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Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2018, Volume 115, Issue 41, pp. E9560 - E9569
The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In ( ),... 
AAA-ATPase | Proteostasis | Mycobacterium tuberculosis | Cryo-EM | Disaggregase | SYSTEM | HSP104 | HSP70 | MULTIDISCIPLINARY SCIENCES | proteostasis | DISAGGREGATION | disaggregase | DNAK | MOLECULAR CHAPERONE | PROTEINS | cryo-EM | CRYO-EM STRUCTURE | Physiological aspects | Genetic aspects | Translocation (Genetics) | Peptides | Observations | Biological Sciences | PNAS Plus
Journal Article
Cell (Cambridge), ISSN 0092-8674, 07/2017, Volume 170, Issue 3, pp. 470 - 482.e11
Voltage-gated sodium (Nav) channels initiate and propagate action potentials. Here, we present the cryo-EM structure of EeNav1.4, the Nav channel from electric... 
Nav1.4 | electromechanical coupling | Nav channels | structural biology | the beta-1 subunit | voltage-gated sodium channels | cryo-EM | fast inactivation | Na(v) channels | Na(v)1.4 | channels | Cryo-EM | 1.4 | The beta-1 subunit | Fast inactivation | Electromechanical coupling | Structural biology | Voltage-gated sodium channels
Journal Article
Proceedings of the National Academy of Sciences - PNAS, ISSN 1091-6490, 2018, Volume 115, Issue 36, pp. 8978 - 8983
Many Gram-positive pathogenic bacteria employ ribosomal protection proteins (RPPs) to confer resistance to clinically important antibiotics. In , the RPP VmlR... 
Ribosome | ABC ATPase | VmlR | Cryo-EM | Antibiotic resistance | TRANSLATIONAL ARREST | COMPLEX | PROTEIN | PEPTIDYL-TRANSFERASE CENTER | SPECIFICITY | MULTIDISCIPLINARY SCIENCES | BOND FORMATION | INHIBITION | antibiotic resistance | ribosome | cryo-EM | CRYO-EM STRUCTURE | STREPTOGRAMIN | Biological Sciences
Journal Article
Cell (Cambridge), ISSN 0092-8674, 2020, Volume 181, Issue 2, pp. 281 - 292.e6
Journal Article
The EMBO journal, ISSN 0261-4189, 2011, Volume 30, Issue 18, pp. 3854 - 3863
Venezuelan equine encephalitis virus (VEEV), a member of the membrane‐containing Alphavirus genus, is a human and equine pathogen, and has been developed as a... 
VEEV | alphavirus | bioweapon | modelling | cryo‐EM | cryo-EM | Cryoelectron Microscopy | Animals | Viral Vaccines | Virulence | Encephalitis Virus, Venezuelan Equine - ultrastructure | Horses | Models, Molecular | Virion - ultrastructure | Viral Proteins - ultrastructure | Viruses | Microbiology | Molecular biology | Biological & chemical weapons
Journal Article
FEBS letters, ISSN 0014-5793, 2017, Volume 591, Issue 17, pp. 2520 - 2533
Journal Article
Science (American Association for the Advancement of Science), ISSN 1095-9203, 2017, Volume 358, Issue 6359, pp. 116 - 119
Journal Article
Nanotechnology, ISSN 1361-6528, 2018, Volume 29, Issue 6, pp. 062001 - 062001
Journal Article