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  • Articles  (48)
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  • American Association for the Advancement of Science (AAAS)  (47)
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  • Articles  (48)
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  • American Association for the Advancement of Science (AAAS)  (47)
  • Springer  (1)
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  • American Meteorological Society
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  • 1
    Electronic Resource
    Electronic Resource
    Effect of fractionation on the enzymatic state and behaviour of enzyme activities in different structural soil units (1987)
    Springer
    Biology and fertility of soils 4 (1987), S. 151-154 
    Details
    ISSN: 1432-0789
    Keywords: Kinetics ; pH activity curves ; Soil enzymes ; Structural soil units ; Thermal stability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Geosciences , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Summary The behaviour and state of soil catalase, dehydrogenases, urease and proteases associated with different soil structural fractions were studied. Assays of the enzymatic sensitivity to pH variation, thermal stability and the calculation of kinetics constants of Michaelis were performed. The results indicated that catalase and urease activity in these soils seem to be of the same type, because the activities presented a similar behaviour in the soil fractions studied. However, their state appeared different in each group of soil units. Dehydrogenases showed a similar state and behaviour while proteases were in a different state and behaviour in each soil fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00256989
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  • 2
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    Dynamic instability in a DNA-segregating prokaryotic actin homolog (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-11-06
    Description: Dynamic instability-the switching of a two-state polymer between phases of steady elongation and rapid shortening-is essential to the cellular function of eukaryotic microtubules, especially during chromosome segregation. Since the discovery of dynamic instability 20 years ago, no other biological polymer has been found to exhibit this behavior. Using total internal reflection fluorescence microscopy and fluorescence resonance energy transfer, we observe that the prokaryotic actin homolog ParM, whose assembly is required for the segregation of large, low-copy number plasmids, displays both dynamic instability and symmetrical, bidirectional polymerization. The dynamic instability of ParM is regulated by adenosine triphosphate (ATP) hydrolysis, and filaments are stabilized by a cap of ATP-bound monomers. ParM is not related to tubulin, so its dynamic instability must have arisen by convergent evolution driven by a set of common constraints on polymer-based segregation of DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garner, Ethan C -- Campbell, Christopher S -- Mullins, R Dyche -- GM61010-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Nov 5;306(5698):1021-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, 600 16th Street, San Francisco, CA 94107, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15528442" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/chemistry ; Adenosine Triphosphate/metabolism ; Bacterial Proteins/*chemistry/physiology/ultrastructure ; Biopolymers/chemistry ; DNA, Bacterial/*metabolism ; Fluorescence Resonance Energy Transfer ; Hydrolysis ; Kinetics ; Microscopy, Fluorescence ; Mutagenesis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Biochemistry. How active sites communicate in thiamine enzymes (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, Frank -- GM-50380/GM/NIGMS NIH HHS/ -- GM-62330/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 29;306(5697):818-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Rutgers University, Newark, NJ 07102, USA. frjordan@newark.rutgers.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15514144" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Binding Sites ; Dihydrolipoyllysine-Residue Acetyltransferase ; Dimerization ; Geobacillus stearothermophilus/*enzymology ; Glutamic Acid/chemistry ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Kinetics ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Protein Subunits ; Protons ; Pyruvate Dehydrogenase (Lipoamide)/*chemistry/*metabolism ; Pyruvate Dehydrogenase Complex/*chemistry/*metabolism ; Thiamine Pyrophosphate/chemistry/*metabolism
    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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  • 4
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    Mutational analysis of the tyrosine phosphatome in colorectal cancers (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-05-25
    Description: Tyrosine phosphorylation, regulated by protein tyrosine phosphatases (PTPs) and kinases (PTKs), is important in signaling pathways underlying tumorigenesis. A mutational analysis of the tyrosine phosphatase gene superfamily in human cancers identified 83 somatic mutations in six PTPs (PTPRF, PTPRG, PTPRT, PTPN3, PTPN13, PTPN14), affecting 26% of colorectal cancers and a smaller fraction of lung, breast, and gastric cancers. Fifteen mutations were nonsense, frameshift, or splice-site alterations predicted to result in truncated proteins lacking phosphatase activity. Five missense mutations in the most commonly altered PTP (PTPRT) were biochemically examined and found to reduce phosphatase activity. Expression of wild-type but not a mutant PTPRT in human cancer cells inhibited cell growth. These observations suggest that the mutated tyrosine phosphatases are tumor suppressor genes, regulating cellular pathways that may be amenable to therapeutic intervention.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Zhenghe -- Shen, Dong -- Parsons, D Williams -- Bardelli, Alberto -- Sager, Jason -- Szabo, Steve -- Ptak, Janine -- Silliman, Natalie -- Peters, Brock A -- van der Heijden, Michiel S -- Parmigiani, Giovanni -- Yan, Hai -- Wang, Tian-Li -- Riggins, Greg -- Powell, Steven M -- Willson, James K V -- Markowitz, Sanford -- Kinzler, Kenneth W -- Vogelstein, Bert -- Velculescu, Victor E -- CA 43460/CA/NCI NIH HHS/ -- CA 57345/CA/NCI NIH HHS/ -- CA 62924/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2004 May 21;304(5674):1164-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sidney Kimmel Comprehensive Cancer Center, Howard Hughes Medical Institute, Johns Hopkins University Medical Institutions, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15155950" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; Cell Division ; Codon, Nonsense ; Colorectal Neoplasms/*enzymology/*genetics ; Computational Biology ; *DNA Mutational Analysis ; Exons ; Frameshift Mutation ; Genes, Tumor Suppressor ; Humans ; Kinetics ; Markov Chains ; *Mutation ; Mutation, Missense ; Nerve Tissue Proteins/chemistry/genetics/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 13 ; Protein Tyrosine Phosphatase, Non-Receptor Type 3 ; Protein Tyrosine Phosphatases/chemistry/*genetics/metabolism ; Receptor-Like Protein Tyrosine Phosphatases, Class 5 ; Signal Transduction ; Transfection ; Tyrosine/*metabolism
    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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  • 5
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    Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-12
    Description: With the use of x-ray absorption spectroscopy, we have found that the Fe-O bond in chloroperoxidase compound II (CPO-II) is much longer than expected for an oxoiron(IV) (ferryl) unit; notably, the experimentally determined bond length of 1.82(1) A accords closely with density functional calculations on a protonated ferryl (Fe(IV)-OH, 1.81 A). The basicity of the CPO-II ferryl [pKa 〉 8.2 (where Ka is the acid dissociation constant)] is attributable to strong electron donation by the axial thiolate. We suggest that the CPO-II protonated ferryl is a good model for the rebound intermediate in the P450 oxygenation cycle;with elevated pKa values after one-electron reduction, thiolate-ligated ferryl radicals are competent to oxygenate saturated hydrocarbons at potentials that can be tolerated by folded polypeptide hosts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Green, Michael T -- Dawson, John H -- Gray, Harry B -- DK19038/DK/NIDDK NIH HHS/ -- GM26730/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 11;304(5677):1653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, PA 16802, USA. mtg10@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15192224" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Chloride Peroxidase/*chemistry/metabolism ; Cytochrome P-450 Enzyme System/*chemistry/metabolism ; Electrons ; Fourier Analysis ; Free Radicals ; Horseradish Peroxidase/chemistry/metabolism ; Hydrocarbons/metabolism ; Hydrogen-Ion Concentration ; Hydroxylation ; Iron/*chemistry ; Kinetics ; Ligands ; Organometallic Compounds/*chemistry/metabolism ; Oxidation-Reduction ; Oxygen/*chemistry ; Physicochemical Phenomena ; Protons ; Spectrum Analysis
    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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  • 6
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    Phosphorylation of proteins by inositol pyrophosphates (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-12-18
    Description: The inositol pyrophosphates IP7 and IP8 contain highly energetic pyrophosphate bonds. Although implicated in various biologic functions, their molecular sites of action have not been clarified. Using radiolabeled IP7, we detected phosphorylation of multiple eukaryotic proteins. We also observed phosphorylation of endogenous proteins by endogenous IP7 in yeast. Phosphorylation by IP7 is nonenzymatic and may represent a novel intracellular signaling mechanism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saiardi, Adolfo -- Bhandari, Rashna -- Resnick, Adam C -- Snowman, Adele M -- Snyder, Solomon H -- DA00074/DA/NIDA NIH HHS/ -- MH068830-02/MH/NIMH NIH HHS/ -- MH18501/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2004 Dec 17;306(5704):2101-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University, School of Medicine, 725 North Wolfe Street, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15604408" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Escherichia coli Proteins/metabolism ; Humans ; Inositol Phosphates/*metabolism ; Kinetics ; Magnesium/metabolism ; Mice ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/chemistry/*metabolism ; Phosphates/metabolism ; Phosphorylation ; Phosphotransferases (Phosphate Group Acceptor)/metabolism ; Protein Kinases/genetics/metabolism ; Proteins/*metabolism ; RNA-Binding Proteins/chemistry/*metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry/*metabolism ; Serine/metabolism ; Signal Transduction ; Temperature
    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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  • 7
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    How enzymes work: analysis by modern rate theory and computer simulations (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-01-13
    Description: Advances in transition state theory and computer simulations are providing new insights into the sources of enzyme catalysis. Both lowering of the activation free energy and changes in the generalized transmission coefficient (recrossing of the transition state, tunneling, and nonequilibrium contributions) can play a role. A framework for understanding these effects is presented, and the contributions of the different factors, as illustrated by specific enzymes, are identified and quantified by computer simulations. The resulting understanding of enzyme catalysis is used to comment on alternative proposals of how enzymes work.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia-Viloca, Mireia -- Gao, Jiali -- Karplus, Martin -- Truhlar, Donald G -- New York, N.Y. -- Science. 2004 Jan 9;303(5655):186-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Supercomputing Institute, University of Minnesota, Minneapolis, MN 55455, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14716003" target="_blank"〉PubMed〈/a〉
    Keywords: *Catalysis ; Computer Simulation ; Enzymes/*chemistry/*metabolism ; Kinetics ; Mathematics ; Models, Chemical ; Models, Molecular ; Protein Conformation ; Thermodynamics
    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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  • 8
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    A functional protein chip for pathway optimization and in vitro metabolic engineering (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-04-17
    Description: Pathway optimization is difficult to achieve owing to complex, nonlinear, and largely unknown interactions of enzymes, regulators, and metabolites. We report a pathway reconstruction using RNA display-derived messenger RNA-enzyme fusion molecules. These chimeras are immobilized by hybridization of their messenger RNA end with homologous capture DNA spotted on a substrate surface. Enzymes thus immobilized retain activity proportional to the amount of capture DNA, allowing modulation of the relative activity of pathway enzymes. Entire pathways can thus be reconstructed and optimized in vitro from genomic information. We provide concept validation with the sequential reactions catalyzed by luciferase and nucleoside diphosphate kinase and further illustrate this method with the optimization of the five-step pathway for trehalose synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jung, Gyoo Yeol -- Stephanopoulos, Gregory -- New York, N.Y. -- Science. 2004 Apr 16;304(5669):428-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemical Engineering, Massachusetts Institute of Technology, Room 56-469, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15087547" target="_blank"〉PubMed〈/a〉
    Keywords: Catalysis ; DNA/genetics/metabolism ; Enzymes, Immobilized/genetics/*metabolism ; Gene Expression ; *Gene Expression Profiling ; *Genetic Engineering ; Glucose/metabolism ; Glucosyltransferases/genetics/metabolism ; Hexokinase/genetics/metabolism ; Kinetics ; Luciferases/genetics/metabolism ; *Metabolism ; Nucleic Acid Hybridization ; Nucleoside-Diphosphate Kinase/genetics/metabolism ; Oligonucleotide Array Sequence Analysis ; Phosphoglucomutase/genetics/metabolism ; Phosphoric Monoester Hydrolases/genetics/metabolism ; *Protein Array Analysis ; Protein Biosynthesis ; RNA, Messenger/*metabolism ; Trehalose/*biosynthesis ; UTP-Glucose-1-Phosphate Uridylyltransferase/genetics/metabolism
    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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  • 9
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    Biochemistry. Completing the view of transcriptional regulation (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉von Hippel, Peter H -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Jul 16;305(5682):350-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, OR 97403, USA. petevh@molbio.uoregon.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15256661" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/*metabolism ; Binding Sites ; DNA, Bacterial/*chemistry/*metabolism ; Diffusion ; Dimerization ; Escherichia coli/chemistry/genetics/metabolism ; Escherichia coli Proteins/chemistry/metabolism ; *Gene Expression Regulation, Bacterial ; Hydrogen Bonding ; Kinetics ; Lac Operon ; Lac Repressors ; Models, Genetic ; Models, Molecular ; Nucleic Acid Conformation ; Operator Regions, Genetic ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Repressor Proteins/*chemistry/*metabolism ; Static Electricity ; Thermodynamics ; *Transcription, Genetic
    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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  • 10
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    Two distinct actin networks drive the protrusion of migrating cells (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-18
    Description: Cell migration initiates by extension of the actin cytoskeleton at the leading edge. Computational analysis of fluorescent speckle microscopy movies of migrating epithelial cells revealed this process is mediated by two spatially colocalized but kinematically, kinetically, molecularly, and functionally distinct actin networks. A lamellipodium network assembled at the leading edge but completely disassembled within 1 to 3 micrometers. It was weakly coupled to the rest of the cytoskeleton and promoted the random protrusion and retraction of the leading edge. Productive cell advance was a function of the second colocalized network, the lamella, where actomyosin contraction was integrated with substrate adhesion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ponti, A -- Machacek, M -- Gupton, S L -- Waterman-Storer, C M -- Danuser, G -- GM67230/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2004 Sep 17;305(5691):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute (TSRI), La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15375270" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/drug effects/*physiology ; Actins/*physiology ; Animals ; Cell Line ; *Cell Movement ; Cells, Cultured ; Cytochalasin D/pharmacology ; *Depsipeptides ; Epithelial Cells/*physiology/ultrastructure ; Heterocyclic Compounds with 4 or More Rings/pharmacology ; Kinetics ; Macropodidae ; Microscopy, Fluorescence ; Motion Pictures as Topic ; Peptides, Cyclic/pharmacology ; Pseudopodia/*physiology/ultrastructure ; Salamandridae
    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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