Zhao, Ziyu, et al. “The Ycf48 Accessory Factor Occupies the Site of the Oxygen-Evolving Manganese Cluster during Photosystem II Biogenesis.”10.1038/s41467-023-40388-6__Nature Communications, vol. 14, 4681, Springer Nature, 2023, doi:10.1038/s41467-023-40388-6.
LibreCat: https://research-explorer.ista.ac.at/record/14040
DOI: 10.1038/s41467-023-40388-6
WoS: 001042606700004

Kravchuk, Vladyslav. Structural and Mechanistic Study of Bacterial Complex I and Its Cyanobacterial Ortholog. Institute of Science and Technology Austria, 2023, doi:10.15479/at:ista:12781.
LibreCat: https://research-explorer.ista.ac.at/record/12781
DOI: 10.15479/at:ista:12781

Vercellino, Irene, and Leonid A. Sazanov. “The Assembly, Regulation and Function of the Mitochondrial Respiratory Chain.”10.1038/s41580-021-00415-0__Nature Reviews Molecular Cell Biology, vol. 23, Springer Nature, 2022, pp. 141–161, doi:10.1038/s41580-021-00415-0.
LibreCat: https://research-explorer.ista.ac.at/record/10182
DOI: 10.1038/s41580-021-00415-0
WoS: 000705697100001
PMID: 34621061

Kampjut, Domen, and Leonid A. Sazanov. “Structure of Respiratory Complex I – An Emerging Blueprint for the Mechanism.”10.1016/j.sbi.2022.102350__Current Opinion in Structural Biology, vol. 74, 102350, Elsevier, 2022, doi:10.1016/j.sbi.2022.102350.
LibreCat: https://research-explorer.ista.ac.at/record/11167
DOI: 10.1016/j.sbi.2022.102350
WoS: 000829029500020
PMID: 35316665

Molina-Granada, David, et al. “Most Mitochondrial DGTP Is Tightly Bound to Respiratory Complex I through the NDUF Subunit.”10.1038/s42003-022-03568-6__Communications Biology, vol. 5, no. 1, 620, Springer Nature, 2022, doi:10.1038/s42003-022-03568-6.
LibreCat: https://research-explorer.ista.ac.at/record/11551
DOI: 10.1038/s42003-022-03568-6
WoS: 000815098500002
PMID:  35739187

Gerle, Christoph, et al. “Structures of Multisubunit Membrane Complexes with the CRYO ARM 200.”10.1093/jmicro/dfac037__Microscopy, vol. 71, no. 5, Oxford University Press, 2022, pp. 249–61, doi:10.1093/jmicro/dfac037.
LibreCat: https://research-explorer.ista.ac.at/record/11648
DOI: 10.1093/jmicro/dfac037
WoS: 000837950900001
PMID: 35861182

Dormeshkin, Dmitri, et al. “Isolation of an Escape-Resistant SARS-CoV-2 Neutralizing Nanobody from a Novel Synthetic Nanobody Library.”10.3389/fimmu.2022.965446__Frontiers in Immunology, vol. 13, 965446, Frontiers Media, 2022, doi:10.3389/fimmu.2022.965446.
LibreCat: https://research-explorer.ista.ac.at/record/12252
DOI: 10.3389/fimmu.2022.965446
WoS: 000862479100001

Amberg, Nicole, et al. “Operation STEM Fatale – How an Equity, Diversity and Inclusion Initiative Has Brought Us to Reflect on the Current Challenges in Cell Biology and Science as a Whole.”10.1242/jcs.260017__Journal of Cell Science, vol. 135, no. 8, 260017, The Company of Biologists, 2022, doi:10.1242/jcs.260017.
LibreCat: https://research-explorer.ista.ac.at/record/12282
DOI: 10.1242/jcs.260017
WoS: 000798123600015
PMID: 35438168

Çoruh, Mehmet Orkun, et al. “PH-Dependent Coloring of Combination Effect Pigments with Anthocyanins from Brassica Oleracea Var. Capitata F. Rubra.”10.3390/colorants1020010__Colorants, vol. 1, no. 2, MDPI, 2022, pp. 149–64, doi:10.3390/colorants1020010.
LibreCat: https://research-explorer.ista.ac.at/record/10945
DOI: 10.3390/colorants1020010

Dormeshkin, Dmitri, et al. “Combining of Synthetic VHH and Immune ScFv Libraries for Pregnancy-Associated Glycoproteins ELISA Development.”10.1007/s00253-022-12022-w__Applied Microbiology and Biotechnology, vol. 106, Springer Nature, 2022, pp. 5093–103, doi:10.1007/s00253-022-12022-w.
LibreCat: https://research-explorer.ista.ac.at/record/11462
DOI: 10.1007/s00253-022-12022-w
WoS: 000813677500001
PMID: 35723693

Kravchuk, Vladyslav, et al. “A Universal Coupling Mechanism of Respiratory Complex I.”10.1038/s41586-022-05199-7__Nature, vol. 609, no. 7928, Springer Nature, 2022, pp. 808–14, doi:10.1038/s41586-022-05199-7.
LibreCat: https://research-explorer.ista.ac.at/record/12138
DOI: 10.1038/s41586-022-05199-7
WoS: 000854788200001
PMID: 36104567

Abas, Lindy, et al. “Naphthylphthalamic Acid Associates with and Inhibits PIN Auxin Transporters.”10.1073/pnas.2020857118__PNAS, vol. 118, no. 1, e2020857118, National Academy of Sciences, 2021, doi:10.1073/pnas.2020857118.
LibreCat: https://research-explorer.ista.ac.at/record/8993
DOI: 10.1073/pnas.2020857118
WoS: 000607270100073
PMID: 33443187

Kampjut, Domen, et al. “Cryo-EM Grid Optimization for Membrane Proteins.”10.1016/j.isci.2021.102139__IScience, vol. 24, no. 3, 102139, Elsevier, 2021, doi:10.1016/j.isci.2021.102139.
LibreCat: https://research-explorer.ista.ac.at/record/9205
DOI: 10.1016/j.isci.2021.102139
WoS: 000631646000012
PMID: 33665558

Vercellino, Irene, and Leonid A. Sazanov. “Structure and Assembly of the Mammalian Mitochondrial Supercomplex CIII<sub>2</sub>CIV.”10.1038/s41586-021-03927-z__Nature, vol. 598, no. 7880, Springer Nature, 2021, pp. 364–67, doi:10.1038/s41586-021-03927-z.
LibreCat: https://research-explorer.ista.ac.at/record/10146
DOI: 10.1038/s41586-021-03927-z
WoS: 000704581600001
PMID: 34616041

Çoruh, Mehmet Orkun, et al. “Cryo-EM Structure of a Functional Monomeric Photosystem I from Thermosynechococcus Elongatus Reveals Red Chlorophyll Cluster.”10.1038/s42003-021-01808-9__Communications Biology, vol. 4, no. 1, 304, Springer , 2021, doi:10.1038/s42003-021-01808-9.
LibreCat: https://research-explorer.ista.ac.at/record/10310
DOI: 10.1038/s42003-021-01808-9
WoS: 000627440700001
PMID: 33686186

Khalfaoui-Hassani, Bahia, et al. “Cysteine Mutants of the Major Facilitator Superfamily-Type Transporter CcoA Provide Insight into Copper Import.”10.1128/mbio.01567-21__MBio, vol. 12, no. 4, e01567, American Society for Microbiology, 2021, doi:10.1128/mbio.01567-21.
LibreCat: https://research-explorer.ista.ac.at/record/15274
DOI: 10.1128/mbio.01567-21
PMID: 34281385

Adjobo-Hermans, Merel J. W., et al. “NDUF Deletion Triggers Loss of NDUF in Nduf/ Mice and Leigh Syndrome Patients: A Stabilizing Role for NDUFA.”10.1016/j.bbabio.2020.148213__Biochimica et Biophysica Acta - Bioenergetics, vol. 1861, no. 8, 148213, Elsevier, 2020, doi:10.1016/j.bbabio.2020.148213.
LibreCat: https://research-explorer.ista.ac.at/record/7788
DOI: 10.1016/j.bbabio.2020.148213
WoS: 000540842000012
PMID: 32335026

Gupta, Chitrak, et al. “Charge Transfer and Chemo-Mechanical Coupling in Respiratory Complex I.”10.1021/jacs.9b13450__Journal of the American Chemical Society, vol. 142, no. 20, American Chemical Society, 2020, pp. 9220–30, doi:10.1021/jacs.9b13450.
LibreCat: https://research-explorer.ista.ac.at/record/8040
DOI: 10.1021/jacs.9b13450
WoS: 000537415600020
PMID: 32347721

Gupta, Chitrak, et al. Charge Transfer and Chemo-Mechanical Coupling in Respiratory Complex I. American Chemical Society, 2020, doi:10.1021/jacs.9b13450.s002.
LibreCat: https://research-explorer.ista.ac.at/record/9326
DOI: 10.1021/jacs.9b13450.s002

Gupta, Chitrak, et al. Supporting Information. American Chemical Society , 2020, doi:10.1021/jacs.9b13450.s001.
LibreCat: https://research-explorer.ista.ac.at/record/9713
DOI: 10.1021/jacs.9b13450.s001

Gupta, Chitrak, et al. Movies. American Chemical Society, 2020, doi:10.1021/jacs.9b13450.s002.
LibreCat: https://research-explorer.ista.ac.at/record/9878
DOI: 10.1021/jacs.9b13450.s002

Gutierrez-Fernandez, Javier, et al. “Key Role of Quinone in the Mechanism of Respiratory Complex I.”10.1038/s41467-020-17957-0__Nature Communications, vol. 11, no. 1, 4135, Springer Nature, 2020, doi:10.1038/s41467-020-17957-0.
LibreCat: https://research-explorer.ista.ac.at/record/8318
DOI: 10.1038/s41467-020-17957-0
WoS: 000607072900001
PMID: 32811817

Andrei, Andreea, et al. “Cu Homeostasis in Bacteria: The Ins and Outs.”10.3390/membranes10090242__Membranes, vol. 10, no. 9, 242, MDPI, 2020, doi:10.3390/membranes10090242.
LibreCat: https://research-explorer.ista.ac.at/record/8579
DOI: 10.3390/membranes10090242
WoS: 000581446000001

Pinke, Gergely, et al. “Cryo-EM Structure of the Entire Mammalian F-Type ATP Synthase.”10.1038/s41594-020-0503-8__Nature Structural and Molecular Biology, vol. 27, no. 11, Springer Nature, 2020, pp. 1077–85, doi:10.1038/s41594-020-0503-8.
LibreCat: https://research-explorer.ista.ac.at/record/8581
DOI: 10.1038/s41594-020-0503-8
WoS: 000569299400004
PMID: 32929284

Kampjut, Domen, and Leonid A. Sazanov. “The Coupling Mechanism of Mammalian Respiratory Complex I.”10.1126/science.abc4209__Science, vol. 370, no. 6516, eab09, American Association for the Advancement of Science, 2020, doi:10.1126/science.abc4209.
LibreCat: https://research-explorer.ista.ac.at/record/8737
DOI: 10.1126/science.abc4209
WoS: 000583031800004
PMID: 32972993

Steiner, Julia. Biochemical and Structural Investigation of the Mrp Antiporter, an Ancestor of Complex I. Institute of Science and Technology Austria, 2020, doi:10.15479/AT:ISTA:8353.
LibreCat: https://research-explorer.ista.ac.at/record/8353
DOI: 10.15479/AT:ISTA:8353

Steiner, Julia, and Leonid A. Sazanov. “Structure and Mechanism of the Mrp Complex, an Ancient Cation/Proton Antiporter.”10.7554/eLife.59407__ELife, vol. 9, e59407, eLife Sciences Publications, 2020, doi:10.7554/eLife.59407.
LibreCat: https://research-explorer.ista.ac.at/record/8284
DOI: 10.7554/eLife.59407
WoS: 000562123600001
PMID: 32735215

Kampjut, Domen. Molecular Mechanisms of Mitochondrial Redox-Coupled Proton Pumping Enzymes. Institute of Science and Technology Austria, 2020, doi:10.15479/AT:ISTA:8340.
LibreCat: https://research-explorer.ista.ac.at/record/8340
DOI: 10.15479/AT:ISTA:8340

Temnov, Andrey Alexandrovich, et al. “Protective Properties of the Cultured Stem Cell Proteome Studied in an Animal Model of Acetaminophen-Induced Acute Liver Failure.”10.1007/s11033-019-04765-z__Molecular Biology Reports, Springer, 2019, doi:10.1007/s11033-019-04765-z.
LibreCat: https://research-explorer.ista.ac.at/record/6352
DOI: 10.1007/s11033-019-04765-z
WoS: 000470332600049

Zhou, Long, and Leonid A. Sazanov. “Structure and Conformational Plasticity of the Intact Thermus Thermophilus V/A-Type ATPase.”10.1126/science.aaw9144__Science, vol. 365, no. 6455, ea, AAAS, 2019, doi:10.1126/science.aaw9144.
LibreCat: https://research-explorer.ista.ac.at/record/6859
DOI: 10.1126/science.aaw9144
WoS: 000482464000043
PMID: 31439765

Qi, Chao, et al. “Structural Basis of Sterol Recognition by Human Hedgehog Receptor PTC.”10.1126/sciadv.aaw6490__Science Advances, vol. 5, no. 9, ea, American Association for the Advancement of Science, 2019, doi:10.1126/sciadv.aaw6490.
LibreCat: https://research-explorer.ista.ac.at/record/6919
DOI: 10.1126/sciadv.aaw6490
WoS: 000491128800062

Letts, James A., et al. “Structures of Respiratory Supercomplex I+II Reveal Functional and Conformational Crosstalk.”10.1016/j.molcel.2019.07.022__Molecular Cell, vol. 75, no. 6, Cell Press, 2019, p. 1131–1146.e6, doi:10.1016/j.molcel.2019.07.022.
LibreCat: https://research-explorer.ista.ac.at/record/7395
DOI: 10.1016/j.molcel.2019.07.022
WoS: 000486614200006
PMID: 31492636

Kampjut, Domen, and Leonid A. Sazanov. “Structure and Mechanism of Mitochondrial Proton-Translocating Transhydrogenase.”10.1038/s41586-019-1519-2__Nature, vol. 573, no. 7773, Springer Nature, 2019, pp. 291–295, doi:10.1038/s41586-019-1519-2.
LibreCat: https://research-explorer.ista.ac.at/record/6848
DOI: 10.1038/s41586-019-1519-2
WoS: 000485415400061
PMID: 31462775

Fiedorczuk, Karol, and Leonid A. Sazanov. “Mammalian Mitochondrial Complex I Structure and Disease Causing Mutations.”10.1016/j.tcb.2018.06.006__Trends in Cell Biology, vol. 28, no. 10, Elsevier, 2018, pp. 835–67, doi:10.1016/j.tcb.2018.06.006.
LibreCat: https://research-explorer.ista.ac.at/record/152
DOI: 10.1016/j.tcb.2018.06.006
WoS: 000445118200007

Sazanov, Leonid A. “Structure of Respiratory Complex I: ‘Minimal’ Bacterial and ‘de Luxe’ Mammalian Versions.”10.1039/9781788010405-00025__Mechanisms of Primary Energy Transduction in Biology , edited by Mårten Wikström, Royal Society of Chemistry, 2017, pp. 25–59, doi:10.1039/9781788010405-00025.
LibreCat: https://research-explorer.ista.ac.at/record/444
DOI: 10.1039/9781788010405-00025

Letts, James A., and Leonid A. Sazanov. “Clarifying the Supercomplex: The Higher-Order Organization of the Mitochondrial Electron Transport Chain.”10.1038/nsmb.3460__Nature Structural and Molecular Biology, vol. 24, no. 10, Nature Publishing Group, 2017, pp. 800–08, doi:10.1038/nsmb.3460.
LibreCat: https://research-explorer.ista.ac.at/record/515
DOI: 10.1038/nsmb.3460

Gutierrez-Fernandez, Javier, et al. “Modular Architecture and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L CbpL Contributing to Pneumococcal Pathogenesis.”10.1038/srep38094__Scientific Reports, vol. 6, 38094, Nature Publishing Group, 2016, doi:10.1038/srep38094.
LibreCat: https://research-explorer.ista.ac.at/record/1186
DOI: 10.1038/srep38094

Letts, James A., et al. “Purification of Ovine Respiratory Complex i Results in a Highly Active and Stable Preparation.”10.1074/jbc.M116.735142__Journal of Biological Chemistry, vol. 291, no. 47, American Society for Biochemistry and Molecular Biology, 2016, pp. 24657–75, doi:10.1074/jbc.M116.735142.
LibreCat: https://research-explorer.ista.ac.at/record/1209
DOI: 10.1074/jbc.M116.735142

Fiedorczuk, Karol, et al. “Atomic Structure of the Entire Mammalian Mitochondrial Complex I.”10.1038/nature19794__Nature, vol. 538, no. 7625, Nature Publishing Group, 2016, pp. 406–10, doi:10.1038/nature19794.
LibreCat: https://research-explorer.ista.ac.at/record/1226
DOI: 10.1038/nature19794
PMID: 27595392

Letts, James A., et al. “The Architecture of Respiratory Supercomplexes.”10.1038/nature19774__Nature, vol. 537, no. 7622, Nature Publishing Group, 2016, pp. 644–48, doi:10.1038/nature19774.
LibreCat: https://research-explorer.ista.ac.at/record/1232
DOI: 10.1038/nature19774

Postila, Pekka, et al. “Atomistic Determinants of Co-Enzyme Q Reduction at the Qi-Site of the Cytochrome B Complex.”10.1038/srep33607__Scientific Reports, vol. 6, 33607, Nature Publishing Group, 2016, doi:10.1038/srep33607.
LibreCat: https://research-explorer.ista.ac.at/record/1276
DOI: 10.1038/srep33607

Holt, Peter, et al. “Reversible FMN Dissociation from Escherichia Coli Respiratory Complex I.”10.1016/j.bbabio.2016.08.008__Biochimica et Biophysica Acta - Bioenergetics, vol. 1857, no. 11, Elsevier, 2016, pp. 1777–85, doi:10.1016/j.bbabio.2016.08.008.
LibreCat: https://research-explorer.ista.ac.at/record/1288
DOI: 10.1016/j.bbabio.2016.08.008

Berrisford, John, et al. “Structure of Bacterial Respiratory Complex I.”10.1016/j.bbabio.2016.01.012__Biochimica et Biophysica Acta - Bioenergetics, vol. 1857, no. 7, Elsevier, 2016, pp. 892–901, doi:10.1016/j.bbabio.2016.01.012.
LibreCat: https://research-explorer.ista.ac.at/record/1521
DOI: 10.1016/j.bbabio.2016.01.012

Sazanov, Leonid A. “A Giant Molecular Proton Pump: Structure and Mechanism of Respiratory Complex I.”10.1038/nrm3997__Nature Reviews Molecular Cell Biology, vol. 16, no. 6, Nature Publishing Group, 2015, pp. 375–88, doi:10.1038/nrm3997.
LibreCat: https://research-explorer.ista.ac.at/record/1638
DOI: 10.1038/nrm3997

Letts, James A., and Leonid A. Sazanov. “Gaining Mass: The Structure of Respiratory Complex I-from Bacterial towards Mitochondrial Versions.”10.1016/j.sbi.2015.08.008__Current Opinion in Structural Biology, vol. 33, no. 8, Elsevier, 2015, pp. 135–45, doi:10.1016/j.sbi.2015.08.008.
LibreCat: https://research-explorer.ista.ac.at/record/1683
DOI: 10.1016/j.sbi.2015.08.008