Results 301 to 310 of about 163,653 (347)

Immunoglobulin variable-region diversity in the zebrafish

Immunogenetics, 2000
As part of an investigation of the immune system in the developing zebrafish, Danio rerio, we cloned and characterized a genomic V(H) segment and a number of cDNAs encoding IgM heavy chains. The genomic V(H) has the characteristic features of V(H) in other vertebrates, including a leader segment interrupted by a short intron, and regulatory and ...
N, Danilova, V S, Hohman, E H, Kim, L A, Steiner   +3 more
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IMMUNOGLOBULIN VARIABLE REGIONS AS IDIOTYPE VACCINES

Infectious Disease Clinics of North America, 1999
This article focuses on the use of immunoglobulin variable regions, including Id, anti-Id, anticlonotypes, and Id engineering as putative vaccines and vaccine strategies for infectious diseases; and specific discussion of Id systems involving antigenic determinants associated with potentially pathogenic organisms.
P S, Hefty, R C, Kennedy
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Selection of Immunoglobulin Variable Regions in Autoimmunity to DNA

Immunological Reviews, 1992
Results from our analyses of variable region gene usage among spontaneous anti-DNA antibodies in autoimmune mice have indicated that both the early IgM and later-appearing IgG autoantibodies to DNA are generated by clonally selected B cells. The recurrent usage of particular variable region genes among all the anti-DNA hybridomas analyzed and reported ...
T N, Marion, D M, Tillman, N T, Jou, R J, Hill   +3 more
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COMMON ORIGIN AND EVOLUTION OF VARIABLE AND CONSTANT REGIONS OF IMMUNOGLOBULINS

International Journal of Immunogenetics, 1976
SUMMARYSequence data show that the immunoglobulins evolved from two sets of paralogous genes: a gene set coding for the V regions and another for the different C regions.A comparison of sequences from these two gene sets shows homology between the V and C sets of genes: this homology is only significant when VH is compared with Cμ1, Cμ2 and Cγ1.
Wuilmart, Christian, Urbain, Jacques
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Identification of genes for variable regions of immunoglobulins that recognize sialylated glycans

Biochemical and Biophysical Research Communications, 2021
We previously reported an antibody (clone ID: FR9, IgM-κ) that recognizes the sialyl oligosaccharide Neu5Acα2,6Galβ1,4GlcNAc as an epitope on glycoproteins and glycolipids. In the present study, we developed an antibody (clone ID: AFR45, IgM-κ) that recognizes Neu5Acα2,3Galβ1,4GlcNAc/Glc as an epitope on glycoproteins and glycolipids and compared the ...
Tetsuya Okuda, Masahiro Kitamara, Shinjiro Kasahara, Katsuya Kato   +3 more
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Immunoglobulin Variable Region Genes

Pathology and Immunopathology Research, 1984
The picture that emerges of a V gene locus, albeit still sketchy, is one of a continuously evolving region, subject on occasion to quite dramatic flux due to the operation of gene conversion, transposing elements, recombination and unequal crossing over.
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Immunoglobulin variable region structure and B-Cell malignancies

International Journal of Hematology, 2001
The enormous diversity of immunoglobulin (Ig) variable (V) gene sequences encoding the antibody repertoire are formed by the somatic recombination of relatively few genetic elements. In B-lineage malignancies, Ig gene rearrangements have been widely used for determining clonality and cell origin.
H, Kiyoi, T, Naoe
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Phylogenetic Aspects of Immunoglobulin Variable Region Diversity

1974
There is now widespread agreement that the antigen-binding function of immunoglobulin molecules is mediated by the variable regions of their heavy and light polypeptide chains. Studies from a number of laboratories have shown that many general features of antibodies, such as the capacity to interact with a given antigen (e.g., dinitrophenyl ...
J M, Kehoe, J D, Capra
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Evolution of unblocked immunoglobulin variable regions in Primates

Journal of Human Evolution, 1972
Abstract Amino-terminal amino acid sequences of unblocked heavy and light chains of immunoglobulin G molecules from adult normal pigtailed monkey, rhesus monkey and human were determined by Edman Degradation using an Automatic Protein Sequencer. These sequences are similar among the three primate species.
An-Chuan Wang, H.Hugh Fudenberg
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Modeling the variable region of immunoglobulins

ImmunoMethods, 1992
The structures of over 30 Fab fragments have been solved using X-ray diffraction methods. The available coordinates are being used to model the variable region of other immunoglobulins for which only the sequence is known. Modeling the combining site of an immunoglobulin is a much more difficult problem than is usually perceived.
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