Search Results - "Maris, Christophe"

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  1. 1

    The RNA recognition motif, a plastic RNA‐binding platform to regulate post‐transcriptional gene expression by Maris, Christophe, Dominguez, Cyril, Allain, Frédéric H.‐T.

    Published in The FEBS journal (01-05-2005)
    “…The RNA recognition motif (RRM), also known as RNA‐binding domain (RBD) or ribonucleoprotein domain (RNP) is one of the most abundant protein domains in…”
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    Journal Article
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    The Solution Structure of the ADAR2 dsRBM-RNA Complex Reveals a Sequence-Specific Readout of the Minor Groove by Stefl, Richard, Oberstrass, Florian C., Hood, Jennifer L., Jourdan, Muriel, Zimmermann, Michal, Skrisovska, Lenka, Maris, Christophe, Peng, Li, Hofr, Ctirad, Emeson, Ronald B., Allain, Frédéric H.-T.

    Published in Cell (15-10-2010)
    “…Sequence-dependent recognition of dsDNA-binding proteins is well understood, yet sequence-specific recognition of dsRNA by proteins remains largely unknown,…”
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    Evidence for cooperative tandem binding of hnRNP C RRMs in mRNA processing by Cieniková, Zuzana, Jayne, Sandrine, Damberger, Fred Franz, Allain, Frédéric Hai-Trieu, Maris, Christophe

    Published in RNA (Cambridge) (01-11-2015)
    “…The human hnRNP C is a ubiquitous cellular protein involved in mRNA maturation. Recently, we have shown that this protein specifically recognizes uridine (U)…”
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  5. 5

    The Signature of the Five-Stranded vRRM Fold Defined by Functional, Structural and Computational Analysis of the hnRNP L Protein by Blatter, Markus, Dunin-Horkawicz, Stanislaw, Grishina, Inna, Maris, Christophe, Thore, Stephane, Maier, Timm, Bindereif, Albrecht, Bujnicki, Janusz M., Allain, Frédéric H.-T.

    Published in Journal of molecular biology (25-09-2015)
    “…The RNA recognition motif (RRM) is the far most abundant RNA binding domain. In addition to the typical β1α1β2β3α2β4 fold, various sub-structural elements have…”
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  6. 6

    Automated and assisted RNA resonance assignment using NMR chemical shift statistics by Aeschbacher, Thomas, Schmidt, Elena, Blatter, Markus, Maris, Christophe, Duss, Olivier, Allain, Frédéric H-T, Güntert, Peter, Schubert, Mario

    Published in Nucleic acids research (01-10-2013)
    “…The three-dimensional structure determination of RNAs by NMR spectroscopy relies on chemical shift assignment, which still constitutes a bottleneck. In order…”
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    Ozone Quenching Properties of Isoprene and Its Antioxidant Role in Leaves by Loreto, Francesco, Michela Mannozzi, Christophe Maris, Pamela Nascetti, Ferranti, Francesco, Pasqualini, Stefania

    Published in Plant physiology (Bethesda) (01-07-2001)
    “…Isoprene is formed in and emitted by plants and the reason for this apparent carbon waste is still unclear. It has been proposed that isoprene stabilizes cell…”
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  8. 8

    Static headspace analysis of aliphatic amines in aqueous samples by Maris, Christophe, Laplanche, Alain, Morvan, Jean, Bloquel, Marianne

    Published in Journal of Chromatography A (18-06-1999)
    “…Static headspace preconcentration was developed for the gas chromatographic analysis of aliphatic amines in aqueous samples. A liquid–gas ratio of 1, an…”
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    Journal Article Conference Proceeding
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    A transient α-helix in the N-terminal RNA recognition motif of polypyrimidine tract binding protein senses RNA secondary structure by Maris, Christophe, Jayne, Sandrine, Damberger, Fred F, Beusch, Irene, Dorn, Georg, Ravindranathan, Sapna, Allain, Frédéric H-T

    Published in Nucleic acids research (07-05-2020)
    “…The polypyrimidine tract binding protein (PTB) is a multi-domain protein involved in alternative splicing, mRNA localization, stabilization, polyadenylation…”
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  10. 10

    Development of instrumentation for simultaneous analysis of total non-methane organic carbon and volatile organic compounds in ambient air by Maris, Christophe, Chung, Myeong Y., Lueb, Richard, Krischke, Udo, Meller, Richard, Fox, Matthew J., Paulson, Suzanne E.

    Published in Atmospheric environment (1994) (2003)
    “…Here we describe the development of a new instrument to measure the total airborne non-methane organic carbon concentration (TNMOC), and the ratio of this…”
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    Journal Article Conference Proceeding
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    N-terminal domain of polypyrimidine-tract binding protein is a dynamic folding platform for adaptive RNA recognition by Damberger, Fred F, Krepl, Miroslav, Arora, Rajika, Beusch, Irene, Maris, Christophe, Dorn, Georg, Šponer, Jiří, Ravindranathan, Sapna, Allain, Frédéric H-T

    Published in Nucleic acids research (23-09-2024)
    “…The N-terminal RNA recognition motif domain (RRM1) of polypyrimidine tract binding protein (PTB) forms an additional C-terminal helix α3, which docks to one…”
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  12. 12

    Structural basis of siRNA recognition by TRBP double‐stranded RNA binding domains by Masliah, Gregoire, Maris, Christophe, König, Sebastian LB, Yulikov, Maxim, Aeschimann, Florian, Malinowska, Anna L, Mabille, Julie, Weiler, Jan, Holla, Andrea, Hunziker, Juerg, Meisner‐Kober, Nicole, Schuler, Benjamin, Jeschke, Gunnar, Allain, Frederic H‐T

    Published in The EMBO journal (15-03-2018)
    “…The accurate cleavage of pre‐micro(mi)RNAs by Dicer and mi/siRNA guide strand selection are important steps in forming the RNA‐induced silencing complex…”
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    Structural and Mechanistic Insights into Poly(uridine) Tract Recognition by the hnRNP C RNA Recognition Motif by Cieniková, Zuzana, Damberger, Fred F, Hall, Jonathan, Allain, Frédéric H.-T, Maris, Christophe

    Published in Journal of the American Chemical Society (15-10-2014)
    “…HnRNP C is a ubiquitous RNA regulatory factor and the principal constituent of the nuclear hnRNP core particle. The protein contains one amino-terminal RNA…”
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  14. 14

    fast, efficient and sequence-independent method for flexible multiple segmental isotope labeling of RNA using ribozyme and RNase H cleavage by Duss, Olivier, Maris, Christophe, von Schroetter, Christine, Allain, Frédéric H.-T

    Published in Nucleic acids research (01-11-2010)
    “…Structural information on RNA, emerging more and more as a major regulator in gene expression, dramatically lags behind compared with information on proteins…”
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    Journal Article
  15. 15

    U1 snRNA Directly Interacts with Polypyrimidine Tract-Binding Protein during Splicing Repression by Sharma, Shalini, Maris, Christophe, Allain, Frédéric H.-T., Black, Douglas L.

    Published in Molecular cell (04-03-2011)
    “…Splicing of the c-src N1 exon is repressed by the polypyrimidine tract-binding protein (PTB or PTBP1). During exon repression, the U1 snRNP binds properly to…”
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    Molecular basis for temperature sensing by an RNA thermometer by Chowdhury, Saheli, Maris, Christophe, Allain, Frédéric H-T, Narberhaus, Franz

    Published in The EMBO journal (07-06-2006)
    “…Regulatory RNA elements, like riboswitches, respond to intracellular signals by three‐dimensional (3D) conformational changes. RNA thermometers employ a…”
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    Sugar-to-base correlation in nucleic acids with a 5D APSY-HCNCH or two 3D APSY-HCN experiments by Krähenbühl, Barbara, Hofmann, Daniela, Maris, Christophe, Wider, Gerhard

    Published in Journal of biomolecular NMR (01-02-2012)
    “…A five-dimensional (5D) APSY (automated projection spectroscopy) HCNCH experiment is presented, which allows unambiguous correlation of sugar to base nuclei in…”
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    The solution structure of the ADAR2 dsRBM-RNA complex reveals a sequence-specific read out of the RNA minor groove by Stefl, Richard, Oberstrass, Florian C., Hood, Jennifer L., Jourdan, Muriel, Zimmermann, Michal, Skrisovska, Lenka, Maris, Christophe, Peng, Li, Hofr, Ctirad, Emeson, Ronald B., Allain, Frédéric H.-T.

    Published in Cell (15-10-2010)
    “…Sequence-dependent recognition of dsDNA-binding proteins are well understood, yet sequence-specific recognition of dsRNA by proteins remains largely unknown,…”
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    Journal Article
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    NMR structure of the apoB mRNA stem-loop and its interaction with the C to U editing APOBEC1 complementary factor by Maris, Christophe, Masse, James, Chester, Ann, Navaratnam, Naveenan, Allain, Frédéric H-T

    Published in RNA (Cambridge) (01-02-2005)
    “…We have solved the NMR structure of the 31-nucleotide (nt) apoB mRNA stem-loop, a substrate of the cytidine deaminase APOBEC1. We found that the edited base…”
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