results provide direct proof for bifunctional alkylation of DNA by MC. Exposure of MC to Micrococcus luteus DNA under reductive conditions and subsequent nuclease digestion yielded adducts formed between MC and deoxyguanosine residues. In addition to the two known monoadducts, a bisadduct was obtained. Reductive MC activation with Na2S2O4 (sodium dithionite) leads to exclusive bifunctional alkylation. The structure of the bisadduct was determined by spectroscopic methods that included proton magnetic resonance, differential Fourier transform infrared spectroscopy, and circular dichroism. Formation of the same bisadduct in vivo was demonstrated upon injection of rats with MC. Computer-generated models of the bisadduct that was incorporated into the center of the duplex B-DNA decamer d(CGTACGTACG)2 indicated that the bisadduct fit snugly into the minor groove with minimal distortion of DNA structure. A mechanistic analysis of the factors that govern monofunctional and bifunctional adduct formation is presented.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomasz, M -- Lipman, R -- Chowdary, D -- Pawlak, J -- Verdine, G L -- Nakanishi, K -- CA 11572/CA/NCI NIH HHS/ -- CA 28681/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1987 Mar 6;235(4793):1204-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3103215" target="_blank"〉PubMed〈/a〉
    Keywords: Chemical Phenomena ; Chemistry ; Cross-Linking Reagents/*isolation & purification ; DNA/*metabolism ; Mass Spectrometry ; Mitomycin ; Mitomycins/*metabolism ; Models, Molecular
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  • 43
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-12-18
    Description: One- and two-dimensional nuclear magnetic resonance (NMR) methods were used to determine a three-dimensional model of an eight-base-pair DNA fragment (d-GGGTACCC) cross-linked with psoralen in solution. Two-dimensional nuclear Overhauser effect experiments were used to assign the spectrum and estimate distances for 171 proton pairs in the cross-linked DNA. The NMR-derived model shows a 53 degree bend into the major groove that occurs primarily at the site of drug addition and a 56 degree unwinding that spans the eight-base-pair duplex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tomic, M T -- Wemmer, D E -- Kim, S H -- GM 31616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Dec 18;238(4834):1722-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3686011" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; *Cross-Linking Reagents ; *Dna ; Magnetic Resonance Spectroscopy/methods ; *Methoxsalen ; Models, Molecular ; Nucleic Acid Conformation ; *Oligodeoxyribonucleotides ; *Thymine
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  • 44
    Publication Date: 1987-11-06
    Description: Cytochrome c and cytochrome b5 form an electrostatically associated electron transfer complex. Computer models of this and related complexes that were generated by docking the x-ray structures of the individual proteins have provided insight into the specificity and mechanism of electron transfer reactions. Previous static modeling studies were extended by molecular dynamics simulations of a cytochrome c-cytochrome b5 intermolecular complex. The simulations indicate that electrostatic interactions at the molecular interface results in a flexible association complex that samples alternative interheme geometries and molecular conformations. Many of these transient geometries appear to be more favorable for electron transfer than those formed in the initial model complex. Of particular interest is a conformational change that occurred in phenylalanine 82 of cytochrome c that allowed the phenyl side chain to bridge the two cytochrome heme groups.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wendoloski, J J -- Matthew, J B -- Weber, P C -- Salemme, F R -- New York, N.Y. -- Science. 1987 Nov 6;238(4828):794-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research and Development Department, E. I. du Pont de Nemours and Company, Wilmington, DE 19898.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2823387" target="_blank"〉PubMed〈/a〉
    Keywords: Computer Graphics ; Cytochrome b Group/*metabolism ; Cytochrome c Group/*metabolism ; Cytochromes b5 ; Electron Transport ; Kinetics ; Models, Molecular ; Protein Binding ; Protein Conformation
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  • 45
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-07-24
    Description: A novel approach to engineering enzyme specificity is presented in which a catalytic group from an enzyme is first removed by site-directed mutagenesis causing inactivation. Activity is then partially restored by substrates containing the missing catalytic functional group. Replacement of the catalytic His with Ala in the Bacillus amyloliquefaciens subtilisin gene (the mutant is designated His64Ala) by site-directed mutagenesis reduces the catalytic efficiency (kcat/Km) by a factor of a million when assayed with N-succinyl-L-Phe-L-Ala-L-Ala-L-Phe-p-nitroanilide (sFAAF-pNA). Model building studies showed that a His side chain at the P2 position of a substrate bound at the active site of subtilisin could be virtually superimposed on the catalytic His side chain of this serine protease. Accordingly, the His64Ala mutant hydrolyzes a His P2 substrate (sFAHF-pNA) up to 400 times faster than a homologous Ala P2 or Gln P2 substrate (sFAAF-pNA or sFAQF-pNA) at pH 8.0. In contrast, the wild-type enzyme hydrolyzes these three substrates with similar catalytic efficiencies. Additional data from substrate-dependent pH profiles and hydrolysis of large polypeptides indicate that the His64Ala mutant enzyme can recover partially the function of the lost catalytic histidine from a His P2 side chain on the substrate. Such "substrate-assisted catalysis" provides a new basis for engineering enzymes with very narrow and potentially useful substrate specificities. These studies also suggest a possible functional intermediate in the evolution of the catalytic triad of serine proteases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, P -- Wells, J A -- New York, N.Y. -- Science. 1987 Jul 24;237(4813):394-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3299704" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Enzymes/*metabolism ; Models, Molecular ; Molecular Conformation ; Mutation ; Protein Binding ; Protein Conformation ; Substrate Specificity ; Subtilisins/genetics/*metabolism
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  • 46
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-06-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jones, B R -- Leise, E M -- New York, N.Y. -- Science. 1987 Jun 26;236(4809):1681-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3603007" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptation, Biological ; Animals ; *Biological Evolution ; Humans ; Nervous System/*anatomy & histology
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  • 47
    Publication Date: 1987-01-23
    Description: The atomic structure of thymidylate synthase from Lactobacillus casei was determined at 3 angstrom resolution. The native enzyme is a dimer of identical subunits. The dimer interface is formed by an unusual association between five-stranded beta sheets present in each monomer. Comparison of known sequences with the Lactobacillus casei structure suggests that they all have a common core structure around which loops are inserted or deleted in different sequences. Residues from both subunits contribute to each active site. Two arginine side chains can contribute to binding phosphate on the substrate. The side chains of several conserved amino acids can account for other determinants of substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hardy, L W -- Finer-Moore, J S -- Montfort, W R -- Jones, M O -- Santi, D V -- Stroud, R M -- AI 19358/AI/NIAID NIH HHS/ -- CA41323/CA/NCI NIH HHS/ -- GM 24485/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 23;235(4787):448-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3099389" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Crystallography ; Deoxyuracil Nucleotides/metabolism ; Lactobacillus casei/enzymology ; Models, Molecular ; Protein Conformation ; Structure-Activity Relationship ; *Thymidylate Synthase/antagonists & inhibitors
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  • 48
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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1987 May 8;236(4802):668-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576191" target="_blank"〉PubMed〈/a〉
    Keywords: *Biological Evolution ; Brain/*physiology ; Esthetics ; Humans ; Language ; Thinking
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  • 49
    Publication Date: 1987-05-15
    Description: A better understanding of the molecular mechanism of protein biosynthesis depends on the availability of a reliable model for the ribosome particle. The application of a diffraction technique, namely, three-dimensional image reconstruction from two-dimensional sheets of the large ribosomal subunits of Bacillus stearothermophilus at a resolution of 30 angstroms is described. The resulting three-dimensional model shows at least four projecting arms, arranged radially near the presumed interface with the 30S subunit. The projecting arms are positioned around a cleft, which turns into a tunnel with a length of 100 to 120 angstroms and a diameter of up to 25 angstroms. This tunnel spans the particle and may provide the path taken by the nascent polypeptide chain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yonath, A -- Leonard, K R -- Wittmann, H G -- GM34360/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 15;236(4803):813-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576200" target="_blank"〉PubMed〈/a〉
    Keywords: Geobacillus stearothermophilus/*ultrastructure ; Microscopy, Electron ; Models, Molecular ; Ribosomes/*ultrastructure
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