Immunoglobulin structure and function as revealed by electron microscopy

KH Roux - International archives of allergy and immunology, 1999 - karger.com
Electron–microscopic (EM) analysis preceded crystallographic analysis [1, 2] of Igs by over a
decade and was for a time the only direct way of analyzing their 3–D molecular structure …

Multivalency in ligand design

VM Krishnamurthy, LA Estroff… - … -based approaches in …, 2006 - Wiley Online Library
We define multivalency to be the operation of multiple molecular recognition events of the
same kind occurring simultaneously between two entities (molecules, molecular aggregates …

Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: a role for flexibility and geometry

KH Roux, L Strelets, OH Brekke, I Sandlie… - the Journal of …, 1998 - journals.aai.org
Various native and hinge-modified forms of Ig with identical Ids were reacted with an anti-Id
mAb, and the resultant immune complexes were analyzed by negative stain immunoelectron …

[HTML][HTML] Solution conformation of wild-type and mutant IgG3 and IgG4 immunoglobulins using crystallohydrodynamics: possible implications for complement activation

Y Lu, SE Harding, TE Michaelsen, E Longman… - Biophysical journal, 2007 - cell.com
We have employed the recently described crystallohydrodynamic approach to compare the
time-averaged domain orientation of human chimeric IgG3wt (wild-type) and IgG4wt as well …

IgG dimers in multidonor-derived immunoglobulins: aspects of generation and function

P Gronski - Current pharmaceutical design, 2006 - ingentaconnect.com
Immunoglobulin G (IgG) concentrates for therapeutic purposes, like passive immunotherapy,
supplementation in inherited or aquired deficiencies or immunomodulation, are prepared …

Human/mouse chimeric monoclonal antibodies with human IgG1, IgG2, IgG3 and IgG4 constant domains: electron microscopic and hydrodynamic characterization

ML Phillips, T Mi-Hua, SL Morrison… - Molecular immunology, 1994 - Elsevier
The unique structure of the human IgG3 constant region with its greatly extended hinge can
clearly be seen in electron micrographs, which compare a series of recombinant proteins …

Idiotypic–anti‐idiotypic complexes and their in vivo metabolism

A Johansson, A Erlandsson, D Eriksson… - … Journal of the …, 2002 - Wiley Online Library
BACKGROUND Different strategies can be used to improve the tumor: non‐tumor ratio of
radiolabeled antibodies in immunotargeting. One approach is to use secondary antibodies …

Variable region domain exchange influences the functional properties of IgG

SL Morrison, SB Porter, KR Trinh, LA Wims… - The Journal of …, 1998 - journals.aai.org
In the present study we have characterized a family of anti-dansyl Abs with the variable
region of the heavy chain on human C κ and the variable region of the light chain on …

Studies on antigen binding by intact and hinge-deleted chimeric antibodies.

C Horgan, K Brown, SH Pincus - Journal of immunology (Baltimore …, 1993 - journals.aai.org
A matched set of chimeric IgG1 and IgG4 antibodies were used to investigate the role of the
IgG hinge in binding to Ag with differing space between the epitopes. Antibodies bearing …

The Fc segment of IgE influences the kinetics of dissociation of a symmetrical bivalent ligand from cyclic dimeric complexes

K Subramanian, D Holowka, B Baird, B Goldstein - Biochemistry, 1996 - ACS Publications
As part of a systematic effort to determine the features of immunoglobulin E− receptor (IgE−
FcεRI) aggregation that are critical for cellular activation, we used fluorescence to examine …