2024
Hemophore-like proteins of the HmuY family in the oral and gut microbiome: unraveling the mystery of their evolution. (Journal article)
Olczak, T., Śmiga, M., Antonyuk, S. V., & Smalley, J. W. (2024). Hemophore-like proteins of the HmuY family in the oral and gut microbiome: unraveling the mystery of their evolution.. Microbiology and molecular biology reviews : MMBR, 88(1), e0013123. doi:10.1128/mmbr.00131-23DOI: 10.1128/mmbr.00131-23
Hossain, M. A., Sarin, R., Donnelly, D. P., Miller, B. C., Weiss, A., McAlary, L., . . . Agar, J. N. (2024). Evaluating protein cross-linking as a therapeutic strategy to stabilize SOD1 variants in a mouse model of familial ALS.. PLoS biology, 22(1), e3002462. doi:10.1371/journal.pbio.3002462DOI: 10.1371/journal.pbio.3002462
Vollmar, M., Nicholls, R., & Antonyuk, S. (2024). Current trends in macromolecular model refinement and validation.. Acta crystallographica. Section D, Structural biology, 80(Pt 1), 1-3. doi:10.1107/s2059798323010823DOI: 10.1107/s2059798323010823
2023
Antonyuk, S. V., Sieminska, K., Smiga, M., Strange, R. W., Wagner, M., Barnett, K. J., & Olczak, T. (2023). <i>Bacteroides fragilis</i> expresses three proteins similar to <i>Porphyromonas gingivalis</i> HmuY: Hemophore-like proteins differentially evolved to participate in heme acquisition in oral and gut microbiomes. FASEB JOURNAL, 37(7). doi:10.1096/fj.202300366RDOI: 10.1096/fj.202300366R
Flynn, A. J., Antonyuk, S. V., Eady, R. R., Muench, S. P., & Hasnain, S. S. (2023). A 2.2Å cryoEM structure of a quinol-dependent NO Reductase shows close similarity to respiratory oxidases. NATURE COMMUNICATIONS, 14(1). doi:10.1038/s41467-023-39140-xDOI: 10.1038/s41467-023-39140-x
Prakash, O., Gupta, N., Milburn, A., McCormick, L., Deugi, V., Fisch, P., . . . Helassa, N. (2023). Calmodulin variant E140G associated with long QT syndrome impairs CaMKIIδ autophosphorylation and L-type calcium channel inactivation. JOURNAL OF BIOLOGICAL CHEMISTRY, 299(1). doi:10.1016/j.jbc.2022.102777DOI: 10.1016/j.jbc.2022.102777
2022
Krissinel, E., Lebedev, A. A., Uski, V., Ballard, C. B., Keegan, R. M., Kovalevskiy, O., . . . Brown, D. G. (2022). <i>CCP</i>4 Cloud for structure determination and project management in macromolecular crystallograpny. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 78, 1079-1089. doi:10.1107/S2059798322007987DOI: 10.1107/S2059798322007987
Rose, S. L., Baba, S., Okumura, H., Antonyuk, S. V., Sasaki, D., Hedison, T. M., . . . Hasnain, S. S. (2022). Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 119(30). doi:10.1073/pnas.2205664119DOI: 10.1073/pnas.2205664119
Amporndanai, K., Pinthong, N., O'Neill, P. M., Hong, W. D., Amewu, R. K., Pidathala, C., . . . Antonyuk, S. V. (2022). Targeting the Ubiquinol-Reduction (Q<sub>i</sub>) Site of the Mitochondrial Cytochrome <i>bc<sub>1</sub></i> Complex for the Development of Next Generation Quinolone Antimalarials. BIOLOGY-BASEL, 11(8). doi:10.3390/biology11081109DOI: 10.3390/biology11081109
CPVT-associated calmodulin variants N531 and A102V dysregulate Ca<SUP>2+</SUP> signalling via different mechanisms (Journal article)
Prakash, O., Held, M., McCormick, L. F., Gupta, N., Lian, L. -Y., Antonyuk, S., . . . Helassa, N. (2022). CPVT-associated calmodulin variants N531 and A102V dysregulate Ca<SUP>2+</SUP> signalling via different mechanisms. JOURNAL OF CELL SCIENCE, 135(2). doi:10.1242/jcs.258796DOI: 10.1242/jcs.258796
2021
de Souza, J. O., Almeida, S. M., Souza, G. E., Zanini, C. L., da Silva, E. M., Calit, J., . . . Guido, R. V. C. (2021). Parasitological profiling shows 4(1H)-quinolone derivatives as new lead candidates for malaria. European Journal of Medicinal Chemistry Reports, 3, 100012. doi:10.1016/j.ejmcr.2021.100012DOI: 10.1016/j.ejmcr.2021.100012
Quinol-dependent Nitric Oxide Reductases are dimers in cryoEM structures (Conference Paper)
Gopalasingam, C. C., Jamali, M. A. M., Tosha, T., Muench, S. P., Antonyuk, S. V., Shiro, Y., & Hasnain, S. S. (2021). Quinol-dependent Nitric Oxide Reductases are dimers in cryoEM structures. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 77 (pp. C585). Retrieved from https://www.webofscience.com/
Rose, S. L., Antonyuk, S. V., Sasaki, D., Yamashita, K., Hirata, K., Ueno, G., . . . Hasnain, S. S. (2021). An unprecedented insight into the catalytic mechanism of copper nitrite reductase from atomic-resolution and damage-free structures. SCIENCE ADVANCES, 7(1). doi:10.1126/sciadv.abd8523DOI: 10.1126/sciadv.abd8523
Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2021). Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction. FEBS JOURNAL, 288(1), 262-280. doi:10.1111/febs.15324DOI: 10.1111/febs.15324
2020
Hough, M. A., Conradie, J., Strange, R. W., Antonyuk, S. V., Eady, R. R., Ghosh, A., & Hasnain, S. S. (n.d.). Nature of the copper-nitrosyl intermediates of copper nitrite reductases during catalysis. Chemical Science. doi:10.1039/d0sc04797jDOI: 10.1039/d0sc04797j
AcGI1, a novel genomic island carrying antibiotic resistance integron In687 in multidrug resistant <i>Achromobacter xylosoxidans</i> in a teaching hospital in Thailand (Journal article)
Pongchaikul, P., Santanirand, P., Antonyuk, S., Winstanley, C., & Darby, A. C. (2020). AcGI1, a novel genomic island carrying antibiotic resistance integron In687 in multidrug resistant <i>Achromobacter xylosoxidans</i> in a teaching hospital in Thailand. FEMS MICROBIOLOGY LETTERS, 367(14). doi:10.1093/femsle/fnaa109DOI: 10.1093/femsle/fnaa109
Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases (Journal article)
Wright, G. S. A., Watanabe, T. F., Amporndanai, K., Plotkin, S. S., Cashman, N. R., Antonyuk, S. V., & Hasnain, S. S. (2020). Purification and Structural Characterization of Aggregation-Prone Human TDP-43 Involved in Neurodegenerative Diseases. iScience, 23(6). doi:10.1016/j.isci.2020.101159DOI: 10.1016/j.isci.2020.101159
Potent Tetrahydroquinolone Eliminates Apicomplexan Parasites (Journal article)
McPhillie, M. J., Zhou, Y., Hickman, M. R., Gordon, J. A., Weber, C. R., Li, Q., . . . McLeod, R. (n.d.). Potent Tetrahydroquinolone Eliminates Apicomplexan Parasites. Frontiers in Cellular and Infection Microbiology, 10. doi:10.3389/fcimb.2020.00203DOI: 10.3389/fcimb.2020.00203
Panmanee, J., Antonyuk, S. V., & Hasnain, S. S. (2020). Structural basis of the dominant inheritance of hypermethioninemia associated with the Arg264His mutation in the <i>MAT1A</i> gene. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 76, 594-607. doi:10.1107/S2059798320006002DOI: 10.1107/S2059798320006002
Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2020). 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. IUCrJ, 7(3), 557-565. doi:10.1107/s2052252520005230DOI: 10.1107/s2052252520005230
Jamali, M. A. M., Gopalasingam, C. C., Johnson, R. M., Tosha, T., Muramoto, K., Muench, S. P., . . . Hasnain, S. S. (2020). The active form of quinol-dependent nitric oxide reductase from Neisseria meningitidis is a dimer. IUCrJ, 7(3), 404-415. doi:10.1107/s2052252520003656DOI: 10.1107/s2052252520003656
McPhillie, M., Zhou, Y., El Bissati, K., Dubey, J., Lorenzi, H., Capper, M., . . . McLeod, R. (2020). New paradigms for understanding and step changes in treating active and chronic, persistent apicomplexan infections (vol 6, 29179, 2016). SCIENTIFIC REPORTS, 10(1). doi:10.1038/s41598-020-62323-1DOI: 10.1038/s41598-020-62323-1
Chantadul, V., Wright, G. S. A., Amporndanai, K., Shahid, M., Antonyuk, S. V., Washbourn, G., . . . Hasnain, S. S. (2020). Ebselen as template for stabilization of A4V mutant dimer for motor neuron disease therapy. COMMUNICATIONS BIOLOGY, 3(1). doi:10.1038/s42003-020-0826-3DOI: 10.1038/s42003-020-0826-3
Long-QT Syndrome-Associated Calmodulin Mutations and Their Interactions at the K<sub>v</sub>7.1 Potassium Channel (Conference Paper)
McCormick, L. F., Gupta, N., Haynes, L. P., Antonyuk, S., Dart, C., & Helassa, N. (2020). Long-QT Syndrome-Associated Calmodulin Mutations and Their Interactions at the K<sub>v</sub>7.1 Potassium Channel. In BIOPHYSICAL JOURNAL Vol. 118 (pp. 404A). Retrieved from https://www.webofscience.com/
Bielecki, M., Antonyuk, S., Strange, R. W., Siemińska, K., Smalley, J. W., Mackiewicz, P., . . . Olczak, T. (2020). Prevotella intermedia produces two proteins homologous to Porphyromonas gingivalis HmuY but with different heme coordination mode. Biochemical Journal, 477(2), 381-405. doi:10.1042/bcj20190607DOI: 10.1042/bcj20190607
2019
Wright, G. S. A., Antonyuk, S. V., & Hasnain, S. S. (2019). The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis.. Quarterly reviews of biophysics, 52, e12. doi:10.1017/s003358351900012xDOI: 10.1017/s003358351900012x
Gopalasingam, C. C., Johnson, R. M., Chiduza, G. N., Tosha, T., Yamamoto, M., Shiro, Y., . . . Samar Hasnain, S. (2019). Dimeric structures of quinol-dependent nitric oxide reductases (qNORs) revealed by cryo–electron microscopy. Science Advances, 5(8). doi:10.1126/sciadv.aax1803DOI: 10.1126/sciadv.aax1803
Sala, F. A., Wrigth, G., Antonyuk, S., Garratt, R. C., & Hasnain, S. S. (2019). THE SOD1-HCCS MECHANISM INVOLVED IN COPPER HOMEOSTASIS. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 75 (pp. E71). doi:10.1107/S2053273319094853DOI: 10.1107/S2053273319094853
Poonsiri, T., Wright, G., Solomon, T., & Antonyuk, S. V. (2019). Crystal Structure of the Japanese Encephalitis VirusCapsid Protein. Viruses, 11(7). doi:10.3390/v11070623DOI: 10.3390/v11070623
Hedison, T. M., Shenoy, R. T., Iorgu, A. I., Heyes, D. J., Fisher, K., Wright, G. S. A., . . . Scrutton, N. S. (2019). Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis. ACS Catalysis, 9(7), 6087-6099. doi:10.1021/acscatal.9b01266DOI: 10.1021/acscatal.9b01266
Halsted, T. P., Yamashita, K., Gopalasingam, C. C., Shenoy, R. T., Hirata, K., Ago, H., . . . Hasnain, S. S. (2019). Catalytically important damage-free structures of a copper nitrite reductase obtained by femtosecond X-ray laser and room-temperature neutron crystallography. IUCRJ, 6, 761-772. doi:10.1107/S2052252519008285DOI: 10.1107/S2052252519008285
Chiduza, G. N., Johnson, R. M., Wright, G. S. A., Antonyuk, S. V., Muench, S. P., & Hasnain, S. S. (2019). LAT1 (SLC7A5) and CD98hc (SLC3A2) complex dynamics revealed by single-particle cryo-EM. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 75, 660-669. doi:10.1107/S2059798319009094DOI: 10.1107/S2059798319009094
Panmanee, J., Bradley-Clarke, J., Mato, J. M., O'Neill, P. M., Antonyuk, S. V., & Hasnain, S. S. (2019). Control and regulation of S‐Adenosylmethionine biosynthesis by the regulatory β subunit and quinolone‐based compounds. The Federation of European Biochemical Societies (FEBS) Journal, 286(11), 2135-2154. doi:10.1111/febs.14790DOI: 10.1111/febs.14790
Lam, W. -H., Sze, K. -H., Ke, Y., Tse, M. -K., Zhang, H., Woo, P. C. Y., . . . Hao, Q. (2019). <i>Talaromyces marneffei</i> Mp1 Protein, a Novel Virulence Factor, Carries Two Arachidonic Acid-Binding Domains To Suppress Inflammatory Responses in Hosts. INFECTION AND IMMUNITY, 87(4). doi:10.1128/IAI.00679-18DOI: 10.1128/iai.00679-18
Muench, S. P., Antonyuk, S. V., & Hasnain, S. S. (2019). The expanding toolkit for structural biology: synchrotrons, X-ray lasers and cryoEM. IUCRJ, 6(2), 167-177. doi:10.1107/S2052252519002422DOI: 10.1107/S2052252519002422
Sala, F. A., Wright, G. S. A., Antonyuk, S. V., Garratt, R. C., & Hasnain, S. S. (2019). Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS. PLOS BIOLOGY, 17(2). doi:10.1371/journal.pbio.3000141DOI: 10.1371/journal.pbio.3000141
Vandebroek, L., Mampaey, Y., Antonyuk, S., Van Meervelt, L., & Parac-Vogt, T. N. (2019). Noncovalent Complexes Formed between Metal-Substituted Polyoxometalates and Hen Egg White Lysozyme. EUROPEAN JOURNAL OF INORGANIC CHEMISTRY, (3-4), 506-511. doi:10.1002/ejic.201801113DOI: 10.1002/ejic.201801113
2018
David Hong, W., Leung, S. C., Amporndanai, K., Davies, J., Priestley, R. S., Nixon, G. L., . . . O'Neill, P. M. (2018). Potent Antimalarial 2-Pyrazolyl Quinolone bc1 (Qi) Inhibitors with Improved Drug-like Properties. ACS Medicinal Chemistry Letters, 9(12), 1205-1210. doi:10.1021/acsmedchemlett.8b00371DOI: 10.1021/acsmedchemlett.8b00371
Bielecki, M., Antonyuk, S., Strange, R. W., Smalley, J. W., Mackiewicz, P., Smiga, M., . . . Olczak, T. (2018). <i>Tannerella</i> <i>forsythia</i> Tfo belongs to <i>Porphyromonas</i> <i>gingivalis</i> HmuY-like family of proteins but differs in heme-binding properties. BIOSCIENCE REPORTS, 38. doi:10.1042/BSR20181325DOI: 10.1042/BSR20181325
Bielecki, M., Antonyuk, S., Strange, R. W., Smalley, J. W., Smiga, M., Stepien, P., . . . Olczak, T. (2018). Porphyromonas gingivalis HmuY and Tannerella forsythia Tfo - two homologous proteins with different heme-binding properties. In FEBS OPEN BIO Vol. 8 (pp. 428). Retrieved from http://gateway.webofknowledge.com/
Amporndanai, K., Fishwick, C., Hasnain, S., Antonyuk, S., & Muench, S. (2018). EM studies of cytochrome bc<sub>1</sub> to elucidate inhibitor binding. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 74 (pp. A121). Retrieved from https://www.webofscience.com/
Hackenberg, C., Hakanpaeae, J., Cai, F., Antonyuk, S., Eigner, C., Meissner, S., . . . Lamzin, V. S. (2018). Structural and functional insights into the unique CBS-CP12 fusion protein family in cyanobacteria. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 115(27), 7141-7146. doi:10.1073/pnas.1806668115DOI: 10.1073/pnas.1806668115
Dong, J., Sasaki, D., Eady, R. R., Antonyuk, S. V., & Hasnain, S. S. (2018). Identification of a tyrosine switch in copper-haem nitrite reductases. IUCrJ, 5(4), 510-518. doi:10.1107/S2052252518008242DOI: 10.1107/S2052252518008242
Horrell, S., Kekilli, D., Sen, K., Owen, R. U., Dworkowski, F. S. N., Antonyuk, S. V., . . . Hough, M. A. (2018). Enzyme catalysis captured using multiple structures from one crystal at varying temperatures. IUCRJ, 5, 283-292. doi:10.1107/S205225251800386XDOI: 10.1107/S205225251800386X
Capper, M. J., Wright, G. S. A., Barbieri, L., Luchinat, E., Mercatelli, E., McAlary, L., . . . Hasnain, S. S. (2018). The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation. NATURE COMMUNICATIONS, 9. doi:10.1038/s41467-018-04114-xDOI: 10.1038/s41467-018-04114-x
Wright, G. S. A., Saeki, A., Hikima, T., Nishizono, Y., Hisano, T., Kamaya, M., . . . Sawai, H. (2018). Architecture of the complete oxygen-sensing FixL-FixJ two-component signal transduction system. SCIENCE SIGNALING, 11(525). doi:10.1126/scisignal.aaq0825DOI: 10.1126/scisignal.aaq0825
Poonsiri, T., Wright, G. S. A., Diamond, M. S., Turtle, L., Solomon, T., & Antonyuk, S. V. (2018). Structural study of the C-terminal domain of non-structural protein 1 from Japanese encephalitis virus. Journal of Virology, 92(7). doi:10.1128/jvi.01868-17DOI: 10.1128/jvi.01868-17
Amporndanai, K., Johnson, R. M., O'Neill, P., Fishwick, C. W. G., Jamson, A. H., Rawson, S., . . . Hasnain, S. (2018). X-ray and cryo-EM structures of inhibitor-bound cytochrome bc1 complexes for structure-based drug discovery. IUCrJ, 5(Pt 2), 200-210. doi:10.1107/S2052252518001616DOI: 10.1107/S2052252518001616
Gonska, N., Young, D., Yuki, R., Okamoto, T., Hisano, T., Antonyuk, S., . . . Adelroth, P. (2018). Characterization of the quinol-dependent nitric oxide reductase from the pathogen <i>Neisseria meningitidis</i>, an electrogenic enzyme. SCIENTIFIC REPORTS, 8. doi:10.1038/s41598-018-21804-0DOI: 10.1038/s41598-018-21804-0
Antonyuk, S. V., Hasnain, S., Gonska, N., Young, D., Yuki, R., Okamoto, T., . . . Ädelroth, P. (n.d.). Characterization of the quinoldependent nitric oxide reductasefrom the pathogen Neisseria meningitidis, an electrogenic enzyme. Scientific Reports. doi:10.1038/s41598-018-21804-0DOI: 10.1038/s41598-018-21804-0
Helassa, N., Antonyuk, S. V., Lian, L. -Y., Haynes, L. P., & Burgoyne, R. D. (2018). Dystonia-Associated Hippocalcin Mutants Dysregulate Cellular Calcium Influx. In BIOPHYSICAL JOURNAL Vol. 114 (pp. 467A-468A). Retrieved from https://www.webofscience.com/
Activation of superoxide dismutase-1 by its copper chaperone is orchestrated by a single methyl group (Conference Paper)
Wright, G., Sala, F., Antonyuk, S., Garratt, R., & Hasnain, S. (2018). Activation of superoxide dismutase-1 by its copper chaperone is orchestrated by a single methyl group. In FEBS OPEN BIO Vol. 8 (pp. 37). Retrieved from https://www.webofscience.com/
Halsted, T. P., Yamashita, K., Hirata, K., Ago, H., Ueno, G., Tosha, T., . . . Hasnain, S. S. (2018). An unprecedented dioxygen species revealed by serial femtosecond rotation crystallography in copper nitrite reductase. IUCRJ, 5, 22-31. doi:10.1107/S2052252517016128DOI: 10.1107/S2052252517016128
Bielecki, M., Antonyuk, S., Strange, R. W., Smalley, J. W., Smiga, M., Stepien, P., . . . Olczak, T. (2018). Prevotella intermedia produces two homologous proteins to <i>Porphyromonas gingivalis</i> HmuY with different heme-binding properties. In FEBS OPEN BIO Vol. 8 (pp. 429). Retrieved from https://www.webofscience.com/
Structural studies of human superoxide dismutase (SOD1) with its metallochaperone (Conference Paper)
Sala, F. A., Wright, G. S. A., Antonyuk, S. V., Garratt, R. C., & Hasnain, S. S. (2018). Structural studies of human superoxide dismutase (SOD1) with its metallochaperone. In FEBS OPEN BIO Vol. 8 (pp. 432-433). Retrieved from https://www.webofscience.com/
2017
MSOX crystallography and simulations to capture redox enzyme catalysis (Conference Paper)
Hough, M. A., Kekilli, D., Horrell, S., Sen, K., Yong, C., Keal, T. W. K., . . . Strange, R. W. (2014). MSOX crystallography and simulations to capture redox enzyme catalysis. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 70 (pp. C651). Retrieved from http://gateway.webofknowledge.com/
MSOX crystallography and simulations to capture redox enzyme catalysis (Conference Paper)
Hough, M. A., Kekilli, D., Horrell, S., Sen, K., Yong, C., Keal, T. W. K., . . . Strange, R. W. (2017). MSOX crystallography and simulations to capture redox enzyme catalysis. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 73 (pp. C651). doi:10.1107/S2053273317089227DOI: 10.1107/S2053273317089227
Biophysical and functional characterization of hippocalcin mutants responsible for human dystonia (Journal article)
Helassa, N., Antonyuk, S. V., Lian, L. -Y., Haynes, L. P., & Burgoyne, R. D. (2017). Biophysical and functional characterization of hippocalcin mutants responsible for human dystonia. Human molecular genetics, 26(13), 2426-2435. doi:10.1093/hmg/ddx133DOI: 10.1093/hmg/ddx133
Dickens, D., Chiduza, G. N., Wright, G. S. A., Pirmohamed, M., Antonyuk, S. V., & Hasnain, S. S. (n.d.). Modulation of LAT1 (SLC7A5) transporter activity and stability by membrane cholesterol.. Scientific Reports, 7. doi:10.1038/srep43580DOI: 10.1038/srep43580
INTRA- AND INTER-MOLECULAR SIGNAL TRANSDUCTION MECHANISMS OF HEME SENSING SYSTEMS (Conference Paper)
Sawai, H., Wright, G. S. A., Saeki, A., Hikima, T., Yamamoto, M., Antonyuk, S., . . . Shiro, Y. (2017). INTRA- AND INTER-MOLECULAR SIGNAL TRANSDUCTION MECHANISMS OF HEME SENSING SYSTEMS. In AMERICAN JOURNAL OF HEMATOLOGY Vol. 92 (pp. E463). Retrieved from https://www.webofscience.com/
2016
Single Crystal Serial Crystallography to Capture Redox Enzyme Catalysis and Dynamics (Conference Paper)
Schneider, G., Pearson, A., Hough, M., Kekilli, D., Horrell, S., Dworkowski, F. S. N., . . . Strange, R. W. (2016). Single Crystal Serial Crystallography to Capture Redox Enzyme Catalysis and Dynamics. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 72 (pp. S38). doi:10.1107/S205327331609940XDOI: 10.1107/S205327331609940X
McPhillie, M., Zhou, Y., El Bissati, K., Dubey, J., Lorenzi, H., Capper, M., . . . McLeod, R. (2016). New paradigms for understanding and step changes in treating active and chronic, persistent apicomplexan infections. SCIENTIFIC REPORTS, 6, 23 pages. doi:10.1038/srep29179DOI: 10.1038/srep29179
Horrell, S., Antonyuk, S. V., Eady, R. R., Hasnain, S. S., Hough, M. A., & Strange, R. W. (2016). Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal. IUCrJ, 3(Part 4), 271-281. doi:10.1107/S205225251600823XDOI: 10.1107/S205225251600823X
Wright, G. S. A., Antonyuk, S. V., & Hasnain, S. S. (2016). A faulty interaction between SOD1 and hCCS in neurodegenerative disease. SCIENTIFIC REPORTS, 6. doi:10.1038/srep27691DOI: 10.1038/srep27691
Fresh insight to functioning of selected enzymes of the nitrogen cycle (Journal article)
Eady, R. R., Antonyuk, S. V., & Hasnain, S. S. (2016). Fresh insight to functioning of selected enzymes of the nitrogen cycle. CURRENT OPINION IN CHEMICAL BIOLOGY, 31, 103-112. doi:10.1016/j.cbpa.2016.02.009DOI: 10.1016/j.cbpa.2016.02.009
Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes (Journal article)
Murray, B., Antonyuk, S. V., Marina, A., Lu, S. C., Mato, J. M., Hasnain, S. S., & Rojas, A. L. (2016). Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes. Proceedings of the National Academy of Sciences of USA, 113(8), 2104-2109. doi:10.1073/pnas.1510959113DOI: 10.1073/pnas.1510959113
2015
Blakeley, M. P., Hasnain, S. S., & Antonyuk, S. V. (2015). Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential. IUCRJ, 2, 464-474. doi:10.1107/S2052252515011239DOI: 10.1107/S2052252515011239
Capper, M., O'Neill, P., Fisher, N., Strange, R., Moss, D., Ward, S., . . . Antonyuk, S. (2015). Antimalarial 4(1H)-pyridones bind to the Qi site of cytochrome bc1. Proceedings of the National Academy of Sciences of the United States of America, 112(3), 755-760. doi:10.1073/pnas.1416611112DOI: 10.1073/pnas.1416611112
2014
Structure and function study of the complex that synthesizes <i>S</i>-adenosylmethionine (Journal article)
Murray, B., Antonyuk, S. V., Marina, A., Van Liempd, S. M., Lu, S. C., Mato, J. M., . . . Rojas, A. L. (2014). Structure and function study of the complex that synthesizes <i>S</i>-adenosylmethionine. IUCRJ, 1, 240-249. doi:10.1107/S2052252514012585DOI: 10.1107/S2052252514012585
Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy (Journal article)
Kekilli, D., Dworkowski, F. S. N., Pompidor, G., Fuchs, M. R., Andrew, C. R., Antonyuk, S., . . . Hough, M. A. (2014). Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 70, 1289-1296. doi:10.1107/S1399004714004039DOI: 10.1107/S1399004714004039
Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life (Journal article)
Austin, J. A., Wright, G. S. A., Watanabe, S., Grossmann, J. G., Antonyuk, S. V., Yamanaka, K., & Hasnain. (2014). Disease causing mutants of TDP-43 nucleic acid binding domains are resistant to aggregation and have increased stability and half-life. Proceedings of the National Academy of Sciences of the United States of America, 111(11), 4309-4314. doi:10.1073/pnas.1317317111DOI: 10.1073/pnas.1317317111
The structure of a purple acid phosphatase involved in plant growth and pathogen defence exhibits a novel immunoglobulin-like fold (Journal article)
Antonyuk, S. V., Olczak, M., Olczak, T., Ciuraszkiewicz, J., & Strange, R. W. (2014). The structure of a purple acid phosphatase involved in plant growth and pathogen defence exhibits a novel immunoglobulin-like fold. IUCRJ, 1, 101-109. doi:10.1107/S205225251400400XDOI: 10.1107/S205225251400400X
Fingerprinting Redox and Ligand States in Haem Protein Crystal Structures using Resonance Raman Spectroscopy (Journal article)
Kekili, D., Dworkowski, F. S. N., Pompidor, G., Fuchs, M. R., Andrew, C. R., Antonyuk, S. V., . . . Hough, M. A. (2014). Fingerprinting Redox and Ligand States in Haem Protein Crystal Structures using Resonance Raman Spectroscopy. ACTA CRYST D: Biological Crystallography, 70, 1289-1296.
Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase (Journal article)
Leferink, N. G. H., Antonyuk, S. V., Houwman, J. A., Scrutton, N. S., Eady, R. R., & Hasnain, S. S. (2014). Impact of residues remote from the catalytic centre on enzyme catalysis of copper nitrite reductase. Nature Communications.
2013
Mechanisms of ligand discrimination in cytochrome c' (Conference Paper)
Kekilli, D., Andrew, C. R., Antonyuk, S. V., Strange, R. W., Eady, R. R., Hasnain, S. S., & Hough, M. A. (2013). Mechanisms of ligand discrimination in cytochrome c'. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 69 (pp. S88). doi:10.1107/S0108767313099224DOI: 10.1107/S0108767313099224
Transport of gabapentin by LAT1 (SLC7A5) (Journal article)
Dickens, D., Webb, S. D., Antonyuk, S., Giannoudis, A., Owen, A., Raedisch, S., . . . Pirmohamed, M. (2013). Transport of gabapentin by LAT1 (SLC7A5). BIOCHEMICAL PHARMACOLOGY, 85(11), 1672-1683. doi:10.1016/j.bcp.2013.03.022DOI: 10.1016/j.bcp.2013.03.022
Transport of gabapentin by LAT1 (SLC7A5) (Journal article)
Dickens, D., Webb, S. D., Antonyuk, S., Giannoudis, A., Owen, A., Rädisch, S., . . . Pirmohamed, M. (2013). Transport of gabapentin by LAT1 (SLC7A5). Biochemical Pharmacology, 85(11), 1672-1683. doi:10.1016/j.bcp.2013.03.022DOI: 10.1016/j.bcp.2013.03.022
Ligand binding and aggregation of pathogenic SOD1 (Journal article)
Wright, G. S. A., Antonyuk, S. V., Kershaw, N. M., Strange, R. W., & Hasnain, S. S. (2013). Ligand binding and aggregation of pathogenic SOD1. NATURE COMMUNICATIONS, 4. doi:10.1038/ncomms2750DOI: 10.1038/ncomms2750
Structures of protein-protein complexes involved in electron transfer (Journal article)
Antonyuk, S. V., Han, C., Eady, R. R., & Hasnain, S. S. (2013). Structures of protein-protein complexes involved in electron transfer. NATURE, 496(7443), 123-127. doi:10.1038/nature11996DOI: 10.1038/nature11996
Structure of the hypothetical DUF1811-family protein GK0453 from <i>Geobacillus kaustophilus</i> HTA426 (Journal article)
Padmanabhan, B., Nakamura, Y., Antonyuk, S. V., Strange, R. W., Hasnain, S. S., Yokoyama, S., & Bessho, Y. (2013). Structure of the hypothetical DUF1811-family protein GK0453 from <i>Geobacillus kaustophilus</i> HTA426. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 69, 342-345. doi:10.1107/S1744309113003369DOI: 10.1107/S1744309113003369
Transport of gabapentin by LAT1 (SLC7A5) (Journal article)
Dickens,, D., Webb,, S. D., Antonyuk,, S., Giannoudis,, A., Owen,, A., Rädisch,, S., . . . Pirmohamed,, M. (2013). Transport of gabapentin by LAT1 (SLC7A5). Biochemical Pharmacology, 85, 1672-1683.
X-ray Crystallography and Computational Docking for the Detection and Development of Protein-Ligand Interactions (Journal article)
Kershaw, N. M., Wright, G. S. A., Sharma, R., Antonyuk, S. V., Strange, R. W., Berry, N. G., . . . Hasnain, S. S. (2013). X-ray Crystallography and Computational Docking for the Detection and Development of Protein-Ligand Interactions. CURRENT MEDICINAL CHEMISTRY, 20(4), 569-575. Retrieved from https://www.webofscience.com/
2012
Structural Evidence for a Copper-Bound Carbonate Intermediate in the Peroxidase and Dismutase Activities of Superoxide Dismutase (Journal article)
Strange, R. W., Hough, M. A., Antonyuk, S. V., & Hasnain, S. S. (2012). Structural Evidence for a Copper-Bound Carbonate Intermediate in the Peroxidase and Dismutase Activities of Superoxide Dismutase. PLOS ONE, 7(9). doi:10.1371/journal.pone.0044811DOI: 10.1371/journal.pone.0044811
Classical-style MAD phasing with wavelength interleaving and kappa goniometry on PROXIMA-1 (Conference Paper)
Bricogne, G., Vonrhein, C., Keller, P., Thompson, A., Legrand, P., Cambillau, C., . . . Elliott, P. (2012). Classical-style MAD phasing with wavelength interleaving and kappa goniometry on PROXIMA-1. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 68 (pp. S18). doi:10.1107/S0108767312099655DOI: 10.1107/S0108767312099655
Crystal structure of D-serine dehydratase from <i>Escherichia coli</i> (Journal article)
Urusova, D. V., Isupov, M. N., Antonyuk, S., Kachalova, G. S., Obmolova, G., Vagin, A. A., . . . Schnackerz, K. D. (2012). Crystal structure of D-serine dehydratase from <i>Escherichia coli</i>. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1824(3), 422-432. doi:10.1016/j.bbapap.2011.10.017DOI: 10.1016/j.bbapap.2011.10.017
2011
Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins (Journal article)
Antonyuk, S. V., Rustage, N., Petersen, C. A., Arnst, J. L., Heyes, D. J., Sharma, R., . . . Hasnain, S. S. (2011). Carbon monoxide poisoning is prevented by the energy costs of conformational changes in gas-binding haemproteins. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(38), 15780-15785. doi:10.1073/pnas.1109051108DOI: 10.1073/pnas.1109051108
Monitoring and validating active site redox states in protein crystals (Journal article)
Antonyuk, S. V., & Hough, M. A. (2011). Monitoring and validating active site redox states in protein crystals. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 1814(6), 778-784. doi:10.1016/j.bbapap.2010.12.017DOI: 10.1016/j.bbapap.2010.12.017
Proton-Coupled Electron Transfer in the Catalytic Cycle of <i>Alcaligenes xylosoxidans</i> Copper-Dependent Nitrite Reductase (Journal article)
Leferink, N. G. H., Han, C., Antonyuk, S. V., Heyes, D. J., Rigby, S. E. J., Hough, M. A., . . . Hasnain, S. S. (2011). Proton-Coupled Electron Transfer in the Catalytic Cycle of <i>Alcaligenes xylosoxidans</i> Copper-Dependent Nitrite Reductase. BIOCHEMISTRY, 50(19), 4121-4131. doi:10.1021/bi200246fDOI: 10.1021/bi200246f
Distal-to-Proximal NO Conversion in Hemoproteins: The Role of the Proximal Pocket (Journal article)
Hough, M. A., Antonyuk, S. V., Barbieri, S., Rustage, N., McKay, A. L., Servid, A. E., . . . Hasnain, S. S. (2011). Distal-to-Proximal NO Conversion in Hemoproteins: The Role of the Proximal Pocket. Journal of Molecular Biology, 405(2), 395-409. doi:10.1016/j.jmb.2010.10.035DOI: 10.1016/j.jmb.2010.10.035
Mechanism of Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase (Journal article)
Leferink, N. G. H., Han, C., Antonyuk, S. V., Heyes, D. J., Rigby, S. E. J., Hough, M. A., . . . Hasnain, S. S. (2011). Mechanism of Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes xylosoxidans Copper-Dependent Nitrite Reductase. Biochemistry, 50, 4121-4131. doi:10.1021/biDOI: 10.1021/bi
2010
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization (Journal article)
Antonyuk, S., Strange, R. W., & Hasnain, S. S. (2010). Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization. JOURNAL OF MEDICINAL CHEMISTRY, 53(3), 1402-1406. doi:10.1021/jm9017948DOI: 10.1021/jm9017948
2009
Structure of D-lactate dehydrogenase from <i>Aquifex aeolicus</i> complexed with NAD<SUP>+</SUP> and lactic acid (or pyruvate) (Journal article)
Antonyuk, S. V., Strange, R. W., Ellis, M. J., Bessho, Y., Kuramitsu, S., Inoue, Y., . . . Hasnain, S. S. (2009). Structure of D-lactate dehydrogenase from <i>Aquifex aeolicus</i> complexed with NAD<SUP>+</SUP> and lactic acid (or pyruvate). ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1209-1213. doi:10.1107/S1744309109044935DOI: 10.1107/S1744309109044935
Structure of SurE protein from <i>Aquifex aeolicus</i> VF5 at 1.5 Å resolution (Journal article)
Antonyuk, S. V., Ellis, M. J., Strange, R. W., Bessho, Y., Kuramitsu, S., Shinkai, A., . . . Hasnain, S. S. (2009). Structure of SurE protein from <i>Aquifex aeolicus</i> VF5 at 1.5 Å resolution. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1204-1208. doi:10.1107/S1744309109043814DOI: 10.1107/S1744309109043814
Structure of a putative β-phosphoglucomutase (TM1254) from <i>Thermotoga maritima</i> (Journal article)
Strange, R. W., Antonyuk, S. V., Ellis, M. J., Bessho, Y., Kuramitsu, S., Shinkai, A., . . . Hasnain, S. S. (2009). Structure of a putative β-phosphoglucomutase (TM1254) from <i>Thermotoga maritima</i>. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1218-1221. doi:10.1107/S1744309109046302DOI: 10.1107/S1744309109046302
Structure of dihydrodipicolinate synthase from <i>Methanocaldococcus jannaschii</i> (Journal article)
Padmanabhan, B., Strange, R. W., Antonyuk, S. V., Ellis, M. J., Hasnain, S. S., Iino, H., . . . Yokoyama, S. (2009). Structure of dihydrodipicolinate synthase from <i>Methanocaldococcus jannaschii</i>. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1222-1226. doi:10.1107/S174430910904651XDOI: 10.1107/S174430910904651X
Structure of glyceraldehyde-3-phosphate dehydrogenase from the archaeal hyperthermophile <i>Methanocaldococcus jannaschii</i> (Journal article)
Malay, A. D., Bessho, Y., Ellis, M. J., Antonyuk, S. V., Strange, R. W., Hasnain, S. S., . . . Yokoyama, S. (2009). Structure of glyceraldehyde-3-phosphate dehydrogenase from the archaeal hyperthermophile <i>Methanocaldococcus jannaschii</i>. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1227-1233. doi:10.1107/S1744309109047046DOI: 10.1107/S1744309109047046
Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from <i>Sulfolobus tokodaii</i> (Journal article)
Antonyuk, S. V., Strange, R. W., Ellis, M. J., Bessho, Y., Kuramitsu, S., Shinkai, A., . . . Hasnain, S. S. (2009). Structure of hypothetical Mo-cofactor biosynthesis protein B (ST2315) from <i>Sulfolobus tokodaii</i>. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1200-1203. doi:10.1107/S1744309109043772DOI: 10.1107/S1744309109043772
Structure of putative 4-amino-4-deoxychorismate lyase from <i>Thermus thermophilus</i> HB8 (Journal article)
Padmanabhan, B., Bessho, Y., Ebihara, A., Antonyuk, S. V., Ellis, M. J., Strange, R. W., . . . Yokoyama, S. (2009). Structure of putative 4-amino-4-deoxychorismate lyase from <i>Thermus thermophilus</i> HB8. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1234-1239. doi:10.1107/S1744309109050052DOI: 10.1107/S1744309109050052
The structure of an archaeal ribose-5-phosphate isomerase from <i>Methanocaldococcus jannaschii</i> (MJ1603) (Journal article)
Strange, R. W., Antonyuk, S. V., Ellis, M. J., Bessho, Y., Kuramitsu, S., Yokoyama, S., & Hasnain, S. S. (2009). The structure of an archaeal ribose-5-phosphate isomerase from <i>Methanocaldococcus jannaschii</i> (MJ1603). ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 65, 1214-1217. doi:10.1107/S1744309109044923DOI: 10.1107/S1744309109044923
A Multi-Spectral Approach to Understanding Catalysis in CU Nitrite Reductase (Conference Paper)
Hough, M., Antonyuk, S., Strange, R., Eady, R., & Hasnain, S. (2009). A Multi-Spectral Approach to Understanding Catalysis in CU Nitrite Reductase. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 65 (pp. S35). doi:10.1107/S0108767309099334DOI: 10.1107/S0108767309099334
The Structure of Human Extracellular Copper-Zinc Superoxide Dismutase at 1.7 Å Resolution: Insights into Heparin and Collagen Binding (Journal article)
Antonyuk, S. V., Strange, R. W., Marklund, S. L., & Hasnain, S. S. (2009). The Structure of Human Extracellular Copper-Zinc Superoxide Dismutase at 1.7 Å Resolution: Insights into Heparin and Collagen Binding. JOURNAL OF MOLECULAR BIOLOGY, 388(2), 310-326. doi:10.1016/j.jmb.2009.03.026DOI: 10.1016/j.jmb.2009.03.026
Crystal structure of human prion protein bound to a therapeutic antibody (Journal article)
Antonyuk, S. V., Trevitt, C. R., Strange, R. W., Jackson, G. S., Sangar, D., Batchelor, M., . . . Collinge, J. (2009). Crystal structure of human prion protein bound to a therapeutic antibody. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 106(8), 2554-2558. doi:10.1073/pnas.0809170106DOI: 10.1073/pnas.0809170106
Small molecules that lower superoxide dismutase SOD1 as potential therapeutics for familial amyotrophic lateral sclerosis (Conference Paper)
Reitz, A. B., Hasnain, S. S., Antonyuk, S. V., Benjamin, D. E., & Kinney, W. A. (2009). Small molecules that lower superoxide dismutase SOD1 as potential therapeutics for familial amyotrophic lateral sclerosis. In ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY Vol. 238. Retrieved from https://www.webofscience.com/
Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A (Journal article)
Galaleldeen, A., Strange, R. W., Whitson, L. J., Antonyuk, S. V., Narayana, N., Taylor, A. B., . . . Hart, P. J. (2009). Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 492(1-2), 40-47. doi:10.1016/j.abb.2009.09.020DOI: 10.1016/j.abb.2009.09.020
2008
Crystallography with X-ray and optical spectroscopies for metalloproteins structural studies (Conference Paper)
Hasnain, S., Strange, R., Hough, M., Eady, R., Antonyuk, S., & Ellis, M. (2008). Crystallography with X-ray and optical spectroscopies for metalloproteins structural studies. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 64 (pp. C110). doi:10.1107/S0108767308096487DOI: 10.1107/S0108767308096487
Seeing hydrogens: X-ray limitations and possibilities at 0.9 Å and synergy with neutron diffraction (Conference Paper)
Antonyuk, S., Eady, R. R., & Hasnain, S. S. (2008). Seeing hydrogens: X-ray limitations and possibilities at 0.9 Å and synergy with neutron diffraction. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 64 (pp. C101). doi:10.1107/S0108767308096761DOI: 10.1107/S0108767308096761
Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis (Journal article)
Cao, X., Antonyuk, S. V., Seetharaman, S. V., Whitson, L. J., Taylor, A. B., Holloway, S. P., . . . Hart, P. J. (2008). Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. JOURNAL OF BIOLOGICAL CHEMISTRY, 283(23), 16169-16177. doi:10.1074/jbc.M801522200DOI: 10.1074/jbc.M801522200
Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase (Journal article)
Hough, M. A., Antonyuk, S. V., Strange, R. W., Eady, R. R., & Hasnain, S. S. (2008). Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductase. JOURNAL OF MOLECULAR BIOLOGY, 378(2), 353-361. doi:10.1016/j.jmb.2008.01.097DOI: 10.1016/j.jmb.2008.01.097
2006
X-ray diffraction study of the complex of the enzyme SAICAR synthase with the reaction product (Journal article)
Urusova, D. V., Levdikov, V. M., Antonyuk, S. V., Grebenko, A. I., Lamzin, V. S., & Melik-Adamyan, V. R. (2006). X-ray diffraction study of the complex of the enzyme SAICAR synthase with the reaction product. CRYSTALLOGRAPHY REPORTS, 51(5), 824-827. doi:10.1134/S1063774506050129DOI: 10.1134/S1063774506050129
Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from <i>Achromobacter cycloclastes</i> (Journal article)
Paraskevopoulos, K., Antonyuk, S. V., Sawers, R. G., Eady, R. R., & Hasnain, S. S. (2006). Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from <i>Achromobacter cycloclastes</i>. JOURNAL OF MOLECULAR BIOLOGY, 362(1), 55-65. doi:10.1016/j.jmb.2006.06.064DOI: 10.1016/j.jmb.2006.06.064
Variable metallation of human superoxide dismutase: Atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes (Journal article)
Strange, R. W., Antonyuk, S. V., Hough, M. A., Doucette, P. A., Valentine, J. S., & Hasnain, S. S. (2006). Variable metallation of human superoxide dismutase: Atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. JOURNAL OF MOLECULAR BIOLOGY, 356(5), 1152-1162. doi:10.1016/j.jmb.2005.11.081DOI: 10.1016/j.jmb.2005.11.081
2005
Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism (Journal article)
Antonyuk, S. V., Strange, R. W., Sawers, G., Eady, R. R., & Hasnain, S. S. (2005). Atomic resolution structures of resting-state, substrate- and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 102(34), 12041-12046. doi:10.1073/pnas.0504207102DOI: 10.1073/pnas.0504207102
High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase (Journal article)
Hough, M. A., Ellis, M. J., Antonyuk, S., Strange, R. W., Sawers, G., Eady, R. R., & Hasnain, S. S. (2005). High resolution structural studies of mutants provide insights into catalysis and electron transfer processes in copper nitrite reductase. JOURNAL OF MOLECULAR BIOLOGY, 350(2), 300-309. doi:10.1016/j.jmb.2005.04.006DOI: 10.1016/j.jmb.2005.04.006
A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler (Conference Paper)
Cianci, M., Antonyuk, S., Bliss, N., Bailey, M. W., Buffey, S. G., Cheung, K. C., . . . Hasnain, S. S. (2005). A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wiggler. In JOURNAL OF SYNCHROTRON RADIATION Vol. 12 (pp. 455-466). doi:10.1107/S0909049505009131DOI: 10.1107/S0909049505009131
Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg (Journal article)
Antonyuk, S., Elam, J. S., Hough, M. A., Strange, R. W., Doucette, P. A., Rodriguez, J. A., . . . Hasnain, S. S. (2005). Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg. PROTEIN SCIENCE, 14(5), 1201-1213. doi:10.1110/ps.041256705DOI: 10.1110/ps.041256705
A high throughput structural biology / proteomics beamline at the SRS on a new multipole wiggler. (Journal article)
Cianci, M., Antonyuk, S., Bliss, N., Buffet, S. G., Cheung, K. C., Clarke, J. A., . . . Hasnain, S. S. (2005). A high throughput structural biology / proteomics beamline at the SRS on a new multipole wiggler.. J. Synchr. Rad., 12, 442-452.
Combined X-ray approach for studying metalloproteins function/misfunction: a powerful approach to metallogenomics (Conference Paper)
Hasnain, S., Strange, R., Antonyuk, S., Grossmann, G., Ellis, M., Hough, M., . . . Cole, R. (2005). Combined X-ray approach for studying metalloproteins function/misfunction: a powerful approach to metallogenomics. In FEBS JOURNAL Vol. 272 (pp. 87-88). Retrieved from https://www.webofscience.com/
Variable metallation of wild type human superoxide dismutase (Conference Paper)
Antonyuk, S. V., Strange, R. W., Hough, M. A., Valentine, J. S., & Hasnain, S. S. (2005). Variable metallation of wild type human superoxide dismutase. In FEBS JOURNAL Vol. 272 (pp. 119). Retrieved from https://www.webofscience.com/
2004
Insights into redox partner interactions and substrate binding in nitrite reductase from <i>Alcaligenes xylosoxidans</i>:: Crystal structures of the TrP138His and His313Gln mutants (Journal article)
Barrett, M. L., Harris, R. L., Antonyuk, S., Hough, M. A., Ellis, M. J., Sawers, G., . . . Hasnain, S. S. (2004). Insights into redox partner interactions and substrate binding in nitrite reductase from <i>Alcaligenes xylosoxidans</i>:: Crystal structures of the TrP138His and His313Gln mutants. BIOCHEMISTRY, 43(51), 16311-16319. doi:10.1021/bi048682gDOI: 10.1021/bi048682g
Observation of an unprecedented Cu bis-His site: Crystal structure of the H129V mutant of nitrite reductase (Journal article)
Ellis, M. J., Antonyuk, S. V., Strange, R. W., Sawers, G., Eady, R. R., & Hasnain, S. S. (2004). Observation of an unprecedented Cu bis-His site: Crystal structure of the H129V mutant of nitrite reductase. INORGANIC CHEMISTRY, 43(24), 7591-7593. doi:10.1021/ic048966pDOI: 10.1021/ic048966p
Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants (Journal article)
Hough, M. A., Grossmann, J. G., Antonyuk, S. V., Strange, R. W., Doucette, P. A., Rodriguez, J. A., . . . Hasnain, S. S. (2004). Dimer destabilization in superoxide dismutase may result in disease-causing properties: Structures of motor neuron disease mutants. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 101(16), 5976-5981. doi:10.1073/pnas.0305143101DOI: 10.1073/pnas.0305143101
Nitrous Oxide Reductase (Chapter)
Eady, R. R., Antonyuk, S. V., & Hasnain, S. S. (2004). Nitrous Oxide Reductase. Wiley. doi:10.1002/0470028637.met205DOI: 10.1002/0470028637.met205
2003
X-ray diffraction study of the complex of the enzyme SAICAR synthase with substrate analogues (Journal article)
Urusova, D. V., Antonyuk, S. V., Grebenko, A. I., Lamzin, V. S., & Melik-Adamyan, V. R. (2003). X-ray diffraction study of the complex of the enzyme SAICAR synthase with substrate analogues. CRYSTALLOGRAPHY REPORTS, 48(5), 763-767. doi:10.1134/1.1612597DOI: 10.1134/1.1612597
Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS (Journal article)
Elam, J. S., Taylor, A. B., Strange, R., Antonyuk, S., Doucette, P. A., Rodriguez, J. A., . . . Hart, P. J. (2003). Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. NATURE STRUCTURAL BIOLOGY, 10(6), 461-467. doi:10.1038/nsb935DOI: 10.1038/nsb935
The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis (Journal article)
Strange, R. W., Antonyuk, S., Hough, M. A., Doucette, P. A., Rodriguez, J. A., Hart, P. J., . . . Hasnain, S. S. (2003). The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. JOURNAL OF MOLECULAR BIOLOGY, 328(4), 877-891. doi:10.1016/S0022-2836(03)00355-3DOI: 10.1016/S0022-2836(03)00355-3
The structure of glyceraldehyde 3-phosphate dehydrogenase from <i>Alcaligenes xylosoxidans</i> at 1.7 Å resolution (Journal article)
Antonyuk, S. V., Eady, R. R., Strange, R. W., & Hasnain, S. S. (2003). The structure of glyceraldehyde 3-phosphate dehydrogenase from <i>Alcaligenes xylosoxidans</i> at 1.7 Å resolution. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 59, 835-842. doi:10.1107/S0907444903041441DOI: 10.1107/S0907444903041441
X-ray diffraction study of the complex of the enzyme SAICAR synthase with substrate analogues (Journal article)
Urusova, D. V., Antonyuk, S. V., Grebenko, A. I., Lamzin, V. S., & Melik-Adamyan, V. R. (2003). X-ray diffraction study of the complex of the enzyme SAICAR synthase with substrate analogues. Kristallografiya, 48(5), 821-826.
2002
HIGH RESOLUTION STRUCTURES OF WILD TYPE AND APO HUMAN CuZn SUPEROXIDE DISMUTASE AND ITS FALSRELATED MUTANTS (Conference Paper)
Antonyuk, S. V., Hough, M. A., Strange, R. W., Doucette, P., Hart, P. J., Valentine, J. S., & Hasnain, S. S. (2002). HIGH RESOLUTION STRUCTURES OF WILD TYPE AND APO HUMAN CuZn SUPEROXIDE DISMUTASE AND ITS FALSRELATED MUTANTS. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 58 (pp. C116). doi:10.1107/S0108767302089687DOI: 10.1107/S0108767302089687
Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from <i>Thiobacillus ferrooxidans</i>:: Insights into the structural relationship with the cupredoxins and the multi copper proteins (Journal article)
Kanbi, L. D., Antonyuk, S., Hough, M. A., Hall, J. F., Dodd, F. E., & Hasnain, S. S. (2002). Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from <i>Thiobacillus ferrooxidans</i>:: Insights into the structural relationship with the cupredoxins and the multi copper proteins. JOURNAL OF MOLECULAR BIOLOGY, 320(2), 263-275. doi:10.1016/S0022-2836(02)00443-6DOI: 10.1016/S0022-2836(02)00443-6
Resolution improvement from '<i>in situ</i> annealing' of copper nitrite reductase crystals (Journal article)
Ellis, M. J., Antonyuk, S., & Hasnain, S. S. (2002). Resolution improvement from '<i>in situ</i> annealing' of copper nitrite reductase crystals. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 58, 456-458. doi:10.1107/S0907444902000136DOI: 10.1107/S0907444902000136
2001
X-ray diffraction study of the complexes of SAICAR synthase with adenosinetriphosphate (Journal article)
Antonyuk, S. V., Grebenko, A. I., Levdikov, V. M., Urusova, D. V., Melik-Adamyan, V. R., Lamzin, V. S., & Wilson, K. S. (2001). X-ray diffraction study of the complexes of SAICAR synthase with adenosinetriphosphate. Kristallografiya, 46(4), 687-691.
X-ray diffraction study of the complexes of SAICAR synthase with adenosinetriphosphate (Journal article)
Antonyuk, S. V., Grebenko, A. I., Levdikov, V. M., Urusova, D. V., Melik-Adamyan, V. R., Lamzin, V. S., & Wilson, K. S. (2001). X-ray diffraction study of the complexes of SAICAR synthase with adenosinetriphosphate. CRYSTALLOGRAPHY REPORTS, 46(4), 620-625. doi:10.1134/1.1387127DOI: 10.1134/1.1387127
Crystal structure of manganese catalase from <i>Lactobacillus plantarum</i> (Journal article)
Barynin, V. V., Whittaker, M. M., Antonyuk, S. V., Lamzin, V. S., Harrison, P. M., Artymiuk, P. J., & Whittaker, J. W. (2001). Crystal structure of manganese catalase from <i>Lactobacillus plantarum</i>. STRUCTURE, 9(8), 725-738. doi:10.1016/S0969-2126(01)00628-1DOI: 10.1016/S0969-2126(01)00628-1
2000
Structures of macromolecular compounds: Three-dimensional structure of the enzyme dimanganese catalase from Thermus thermophilus at 1 Å resolution (Journal article)
Antonyuk, S. V., Melik-Adamyan, V. R., Popov, A. N., Lamzin, V. S., Hempstead, P. D., HarrisoN, R. M., . . . Barynin, V. V. (2000). Structures of macromolecular compounds: Three-dimensional structure of the enzyme dimanganese catalase from Thermus thermophilus at 1 Å resolution. Kristallografiya, 45(1), 111-122.
The structure of SAICAR synthase-substrate complexes at 1Å resolution (Conference Paper)
Antonyuk, S. V., Levdikov, V. M., Barynin, V. V., Grebenko, A. I., Urusova, D. V., Popov, A. N., . . . Lamzin, V. S. (2000). The structure of SAICAR synthase-substrate complexes at 1Å resolution. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 56 (pp. S243). doi:10.1107/S010876730002523XDOI: 10.1107/S010876730002523X
Improving the X-ray resolution by reversible flash-cooling combined with concentration screening, as exemplified with PPase (Journal article)
Samygina, V. R., Antonyuk, S. V., Lamzin, V. S., & Popov, A. N. (2000). Improving the X-ray resolution by reversible flash-cooling combined with concentration screening, as exemplified with PPase. ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY, 56, 595-603. doi:10.1107/S0907444900002493DOI: 10.1107/S0907444900002493
The structure of dimanganese catalase from Thermus thermophilus at 1 Å resolution. (Journal article)
Antonyuk, S. V., Melik-Adamyan, W. R., Popov, A. N., Lamzin, V. S., Hepstread, P. D., Harrison, P. M., . . . Barynin, V. V. (2000). The structure of dimanganese catalase from Thermus thermophilus at 1 Å resolution.. Cryst. Reports, 45(1), 11-22.
Three-dimensional structure of the enzyme dimanganese catalase from <i>Thermus thermophilus</i> at 1 Å resolution (Journal article)
Antonyuk, S. V., Melik-Adamyan, V. R., Popov, A. N., Lamzin, V. S., Hempstead, P. D., Harrison, P. M., . . . Barynin, V. V. (2000). Three-dimensional structure of the enzyme dimanganese catalase from <i>Thermus thermophilus</i> at 1 Å resolution. CRYSTALLOGRAPHY REPORTS, 45(1), 105-116. doi:10.1134/1.171145DOI: 10.1134/1.171145
1999
The oxidized (3,3) state of manganese catalase.: Comparison of enzymes from <i>Thermus thermophilus</i> and <i>Lactobacillus plantarum</i> (Journal article)
Whittaker, M. M., Barynin, V. V., Antonyuk, S. V., & Whittaker, J. (1999). The oxidized (3,3) state of manganese catalase.: Comparison of enzymes from <i>Thermus thermophilus</i> and <i>Lactobacillus plantarum</i>. BIOCHEMISTRY, 38(28), 9126-9136. doi:10.1021/bi990499dDOI: 10.1021/bi990499d
THE STRUCTURE OF DI-MANGANESE CATALASE FROM <i>LACTOBACILLUS PLANTARUM</i> AT 1.8 Å RESOLUTION. (Conference Paper)
Barynin, V. V., Harrison, P. M., Artymiuk, P. J., Antonyuk, S. V., Lamzin, V. S., Whittaker, M. M., & Whittaker, J. W. (1999). THE STRUCTURE OF DI-MANGANESE CATALASE FROM <i>LACTOBACILLUS PLANTARUM</i> AT 1.8 Å RESOLUTION.. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 55 (pp. 344). Retrieved from https://www.webofscience.com/
THE STRUCTURE OF DI-MANGANESE CATALASE FROM <i>THERMUS THERMOPHILUS</i> AT 1.0 Å RESOLUTION. (Conference Paper)
Antonyuk, S. V., Melik-Adamyan, W. R., Popov, A. V., Lamzin, V. S., Harrison, P. M., Artymiuk, P. J., & Barynin, V. V. (1999). THE STRUCTURE OF DI-MANGANESE CATALASE FROM <i>THERMUS THERMOPHILUS</i> AT 1.0 Å RESOLUTION.. In ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES Vol. 55 (pp. 339). Retrieved from https://www.webofscience.com/
1990
MANGANESE-CONTAINING CATALASE FROM THERMUS-THERMOPHILUS PEROXIDE-INDUCED REDOX TRANSFORMATION OF MANGANESE IONS IN PRESENCE OF SPECIFIC INHIBITORS OF CATALASE ACTIVITY (Journal article)
KHANGULOV, S. V., BARYNIN, V. V., & ANTONYUKBARYNINA, S. V. (1990). MANGANESE-CONTAINING CATALASE FROM THERMUS-THERMOPHILUS PEROXIDE-INDUCED REDOX TRANSFORMATION OF MANGANESE IONS IN PRESENCE OF SPECIFIC INHIBITORS OF CATALASE ACTIVITY. BIOCHIMICA ET BIOPHYSICA ACTA, 1020(1), 25-33. doi:10.1016/0005-2728(90)90089-MDOI: 10.1016/0005-2728(90)90089-M
Manganese-containing catalase from Thermus thermophilus peroxide induce redox transformations of binuclear cluster of manganese ions. (Journal article)
Khangulov, S. V., Barynin, V. V., & Barynina-Antonyuk, S. V. (1990). Manganese-containing catalase from Thermus thermophilus peroxide induce redox transformations of binuclear cluster of manganese ions.. Biochim. and Biophis. Acta, 1041(2), 25-33.
