Search Results - "Raja, K. Muruga Poopathi"

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  1. 1

    Specific Inhibition of β-Secretase Processing of the Alzheimer Disease Amyloid Precursor Protein by Ben Halima, Saoussen, Mishra, Sabyashachi, Raja, KMuruga Poopathi, Willem, Michael, Baici, Antonio, Simons, Kai, Brüstle, Oliver, Koch, Philipp, Haass, Christian, Caflisch, Amedeo, Rajendran, Lawrence

    Published in Cell reports (Cambridge) (08-03-2016)
    “…Development of disease-modifying therapeutics is urgently needed for treating Alzheimer disease (AD). AD is characterized by toxic β-amyloid (Aβ) peptides…”
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  2. 2

    Polypeptide Helices in Hybrid Peptide Sequences by Ananda, Kuppanna, Vasudev, Prema G, Sengupta, Anindita, Poopathi Raja, K. Muruga, Shamala, Narayanaswamy, Balaram, Padmanabhan

    Published in Journal of the American Chemical Society (30-11-2005)
    “…A new class of polypeptide helices in hybrid sequences containing α-, β-, and γ-residues is described. The molecular conformations in crystals determined for…”
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  3. 3

    Engineering polypeptide folding through trans double bonds: transformation of miniature β-meanders to hybrid helices by Ganesh Kumar, Mothukuri, Benke, Sushil N, Poopathi Raja, K Muruga, Gopi, Hosahudya N

    “…Utilization of conjugated double bonds to engineer the novel folded miniature β-meander type structures, single step transformation of miniature β-meanders…”
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  4. 4

    Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of α,γ-Hybrid Peptide Foldamers by Ganesh Kumar, Mothukuri, Thombare, Varsha J., Katariya, Mona M., Veeresh, Kuruva, Raja, K. Muruga Poopathi, Gopi, Hosahudya N.

    Published in Angewandte Chemie International Edition (27-06-2016)
    “…The impact of geometrically constrained cis α,β‐unsaturated γ‐amino acids on the folding of α,γ‐hybrid peptides was investigated. Structure analysis in single…”
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  5. 5

    Modulating the Structural Properties of α,γ‐Hybrid Peptides by α‐Amino Acid Residues: Uniform 12‐Helix Versus “Mixed” 12/10‐Helix by Misra, Rajkumar, Raja, K. Muruga Poopathi, Hofmann, Hans‐Jörg, Gopi, Hosahudya N

    Published in Chemistry : a European journal (21-11-2017)
    “…The most important natural α‐ and 310‐helices are stabilized by unidirectional intramolecular hydrogen bonds along the helical cylinder. In contrast, we report…”
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  6. 6

    Structural Dimorphism of Achiral α,γ‐Hybrid Peptide Foldamers: Coexistence of 12‐ and 15/17‐Helices by Misra, Rajkumar, Saseendran, Abhijith, George, Gijo, Veeresh, Kuruva, Raja, K. Muruga Poopathi, Raghothama, Srinivasarao, Hofmann, Hans‐Jörg, Gopi, Hosahudya N.

    Published in Chemistry : a European journal (13-03-2017)
    “…Here, novel 12‐helices in α,γ‐hybrid peptides composed of achiral α‐aminoisobutyric acid (Aib) and 4‐aminoisocaproic acid (Aic, doubly homologated Aib)…”
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  7. 7

    Design of Stable β‑Hairpin Mimetics through Backbone Disulfide Bonds by Ganesh Kumar, Mothukuri, Mali, Sachitanand M, Raja, K. Muruga Poopathi, Gopi, Hosahudya N

    Published in Organic letters (16-01-2015)
    “…The synthesis and utilization of novel thiostatines (β-SH-substituted γ-amino acids) in the design of backbone-disulfide-stabilized β-hairpin mimetics,…”
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  8. 8

    Synthesis and Structural Investigations of Functionalizable Hybrid β-Hairpin by Bandyopadhyay, Anupam, Mali, Sachitanand M, Lunawat, Pooja, Raja, K. Muruga Poopathi, Gopi, Hosahudya N

    Published in Organic letters (02-09-2011)
    “…The solution and solid state conformations of a designed β-hairpin containing functionalizable α,β-unsaturated γ-amino acids at the antiparallel β-strands and…”
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  9. 9

    Structural studies of model peptides containing beta-, gamma- and delta-amino acids by Sengupta, Anindita, Aravinda, Subrayashastry, Shamala, Narayanaswamy, Raja, K Muruga Poopathi, Balaram, Padmanabhan

    Published in Organic & biomolecular chemistry (01-01-2006)
    “…The crystal structures of five model peptides Piv-Pro-Gly-NHMe (1), Piv-Pro-betaGly-NHMe (2), Piv-Pro-betaGly-OMe (3), Piv-Pro-deltaAva-OMe (4) and…”
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  10. 10

    Stereochemistry of gabapentin and several derivatives: Solid state conformations and solution equilibria by Ananda, K., Aravinda, S., Vasudev, Prema G., Raja, K. Muruga Poopathi, Sivaramakrishnan, H., Nagarajan, K., Shamala, N., Balaram, P.

    Published in Current science (Bangalore) (10-10-2003)
    “…Gabapentin (1-(aminomethyl)cycloheaxaneacetic acid; Gpn) is a widely used anti-epileptic drug. The target site of action of Gpn remains controversial. Gpn can…”
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  11. 11

    Modulating the Structural Properties of [alpha],[gamma]-Hybrid Peptides by [alpha]-Amino Acid Residues: Uniform 12-Helix Versus "Mixed" 12/10-Helix by Misra, Rajkumar, Raja, K Muruga Poopathi, Hofmann, Hans-Jörg, Gopi, Hosahudya N

    Published in Chemistry : a European journal (21-11-2017)
    “…The most important natural [alpha]- and 310-helices are stabilized by unidirectional intramolecular hydrogen bonds along the helical cylinder. In contrast, we…”
    Get full text
    Journal Article
  12. 12

    Structural Dimorphism of Achiral [alpha],[gamma]-Hybrid Peptide Foldamers: Coexistence of 12- and 15/17-Helices by Misra, Rajkumar, Saseendran, Abhijith, George, Gijo, Veeresh, Kuruva, Raja, K Muruga Poopathi, Raghothama, Srinivasarao, Hofmann, Hans-Jörg, Gopi, Hosahudya N

    Published in Chemistry : a European journal (13-03-2017)
    “…Here, novel 12-helices in [alpha],[gamma]-hybrid peptides composed of achiral [alpha]-aminoisobutyric acid (Aib) and 4-aminoisocaproic acid (Aic, doubly…”
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    Journal Article
  13. 13

    Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of [alpha],[gamma]-Hybrid Peptide Foldamers by GaneshKumar, Mothukuri, Thombare, Varsha J, Katariya, Mona M, Veeresh, Kuruva, Raja, K Muruga Poopathi, Gopi, Hosahudya N

    Published in Angewandte Chemie International Edition (27-06-2016)
    “…The impact of geometrically constrained cis [alpha],[beta]-unsaturated [gamma]-amino acids on the folding of [alpha],[gamma]-hybrid peptides was investigated…”
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    Journal Article
  14. 14

    Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of [alpha],[gamma]-Hybrid Peptide Foldamers by GaneshKumar, Mothukuri, Thombare, Varsha J, Katariya, Mona M, Veeresh, Kuruva, Raja, K Muruga Poopathi, Gopi, Hosahudya N

    Published in Angewandte Chemie (27-06-2016)
    “…The impact of geometrically constrained cis [alpha],[beta]-unsaturated [gamma]-amino acids on the folding of [alpha],[gamma]-hybrid peptides was investigated…”
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    Journal Article
  15. 15

    C−H⋅⋅⋅O Hydrogen Bond Mediated Chain Reversal in a Peptide Containing a γ-Amino Acid Residue, Determined Directly from Powder X-ray Diffraction Data by Cheung, Eugene Y., McCabe, Emma E., Harris, Kenneth D. M., Johnston, Roy L., Tedesco, Emilio, Raja, K. Muruga Poopathi, Balaram, Padmanabhan

    Published in Angewandte Chemie International Edition (01-02-2002)
    “…Similar to the classical β turn: An intramolecular cyclic 10‐atom motif is defined in the molecular conformation of Piv‐lPro‐γ‐Abu‐NHMe (see powder X‐ray…”
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  16. 16

    Non-classical Helices with cis Carbon-Carbon Double Bonds in the Backbone: Structural Features of α,γ-Hybrid Peptide Foldamers by Ganesh Kumar, Mothukuri, Thombare, Varsha J., Katariya, Mona M., Veeresh, Kuruva, Raja, K. Muruga Poopathi, Gopi, Hosahudya N.

    Published in Angewandte Chemie (27-06-2016)
    “…The impact of geometrically constrained cis α,β‐unsaturated γ‐amino acids on the folding of α,γ‐hybrid peptides was investigated. Structure analysis in single…”
    Get full text
    Journal Article
  17. 17
  18. 18

    C−H⋅⋅⋅O Hydrogen Bond Mediated Chain Reversal in a Peptide Containing a γ-Amino Acid Residue, Determined Directly from Powder X-ray Diffraction Data by Cheung, Eugene Y., McCabe, Emma E., Harris, Kenneth D. M., Johnston, Roy L., Tedesco, Emilio, Raja, K. Muruga Poopathi, Balaram, Padmanabhan

    Published in Angewandte Chemie (01-02-2002)
    “…Der klassischen β‐Schleife ähnlich ist ein cyclisches, aus zehn Atomen bestehendes Strukturmotiv, das durch eine intramolekulare C−H⋅⋅⋅O‐Wechselwirkung bei…”
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  19. 19