Nanobodies: natural single-domain antibodies.

By S. Muyldermans. 2013

2,047 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Radiology, Nuclear Medicine and Imaging

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Citations in the corpus

Accelerating Protein Design Using Autoregressive Generative Models (2019, background): “These sequences contain four highly conserved framework regions interspersed with three variable length, hypermutated complementarity determining regions (CDRs), which makes high-conﬁdence alignments difﬁcult to construct (Muyldermans, 2013).”
Antibody Structure and Function: The Basis for Engineering Therapeutics (2019, background): “The VHH domain structure lacks the human or mouse mAb HC-LC structure (which are hydrophobic at their pairing interface), resulting in a surface that is much more hydrophilic than that of an IgG Fab region [298,299].”
Exploiting sequence and stability information for directing nanobody stability engineering (2017, background): “A general feature of nanobody sequences is their preferential use of more polar residues at four, so-called hallmark positions, which establish the binding to the light chain variable domain (VL) in conventional binders [5] (MSA numbering: positions 40, 47, 49 and 51; Kabat numbering: positions 37, ”
Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice (2021, neutral): “Nanobodies are ∼ 12 to 15 kDa in size, highly stable across a wide range of pH and temperature, display strong binding affinities to target proteins, and can be expressed with high yields in bacterial, yeast, and mammalian expression systems (27, 28).”
Protein design and variant prediction using autoregressive generative models (2021, background): “Antibodies are valuable tools for molecular biology and therapeutics because they can detect low concentrations of target antigens with high sensitivity and speci ﬁ city 6 .”