Institution
Martin Luther University of Halle-Wittenberg
Education•Halle, Germany•
About: Martin Luther University of Halle-Wittenberg is a education organization based out in Halle, Germany. It is known for research contribution in the topics: Population & Liquid crystal. The organization has 20232 authors who have published 38773 publications receiving 965004 citations. The organization is also known as: MLU & University of Wittenberg.
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TL;DR: CueO from Escherichia coli has a robust cuprous oxidase activity, severalfold higher than any homologue, and data suggest that a functional role for CueO in protecting against copper toxicity in vivo includes the removal of Cu(I).
Abstract: We have found CueO from Escherichia coli to have a robust cuprous oxidase activity, severalfold higher than any homologue. These data suggest that a functional role for CueO in protecting against copper toxicity in vivo includes the removal of Cu(I).
190 citations
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TL;DR: The data support the model in which the AvrBs3 effector localizes to the nucleus, where the Bs3-mediated surveillance system of resistant plants detects AvRBs3 through its interference with host gene transcription.
Abstract: The AvrBs3 protein of the phytopathogenic bacterium Xanthomonas campestris pv. vesicatoria is targeted to host-plant cells by the bacterial Hrp type III secretion system. In pepper plants containing the Bs3 resistance gene, AvrBs3 induces the hypersensitive response (HR). AvrBs3 recognition is thought to occur in the plant cell nucleus as HR induction is dependent on nuclear localization signals (NLSs) and an acidic transcription activation domain (AAD). In a search for AvrBs3-interacting pepper proteins using the yeast two-hybrid system, we have isolated eight different classes of cDNA inserts including two genes for importin alpha proteins. Importin alpha is part of the nuclear import machinery and interacts with AvrBs3 through an NLS in the carboxy-terminus of the protein, both in yeast and in vitro. The mechanism of AvrBs3 recognition was further studied by analysis of the C-terminal AAD. This putative transcription-activation domain was shown to be required for AvrBs3 HR-inducing activity, and could be functionally replaced with the VP16 AAD from the Herpes simplex virus. Our data support the model in which the AvrBs3 effector localizes to the nucleus, where the Bs3-mediated surveillance system of resistant plants detects AvrBs3 through its interference with host gene transcription.
189 citations
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TL;DR: A diverse set of suramin analogues were tested to elucidate the inhibition of the NAD+‐dependent histone deacetylases SIRT1 and SIRT2 and selective inhibitors of human sirtuins with potency in the two‐digit nanomolar range were discovered.
Abstract: Suramin is a symmetric polyanionic naphthylurea originally used for the treatment of trypanosomiasis and onchocerciasis. Suramin and diverse analogues exhibit a broad range of biological actions in vitro and in vivo, including, among others, antiproliferative and antiviral activity. Suramin derivatives usually target purinergic binding sites. Class III histone deacetylases (sirtuins) are amidohydrolases that require nicotinamide adenine dinucleotide (NAD(+)) as a cofactor for their catalytic mechanism(.) Deacetylation of the target proteins leads to a change in conformation and alters the activity of the proteins in question. Suramin was reported to inhibit human sirtuin 1 (SIRT1). We tested a diverse set of suramin analogues to elucidate the inhibition of the NAD(+)-dependent histone deacetylases SIRT1 and SIRT2 and discovered selective inhibitors of human sirtuins with potency in the two-digit nanomolar range. In addition, the structural requirements for the binding of suramin derivatives to sirtuins were investigated by molecular docking. The recently published X-ray crystal structure of human SIRT5 in complex with suramin and the human SIRT2 structure were used to analyze the interaction mode of the novel suramin derivatives.
189 citations
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189 citations
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TL;DR: Dual avirulence and virulence functions in tomato and bean, respectively, were identified in virPphA homologues but only avrPtoB strongly enhanced virulence to Arabidopsis, overcoming basal defences operating against RW60.
Abstract: The virulence and avirulence activities of members of the Pseudomonas syringae HopAB family of effectors and AvrPto were examined in bean, tomato and Arabidopsis. Proteins were delivered by the RW60 strain of P. syringae pv. phaseolicola. RW60 causes a hypersensitive reaction (HR) in bean and tomato but is restricted without the HR in Arabidopsis. Dual avirulence and virulence functions in tomato and bean, respectively, were identified in virPphA homologues but only avrPtoB strongly enhanced virulence to Arabidopsis, overcoming basal defences operating against RW60. Virulence activity in both bean and Arabidopsis required regions of the C-terminus of the AvrPtoB protein, whereas elicitation of the rapid HR in tomato, with the matching Pto resistance gene, did not. The effect of AvrPtoB on Arabidopsis was accession-specific; most obvious in Wassilewskija (Ws-3), intermediate in Columbia and not detectable in Niedersenz (Nd-1) after inoculation with RW60 + avrPtoB. Analysis of crosses between Ws-3 and Nd-1 indicated co-segregation for the AvrPtoB virulence function with the absence of the Nd-1 FLS2 gene which mediates recognition of bacterial flagellin. In planta expression of AvrPtoB did not prevent the HR activated by P. syringae pv. tomato DC3000 + avrB, avrRpm1, avrRps4 or avrRpt2, but suppressed cell wall alterations, including callose deposition, characteristic of basal defence and was associated with reprogramming of the plant's transcriptional response. The success or failure of AvrPtoB in suppressing basal defences in Nd-1 depended on the timing of exposure of plant cells to the effector and the flagellin flg22 peptide.
189 citations
Authors
Showing all 20466 results
Name | H-index | Papers | Citations |
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Niels Birbaumer | 142 | 835 | 77853 |
Michael Schmitt | 134 | 2007 | 114667 |
Niels E. Skakkebæk | 127 | 596 | 59925 |
Stefan D. Anker | 117 | 415 | 104945 |
Pedro W. Crous | 115 | 809 | 51925 |
Eric Verdin | 115 | 370 | 47971 |
Bernd Nilius | 112 | 496 | 44812 |
Josep Tabernero | 111 | 803 | 68982 |
Hans-Dieter Volk | 107 | 784 | 46622 |
Dan Rujescu | 106 | 552 | 60406 |
John I. Nurnberger | 105 | 522 | 51402 |
Ulrich Gösele | 102 | 603 | 46223 |
Wolfgang J. Parak | 102 | 469 | 43307 |
Martin F. Bachmann | 100 | 415 | 34124 |
Munir Pirmohamed | 97 | 675 | 39822 |