scispace - formally typeset
S

Serge Muyldermans

Researcher at Vrije Universiteit Brussel

Publications -  323
Citations -  30516

Serge Muyldermans is an academic researcher from Vrije Universiteit Brussel. The author has contributed to research in topics: Single-domain antibody & Antibody. The author has an hindex of 80, co-authored 305 publications receiving 26561 citations. Previous affiliations of Serge Muyldermans include Dalian University of Technology & Université libre de Bruxelles.

Papers
More filters
Journal ArticleDOI

Efficient Cancer Therapy with a Nanobody-Based Conjugate

TL;DR: In vivo studies demonstrated that the nanobody-enzyme conjugate had an excellent biodistribution profile and induced regressions and cures of established tumor xenografts, making nanobodies promising vehicles for new generation cancer therapeutics.
Journal ArticleDOI

Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs.

TL;DR: The easy generation steps and the biophysical properties of these bispecific and bivalent constructs based on camel single-domain antibody fragments makes them particularly attractive for use in therapeutic or diagnostic programs.
Journal ArticleDOI

Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains

TL;DR: The mutations and structural adaptations that have taken place to reshape a VH of a Vh-VL pair into a single-domain VHH with retention of a sufficient variability are reviewed.
Journal ArticleDOI

The Therapeutic Potential of Nanobodies

TL;DR: Today, bio-medical efforts are entering the subcellular level, which is witnessed with the fast-developing fields of nanomedicine, nanodiagnostics and nanotherapy in conjunction with the implementation of nanoparticles for disease prevention, diagnosis, therapy and follow-up.
Journal ArticleDOI

Beta-lactamase inhibitors derived from single-domain antibody fragments elicited in the camelidae.

TL;DR: Addition of the VHHs to the TEM-1 β-lactamase, expressed on the surface of bacteria, leads to a higher ampicillin sensitivity of the bacteria, which could generate multiple potent inhibitors for all types of β- lactamases.