Search Results - "Elif Nihal Korkmaz"

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  1. 1

    Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly by Taylor, Keenan C, Massimo Buvoli, Elif Nihal Korkmaz, Ada Buvoli, Yuqing Zheng, Nathan T. Heinze, Qiang Cui, Leslie A. Leinwand, Ivan Rayment

    “…The rod of sarcomeric myosins directs thick filament assembly and is characterized by the insertion of four skip residues that introduce discontinuities in the…”
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    Journal Article
  2. 2

    Identification of the Ah-receptor structural determinants for ligand preferences by Xing, Yongna, Nukaya, Manabu, Satyshur, Kenneth A, Jiang, Li, Stanevich, Vitali, Korkmaz, Elif Nihal, Burdette, Lisa, Kennedy, Gregory D, Cui, Qiang, Bradfield, Christopher A

    Published in Toxicological sciences (01-09-2012)
    “…The aryl hydrocarbon receptor (AHR) is a transcription factor that responds to diverse ligands and plays a critical role in toxicology, immune function, and…”
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  3. 3

    Conformational control of the binding of the transactivation domain of the MLL protein and c-Myb to the KIX domain of CREB by Korkmaz, Elif Nihal, Nussinov, Ruth, Haliloğlu, Türkan

    Published in PLoS computational biology (2012)
    “…The KIX domain of CBP is a transcriptional coactivator. Concomitant binding to the activation domain of proto-oncogene protein c-Myb and the transactivation…”
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  4. 4
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    Specificity landscapes unmask submaximal binding site preferences of transcription factors by Bhimsaria, Devesh, Rodríguez-Martínez, José A., Pan, Junkun, Roston, Daniel, Korkmaz, Elif Nihal, Cui, Qiang, Ramanathan, Parameswaran, Ansari, Aseem Z.

    “…We have developed Differential Specificity and Energy Landscape (DiSEL) analysis to comprehensively compare DNA–protein interactomes (DPIs) obtained by…”
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  6. 6

    Interplay of Electrostatics and Hydrophobic Effects in the Metamorphic Protein Human Lymphotactin by Korkmaz, Elif Nihal, Volkman, Brian F, Cui, Qiang

    Published in The journal of physical chemistry. B (30-07-2015)
    “…The human lymphotactin (hLtn) is a protein that features two native states both of which are physiologically relevant: it is a monomer (hLtn10) at 10 °C with…”
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    Journal Article