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Two distinct DNA sequences recognized by transcription factors represent enthalpy and entropy optima
Morgunova E, Yin Y, Das Pk, Jolma A, Zhu F, Popov A, et al
eLife 2018;7():-

Damaging heterozygous mutations in NFKB1 lead to diverse immunologic phenotypes
Kaustio M, Haapaniemi E, Göös H, Hautala T, Park G, Syrjänen J, et al
The Journal of allergy and clinical immunology 2017;140(3):782-796

Impact of cytosine methylation on DNA binding specificities of human transcription factors
Yin Y, Morgunova E, Jolma A, Kaasinen E, Sahu B, Khund-sayeed S, et al
Science (New York, N.Y.) 2017;356(6337):-

Structural perspective of cooperative transcription factor binding
Morgunova E, Taipale J
Current opinion in structural biology 2017;47():1-8

Conservation of transcription factor binding specificities across 600 million years of bilateria evolution
Nitta Kr, Jolma A, Yin Y, Morgunova E, Kivioja T, Akhtar J, et al
eLife 2015;4():-

DNA-dependent formation of transcription factor pairs alters their binding specificity
Jolma A, Yin Y, Nitta Kr, Dave K, Popov A, Taipale M, et al
Nature 2015;527(7578):384-8

Structural insights into the DNA-binding specificity of E2F family transcription factors
Morgunova E, Yin Y, Jolma A, Dave K, Schmierer B, Popov A, et al
Nature communications 2015;6():10050-

Whole-Genome Sequencing Identifies STAT4 as a Putative Susceptibility Gene in Classic Kaposi Sarcoma
Aavikko M, Kaasinen E, Nieminen Jk, Byun M, Donner I, Mancuso R, et al
The Journal of infectious diseases 2015;211(11):1842-51

DNA-binding specificities of human transcription factors
Jolma A, Yan J, Whitington T, Toivonen J, Nitta Kr, Rastas P, et al
Cell 2013;152(1-2):327-39

An intact eight-membered water chain in drosophilid alcohol dehydrogenases is essential for optimal enzyme activity
Wuxiuer Y, Morgunova E, Cols N, Popov A, Karshikoff A, Sylte I, et al
The FEBS journal 2012;279(16):2940-56

Loss of SUFU function in familial multiple meningioma
Aavikko M, Li Sp, Saarinen S, Alhopuro P, Kaasinen E, Morgunova E, et al
American journal of human genetics 2012;91(3):520-6

Novel mutation in Wilms' tumour 1 gene associated with steroid-resistant nephrotic syndrome
Beltcheva O, Boueva A, Morgunova E, Boiadjieva E, Marinova S, Kaneva R, et al
NDT plus 2011;4(1):17-9

Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis
Morgunova E, Illarionov B, Saller S, Popov A, Sambaiah T, Bacher A, et al
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 2010;:1001-11

Virtual screening, selection and development of a benzindolone structural scaffold for inhibition of lumazine synthase
Talukdar A, Morgunova E, Duan Jx, Meining W, Foloppe N, Nilsson L, et al
BIOORGANIC & MEDICINAL CHEMISTRY 2010;18(10):3518-34

Structural insights into the adaptation of proliferating cell nuclear antigen (PCNA) from Haloferax volcanii to a high-salt environment
Morgunova E, Gray Fc, Macneill Sa, Ladenstein R
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY 2009;:1081-8

N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives as inhibitors of lumazine synthase and riboflavin synthase: Design, synthesis, biochemical evaluation, crystallography, and mechanistic implications
Zhang Yl, Illarionov B, Morgunova E, Jin Gy, Bacher A, Fischer M, et al
JOURNAL OF ORGANIC CHEMISTRY 2008;73(7):2715-24

Lumazine synthase from Candida albicans as an anti-fungal target enzyme - Structural and biochemical basis for drug design
Morgunova E, Saller S, Haase I, Cushman M, Bacher A, Fischer M, et al
JOURNAL OF BIOLOGICAL CHEMISTRY 2007;282(23):17231-41

Purification, crystallization and preliminary X-ray study of the fungal laccase from Cerrena maxima
Lyashenko Av, Zhukhlistova Ne, Gabdoulkhakov Ag, Zhukova Yn, Voelter W, Zaitsev Vn, et al
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 2006;:954-7

Structural and thermodynamic insights into the binding mode of five novel inhibitors of lumazine synthase from Mycobacterium tuberculosis
Morgunova E, Illarionov B, Sambaiah T, Haase I, Bacher A, Cushman M, et al
FEBS JOURNAL 2006;273(20):4790-804

X-ray structural studies of the fungal laccase from Cerrena maxima
Lyashenko Av, Bento I, Zaitsev Vn, Zhukhlistova Ne, Zhukova Yn, Gabdoulkhakov Ag, et al
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY 2006;11(8):963-73

Characterization of the interactions of the nephrin intracellular domain - Evidence that the scaffolding protein IQGAP1 associates with nephrin
Liu Xl, Kilpelainen P, Hellman U, Sun Y, Wartiovaara J, Morgunova E, et al
FEBS JOURNAL 2005;272(1):228-43

Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: Binding mode of a new class of purinetrione inhibitors
Morgunova E, Meining W, Illarionov B, Haase I, Jin Gy, Bacher A, et al
BIOCHEMISTRY 2005;44(8):2746-58

Preliminary investigation of the three-dimensional structure of Salmonella typhimurium uridine phosphorylase in the crystalline state
Dontsova Mv, Gabdoulkhakov Ag, Molchan Ok, Lashkov Aa, Garber Mb, Mironov As, et al
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS 2005;:337-40

Characterization of recombinant soluble macrophage scavenger receptor MARCO
Sankala M, Brannstrom A, Schulthess T, Bergmann U, Morgunova E, Engel J, et al
JOURNAL OF BIOLOGICAL CHEMISTRY 2002;277(36):33378-85

Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2
Morgunova E, Tuuttila A, Bergmann U, Tryggvason K
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 2002;99(11):7414-9

Structure of human pro-matrix metalloproteinase-2: Activation mechanism revealed
Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, et al
SCIENCE 1999;284(5420):1667-70

Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 angstrom resolution
Tuuttila A, Morgunova E, Bergmann U, Lindqvist Y, Maskos K, Fernandez-catalan C, et al
JOURNAL OF MOLECULAR BIOLOGY 1998;284(4):1133-40

ATOMIC-STRUCTURE AT 2.5 ANGSTROM RESOLUTION OF URIDINE PHOSPHORYLASE FROM ESCHERICHIA-COLI AS REFINED IN THE MONOCLINIC CRYSTAL-LATTICE
Morgunova Ey, Mikhailov Am, Popov An, Blagova Ev, Smirnova Ea, Vainshtein Bk, et al
FEBS LETTERS 1995;367(2):183-187

Atomic structure at 2.5 A resolution of uridine phosphorylase from E. coli as refined in the monoclinic crystal lattice
Morgunova Eyu , Mikhailov Am, Popov An, Blagova Ev, Smirnova Ea, Vainshtein Bk, et al
FEBS letters 1995;367(2):183-7

NEW APPROACHES TO CHROMATOGRAPHIC PURIFICATION OF BOVINE DOPAMINE-BETA-HYDROXYLASE
Varlamov Vp, Lopatin Sa, Ilyina Av, Bannikova Ge, Chlenov Ma, Vasiyarov Gg, et al
JOURNAL OF CHROMATOGRAPHY A 1995;711(1):113-8

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