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  1. Article ; Online: Seventy years of publications

    S. Samar Hasnain

    IUCrJ, Vol 4, Iss 5, Pp 512-

    2017  Volume 513

    Keywords editorial ; IUCr Journals ; Science ; Q
    Language English
    Publishing date 2017-09-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: John C. H. Spence (1946–2021)

    Henry N. Chapman / S. Samar Hasnain / Uwe Weierstall

    IUCrJ, Vol 8, Iss 5, Pp 705-

    2021  Volume 708

    Keywords obituary ; x-ray imaging ; high-resolution electron microscopy ; serial femtosecond crystallography ; x-ray free-electron lasers ; Science ; Q
    Language English
    Publishing date 2021-09-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Crystallography in the 21st century

    S. Samar Hasnain

    IUCrJ, Vol 2, Iss 6, Pp 602-

    2015  Volume 604

    Keywords cryoEM ; crystallography ; editorial ; GPCR ; ribosome ; serial crystallography ; synchrotron radiation ; XFELs ; Science ; Q
    Language English
    Publishing date 2015-11-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: IUCrJ celebrates its first year of publication

    S. Samar Hasnain

    IUCrJ, Vol 2, Iss 1, Pp 1-

    2015  Volume 2

    Keywords crystallography ; editorial ; IUCrJ ; Science ; Q
    Language English
    Publishing date 2015-01-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: A 2.2 Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases

    Alex J. Flynn / Svetlana V. Antonyuk / Robert R. Eady / Stephen P. Muench / S. Samar Hasnain

    Nature Communications, Vol 14, Iss 1, Pp 1-

    2023  Volume 12

    Abstract: Abstract Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune ...

    Abstract Abstract Quinol-dependent nitric oxide reductases (qNORs) are considered members of the respiratory heme-copper oxidase superfamily, are unique to bacteria, and are commonly found in pathogenic bacteria where they play a role in combating the host immune response. qNORs are also essential enzymes in the denitrification pathway, catalysing the reduction of nitric oxide to nitrous oxide. Here, we determine a 2.2 Å cryoEM structure of qNOR from Alcaligenes xylosoxidans, an opportunistic pathogen and a denitrifying bacterium of importance in the nitrogen cycle. This high-resolution structure provides insight into electron, substrate, and proton pathways, and provides evidence that the quinol binding site not only contains the conserved His and Asp residues but also possesses a critical Arg (Arg720) observed in cytochrome bo 3 , a respiratory quinol oxidase.
    Keywords Science ; Q
    Language English
    Publishing date 2023-06-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: 100 years of crystallography

    S. Samar Hasnain

    IUCrJ, Vol 1, Iss 1, Pp 1-

    the IUCr launches a comprehensive open-access journal, IUCrJ

    2014  Volume 2

    Keywords crystallography ; editorial ; IUCrJ ; Science ; Q
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Acta E transforms from Structure Reports Online to Crystallographic Communications

    S. Samar Hasnain

    Acta Crystallographica Section E, Vol 70, Iss 7, Pp 1-

    2014  Volume 2

    Keywords crystallography ; editorial ; Acta E ; Chemistry ; QD1-999
    Language English
    Publishing date 2014-07-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: The expanding toolkit for structural biology

    Stephen P. Muench / Svetlana V. Antonyuk / S. Samar Hasnain

    IUCrJ, Vol 6, Iss 2, Pp 167-

    synchrotrons, X-ray lasers and cryoEM

    2019  Volume 177

    Abstract: Structural biology continues to benefit from an expanding toolkit, which is helping to gain unprecedented insight into the assembly and organization of multi-protein machineries, enzyme mechanisms and ligand/inhibitor binding. The combination of results ... ...

    Abstract Structural biology continues to benefit from an expanding toolkit, which is helping to gain unprecedented insight into the assembly and organization of multi-protein machineries, enzyme mechanisms and ligand/inhibitor binding. The combination of results from X-ray free-electron lasers (XFELs), modern synchrotron crystallographic beamlines and cryo-electron microscopy (cryoEM) is proving to be particularly powerful. The highly brilliant undulator beamlines at modern synchrotron facilities have empowered the crystallographic revolution of high-throughput structure determination at high resolution. The brilliance of the X-rays at these crystallographic beamlines has enabled this to be achieved using microcrystals, but at the expense of an increased absorbed X-ray dose and a consequent vulnerability to radiation-induced changes. The advent of serial femtosecond crystallography (SFX) with X-ray free-electron lasers provides a new opportunity in which damage-free structures can be obtained from much smaller crystals (2 µm) and more complex macromolecules, including membrane proteins and multi-protein complexes. For redox enzymes, SFX provides a unique opportunity by providing damage-free structures at both cryogenic and ambient temperatures. The promise of being able to visualize macromolecular structures and complexes at high resolution without the need for crystals using X-rays has remained a dream, but recent technological advancements in cryoEM have made this come true and hardly a month goes by when the structure of a new/novel macromolecular assembly is not revealed. The uniqueness of cryoEM in providing structural information for multi-protein complexes, particularly membrane proteins, has been demonstrated by examples such as respirasomes. The synergistic use of cryoEM and crystallography in lead-compound optimization is highlighted by the example of the visualization of antimalarial compounds in cytochrome bc1. In this short review, using some recent examples including our own work, we share the excitement of these powerful structural biology methods.
    Keywords synchrotron crystallography ; serial femtosecond crystallography ; cryoEM ; MSOX ; Science ; Q
    Subject code 500
    Language English
    Publishing date 2019-03-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes

    Daisuke Sasaki / Tatiana F. Watanabe / Robert R. Eady / Richard C. Garratt / Svetlana V. Antonyuk / S. Samar Hasnain

    IUCrJ, Vol 7, Iss 3, Pp 557-

    2020  Volume 565

    Abstract: Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitrogen cycle where nitrate is used in place of dioxygen as an electron acceptor in respiratory ... ...

    Abstract Copper-containing nitrite reductases (CuNiRs) are found in all three kingdoms of life and play a major role in the denitrification branch of the global nitrogen cycle where nitrate is used in place of dioxygen as an electron acceptor in respiratory energy metabolism. Several C- and N-terminal redox domain tethered CuNiRs have been identified and structurally characterized during the last decade. Our understanding of the role of tethered domains in these new classes of three-domain CuNiRs, where an extra cytochrome or cupredoxin domain is tethered to the catalytic two-domain CuNiRs, has remained limited. This is further compounded by a complete lack of substrate-bound structures for these tethered CuNiRs. There is still no substrate-bound structure for any of the as-isolated wild-type tethered enzymes. Here, structures of nitrite and product-bound states from a nitrite-soaked crystal of the N-terminal cupredoxin-tethered enzyme from the Hyphomicrobium denitrificans strain 1NES1 (Hd1NES1NiR) are provided. These, together with the as-isolated structure of the same species, provide clear evidence for the role of the N-terminal peptide bearing the conserved His27 in water-mediated anchoring of the substrate at the catalytic T2Cu site. Our data indicate a more complex role of tethering than the intuitive advantage for a partner-protein electron-transfer complex by narrowing the conformational search in such a combined system.
    Keywords nitrogen cycle ; denitrification ; copper-containing nitrite reductase ; electron transfer ; catalysis ; structural biology ; Crystallography ; QD901-999
    Subject code 500
    Language English
    Publishing date 2020-05-01T00:00:00Z
    Publisher International Union of Crystallography
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Novel Selenium-based compounds with therapeutic potential for SOD1-linked amyotrophic lateral sclerosis

    Kangsa Amporndanai / Michael Rogers / Seiji Watanabe / Koji Yamanaka / Paul M. O'Neill / S. Samar Hasnain

    EBioMedicine, Vol 59, Iss , Pp 102980- (2020)

    2020  

    Abstract: Background: Amyotrophic lateral sclerosis (ALS), also known as motor neuron disease as well as Lou Gehrig's disease, is a progressive neurological disorder selectively affecting motor neurons with no currently known cure. Around 20% of the familial ALS ... ...

    Abstract Background: Amyotrophic lateral sclerosis (ALS), also known as motor neuron disease as well as Lou Gehrig's disease, is a progressive neurological disorder selectively affecting motor neurons with no currently known cure. Around 20% of the familial ALS cases arise from dominant mutations in the sod1 gene encoding superoxide dismutase1 (SOD1) enzyme. Aggregation of mutant SOD1 in familial cases and of wild-type SOD1 in at least some sporadic ALS cases is one of the known causes of the disease. Riluzole, approved in 1995 and edaravone in 2017 remain the only drugs with limited therapeutic benefits. Methods: We have utilised the ebselen template to develop novel compounds that redeem stability of mutant SOD1 dimer and prevent aggregation. Binding modes of compounds have been visualised by crystallography. In vitro neuroprotection and toxicity of lead compounds have been performed in mouse neuronal cells and disease onset delay of ebselen has been demonstrated in transgenic ALS mice model. Finding: We have developed a number of ebselen-based compounds with improvements in A4V SOD1 stabilisation and in vitro therapeutic effects with significantly better potency than edaravone. Structure-activity relationship of hits has been guided by high resolution structures of ligand-bound A4V SOD1. We also show clear disease onset delay of ebselen in transgenic ALS mice model holding encouraging promise for potential therapeutic compounds. Interpretation: Our finding established the new generation of organo-selenium compounds with better in vitro neuroprotective activity than edaravone. The potential of this class of compounds may offer an alternative therapeutic agent for ALS treatment. The ability of these compounds to target cysteine 111 in SOD may have wider therapeutic applications targeting cysteines of enzymes involved in pathogenic and viral diseases including main protease of SARS-Cov-2 (COVID-19). Funding: Project funding was supported by the ALS Association grant (WA1128) and Fostering Joint International Research ...
    Keywords SOD1 ; Ebselen ; Drug design ; Neurodegeneration ; Motor neuron disease ; COVID-19 ; Medicine ; R ; Medicine (General) ; R5-920
    Subject code 500
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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