Publications
Found 25 results
Filters: Author is Jin, Rongsheng [Clear All Filters]
(2012)
A camelid single-domain antibody neutralizes botulinum neurotoxin A by blocking host receptor binding. Sci Rep. 7, 7438
(2017) (2009) Crystal Structure of the Receptor-Binding Domain of Botulinum Neurotoxin Type HA, Also Known as Type FA or H. Toxins (Basel). 10.3390/toxins9030093
(2017) (2023) High-resolution crystal structure of HA33 of botulinum neurotoxin type B progenitor toxin complex. Biochem Biophys Res Commun. 446, 568-73
(2014) The hypothetical protein P47 of Clostridium botulinum E1 strain Beluga has a structural topology similar to bactericidal/permeability-increasing protein. Toxicon. 10.1016/j.toxicon.2017.10.012
(2017) (2015)
(2017)
Molecular basis for disruption of E-cadherin adhesion by botulinum neurotoxin A complex. Science. 344, 1405-10
(2014) Neutralizing epitopes on toxin A revealed by the structures of two camelid VHH antibodies. Front Immunol. 13, 978858
(2022) N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A. Nat Struct Mol Biol. 23, 656-62
(2016) (2022)
Structural and biochemical characterization of the protease domain of the mosaic botulinum neurotoxin type HA. Pathog Dis. 10.1093/femspd/fty044
(2018) Structural basis for botulinum neurotoxin E recognition of synaptic vesicle protein 2. Nat Commun. 14, 2338
(2023) (2018) (2021) (2012) Structural Insights into Rational Design of Single-Domain Antibody-Based Antitoxins against Botulinum Neurotoxins. Cell Rep. 30, 2526-2539.e6
(2020) Structure and conformational dynamics of toxin A. Life Sci Alliance. 10.26508/lsa.202201383
(2022) Structure of a bimodular botulinum neurotoxin complex provides insights into its oral toxicity. PLoS Pathog. 9, e1003690
(2013) Structure of the full-length Clostridium difficile toxin B. Nat Struct Mol Biol. 10.1038/s41594-019-0268-0
(2019) (2022) Two VHH Antibodies Neutralize Botulinum Neurotoxin E1 by Blocking Its Membrane Translocation in Host Cells. Toxins (Basel). 10.3390/toxins12100616
(2020) (2018)