Publications
Retrouvez les publications importantes de NabGen Technology.
Sélection de publications.
Biosynthetic proteins targeting the SARS-CoV-2 spike as anti-virals, Thébault et al, 2022, PLoS pathogene
SARS-CoV-2 detection using a nanobody-functionalized voltammetric device, Pagneux et al, 2022, Communication medicine
The role of the surface ligand on the performance of electrochemical SARS-CoV-2 antigen biosensors, Szuneritz et al, 2022, Analytical and bioanalytical chemistryPreanalytical
Issues and Cycle Threshold Values in SARS-CoV-2 Real-Time RT-PCR Testing: Should Test Results Include These?, Engelmann et al, 2021, ACS Omega
Extracellular Vesicles as a Platform to Study Cell-Surface Membrane Proteins, Delauzun et al, 2020, Methods
Bivalent Llama Single-Domain Antibody Fragments against Tumor Necrosis Factor have Picomolar Potencies due to Intramolecular Interactions, Beirnaert, 2017, Front. Immunol.
Camelid nanobodies used as crystallization chaperones for different constructs of PorM, a component of the type IX secretion system from Porphyromonas gingivalis, Duhoo et al., 2017, Acta Crystallogr F Struct Biol Commun
Type VI secretion TssK baseplate protein exhibits structural similarity with phage receptor-binding proteins and evolved to bind the membrane complex, Van Son Nguyen, 2017, Nature Microbiologie
Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine-Nanobody Complex, Desmyter et al, 2017, Front Immunol
Biogenesis and structure of the bacterial Type VI secretion membrane core complex, Durand et al, 2015, Nature
Inhibition of Type VI Secretion by an Anti-TssM Llama Nanobody, Nguyen et al, 2015, PLoS One
Production, crystallization and X-ray diffraction analysis of a complex between a fragment of the TssM T6SS protein and a camelid nanobody, Nguyen et al, 2015, Acta Crystallogr F Struct Biol Commun
Camelid nanobodies: killing two birds with one stone, Desmyter et al, 2015, Current Opinion in Structural Biology
Viral infection modulation and neutralization by camelid nanobodies, Desmyter et al, 2013, Proc Natl Acad Sci
Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase, Conrath et al, 2009, Protein Sci
Lateral Recognition of a Dye Hapten by a Llama VHH Domain, Spinelli et al, 2001, J. Mol. Biol.
Camelids heavy chain variable domains provide efficient combining sites to haptens, Spinelli et al, 2000, Biochemistry
The crystal structure of a llama heavy chain variable domain, Spinelli et al, 1996, Nature Structural Biologie
