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  • AGRIS (United Nations, Food and Agriculture Organization)  (37)
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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 05 March 2013, Vol.110(10), pp.3782-7
    Description: The study of genetic disease mechanisms relies mostly on targeted mouse mutants that are derived from engineered embryonic stem (ES) cells. Nevertheless, the establishment of mutant ES cells is laborious and time-consuming, restricting the study of the increasing number of human disease mutations discovered by high-throughput genomic analysis. Here, we present an advanced approach for the production of mouse disease models by microinjection of transcription activator-like effector nucleases (TALENs) and synthetic oligodeoxynucleotides into one-cell embryos. Within 2 d of embryo injection, we created and corrected chocolate missense mutations in the small GTPase RAB38; a regulator of intracellular vesicle trafficking and phenotypic model of Hermansky-Pudlak syndrome. Because ES cell cultures and targeting vectors are not required, this technology enables instant germline modifications, making heterozygous mutants available within 18 wk. The key features of direct mutagenesis by TALENs and oligodeoxynucleotides, minimal effort and high speed, catalyze the generation of future in vivo models for the study of human disease mechanisms and interventions.
    Keywords: Disease Models, Animal ; Germ-Line Mutation ; Genetic Diseases, Inborn -- Genetics ; Oligodeoxyribonucleotides -- Administration & Dosage
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 2
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 2012, Vol.109(24), pp.9354-9359
    Description: Gene targeting by zinc-finger nucleases in one-cell embryos provides an expedite mutagenesis approach in mice, rats, and rabbits. This technology has been recently used to create knockout and knockin mutants through the deletion or insertion of nucleotides. Here we apply zinc-finger nucleases in one-cell mouse embryos to generate disease-related mutants harboring single nucleotide or codon replacements. Using a gene-targeting vector or a synthetic oligodesoxynucleotide as template for homologous recombination, we introduced missense and silent mutations into the Rab38 gene, encoding a small GTPase that regulates intracellular vesicle trafficking. These results demonstrate the feasibility of seamless gene editing in one-cell embryos to create genetic disease models and establish synthetic oligodesoxynucleotides as a simplified mutagenesis tool. ; p. 9354-9359.
    Keywords: Nucleases ; Mice ; Physiological Transport ; Gene Targeting ; Rabbits ; Genes ; Disease Models ; Mutagenesis ; Genetic Disorders ; Nucleotides ; Homologous Recombination ; Guanosinetriphosphatase ; Rats ; Mutants
    ISSN: 0027-8424
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  • 3
    In: Journal of Neurochemistry, June 2010, Vol.113(5), pp.1240-1251
    Description: To authenticate to the full-text of this article, please visit this link: http://dx.doi.org/10.1111/j.1471-4159.2010.06693.x Keywords: advanced glycation end products; anxiety; copy number variant; depression; high anxiety-related behavior Abstract: J. Neurochem. (2010) 113, 1240-1251. Abstract Methylglyoxal (MG) is a highly reactive metabolite that forms adducts with basic amino acid side chains in proteins. MG is degraded by glyoxalase1 (GLO1), an enzyme shown to be differentially expressed in several mouse models of anxiety-related behavior. As yet, molecular mechanisms by which altered GLO1 expression influences emotionality have not been elucidated. Here we report that both MG concentration and protein modification are altered in brain tissue of a mouse model for trait anxiety, with elevated levels in low anxiety-related behavior relative to high anxiety-related behavior animals. Accordingly, repeated intracerebroventricular injections of MG mediated anxiolysis in inbred high anxiety-related behavior and outbred CD1 mice. We found that anxiolytic-like properties of MG were independent of GLO1 expression. In contrast, antidepressant-like properties of intracerebroventricular MG were suppressed in CD1 mice carrying extra copies of the GLO1 gene. Moreover, MG treatment increased expression of GLO1 only in CD1 mice that did not have extra copies of GLO1. Taken together, these results suggest that the MG levels in brain are negatively correlated with anxiety. Thereby, we identified a novel molecular mechanism for anxiety-related behavior in mice that may help to elucidate genesis of psychiatric disorders in humans. Author Affiliation: (*)Department of Behavioral Neuroendocrinology, Max Planck Institute of Psychiatry, Munich, Germany ([dagger])Department of Medical Technology, Fooyin University, Ta-Liao Hsiang, Kaohsiung Hsien, Taiwan ([double dagger])Department of Neuronal Network Dynamics, Max Planck Institute of Psychiatry, Munich, Germany (s.)Department of Proteomics and Biomarkers, Max Planck Institute of Psychiatry, Munich, Germany Article History: Received January 25, 2010; revised manuscript received March 1, 2010; accepted March 14, 2010. Article note: Address correspondence and reprint requests to Dr Boris Hambsch, Department of Behavioral Neuroendocrinology, Max Planck Institute of Psychiatry, Kraepelinstr.2, 80804 Munich, Germany. E-mail: hambsch@mpipsykl.mpg.de
    Keywords: Advanced Glycation End Products ; Anxiety ; Copy Number Variant ; Depression ; High Anxiety‐Related Behavior
    ISSN: 0022-3042
    E-ISSN: 1471-4159
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  • 4
    Language: English
    In: Science (New York, N.Y.), 22 September 2006, Vol.313(5794), pp.1781-4
    Description: Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-beta (Abeta)-containing brain extracts from humans with Alzheimer's disease or beta-amyloid precursor protein (APP) transgenic mice induced cerebral beta-amyloidosis and associated pathology in APP transgenic mice in a time- and concentration-dependent manner. The seeding activity of brain extracts was reduced or abolished by Abeta immunodepletion, protein denaturation, or by Abeta immunization of the host. The phenotype of the exogenously induced amyloidosis depended on both the host and the source of the agent, suggesting the existence of polymorphic Abeta strains with varying biological activities reminiscent of prion strains.
    Keywords: Amyloid Beta-Peptides -- Administration & Dosage ; Amyloid Beta-Protein Precursor -- Administration & Dosage ; Amyloidosis -- Metabolism ; Brain Diseases -- Metabolism ; Hippocampus -- Chemistry
    ISSN: 00368075
    E-ISSN: 1095-9203
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  • 5
    Language: English
    In: 2015
    Keywords: Nucleases ; Mice ; Germ Cells ; Zygote ; Gene Targeting ; Embryonic Stem Cells ; Genes ; Loci ; Homologous Recombination ; Mutants
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
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  • 6
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America 21 , 7659-7664., 2014
    Description: The lariat-capping (LC) ribozyme is a natural ribozyme isolated from eukaryotic microorganisms. Despite apparent structural similarity to group I introns, the LC ribozyme catalyzes cleavage by a 2',5' branching reaction, leaving the 3' product with a 3-nt lariat cap that functionally substitutes for a conventional mRNA cap in the downstream pre-mRNA encoding a homing endonuclease. We describe the crystal structures of the precleavage and postcleavage LC ribozymes, which suggest that structural features inherited from group I ribozymes have undergone speciation due to profound changes in molecular selection pressure, ultimately giving rise to an original branching ribozyme family. The structures elucidate the role of key elements that regulate the activity of the LC ribozyme by conformational switching and suggest a mechanism by which the signal for branching is transmitted to the catalytic core. The structures also show how conserved interactions twist residues, forming the lariat to join chemical groups involved in branching.
    Keywords: Arn ; Ribozyme ; Rna Structure;Rna Catalysis;Gir1;Crystallography;Saxs
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
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  • 7
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America 21 , 7659-7664., 2014
    Description: The lariat-capping (LC) ribozyme is a natural ribozyme isolated from eukaryotic microorganisms. Despite apparent structural similarity to group I introns, the LC ribozyme catalyzes cleavage by a 2',5' branching reaction, leaving the 3' product with a 3-nt lariat cap that functionally substitutes for a conventional mRNA cap in the downstream pre-mRNA encoding a homing endonuclease. We describe the crystal structures of the precleavage and postcleavage LC ribozymes, which suggest that structural features inherited from group I ribozymes have undergone speciation due to profound changes in molecular selection pressure, ultimately giving rise to an original branching ribozyme family. The structures elucidate the role of key elements that regulate the activity of the LC ribozyme by conformational switching and suggest a mechanism by which the signal for branching is transmitted to the catalytic core. The structures also show how conserved interactions twist residues, forming the lariat to join chemical groups involved in branching.
    Keywords: Arn ; Ribozyme ; Rna Structure;Rna Catalysis;Gir1;Crystallography;Saxs
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
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  • 8
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 10 March 2009, Vol.106(10), pp.4012-4017
    Description: Synapse loss correlates with a cognitive decline in Alzheimer's disease (AD), but whether this is caused by fibrillar deposits known as senile plaques or soluble oligomeric forms of amyloid β(Aβ) is controversial. By using array tomography, a technique that combines ultrathin sectioning of tissue with immunofluorescence, allowing precise quantification of small structures, such as synapses, we have tested the hypothesis that oligomeric Aβ surrounding plaques contributes to synapse loss in a mouse model of AD. We find that senile plaques are surrounded by a halo of oligomeric Aβ. Analysis of 〉 14,000 synapses (represented by PSD95-stained excitatory synapses) shows that there is a 60% loss of excitatory synapses in the halo of oligomeric Aβ surrounding plaques and that the density increases to reach almost control levels in volumes further than 50 μm from a plaque in an approximately linear fashion (linear regression, r² = 0.9; P 〈 0.0001). Further, in transgenic cortex, microdeposits of oligomeric Aβ associate with a subset of excitatory synapses, which are significantly smaller than those not in contact with oligomeric Aβ. The proportion of excitatory synapses associated with Aβ correlates with decreasing density (correlation, -0.588; P 〈 0.0001). These data show that senile plaques are a potential reservoir of oligomeric Aβ, which colocalizes with the postsynaptic density and is associated with spine collapse, reconciling the apparently competing schools of thought of "plaque" vs. "oligomeric Aβ" as the synaptotoxic species in the brain of AD patients.
    Keywords: Biological sciences -- Biology -- Cytology -- Postsynaptic density ; Physical sciences -- Chemistry -- Chemical compounds -- Postsynaptic density ; Biological sciences -- Biology -- Zoology -- Postsynaptic density ; Health sciences -- Medical sciences -- Immunology -- Postsynaptic density ; Health sciences -- Medical diagnosis -- Diagnostic methods -- Postsynaptic density ; Biological sciences -- Biology -- Anatomy -- Postsynaptic density ; Biological sciences -- Biology -- Cytology -- Postsynaptic density ; Biological sciences -- Biology -- Anatomy -- Postsynaptic density ; Health sciences -- Medical conditions -- Symptoms -- Postsynaptic density ; Health sciences -- Medical conditions -- Diseases -- Postsynaptic density ; Biological sciences -- Biology -- Cytology -- Postsynaptic density ; Physical sciences -- Chemistry -- Chemical compounds -- Postsynaptic density ; Biological sciences -- Biology -- Zoology -- Postsynaptic density ; Health sciences -- Medical sciences -- Immunology -- Postsynaptic density ; Health sciences -- Medical diagnosis -- Diagnostic methods -- Postsynaptic density ; Biological sciences -- Biology -- Anatomy -- Postsynaptic density ; Biological sciences -- Biology -- Cytology -- Postsynaptic density ; Biological sciences -- Biology -- Anatomy -- Postsynaptic density ; Health sciences -- Medical conditions -- Symptoms -- Postsynaptic density ; Health sciences -- Medical conditions -- Diseases -- Postsynaptic density
    ISSN: 00278424
    E-ISSN: 10916490
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  • 9
    Language: English
    In: Phytochemistry, 2006, Vol.67(3), pp.255-263
    Description: Biochemical characterization of the apple polygalacturonase inhibiting protein1 was carried out by expression in a heterologous plant host, thus defining the activity of the product of this specific apple gene. Extracts from apple fruit (cultivar “Granny Smith”) inhibited the cell-wall degrading polygalacturonase (PG) activity of , the causal agent of anthracnose on lupins, as well as PG. Southern blot analysis indicated that this cultivar of apple has a small gene family of polygalacturonase inhibiting proteins ( ), and therefore heterologous expression in transgenic tobacco was used to identify the specific gene product responsible for the inhibitory activity. A previously isolated gene, termed , was introduced into tobacco ( ) by Agrobacterium-mediated transformation. The mature MdPGIP1 protein was purified to apparent homogeneity from tobacco leaves by high salt extraction, clarification by DEAE-Sepharose and cation exchange HPLC. Purified MdPGIP1 inhibited PGs from and PGs from two economically important pathogens of apple trees, and . It did not inhibit the PG, which was in contrast to the apple fruit extract used in this study. We conclude that there are at least two active PGIPs expressed in apple, which differ in their charge properties and ability to inhibit PG.
    Keywords: Apple ; Aspergillus Niger ; Botryosphaeria Obtusa ; Colletotrichum Lupini ; Diaporthe Ambigua ; Malus Domestica ; Nicotiana Tabacum ; Polygalacturonase ; Pgip ; Botany
    ISSN: 0031-9422
    E-ISSN: 1873-3700
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  • 10
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 2009, Vol.106(10), pp.4012-4017
    Description: Synapse loss correlates with a cognitive decline in Alzheimer's disease (AD), but whether this is caused by fibrillar deposits known as senile plaques or soluble oligomeric forms of amyloid β (Aβ) is controversial. By using array tomography, a technique that combines ultrathin sectioning of tissue with immunofluorescence, allowing precise quantification of small structures, such as synapses, we have tested the hypothesis that oligomeric Aβ surrounding plaques contributes to synapse loss in a mouse model of AD. We find that senile plaques are surrounded by a halo of oligomeric Aβ. Analysis of 〉14,000 synapses (represented by PSD95-stained excitatory synapses) shows that there is a 60% loss of excitatory synapses in the halo of oligomeric Aβ surrounding plaques and that the density increases to reach almost control levels in volumes further than 50 μm from a plaque in an approximately linear fashion (linear regression, r² = 0.9; P 〈 0.0001). Further, in transgenic cortex, microdeposits of oligomeric Aβ associate with a subset of excitatory synapses, which are significantly smaller than those not in contact with oligomeric Aβ. The proportion of excitatory synapses associated with Aβ correlates with decreasing density (correlation, -0.588; P 〈 0.0001). These data show that senile plaques are a potential reservoir of oligomeric Aβ, which colocalizes with the postsynaptic density and is associated with spine collapse, reconciling the apparently competing schools of thought of "plaque" vs. "oligomeric Aβ" as the synaptotoxic species in the brain of AD patients. ; p. 4012-4017.
    Keywords: Tomography ; Cortex ; Patients ; Alzheimer Disease ; Animal Models ; Genetically Modified Organisms ; Synapse ; Fluorescent Antibody Technique ; Brain ; Amyloid ; Linear Models
    ISSN: 0027-8424
    Source: AGRIS (Food and Agriculture Organization of the United Nations)
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