Хайлтын үр дүнгүүд - Mazdak Radjainia

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  1. 1
    Cryo-EM structure of haemoglobin at 3.2 Å determined with the Volta phase plate

    Cryo-EM structure of haemoglobin at 3.2 Å determined with the Volta phase plate -н Maryam Khoshouei, Mazdak Radjainia, Wolfgang Baumeister, Radostin Danev

    Хэвлэсэн 2017
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    Artigo
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  2. 2
    The Structure of the Oligomerization Domain of Lsr2 from Mycobacterium tuberculosis Reveals a Mechanism for Chromosome Organization and Protection

    The Structure of the Oligomerization Domain of Lsr2 from Mycobacterium tuberculosis Reveals a Mechanism for Chromosome Organization and Protection -н E.L. Summers, K. Meindl, Isabel Usón, Alok K. Mitra, Mazdak Radjainia, Roberto Colangeli, David Alland, Vickery L. Arcus

    Хэвлэсэн 2012
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    Artigo
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  3. 3
    Volta phase plate cryo-EM of the small protein complex Prx3

    Volta phase plate cryo-EM of the small protein complex Prx3 -н Maryam Khoshouei, Mazdak Radjainia, Amy Phillips, Juliet A. Gerrard, Alok K. Mitra, Jürgen M. Plitzko, Wolfgang Baumeister, Radostin Danev

    Хэвлэсэн 2016
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    Artigo
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  4. 4
    Direct cell extraction of membrane proteins for structure–function analysis

    Direct cell extraction of membrane proteins for structure–function analysis -н Ieva Drulyte, Aspen Rene Gutgsell, Pilar Lloris-Garcerá, Michael A. Liss, Stefan Geschwindner, Mazdak Radjainia, Jens Frauenfeld, Robin Löving

    Хэвлэсэн 2023
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    Artigo
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  5. 5
    Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State

    Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State -н N. Amy Yewdall, Hariprasad Venugopal, Ambroise Desfosses, Vahid Abrishami, Y. Yosaatmadja, Mark B. Hampton, Juliet A. Gerrard, David C. Goldstone, Alok K. Mitra, Mazdak Radjainia

    Хэвлэсэн 2016
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    Artigo
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  6. 6
    The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates

    The multifunctional histone-like protein Lsr2 protects mycobacteria against reactive oxygen intermediates -н Roberto Colangeli, Aqdus Haq, Vickery L. Arcus, E.L. Summers, Richard S. Magliozzo, Amanda McBride, Alok K. Mitra, Mazdak Radjainia, Abdelahad Khajo, William R. Jacobs, Padmini Salgame, David Alland

    Хэвлэсэн 2009
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    Artigo
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  7. 7
    Structural Basis for Linezolid Binding Site Rearrangement in the <i>Staphylococcus aureus</i> Ribosome

    Structural Basis for Linezolid Binding Site Rearrangement in the <i>Staphylococcus aureus</i> Ribosome -н Matthew J. Belousoff, Zohar Eyal, Mazdak Radjainia, Tofayel Ahmed, Rebecca S. Bamert, Donna Matzov, Anat Bashan, Ella Zimmerman, Satabdi Mishra, David R. Cameron, Hans Elmlund, Anton Y. Peleg, Shashi Bhushan, Trevor Lithgow, Ada Yonath

    Хэвлэсэн 2017
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    Artigo
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  8. 8
    The first transmembrane region of complement component-9 acts as a brake on its self-assembly

    The first transmembrane region of complement component-9 acts as a brake on its self-assembly -н Bradley A. Spicer, Ruby H. P. Law, Tom T. Caradoc-Davies, Sue M. Ekkel, Charles Bayly-Jones, Siew-Siew Pang, Paul J. Conroy, Georg Ramm, Mazdak Radjainia, Hariprasad Venugopal, James C. Whisstock, Michelle A. Dunstone

    Хэвлэсэн 2018
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    Artigo
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  9. 9
    Cryo-EM structure of the active, Gs-protein complexed, human CGRP receptor

    Cryo-EM structure of the active, Gs-protein complexed, human CGRP receptor -н Yi-Lynn Liang, Maryam Khoshouei, Giuseppe Deganutti, Alisa Glukhova, Cassandra Koole, Thomas S. Peat, Mazdak Radjainia, Jürgen M. Plitzko, Wolfgang Baumeister, Laurence J. Miller, Debbie L. Hay, Arthur Christopoulos, Christopher A. Reynolds, Denise Wootten, Patrick M. Sexton

    Хэвлэсэн 2018
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    Artigo
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  10. 10
    Phase-plate cryo-EM structure of a class B GPCR–G-protein complex

    Phase-plate cryo-EM structure of a class B GPCR–G-protein complex -н Yi-Lynn Liang, Maryam Khoshouei, Mazdak Radjainia, Yan Zhang, Alisa Glukhova, Jeffrey Tarrasch, David M. Thal, Sebastian G. B. Furness, George Christopoulos, Thomas Coudrat, Radostin Danev, Wolfgang Baumeister, Laurence J. Miller, Arthur Christopoulos, Brian K. Kobilka, Denise Wootten, Georgios Skiniotis, Patrick M. Sexton

    Хэвлэсэн 2017
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    Artigo
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  11. 11
    The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1

    The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1 -н Siew Siew Pang, Charles Bayly-Jones, Mazdak Radjainia, Bradley A. Spicer, Ruby H. P. Law, Adrian W. Hodel, Edward S. Parsons, Susan M. Ekkel, Paul J. Conroy, Georg Ramm, Hariprasad Venugopal, Phillip I. Bird, Bart W. Hoogenboom, Ilia Voskoboinik, Yann Gambin, Emma Sierecki, Michelle A. Dunstone, James C. Whisstock

    Хэвлэсэн 2019
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    Artigo
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