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  • 1
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    A bacterial virulence protein suppresses host innate immunity to cause plant disease (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-15
    Description: Plants have evolved a powerful immune system to defend against infection by most microbial organisms. However, successful pathogens, such as Pseudomonas syringae, have developed countermeasures and inject virulence proteins into the host plant cell to suppress immunity and cause devastating diseases. Despite intensive research efforts, the molecular targets of bacterial virulence proteins that are important for plant disease development have remained obscure. Here, we show that a conserved P. syringae virulence protein, HopM1, targets an immunity-associated protein, AtMIN7, in Arabidopsis thaliana. HopM1 mediates the destruction of AtMIN7 via the host proteasome. Our results illustrate a strategy by which a bacterial pathogen exploits the host proteasome to subvert host immunity and causes infection in plants.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nomura, Kinya -- Debroy, Sruti -- Lee, Yong Hoon -- Pumplin, Nathan -- Jones, Jonathan -- He, Sheng Yang -- New York, N.Y. -- Science. 2006 Jul 14;313(5784):220-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16840699" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/metabolism ; Arabidopsis/*immunology/metabolism/*microbiology ; Arabidopsis Proteins/*metabolism ; Bacterial Proteins/genetics/metabolism ; Brefeldin A/pharmacology ; Glucans/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Immunity, Innate ; Mutation ; Plant Diseases/*microbiology ; Plant Leaves/metabolism/microbiology ; Plants, Genetically Modified ; Proteasome Endopeptidase Complex/metabolism ; Protein Transport ; Pseudomonas syringae/genetics/growth & development/*pathogenicity ; Tobacco/metabolism ; Two-Hybrid System Techniques ; Ubiquitins/metabolism ; Virulence Factors/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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  • 2
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    Suppression of the microRNA pathway by bacterial effector proteins (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-08-16
    Description: Plants and animals sense pathogen-associated molecular patterns (PAMPs) and in turn differentially regulate a subset of microRNAs (miRNAs). However, the extent to which the miRNA pathway contributes to innate immunity remains unknown. Here, we show that miRNA-deficient mutants of Arabidopsis partly restore growth of a type III secretion-defective mutant of Pseudomonas syringae. These mutants also sustained growth of nonpathogenic Pseudomonas fluorescens and Escherichia coli strains, implicating miRNAs as key components of plant basal defense. Accordingly, we have identified P. syringae effectors that suppress transcriptional activation of some PAMP-responsive miRNAs or miRNA biogenesis, stability, or activity. These results provide evidence that, like viruses, bacteria have evolved to suppress RNA silencing to cause disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570098/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2570098/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Navarro, Lionel -- Jay, Florence -- Nomura, Kinya -- He, Sheng Yang -- Voinnet, Olivier -- 5R01AI060761/AI/NIAID NIH HHS/ -- R01 AI060761/AI/NIAID NIH HHS/ -- R01 AI060761-03/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2008 Aug 15;321(5891):964-7. doi: 10.1126/science.1159505.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Biologie Moleculaire des Plantes, CNRS UPR 2353-Universite Louis Pasteur, 12 Rue du General Zimmer, 67084 Strasbourg Cedex, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18703740" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/immunology/*microbiology/virology ; Bacterial Proteins/*metabolism ; Escherichia coli/growth & development ; Immunity, Innate ; MicroRNAs/genetics/*metabolism ; Mutation ; Plant Diseases/immunology/*microbiology ; Plant Leaves/metabolism/microbiology ; Plants, Genetically Modified ; Potyvirus/physiology ; Pseudomonas fluorescens/growth & development ; Pseudomonas syringae/genetics/*growth & development/metabolism/pathogenicity ; RNA Interference ; RNA Stability ; RNA, Plant/genetics/*metabolism ; 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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  • 3
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    Altered telomeres in tumors with ATRX and DAXX mutations (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-07-02
    Description: The proteins encoded by ATRX and DAXX participate in chromatin remodeling at telomeres and other genomic sites. Because inactivating mutations of these genes are common in human pancreatic neuroendocrine tumors (PanNETs), we examined the telomere status of these tumors. We found that 61% of PanNETs displayed abnormal telomeres that are characteristic of a telomerase-independent telomere maintenance mechanism termed ALT (alternative lengthening of telomeres). All of the PanNETs exhibiting these abnormal telomeres had ATRX or DAXX mutations or loss of nuclear ATRX or DAXX protein. ATRX mutations also correlate with abnormal telomeres in tumors of the central nervous system. These data suggest that an alternative telomere maintenance function may operate in human tumors with alterations in the ATRX or DAXX genes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3174141/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3174141/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heaphy, Christopher M -- de Wilde, Roeland F -- Jiao, Yuchen -- Klein, Alison P -- Edil, Barish H -- Shi, Chanjuan -- Bettegowda, Chetan -- Rodriguez, Fausto J -- Eberhart, Charles G -- Hebbar, Sachidanand -- Offerhaus, G Johan -- McLendon, Roger -- Rasheed, B Ahmed -- He, Yiping -- Yan, Hai -- Bigner, Darell D -- Oba-Shinjo, Sueli Mieko -- Marie, Suely Kazue Nagahashi -- Riggins, Gregory J -- Kinzler, Kenneth W -- Vogelstein, Bert -- Hruban, Ralph H -- Maitra, Anirban -- Papadopoulos, Nickolas -- Meeker, Alan K -- P01 CA134292/CA/NCI NIH HHS/ -- P01 CA134292-01A1/CA/NCI NIH HHS/ -- P50 CA062924/CA/NCI NIH HHS/ -- P50 CA062924-06/CA/NCI NIH HHS/ -- P50 NS020023/NS/NINDS NIH HHS/ -- P50 NS020023-28/NS/NINDS NIH HHS/ -- R01 CA113669/CA/NCI NIH HHS/ -- R01 CA113669-06/CA/NCI NIH HHS/ -- R01 CA121113/CA/NCI NIH HHS/ -- R01 CA121113-01/CA/NCI NIH HHS/ -- R01 CA140316/CA/NCI NIH HHS/ -- R01 CA140316-01A1/CA/NCI NIH HHS/ -- R01 NS055089/NS/NINDS NIH HHS/ -- R01 NS055089-01A2/NS/NINDS NIH HHS/ -- R37 CA011898/CA/NCI NIH HHS/ -- R37 CA011898-41/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2011 Jul 22;333(6041):425. doi: 10.1126/science.1207313. Epub 2011 Jun 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Sol Goldman Pancreatic Cancer Research Center, Johns Hopkins Medical Institutions, Baltimore, MD 21231, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21719641" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*genetics/metabolism ; Carcinoma, Neuroendocrine/*genetics/pathology/physiopathology ; Cell Nucleus/metabolism ; Central Nervous System Neoplasms/*genetics/pathology/physiopathology ; Chromatin Assembly and Disassembly ; DNA Helicases/*genetics/metabolism ; Humans ; In Situ Hybridization, Fluorescence ; Mutant Proteins/genetics/metabolism ; Mutation ; Nuclear Proteins/*genetics/metabolism ; Pancreatic Neoplasms/*genetics/pathology/physiopathology ; Phenotype ; Telomere/*physiology/ultrastructure
    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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    Regulation of flowering time by histone acetylation in Arabidopsis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-01
    Description: The Arabidopsis autonomous floral-promotion pathway promotes flowering independently of the photoperiod and vernalization pathways by repressing FLOWERING LOCUS C (FLC), a MADS-box transcription factor that blocks the transition from vegetative to reproductive development. Here, we report that FLOWERING LOCUS D (FLD), one of six genes in the autonomous pathway, encodes a plant homolog of a protein found in histone deacetylase complexes in mammals. Lesions in FLD result in hyperacetylation of histones in FLC chromatin, up-regulation of FLC expression, and extremely delayed flowering. Thus, the autonomous pathway regulates flowering in part by histone deacetylation. However, not all autonomous-pathway mutants exhibit FLC hyperacetylation, indicating that multiple means exist by which this pathway represses FLC expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Yuehui -- Michaels, Scott D -- Amasino, Richard M -- New York, N.Y. -- Science. 2003 Dec 5;302(5651):1751-4. Epub 2003 Oct 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593187" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Arabidopsis/genetics/*growth & development/metabolism ; Arabidopsis Proteins/chemistry/*genetics/*metabolism ; Chromatin/metabolism ; Flowers/*growth & development ; Gene Expression Regulation, Plant ; Genes, Plant ; Histone Deacetylases/chemistry/genetics/*metabolism ; Histones/*metabolism ; Humans ; Introns ; MADS Domain Proteins/chemistry/*genetics/*metabolism ; Molecular Sequence Data ; Mutation ; Phenotype ; Plants, Genetically Modified ; Precipitin Tests ; Protein Structure, Tertiary ; Regulatory Sequences, Nucleic Acid ; Repressor Proteins/chemistry/metabolism ; Sequence Deletion ; 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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  • 5
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    Nitric oxide represses the Arabidopsis floral transition (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-28
    Description: The correct timing of flowering is essential for plants to maximize reproductive success and is controlled by environmental and endogenous signals. We report that nitric oxide (NO) repressed the floral transition in Arabidopsis thaliana. Plants treated with NO, as well as a mutant overproducing NO (nox1), flowered late, whereas a mutant producing less NO (nos1) flowered early. NO suppressed CONSTANS and GIGANTEA gene expression and enhanced FLOWERING LOCUS C expression, which indicated that NO regulates the photoperiod and autonomous pathways. Because NO is induced by environmental stimuli and constitutively produced, it may integrate both external and internal cues into the floral decision.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Yikun -- Tang, Ru-Hang -- Hao, Yi -- Stevens, Robert D -- Cook, Charles W -- Ahn, Sun M -- Jing, Liufang -- Yang, Zhongguang -- Chen, Longen -- Guo, Fangqing -- Fiorani, Fabio -- Jackson, Robert B -- Crawford, Nigel M -- Pei, Zhen-Ming -- New York, N.Y. -- Science. 2004 Sep 24;305(5692):1968-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Duke University, Durham, NC 27708, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15448272" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/drug effects/genetics/*physiology ; Arabidopsis Proteins/genetics/physiology ; Carrier Proteins/genetics/physiology ; Flowers/growth & development/*physiology ; Membrane Proteins/genetics/physiology ; Mutation ; Nitric Oxide/genetics/*physiology ; Nitroprusside/pharmacology ; Photoperiod ; *Saccharomyces cerevisiae Proteins
    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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    Drosophila NOMPC is a mechanotransduction channel subunit for gentle-touch sensation (2012)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2012-12-12
    Description: Touch sensation is essential for behaviours ranging from environmental exploration to social interaction; however, the underlying mechanisms are largely unknown. In Drosophila larvae, two types of sensory neurons, class III and class IV dendritic arborization neurons, tile the body wall. The mechanotransduction channel PIEZO in class IV neurons is essential for sensing noxious mechanical stimuli but is not involved in gentle touch. On the basis of electrophysiological-recording, calcium-imaging and behavioural studies, here we report that class III dendritic arborization neurons are touch sensitive and contribute to gentle-touch sensation. We further identify NOMPC (No mechanoreceptor potential C), a member of the transient receptor potential (TRP) family of ion channels, as a mechanotransduction channel for gentle touch. NOMPC is highly expressed in class III neurons and is required for their mechanotransduction. Moreover, ectopic NOMPC expression confers touch sensitivity to the normally touch-insensitive class IV neurons. In addition to the critical role of NOMPC in eliciting gentle-touch-mediated behavioural responses, expression of this protein in the Drosophila S2 cell line also gives rise to mechanosensitive channels in which ion selectivity can be altered by NOMPC mutation, indicating that NOMPC is a pore-forming subunit of a mechanotransduction channel. Our study establishes NOMPC as a bona fide mechanotransduction channel that satisfies all four criteria proposed for a channel to qualify as a transducer of mechanical stimuli and mediates gentle-touch sensation. Our study also suggests that different mechanosensitive channels may be used to sense gentle touch versus noxious mechanical stimuli.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3917554/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3917554/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, Zhiqiang -- Zhang, Wei -- He, Ye -- Gorczyca, David -- Xiang, Yang -- Cheng, Li E -- Meltzer, Shan -- Jan, Lily Yeh -- Jan, Yuh Nung -- 5R01MH084234/MH/NIMH NIH HHS/ -- P30 DK063720/DK/NIDDK NIH HHS/ -- R01 MH084234/MH/NIMH NIH HHS/ -- R37 NS040929/NS/NINDS NIH HHS/ -- R37NS040929/NS/NINDS NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2013 Jan 10;493(7431):221-5. doi: 10.1038/nature11685. Epub 2012 Dec 9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Physiology, University of California, San Francisco, San Francisco, California 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/23222543" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Dendrites/physiology ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster/cytology/growth & development/*physiology ; Larva/cytology/physiology ; Mechanotransduction, Cellular/*physiology ; Molecular Sequence Data ; Mutation ; Protein Subunits/chemistry/genetics/*metabolism ; Sequence Alignment ; Touch/*physiology ; Transient Receptor Potential Channels/chemistry/genetics/*metabolism
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 7
    Electronic Resource
    Electronic Resource
    Analysis of titanium dental implants after failure of osseointegration: Combined histological, electron microscopy, and X-ray photoelectron spectroscopy approach (1998)
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 43 (1998), S. 300-312 
    Details
    ISSN: 0021-9304
    Keywords: titanium ; dental implant ; osseointegration failure ; surface analysis ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: A multitechnique approach has been used to characterize the surface of nonosseointegrated titanium implants and the surrounding biological tissues. Five pure titanium dental implants were used as reference, and 25 removed implants were studied. Surface and in-depth chemical compositions of the implants (from a total of 16 patients) were investigated by X-ray photoelectron spectroscopy (XPS). Histological slides of the surrounding tissues were examined by light microscopy, XPS, and electron microprobe analysis. None of the failed implants presented the regular surface composition and depth profile of the TiO2 overlayer; foreign elements (Ca, Na, P, Si, Cl, Zn, Pb, and Al) were observed on some implants. Fibrosis, lymphocytic and plasmocytic infiltrates, and granulomatous lesions were detected in the surrounding tissues. XPS and electron microprobe analysis indicated the presence of Zn, Fe, Sn, and Ti in the tissues. As a possible scenario for implant failure, we propose and discuss a oxidoreduction mechanism, leading to a partial dissolution or the complete dissociation of the protective titanium dioxide overlayer and to ion diffusion through the surrounding tissues. © 1998 John Wiley & Sons, Inc. J Biomed Mater Res (Appl Biomater) 43: 300-312, 1998
    Additional Material: 11 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    Effects of nitric oxide on the thermal decomposition of methyl nitrite: Overall kinetics and rate constants for the HNO + HNO and HNO + 2NO reactions (1992)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 24 (1992), S. 743-760 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The effects of NO on the decomposition of CH3ONO have been investigated in the temperature range 450-520 K at a constant pressure of 710 torr using He as buffer gas. The measured time-dependent concentration profiles of CH3ONO, NO, N2O, and CH2O can be quantitatively accounted for with a general mechanism consisting of various reactions of CH3O, HNO, and (HNO)2. The results of kinetic modeling with sensitivity analyses indicate that the disappearance rate of CH3ONO is weakly affected by NO addition, whereas that of the HNO intermediate strongly altered by the added NO. In the presence of low NO concentrations, the modeling of N2O yields leads to the rate constant for the bimolecular reaction, HNO + HNO → N2O + H2O (25): \documentclass{article}\pagestyle{empty}\begin{document}$$ k_{25} = 10^{8.93 \pm 0.30}\, \,e^{-1,550 \pm 150/{\rm T}} {\rm cm}^3 /{\rm mol}\,{\rm s} $$\end{document} In the presence of high NO concentrations (PNO 〉 50 torr), the modeling of CH2O yields gives the rate constant for the termolecular radical formation channel, HNO + 2NO → HN2O + NO2 (35): \documentclass{article}\pagestyle{empty}\begin{document}$$ k_{35} = 10^{11.2 \pm 0.3}\, \,e^{-1050 \pm 200/{\rm T}} {\rm cm}^6 /{\rm mol}^2\,{\rm s} $$\end{document} Discussion on the mechanisms for reactions (25) and (35), and the alkyl homolog of (35), RNO + 2NO, is presented herein. © John Wiley & Sons, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/kin.550240808
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  • 9
    Electronic Resource
    Electronic Resource
    Thermal reaction of HNCO with NO2 at moderate temperatures (1993)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 25 (1993), S. 845-863 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The thermal reaction of HNCO with NO2 has been studied in the temperature range of 623 to 773 K by FTIR spectrometry. Major products measured are CO2 and NO with a small amount of N2O. Kinetic modeling of the time resolved concentration profiles of the reactants and products, aided by the thermochemical data of various likely reactive intermediates computed by means of the BAC-MP4 method, allows us to conclude that the reaction is initiated exclusively by a new bimolecular process: with a rate constant, k1 = 2.5 × 1012e-13,100/T cm3/mols. The well-known bimolecular reaction is the only strong competitive process in this important reactive system throughout the temperature range studied. Kinetic modeling of NO formation and NO2 decay rates gave rise to values of k10 which were in close agreement with literature data. © 1993 John Wiley & Sons, Inc.
    Additional Material: 6 Ill.
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    URL: http://dx.doi.org/10.1002/kin.550251006
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  • 10
    Electronic Resource
    Electronic Resource
    The thermal reaction of HNCO at moderate temperatures (1991)
    New York, NY : Wiley-Blackwell
    International Journal of Chemical Kinetics 23 (1991), S. 1129-1149 
    Details
    ISSN: 0538-8066
    Keywords: Chemistry ; Physical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The thermal reaction of HNCO has been studied in a static cell at temperatures between 873 and 1220 K and a constant pressure of 800 torr under highly diluted conditions. The reaction was measurable above 1000 K by FTIR spectrometry. The products detected include CO, CO2, HCN, NH3, and the unreacted HNCO. In this moderate temperature regime, the rates of product formation and HNCO decay cannot be accounted for by a previously established high-temperature mechanism, assuming HNCO → NH + CO (1) as the initiation process. Instead, a new bimolecular reaction, 2HNCO → CO2 + HNCNH (2), has been invoked to interpret the disappearance of HNCO as well as the formation of various products, most importantly CO2.The concentration profiles of all measured species can be quantitatively modeled, throughout the temperature range analyzed, by varying k2 using a modified mechanism. The kinetically modeled values of k2 can be effectively represented by \documentclass{article}\pagestyle{empty}\begin{document}$$ k_{\rm 2} = 10^{10.84 \pm 0.07} {\rm \,exp}(- 21,240 \pm 1,960/{\rm T}){\rm\, cm}^3 /{\rm mol\, s}{\rm .} $$\end{document}This result agrees closely with that computed with the conventional transition-state theory using the TST parameters predicted by the BAC-MP4 method: \documentclass{article}\pagestyle{empty}\begin{document}$$ k_2 ({\rm BAC} - {\rm MP}4) = 10^{11.13} {\rm \,exp(- 21,600/T) cm}^{\rm 3} /{\rm mol s}{\rm .} $$\end{document}The bimolecular reaction takes place via a stable 4-membered ring intermediate which is isoelectronic with diketene; viz.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/kin.550231206
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