ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    facet.materialart.
    Unknown
    Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector (1999)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1999-09-18
    Description: The bacterial pathogen Yersinia uses a type III secretion system to inject several virulence factors into target cells. One of the Yersinia virulence factors, YopJ, was shown to bind directly to the superfamily of MAPK (mitogen-activated protein kinase) kinases (MKKs) blocking both phosphorylation and subsequent activation of the MKKs. These results explain the diverse activities of YopJ in inhibiting the extracellular signal-regulated kinase, c-Jun amino-terminal kinase, p38, and nuclear factor kappa B signaling pathways, preventing cytokine synthesis and promoting apoptosis. YopJ-related proteins that are found in a number of bacterial pathogens of animals and plants may function to block MKKs so that host signaling responses can be modulated upon infection.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orth, K -- Palmer, L E -- Bao, Z Q -- Stewart, S -- Rudolph, A E -- Bliska, J B -- Dixon, J E -- 18024/PHS HHS/ -- AI35175/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1999 Sep 17;285(5435):1920-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109-0606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10489373" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*physiology ; Calcium-Calmodulin-Dependent Protein Kinases/*antagonists & inhibitors ; Cell Line ; Enzyme Activation ; Enzyme Inhibitors/*pharmacology ; HeLa Cells ; Humans ; *MAP Kinase Kinase Kinase 1 ; NF-kappa B/metabolism ; Phosphorylation ; Protein Binding ; Protein-Serine-Threonine Kinases/genetics/metabolism ; Recombinant Fusion Proteins/genetics/metabolism ; Transfection ; Virulence ; Yersinia pseudotuberculosis/genetics/metabolism/pathogenicity/*physiology
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 2
    facet.materialart.
    Unknown
    Disruption of signaling by Yersinia effector YopJ, a ubiquitin-like protein protease (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-25
    Description: Homologs of the Yersinia virulence effector YopJ are found in both plant and animal bacterial pathogens, as well as plant symbionts. These YopJ family members were shown to act as cysteine proteases. The catalytic triad of the protease was required for inhibition of the mitogen-activated protein kinase (MAPK) and nuclear factor kappaB (NF-kappaB) signaling in animal cells and for induction of localized cell death in plants. The substrates for YopJ were shown to be highly conserved ubiquitin-like molecules, which are covalently added to numerous regulatory proteins. YopJ family members exert their pathogenic effect on cells by disrupting this posttranslational modification.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Orth, K -- Xu, Z -- Mudgett, M B -- Bao, Z Q -- Palmer, L E -- Bliska, J B -- Mangel, W F -- Staskawicz, B -- Dixon, J E -- 18024/PHS HHS/ -- AI41599/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1594-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109-0606, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090361" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/*chemistry/genetics/*metabolism ; Catalysis ; Catalytic Domain ; Cell Line ; Cysteine Endopeptidases/chemistry/genetics/*metabolism ; Humans ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Plant Leaves/cytology/virology ; SUMO-1 Protein ; Sequence Alignment ; Signal Transduction ; Transfection ; Ubiquitins/metabolism ; Virulence ; Xanthomonas campestris/enzymology/pathogenicity ; Yersinia pseudotuberculosis/enzymology/metabolism/*pathogenicity
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 3
    facet.materialart.
    Unknown
    Maize genome sequencing by methylation filtration (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-12-20
    Description: Gene enrichment strategies offer an alternative to sequencing large and repetitive genomes such as that of maize. We report the generation and analysis of nearly 100,000 undermethylated (or methylation filtration) maize sequences. Comparison with the rice genome reveals that methylation filtration results in a more comprehensive representation of maize genes than those that result from expressed sequence tags or transposon insertion sites sequences. About 7% of the repetitive DNA is unmethylated and thus selected in our libraries, but potentially active transposons and unmethylated organelle genomes can be identified. Reverse transcription polymerase chain reaction can be used to finish the maize transcriptome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palmer, Lance E -- Rabinowicz, Pablo D -- O'Shaughnessy, Andrew L -- Balija, Vivekanand S -- Nascimento, Lidia U -- Dike, Sujit -- de la Bastide, Melissa -- Martienssen, Robert A -- McCombie, W Richard -- 2 T32-CA09311-25/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Dec 19;302(5653):2115-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14684820" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Chromosomes, Artificial, Bacterial ; Cloning, Molecular ; Computational Biology ; Conserved Sequence ; Contig Mapping ; CpG Islands ; *DNA Methylation ; DNA Transposable Elements ; DNA, Chloroplast/genetics ; DNA, Complementary ; DNA, Mitochondrial/genetics ; DNA, Plant/genetics ; Databases, Nucleic Acid ; Escherichia coli/genetics ; Exons ; Expressed Sequence Tags ; Genes, Plant ; *Genome, Plant ; Genomic Library ; Oryza/genetics ; Repetitive Sequences, Nucleic Acid ; Retroelements ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, DNA/*methods ; Zea mays/*genetics
    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)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
  • 4
    facet.materialart.
    Unknown
    Note: Proof of principle of a new type of cluster beam source with potential for scale-up (2016)
    American Institute of Physics (AIP)
    Details
    Publication Date: 2016-04-21
    Description: We introduce a new type of cluster beam source based on the assembly of (metal) clusters within a condensed (rare gas) matrix. The “Matrix Assembly Cluster Source” employs an ion beam to enhance collisions between metal atoms in the matrix and to sputter out clusters to form a beam. We demonstrate the formation and deposition of gold and silver nanoclusters with mean size tunable from a few atoms to a few thousand atoms. The cluster flux is equivalent to a current nanoAmp regime but potentially scalable to milliAmps, which would open up a number of interesting experiments and applications.
    Print ISSN: 0034-6748
    Electronic ISSN: 1089-7623
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Published by American Institute of Physics (AIP)
    Location Call Number Expected Availability
    BibTip Others were also interested in ...
    PAPER CURRENT
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...