Search Results - (Author, Cooperation:J. M. Arnold)

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  1. 1
    J. A. Miller ; S. L. Ding ; S. M. Sunkin ; K. A. Smith ; L. Ng ; A. Szafer ; A. Ebbert ; Z. L. Riley ; J. J. Royall ; K. Aiona ; J. M. Arnold ; C. Bennet ; D. Bertagnolli ; K. Brouner ; S. Butler ; S. Caldejon ; A. Carey ; C. Cuhaciyan ; R. A. Dalley ; N. Dee ; T. A. Dolbeare ; B. A. Facer ; D. Feng ; T. P. Fliss ; G. Gee ; J. Goldy ; L. Gourley ; B. W. Gregor ; G. Gu ; R. E. Howard ; J. M. Jochim ; C. L. Kuan ; C. Lau ; C. K. Lee ; F. Lee ; T. A. Lemon ; P. Lesnar ; B. McMurray ; N. Mastan ; N. Mosqueda ; T. Naluai-Cecchini ; N. K. Ngo ; J. Nyhus ; A. Oldre ; E. Olson ; J. Parente ; P. D. Parker ; S. E. Parry ; A. Stevens ; M. Pletikos ; M. Reding ; K. Roll ; D. Sandman ; M. Sarreal ; S. Shapouri ; N. V. Shapovalova ; E. H. Shen ; N. Sjoquist ; C. R. Slaughterbeck ; M. Smith ; A. J. Sodt ; D. Williams ; L. Zollei ; B. Fischl ; M. B. Gerstein ; D. H. Geschwind ; I. A. Glass ; M. J. Hawrylycz ; R. F. Hevner ; H. Huang ; A. R. Jones ; J. A. Knowles ; P. Levitt ; J. W. Phillips ; N. Sestan ; P. Wohnoutka ; C. Dang ; A. Bernard ; J. G. Hohmann ; E. S. Lein
    Nature Publishing Group (NPG)
    Published 2014
    Staff View
    Publication Date:
    2014-04-04
    Publisher:
    Nature Publishing Group (NPG)
    Print ISSN:
    0028-0836
    Electronic ISSN:
    1476-4687
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Anatomy, Artistic ; Animals ; Atlases as Topic ; Brain/embryology/*metabolism ; Conserved Sequence/genetics ; Fetus/cytology/embryology/*metabolism ; Gene Expression Regulation, Developmental/*genetics ; Gene Regulatory Networks/genetics ; Humans ; Mice ; Neocortex/embryology/metabolism ; Species Specificity ; *Transcriptome
    Published by:
    http://www.nature.com/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    Publication Date:
    2018-04-04
    Publisher:
    National Academy of Sciences
    Print ISSN:
    0027-8424
    Electronic ISSN:
    1091-6490
    Topics:
    Biology
    Medicine
    Natural Sciences in General
    Published by:
    http://www.nasonline.org/

    Latest Papers from Table of Contents or Articles in Press
  3. 3
    Nouwen, Nico ; Driessen, Arnold J. M.

    Oxford, UK : Blackwell Science Ltd.
    Published 2002
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    The Escherichia coli preprotein translocase is composed of a ‘preprotein conducting channel’ domain that consists of the peripherally bound translocation ATPase SecA and the heterotrimeric SecYEG membrane protein complex. SecD, SecF, and YajC form another heterotrimeric complex that can associate with the SecYEG complex. YidC is an essential membrane protein that plays a role in the integration of newly synthesized membrane proteins, and has been shown to co-purify with SecYEG when all translocase components are overproduced. Here, we demonstrate that under conditions that YidC co-purifies with overproduced SecDFyajC it does not co-purify with overproduced SecYEG. Moreover, this interaction of YidC with the SecDFyajC complex is also found at chromosomal protein levels of SecD, SecF and YajC. Closer examination of the SecDFyajC–YidC complex showed that YidC binds to SecD and SecF, whereas YajC interacts only with SecF. As SecF and YajC have previously been shown to interact with SecY, we propose that these two proteins link the heterotetrameric SecDFyajC–YidC complex to the SecYEG complex.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.2002.02972.x

    Articles: DFG German National Licenses
  4. 4
    Scheffers, Dirk-Jan ; Driessen, Arnold J. M.

    Oxford, UK : Blackwell Science Ltd
    Published 2002
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    To understand the polymerization dynamics of FtsZ, a bacterial cell division protein similar to tubulin, insight is required into the nature of the nucleotide bound to the polymerized protein. In a previous study, we showed that the FtsZ polymers contain mostly GDP. A recent study challenged this result, suggesting that the polymerized FtsZ is in a GTP-bound state. Here, we show that, when radiolabelled [γ-32P]-GTP is used to polymerize FtsZ, GTP is hydrolysed instantaneously. The FtsZ polymer contains both GDP and the radiolabelled inorganic phosphate.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.2002.02828.x

    Articles: DFG German National Licenses
  5. 5
    Elferink, Marieke G. L. ; Albers, Sonja-V. ; Konings, Wil N. ; Driessen, Arnold J. M.

    Oxford, UK : Blackwell Science, Ltd
    Published 2001
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    The extreme thermoacidophilic archaeon Sulfolobus solfataricus grows optimally at 80°C and pH 3 and uses a variety of sugars as sole carbon and energy source. Glucose transport in this organism is mediated by a high-affinity binding protein-dependent ATP-binding cassette (ABC) transporter. Sugar-binding studies revealed the presence of four additional membrane-bound binding proteins for arabinose, cellobiose, maltose and trehalose. These glycosylated binding proteins are subunits of ABC transporters that fall into two distinct groups: (i) monosaccharide transporters that are homologous to the sugar transport family containing a single ATPase and a periplasmic-binding protein that is processed at an unusual site at its amino-terminus; (ii) di- and oligosaccharide transporters, which are homologous to the family of oligo/dipeptide transporters that contain two different ATPases, and a binding protein that is synthesized with a typical bacterial signal sequence. The latter family has not been implicated in sugar transport before. These data indicate that binding protein-dependent transport is the predominant mechanism of transport for sugars in S. solfataricus.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.2001.02336.x

    Articles: DFG German National Licenses
  6. 6
    Scheffers, Dirk-Jan ; Den Blaauwen, Tanneke ; Driessen, Arnold J. M.

    Oxford, UK : Blackwell Science Ltd
    Published 2000
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    FtsZ, a tubulin homologue, forms a cytokinetic ring at the site of cell division in prokaryotes. The ring is thought to consist of polymers that assemble in a strictly GTP-dependent way. GTP, but not guanosine-5′-O-(3-thiotriphosphate) (GTP-γ-S), has been shown to induce polymerization of FtsZ, whereas in vitro Ca2+ is known to inhibit the GTP hydrolysis activity of FtsZ. We have studied FtsZ dynamics at limiting GTP concentrations in the presence of 10 mM Ca2+. GTP and its non-hydrolysable analogue GTP-γ-S bind FtsZ with similar affinity, whereas the non-hydrolysable analogue guanylyl-imidodiphosphate (GMP-PNP) is a poor substrate. Preformed FtsZ polymers can be stabilized by GTP-γ-S and are destabilized by GDP. As more than 95% of the nucleotide associated with the FtsZ polymer is in the GDP form, it is concluded that GTP hydrolysis by itself does not trigger FtsZ polymer disassembly. Strikingly, GTP-γ-S exchanges only a small portion of the FtsZ polymer-bound GDP. These data suggest that FtsZ polymers are stabilized by a small fraction of GTP-containing FtsZ subunits. These subunits may be located either throughout the polymer or at the polymer ends, forming a GTP cap similar to tubulin.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.2000.01791.x

    Articles: DFG German National Licenses
  7. 7
    Manting, Erik H. ; Driessen, Arnold J. M.

    Oxford, UK : Blackwell Science Ltd
    Published 2000
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    Protein translocation across the bacterial cytoplasmic membrane has been studied extensively in Escherichia coli. The identification of the components involved and subsequent reconstitution of the purified translocation reaction have defined the minimal constituents that allowed extensive biochemical characterization of the so-called translocase. This functional enzyme complex consists of the SecYEG integral membrane protein complex and a peripherally bound ATPase, SecA. Under translocation conditions, four SecYEG heterotrimers assemble into one large protein complex, forming a putative protein-conducting channel. This tetrameric arrangement of SecYEG complexes and the highly dynamic SecA dimer together form a proton-motive force- and ATP-driven molecular machine that drives the stepwise translocation of targeted polypeptides across the cytoplasmic membrane. Recent findings concerning the translocase structure and mechanism of protein translocation are discussed and shine new light on controversies in the field.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.2000.01980.x

    Articles: DFG German National Licenses
  8. 8
    Driessen, Arnold J. M. ; Jacobs, Mariken H. J. ; Konings, Wil N.

    Oxford UK : Blackwell Science Ltd
    Published 1997
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.1997.4071742.x

    Articles: DFG German National Licenses
  9. 9
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    SecA is the dissociable ATPase subunit of the Escherichia coli preprotein translocase, and cycles in a nucleotide-modulated manner between the cytosol and the membrane. Overproduction of the integral subunits of the translocase,the SecY, SecE and SecG polypeptides, results in an increased level of membrane-bound SecA. This fraction of SecA is firmly associated with the membrane as it is resistant to extraction with the chaotropic agent urea, and appears to be anchored by SecYEG rather than by lipids. Topology analysis of this membrane-associated form of SecA indicates that it exposes a carboxy-terminal domain to the periplasmic face of the membrane.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.1996.d01-1712.x

    Articles: DFG German National Licenses
  10. 10
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    In Escherichia coli, precursor proteins are targeted to the membrane-bound translocase by the cytosolic chaperone SecB. SecB binds to the extreme carboxy-terminus of the SecA ATPase translocase subunit, and this interaction is promoted by preproteins. The mutant SecB proteins, L75Q and E77K, which interfere with preprotein translocation in vivo, are unable to stimulate in vitro translocation. Both mutants bind proOmpA but fail to support the SecA-dependent membrane binding of proOmpA because of a marked reduction in their binding affinities for SecA. The stimulatory effect of preproteins on the interaction between SecB and SecA exclusively involves the signal sequence domain of the preprotein, as it can be mimicked by a synthetic signal peptide and is not observed with a mutant preprotein (Δ8proOmpA) bearing a non-functional signal sequence. Δ8proOmpA is not translocated across wild-type membranes, but the translocation defect is suppressed in inner membrane vesicles derived from a prlA4 strain. SecB reduces the translocation of Δ8proOmpA into these vesicles and almost completely prevents translocation when, in addition, the SecB binding site on SecA is removed. These data demonstrate that efficient targeting of preproteins by SecB requires both a functional signal sequence and a SecB binding domain on SecA. It is concluded that the SecB–SecA interaction is needed to dissociate the mature preprotein domain from SecB and that binding of the signal sequence domain to SecA is required to ensure efficient transfer of the preprotein to the translocase.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.1998.00997.x

    Articles: DFG German National Licenses
  11. 11
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.1998.01001.x

    Articles: DFG German National Licenses
  12. 12
    Rowe, John J. ; Ubbink-Kok, Trees ; Molenaar, Douwe ; Konings, Wil N. ; Driessen, Arnold J. M.

    Oxford, UK : Blackwell Publishing Ltd
    Published 1994
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Notes:
    Escherichia coli can use nitrate as a terminal electron acceptor for anaerobic respiration. A polytopic membrane protein, termed NarK, has been implicated in nitrate uptake and nitrite excretion and is thought to function as a nitrate/nitrite antiporter. The longest-lived radioactive isotope of nitrogen, 13N-nitrate (half-life = 9.96 min) and the nitrite-sensitive fluorophore N-(ethoxycarbonylmethyl)-6-methoxyquinolinium bromide have now been used to define the function of NarK. At low concentrations of nitrate, NarK mediates the electrogenic excretion of nitrite rather than nitrate/nitrite exchange. This process prevents intracellular accumulation of toxic levels of nitrite and allows further detoxification in the periplasm through the action of nitrite reductase.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1111/j.1365-2958.1994.tb01044.x

    Articles: DFG German National Licenses
  13. 13
    Albers, Sonja-Verena ; Konings, Wil N. ; Driessen, Arnold J. M.

    Oxford BSL : Blackwell Science Ltd
    Published 1999
    Staff View
    ISSN:
    1365-2958
    Source:
    Blackwell Publishing Journal Backfiles 1879-2005
    Topics:
    Biology
    Medicine
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1046/j.1365-2958.1999.01286.x

    Articles: DFG German National Licenses
  14. 14
    Driessen, Arnold J. M.

    [s.l.] : Nature Publishing Group
    Published 2005
    Staff View
    ISSN:
    1476-4687
    Source:
    Nature Archives 1869 - 2009
    Topics:
    Biology
    Chemistry and Pharmacology
    Medicine
    Natural Sciences in General
    Physics
    Notes:
    [Auszug] A cell's membrane bristles with proteins that sense and communicate with its environment, and the cell secretes other proteins to send messages farther afield. To reach their destination, these proteins must travel from the aqueous environment of the cytoplasm where they are synthesized, through ...
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1038/438299a

    Articles: DFG German National Licenses
  15. 15
    Hutchings, D. C. ; Arnold, J. M. ; Aitchison, J. S.
    Springer
    Published 1998
    Staff View
    ISSN:
    1572-817X
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Electrical Engineering, Measurement and Control Technology
    Physics
    Notes:
    Abstract Polarization dynamics are considered in the presence of an anisotropic Kerr non-linearity in the most common semiconductor waveguide geometry. The equations of motion are formulated in terms of Stokes polarization parameters and their Hamiltonian form is derived. Stationary solutions and their stability are found for plane-wave propagation. It is found that the non-integrable problem of mixed-polarization spatial soliton dynamics can be largely explained in terms of the equivalent plane-wave solutions.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1023/A:1006933214770

    Articles: DFG German National Licenses
  16. 16
    Crone, G. A. E. ; Arnold, J. M.
    Springer
    Published 1980
    Staff View
    ISSN:
    1572-817X
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Electrical Engineering, Measurement and Control Technology
    Physics
    Notes:
    Abstract It is shown, by means of computation on a specific model, how pulse broadening in multimode gradedindex optical waveguides is significantly affected by the levels of excitation of the high-order modes. Pulse widths are computed as functions of the profile parameterα, under conditions of equal excitation, high-order mode suppression and GaAs laser excitation.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00619924

    Articles: DFG German National Licenses
  17. 17
    Arnold, J. M.
    Springer
    Published 1998
    Staff View
    ISSN:
    1572-817X
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Electrical Engineering, Measurement and Control Technology
    Physics
    Notes:
    Abstract A summary is presented of the principal types of completely integrable partial differential equations having soliton solutions. Each type is derived from an appropriate physical model of an electromagnetic wave problem, with the intention to show how known mathematical results apply to a coherent class of physical problems in electromagnetic waves. The non-linear Schrödinger (NS) equation appears when the induced non-linear dielectric polarization is expanded in a series of powers of the electric field, only the linear and third-order polarizations are retained, and the temporal spectrum of the wave is a narrow band far removed from any resonance of the medium. The sine-Gordon equation appears from a similar optical model of propagation in a dielectric consisting of identical 2-level atomic systems, but resonance occurs between the carrier frequency of the wave and the transition frequency of the atoms. The Boussinesq and Korteweg– de Vries equations appear at different levels of approximation to a potential wave on a transmission line having a non-linear capacitance such that the charge stored is a non-linear function of the line potential. In all cases the evolution variable is the propagation distance; the transverse variable is time, but in the case of the NS equation it may alternatively be a spatial coordinate, giving rise to the possibility of spatial solitons as well as temporal solitons for NS-type problems. Two examples are derived of non-integrable Hamiltonian systems having spatial solitary waves, namely the second-order cascade interaction and vector spatial solitary waves of the third-order interaction, and a brief survey of the analytical solutions for the plane waves and solitary waves of these two types is presented. Finally, the addition of a second spatial dimension to the non-linear transmission line problem leads to the Kadomtsev–Petviashvili equations, and a further approximation for weakly modulated travelling waves leads to the Davey–Stewartson equations. Both of these completely integrable systems support combined spatial–temporal solitons.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1023/A:1006998418231

    Articles: DFG German National Licenses
  18. 18
    Staff View
    ISSN:
    1433-4909
    Keywords:
    Key wordsPicrophilus oshimae ; Cytoplasmic membrane ; Permeability ; Solute transport
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract Picrophilus oshimae is an extremely acidophilic, thermophilic archaeon that grows optimally at 60°C and at pH 0.7. It is an obligatory acidophile that does not grow at pH values above 4.0. The proton motive force in respiring cells is composed of a large transmembrane pH gradient, inside less acid, and a reversed transmembrane electrical potential, inside positive. Cells maintain an intracellular pH at around 4.6 at extracellular pH values ranging from 0.8 to 4.0. Above pH 4.0 cells lyse rapidly and lose their viability. Liposomes prepared from lipids derived from P. oshimae have an extremely low proton permeability at acidic pH. However, at neutral pH, the lipids are unable to assemble into regular liposomal structures. These observations suggest that the loss of viability and cell integrity above pH 4.0 is due to an impairment of the barrier function of the cytoplasmic membrane.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s007920050044

    Articles: DFG German National Licenses
  19. 19
    Driessen, Arnold J. M.
    Springer
    Published 1989
    Staff View
    ISSN:
    1572-9699
    Keywords:
    amino acids ; Lactococcus lactis ; membrane fusion ; phospholipids ; protonmotive force ; solute transport
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract Lactococci are fastidious bacteria which require an external source of amino acids and many other nutrients. These compounds have to pass the membrane. However, detailed analysis of transport processes in membrane vesicles has been hampered by the lack of a suitable protonmotive force (pmf)-generating system in these model systems. A membrane-fusion procedure has been developed by which pmf-generating systems can be functionally incorporated into the bacterial membrane. This improved model system has been used to analyze the properties of amino acid transport systems in lactococci. Detailed studies have been made of the specificity and kinetics of amino acid transport and also of the interaction of the transport systems with their lipid environment. The properties of a pmf-independent, arginine-catabolism specific transport system in lactococci will be discussed.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/BF00399978

    Articles: DFG German National Licenses
  20. 20
    Staff View
    ISSN:
    1432-041X
    Keywords:
    Key words Ascidian ; Serine protease ; Differential display ; Gene expression ; In situ hybridization
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Notes:
    Abstract  We have studied gene expression during ascidian embryonic development using the technique of differential display and isolated partial cDNA sequences of 12 genes. Developmental regulation of these genes has been confirmed by northern hybridization analysis. Further cDNA cloning and sequence analysis of an mRNA that is present during gastrulation, neurulation and tailbud formation reveals that it encodes a novel serine protease containing a single kringle motif and catalytic domain. The spatial expression of this gene, designated Hmserp1, is restricted to precursor cells of the epidermis. The structure and expression of Hmserp1 is discussed in relation to possible functions during development.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/s004270050075

    Articles: DFG German National Licenses