Immunogenicity and therapeutic targeting of a public neoantigen derived from mutated PIK3CA.
The 2022 SER-CAT Outstanding Science Award was presented to Dr. Brian M. Baker, of the Harper Cancer Research Institute, University of Notre Dame, South Bend, IN, USA, for his outstanding work entitled: Immunogenicity and therapeutic targeting of a public neoantigen derived from mutated PIK3CA.
Award was presented by: SER-CAT Director Professor Bi-Cheng Wang.
Molecular mechanism regulating transcriptional control of the hig toxin‐antitoxin locus of antibiotic-resistance plasmid Rts1 from Proteus vulgaris.
The 2022 SER-CAT Young Investigator Award was presented to Dr. Ian Pavelich, of Emory University School of Medicine, Atlanta, GA, USA, for his outstanding work entitled: Molecular mechanism regulating transcriptional control of the hig toxin-antitoxin locus of antibiotic-resistance plasmid Rts1 from Proteus vulgaris.
Award was presented by: SER-CAT Director Professor Bi-Cheng Wang.
Structure of anhydrotetracycline‐bound Tet(X6) reveals the mechanism for inhibition of type 1 tetracycline destructases.
Inactivation of tetracycline antibiotics by tetracycline destructases (TDases) remains a clinical and agricultural threat. TDases can be classified as type 1 Tet(X)-like TDases and type 2 soil-derived TDases. Type 1 TDases are widely identified in clinical pathogens. A combination therapy of tetracycline and a TDase inhibitor is much needed to rescue the clinical efficacy of tetracyclines. Anhydrotetracycline is a pan-TDase inhibitor that inhibits both type 1 and type 2 TDases...
Regions of hepatitis C virus E2 required for membrane association.
Hepatitis C virus (HCV) uses a hybrid entry mechanism. Current structural data suggest that upon exposure to low pH and Cluster of Differentiation 81 (CD81), the amino terminus of envelope glycoprotein E2 becomes ordered and releases an internal loop with two invariant aromatic residues into the host membrane. Here, we present the structure of an amino-terminally truncated E2 with the membrane binding loop in a bent conformation and the aromatic side chains sequestered...
Structural characterization of protective non‐neutralizing antibodies targeting Crimean‐Congo hemorrhagic fever virus.
Crimean-Congo Hemorrhagic Fever Virus (CCHFV) causes a life-threatening disease with up to a 40% mortality rate. With no approved medical countermeasures, CCHFV is considered a public health priority agent. The non-neutralizing mouse monoclonal antibody (mAb) 13G8 targets CCHFV glycoprotein GP38 and protects mice from lethal CCHFV challenge when administered prophylactically or therapeutically. Here, we reveal the structures of GP38 bound with a human chimeric 13G8 mAb and a newly isolated CC5-17 mAb from a human survivor...
Structure of the catalytically active APOBEC3G bound to a DNA oligonucleotide inhibitor reveals tetrahedral geometry of the transition state.
APOBEC3 proteins (A3s) are enzymes that catalyze the deamination of cytidine to uridine in single-stranded DNA (ssDNA) substrates, thus playing a key role in innate antiviral immunity. However, the APOBEC3 family has also been linked to many mutational signatures in cancer cells, which has led to an intense interest to develop inhibitors of A3's catalytic activity as therapeutics as well as tools to study A3's biochemistry, structure, and cellular function...
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