Results 251 to 260 of about 861,248 (298)

Correction to: New CEACAM-targeting 2A3 single-domain antibody-based chimeric antigen receptor T-cells produce anticancer effects in vitro and in vivo. [PDF]

Cancer Immunol Immunother
Jancewicz I, Śmiech M, Winiarska M, Zagozdzon R, Wisniewski P.   +4 more
europepmc   +1 more source

Single domain antibody-scFv conjugate targeting amyloid β and TfR penetrates the blood-brain barrier and interacts with amyloid β. [PDF]

MAbs
Faresjö R, Sjöström EO, Dallas T, Berglund MM, Eriksson J, Sehlin D, Syvänen S.   +6 more
europepmc   +1 more source

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Single-domain antibodies applied as antiviral immunotherapeutics

Journal of Virological Methods, 2023
Viral infections have been the cause of high mortality rates throughout different periods in history. Over the last two decades, outbreaks caused by zoonotic diseases and transmitted by arboviruses have had a significant impact on human health. The emergence of viral infections in different parts of the world encourages the search for new inputs to ...
Nidiane Dantas Reis, Prado, Nairo, Brilhante-Da-Silva, Rosa Maria Oliveira, Sousa, Michelle Suelen da Silva, Morais, Sibele Andrade, Roberto, Marcos Barros, Luiz, Livia Coelho de, Assis, Anna Carolina M, Marinho, Luiz Felipe Lemes de, Araujo, Rafael de Souza, Pontes, Rodrigo Guerino, Stabeli, Carla Freire Celedonio, Fernandes, Soraya Dos Santos, Pereira   +12 more
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Engineering pH-Sensitive Single-Domain Antibodies

2022
There is increasing interest in expanding an antibody beyond high affinity and specificity. One such feature is custom regulation of the binding event, such as pH-dependent control. Here, we provide a methodology for generating single-domain antibodies (sdAbs) that bind their antigen in a pH-dependent fashion.
Tosha M, Laughlin, James R, Horn
openaire   +2 more sources

Single-domain antibodies

2009
The antigen-binding entity of an antibody, reduced in size to one single domain, is referred to as a "single-domain antibody". Various strategies have been explored with variable success to arrive at functional sinlge-domain antibodies. The potential of single-domain antibodies, as research tools or in medicine, is reflected by the three companies ...
Muyldermans, Serge, Hassanzadeh Ghassabeh, Gholamreza, Saerens, Dirk   +2 more
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Nanobodies: Natural Single-Domain Antibodies

Annual Review of Biochemistry, 2013
Sera of camelids contain both conventional heterotetrameric antibodies and unique functional heavy (H)-chain antibodies (HCAbs). The H chain of these homodimeric antibodies consists of one antigen-binding domain, the VHH, and two constant domains.
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Single-Domain Antibodies for Intracellular Toxin Neutralization

2022
Ricin is a plant-derived toxin with a history as a biothreat agent. The toxin's enzymatic subunit, ricin toxin A chain (RTA), is a ribosome-inactivating protein that, when delivered into the cytoplasm of mammalian cells, arrests protein synthesis with extraordinary efficiency.
Timothy F, Czajka, Nicholas J, Mantis
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Multivalent Display of Single-Domain Antibodies

2012
Antigen-binding fragments, such as single-domain antibodies (sdAbs), can now be readily isolated by in vitro technologies. Antibody fragment libraries derived from immune or nonimmune sources are presented in a molecular display format, typically phage display, and binders to individual antigens are selected from the libraries by a so-called panning ...
Zhang, J., MacKenzie, C.R.
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Humanization of Camelid Single-Domain Antibodies

2022
Humanization of therapeutic antibodies derived from animal immunizations is often required to minimize immunogenicity risks in humans, which can cause potentially harmful and serious side effects and reduce antibody efficacy. Humanization is typically applied to conventional monoclonal antibodies derived in rodents as well as single-domain antibodies ...
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Single domain camel antibodies: current status

Reviews in Molecular Biotechnology, 2001
The antigen-binding capacity of the paired variable domains of an antibody is well established. The observation that the isolated heavy chains of anti-hapten antibodies retain some antigen-binding capacity in the absence of light chains led to attempts to obtain an even smaller antigen-binding unit in a VH format.
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