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  • 1
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    Carrier-Wave Rabi-Flopping Signatures in High-Order Harmonic Generation for Alkali Atoms (2015)
    American Physical Society (APS)
    Details
    Publication Date: 2015-04-09
    Description: Author(s): M. F. Ciappina, J. A. Pérez-Hernández, A. S. Landsman, T. Zimmermann, M. Lewenstein, L. Roso, and F. Krausz We present a theoretical investigation of carrier-wave Rabi flopping in real atoms by employing numerical simulations of high-order harmonic generation (HHG) in alkali species. Given the short HHG cutoff, related to the low saturation intensity, we concentrate on the features of the third harmonic o... [Phys. Rev. Lett. 114, 143902] Published Wed Apr 08, 2015
    Keywords: Nonlinear Dynamics, Fluid Dynamics, Classical Optics, etc.
    Print ISSN: 0031-9007
    Electronic ISSN: 1079-7114
    Topics: Physics
    Published by American Physical Society (APS)
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  • 2
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    Anisotropic emission in quantum-beat spectroscopy of helium excited states (2015)
    American Physical Society (APS)
    Details
    Publication Date: 2015-06-11
    Description: Author(s): M. Lucchini, A. Ludwig, T. Zimmermann, L. Kasmi, J. Herrmann, A. Scrinzi, A. S. Landsman, L. Gallmann, and U. Keller We present quantum-beat spectroscopy of excited states of helium atoms populated selectively with high-order-harmonic emission below the atomic ionization potential by means of low-pass filtering of the pump radiation. The created electron wave packet is ionized by few-cycle infrared (IR) pulses lea... [Phys. Rev. A 91, 063406] Published Wed Jun 10, 2015
    Keywords: Atomic and molecular processes in external fields, including interactions with strong fields and short pulses
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 3
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    Combining Statistical Potentials with Dynamics-Based Entropies Improves Selection from Protein Decoys and Docking Poses (2012)
    American Chemical Society (ACS)
    Details
    Publication Date: 2012-04-24
    Description: The Journal of Physical Chemistry B DOI: 10.1021/jp2120143
    Electronic ISSN: 1520-5207
    Topics: Chemistry and Pharmacology , Physics
    Published by American Chemical Society (ACS)
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  • 4
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    Clinical Proteome Informatics Workbench Detects Pathogenic Mutations in Hereditary Amyloidoses (2014)
    American Chemical Society (ACS)
    Details
    Publication Date: 2014-04-04
    Description: Journal of Proteome Research DOI: 10.1021/pr4011475
    Print ISSN: 1535-3893
    Electronic ISSN: 1535-3907
    Topics: Chemistry and Pharmacology
    Published by American Chemical Society (ACS)
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  • 5
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    Interpreting electron-momentum distributions and nonadiabaticity in strong-field ionization (2014)
    American Physical Society (APS)
    Details
    Publication Date: 2014-10-09
    Description: Author(s): C. Hofmann, A. S. Landsman, A. Zielinski, C. Cirelli, T. Zimmermann, A. Scrinzi, and U. Keller We investigate whether nonadiabatic effects, rather than an initial longitudinal momentum spread, can explain the additional final momentum spread measured in strong-field ionization experiments with ultrafast laser pulses. We find that, when used consistently, a well-known nonadiabatic theory which... [Phys. Rev. A 90, 043406] Published Wed Oct 08, 2014
    Keywords: Atomic and molecular processes in external fields, including interactions with strong fields and short pulses
    Print ISSN: 1050-2947
    Electronic ISSN: 1094-1622
    Topics: Physics
    Published by American Physical Society (APS)
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  • 6
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    Crystal structures of the CusA efflux pump suggest methionine-mediated metal transport (2010)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2010-09-25
    Description: Gram-negative bacteria, such as Escherichia coli, frequently use tripartite efflux complexes in the resistance-nodulation-cell division (RND) family to expel various toxic compounds from the cell. The efflux system CusCBA is responsible for extruding biocidal Cu(I) and Ag(I) ions. No previous structural information was available for the heavy-metal efflux (HME) subfamily of the RND efflux pumps. Here we describe the crystal structures of the inner-membrane transporter CusA in the absence and presence of bound Cu(I) or Ag(I). These CusA structures provide new structural information about the HME subfamily of RND efflux pumps. The structures suggest that the metal-binding sites, formed by a three-methionine cluster, are located within the cleft region of the periplasmic domain. This cleft is closed in the apo-CusA form but open in the CusA-Cu(I) and CusA-Ag(I) structures, which directly suggests a plausible pathway for ion export. Binding of Cu(I) and Ag(I) triggers significant conformational changes in both the periplasmic and transmembrane domains. The crystal structure indicates that CusA has, in addition to the three-methionine metal-binding site, four methionine pairs-three located in the transmembrane region and one in the periplasmic domain. Genetic analysis and transport assays suggest that CusA is capable of actively picking up metal ions from the cytosol, using these methionine pairs or clusters to bind and export metal ions. These structures suggest a stepwise shuttle mechanism for transport between these sites.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2946090/" 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/PMC2946090/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Long, Feng -- Su, Chih-Chia -- Zimmermann, Michael T -- Boyken, Scott E -- Rajashankar, Kanagalaghatta R -- Jernigan, Robert L -- Yu, Edward W -- GM 072014/GM/NIGMS NIH HHS/ -- GM 074027/GM/NIGMS NIH HHS/ -- GM 081680/GM/NIGMS NIH HHS/ -- GM 086431/GM/NIGMS NIH HHS/ -- R01 GM072014/GM/NIGMS NIH HHS/ -- R01 GM074027/GM/NIGMS NIH HHS/ -- R01 GM074027-05/GM/NIGMS NIH HHS/ -- R01 GM086431/GM/NIGMS NIH HHS/ -- R01 GM086431-01A2/GM/NIGMS NIH HHS/ -- RR-15301/RR/NCRR NIH HHS/ -- England -- Nature. 2010 Sep 23;467(7314):484-8. doi: 10.1038/nature09395.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular, Cellular and Developmental Biology Interdepartmental Graduate Program, Iowa State University, Iowa 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20865003" target="_blank"〉PubMed〈/a〉
    Keywords: Apoproteins/chemistry/metabolism ; Binding Sites ; Cell Membrane/metabolism ; Copper/chemistry/*metabolism ; Crystallography, X-Ray ; Cytosol/metabolism ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/*metabolism ; Ion Transport ; Membrane Transport Proteins/*chemistry/*metabolism ; Methionine/*metabolism ; Models, Biological ; Models, Molecular ; Periplasm/metabolism ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Silver/chemistry/*metabolism ; Structure-Activity Relationship
    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
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    Crystal structure of the CusBA heavy-metal efflux complex of Escherichia coli (2011)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2011-02-26
    Description: Gram-negative bacteria, such as Escherichia coli, expel toxic chemicals through tripartite efflux pumps that span both the inner and outer membrane. The three parts are an inner membrane, substrate-binding transporter; a membrane fusion protein; and an outer-membrane-anchored channel. The fusion protein connects the transporter to the channel within the periplasmic space. A crystallographic model of this tripartite efflux complex has been unavailable because co-crystallization of the various components of the system has proven to be extremely difficult. We previously described the crystal structures of both the inner membrane transporter CusA and the membrane fusion protein CusB of the CusCBA efflux system of E. coli. Here we report the co-crystal structure of the CusBA efflux complex, showing that the transporter (or pump) CusA, which is present as a trimer, interacts with six CusB protomers and that the periplasmic domain of CusA is involved in these interactions. The six CusB molecules seem to form a continuous channel. The affinity of the CusA and CusB interaction was found to be in the micromolar range. Finally, we have predicted a three-dimensional structure for the trimeric CusC outer membrane channel and developed a model of the tripartite efflux assemblage. This CusC(3)-CusB(6)-CusA(3) model shows a 750-kilodalton efflux complex that spans the entire bacterial cell envelope and exports Cu I and Ag I ions.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3078058/" 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/PMC3078058/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Su, Chih-Chia -- Long, Feng -- Zimmermann, Michael T -- Rajashankar, Kanagalaghatta R -- Jernigan, Robert L -- Yu, Edward W -- R01 GM072014/GM/NIGMS NIH HHS/ -- R01 GM074027/GM/NIGMS NIH HHS/ -- R01 GM074027-05/GM/NIGMS NIH HHS/ -- R01 GM086431/GM/NIGMS NIH HHS/ -- R01 GM086431-01A2/GM/NIGMS NIH HHS/ -- R01GM072014/GM/NIGMS NIH HHS/ -- R01GM074027/GM/NIGMS NIH HHS/ -- R01GM081680/GM/NIGMS NIH HHS/ -- R01GM086431/GM/NIGMS NIH HHS/ -- RR-15301/RR/NCRR NIH HHS/ -- England -- Nature. 2011 Feb 24;470(7335):558-62. doi: 10.1038/nature09743.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Iowa State University, Ames, Iowa 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21350490" target="_blank"〉PubMed〈/a〉
    Keywords: Copper/metabolism ; Crystallization ; Crystallography, X-Ray ; Escherichia coli/*chemistry ; Escherichia coli Proteins/*chemistry/metabolism ; Membrane Transport Proteins/*chemistry/metabolism ; Metals, Heavy/*metabolism ; Models, Molecular ; Multiprotein Complexes/*chemistry/metabolism ; Protein Binding ; Protein Multimerization ; Protein Structure, Quaternary ; Protein Structure, Tertiary ; Silver/metabolism ; Static Electricity
    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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  • 8
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    Wnt induces LRP6 signalosomes and promotes dishevelled-dependent LRP6 phosphorylation (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-06-16
    Description: Multiple signaling pathways, including Wnt signaling, participate in animal development, stem cell biology, and human cancer. Although many components of the Wnt pathway have been identified, unresolved questions remain as to the mechanism by which Wnt binding to its receptors Frizzled and Low-density lipoprotein receptor-related protein 6 (LRP6) triggers downstream signaling events. With live imaging of vertebrate cells, we show that Wnt treatment quickly induces plasma membrane-associated LRP6 aggregates. LRP6 aggregates are phosphorylated and can be detergent-solubilized as ribosome-sized multiprotein complexes. Phospho-LRP6 aggregates contain Wnt-pathway components but no common vesicular traffic markers except caveolin. The scaffold protein Dishevelled (Dvl) is required for LRP6 phosphorylation and aggregation. We propose that Wnts induce coclustering of receptors and Dvl in LRP6-signalosomes, which in turn triggers LRP6 phosphorylation to promote Axin recruitment and beta-catenin stabilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bilic, Josipa -- Huang, Ya-Lin -- Davidson, Gary -- Zimmermann, Timo -- Cruciat, Cristina-Maria -- Bienz, Mariann -- Niehrs, Christof -- MC_U105192713/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2007 Jun 15;316(5831):1619-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Embryology, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17569865" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*metabolism ; Animals ; Axin Protein ; Cell Line ; Cell Line, Tumor ; Cell Membrane/metabolism ; Centrifugation, Density Gradient ; Cytoplasm/metabolism ; Drosophila ; Glycogen Synthase Kinase 3/analysis/metabolism ; HeLa Cells ; Humans ; LDL-Receptor Related Proteins/analysis/genetics/*metabolism ; Low Density Lipoprotein Receptor-Related Protein-6 ; Mice ; Models, Biological ; Phosphoproteins/*metabolism ; Phosphorylation ; Repressor Proteins/analysis/metabolism ; *Signal Transduction ; Transfection ; Wnt Proteins/*metabolism ; Wnt3 Protein ; beta Catenin/metabolism
    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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  • 9
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    Diabetic liver injury from streptozotocin is regulated through the caspase-8 homolog cFLIP involving activation of JNK2 and intrahepatic immunocompetent cells (2013)
    Springer Nature
    Details
    Publication Date: 2013-07-05
    Description: Diabetic liver injury from streptozotocin is regulated through the caspase-8 homolog cFLIP involving activation of JNK2 and intrahepatic immunocompetent cells Cell Death and Disease 4, e712 (July 2013). doi:10.1038/cddis.2013.228 Authors: T Kohl, N Gehrke, A Schad, M Nagel, M A Wörns, M F Sprinzl, T Zimmermann, Y-W He, P R Galle, M Schuchmann & J M Schattenberg
    Keywords: apoptosisliver injuryJNK2hyperglycemiacFLIP
    Electronic ISSN: 2041-4889
    Topics: Biology , Medicine
    Published by Springer Nature
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  • 10
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    Entropy, Vol. 14, Pages 687-700: Protein Loop Dynamics Are Complex and Depend on the Motions of the Whole Protein (2012)
    MDPI Publishing
    In: Entropy
    Details
    Publication Date: 2012-08-11
    Description: We investigate the relationship between the motions of the same peptide loop segment incorporated within a protein structure and motions of free or end-constrained peptides. As a reference point we also compare against alanine chains having the same length as the loop. Both the analysis of atomic molecular dynamics trajectories and structure-based elastic network models, reveal no general dependence on loop length or on the number of solvent exposed residues. Rather, the whole structure affects the motions in complex ways that depend strongly and specifically on the tertiary structure of the whole protein. Both the Elastic Network Models and Molecular Dynamics confirm the differences in loop dynamics between the free and structured contexts; there is strong agreement between the behaviors observed from molecular dynamics and the elastic network models. There is no apparent simple relationship between loop mobility and its size, exposure, or position within a loop. Free peptides do not behave the same as the loops in the proteins. Surface loops do not behave as if they were random coils, and the tertiary structure has a critical influence upon the apparent motions. This strongly implies that entropy evaluation of protein loops requires knowledge of the motions of the entire protein structure.
    Electronic ISSN: 1099-4300
    Topics: Chemistry and Pharmacology , Physics
    Published by MDPI Publishing
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