Cerebrospinal-fluid-derived Immunoglobulin G of Different Multiple Sclerosis Patients Shares Mutated Sequences in Complementarity Determining Regions [PDF]
Molecular and Cellular Proteomics, 2013 B lymphocytes play a pivotal role in multiple sclerosis pathology, possibly via both antibody-dependent and -independent pathways. Intrathecal immunoglobulin G in multiple sclerosis is produced by clonally expanded B-cell populations.
Vaibhav Singh +2 more
exaly +4 more sources
Functional Consequences of Insertions and Deletions in the Complementarity-determining Regions of Human Antibodies [PDF]
Journal of Biological Chemistry, 2002 Insertions and deletions of nucleotides in the genes encoding the variable domains of antibodies are natural components of the hypermutation process, which may expand the available repertoire of hypervariable loop lengths and conformations. Although insertion of amino acids has also been utilized in antibody engineering, little is known about the ...
Johan, Lantto, Mats, Ohlin
core +6 more sources
Impact of Tryptophan Oxidation in Complementarity-Determining Regions of Two Monoclonal Antibodies on Structure-Function Characterized by Hydrogen-Deuterium Exchange Mass Spectrometry and Surface Plasmon Resonance [PDF]
Pharmaceutical Research, 2018 This work is licensed under a Creative Commons Attribution 4.0 International License.Purpose Tryptophan’s (Trp) unique hydrophobic and structural properties make it an important antigen binding motif when positioned in complementarity-determining ...
Hui Wei, Tapan K Das
exaly +5 more sources
Oxidation in the complementarity-determining regions differentially influences the properties of therapeutic antibodies. [PDF]
MAbs, 2016 Therapeutic antibodies can undergo a variety of chemical modification reactions in vitro. Depending on the site of modification, either antigen binding or Fc-mediated functions can be affected. Oxidation of tryptophan residues is one of the post-translational modifications leading to altered antibody functionality.
Dashivets T +6 more
europepmc +4 more sources
AbFlex: designing antibody complementarity determining regions with flexible CDR definition. [PDF]
BioinformaticsAbstract Motivation Antibodies are proteins that the immune system produces in response to foreign pathogens. Designing antibodies that specifically bind to antigens is a key step in developing antibody therapeutics. The complementarity determining regions (CDRs) of the antibody are mainly responsible
Jeon W, Kim D.
europepmc +3 more sources
Mapping the TNFR2-targeting antibody patent landscape: Insights from macro trends to structural signatures [PDF]
Human Vaccines & ImmunotherapeuticsPharmacological modulation of TNFR2 function has emerged as an effective strategy for modulating immune responses in cancer and inflammatory diseases. Both academic and industrial efforts have pursued therapeutic approaches targeting TNFR2, leading to a ...
Shiyun Chen +6 more
doaj +2 more sources
Tokenizing loops of antibodies [PDF]
mAbsThe complementarity-determining regions (CDRs) of antibodies are loop structures that are key to their interactions with antigens and are of high importance to the design of novel biologics.
Ada Fang +3 more
doaj +2 more sources
Predicting antibody complementarity determining region structures without classification [PDF]
Molecular BioSystems, 2011 Abstract Antibodies are used extensively in medical and biological research. Their complementarity determining regions (CDRs) define the majority of their antigen binding functionality. CDR structures have been intensively studied and classified (canonical structures).
Choi, Y, Deane, C
openaire +3 more sources
Cloning of Size-Selected Human Immunoglobulin Heavy-Chain Rearrangements from Third Complementarity-Determining Region Fingerprint Profiles [PDF]
BioTechniques, 1996 Methods have been developed to rapidly visualize the size distribution of third complementarity-determining regions (CDR3) in immunoglobulin (Ig) and T-cell receptor (TCR) molecules.
Frank M. Raaphorst +2 more
doaj +2 more sources
Human antibody polyreactivity is governed primarily by the heavy-chain complementarity-determining regions. [PDF]
Cell RepAlthough antibody variable regions mediate antigen-specific binding, they can also mediate non-specific interactions with non-cognate antigens, impacting diverse immunological processes and the efficacy, safety, and half-life of antibody therapeutics.
Chen HT +12 more
europepmc +3 more sources