Immunoglobulin kappa-Chains
"Immunoglobulin kappa-Chains" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
One of the types of light chains of the immunoglobulins with a molecular weight of approximately 22 kDa.
Descriptor ID |
D007145
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MeSH Number(s) |
D12.776.124.486.485.705.750.530 D12.776.124.790.651.705.750.530 D12.776.377.715.548.705.750.530
|
Concept/Terms |
Immunoglobulin kappa-Chains- Immunoglobulin kappa-Chains
- Immunoglobulin kappa Chains
- kappa-Chains, Immunoglobulin
- kappa-Immunoglobulin Light Chains
- Light Chains, kappa-Immunoglobulin
- kappa Immunoglobulin Light Chains
- kappa-Chain Immunoglobulins
- kappa Chain Immunoglobulins
- kappa-Immunoglobulin Light Chain
- Light Chain, kappa-Immunoglobulin
- kappa Immunoglobulin Light Chain
- Immunoglobulin kappa-Chain
- Immunoglobulin kappa Chain
- kappa-Chain, Immunoglobulin
- Immunoglobulins, kappa-Chain
- Immunoglobulins, kappa Chain
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Below are MeSH descriptors whose meaning is more general than "Immunoglobulin kappa-Chains".
Below are MeSH descriptors whose meaning is more specific than "Immunoglobulin kappa-Chains".
This graph shows the total number of publications written about "Immunoglobulin kappa-Chains" by people in this website by year, and whether "Immunoglobulin kappa-Chains" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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2002 | 0 | 1 | 1 |
2016 | 0 | 1 | 1 |
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Below are the most recent publications written about "Immunoglobulin kappa-Chains" by people in Profiles.
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Antigen nature and complexity influence human antibody light chain usage and specificity. Vaccine. 2016 05 27; 34(25):2813-20.
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High frequency of matrix attachment regions and cut-like protein x/CCAAT-displacement protein and B cell regulator of IgH transcription binding sites flanking Ig V region genes. J Immunol. 2002 Sep 01; 169(5):2477-87.
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Comparison of the three-dimensional structures of a humanized and a chimeric Fab of an anti-gamma-interferon antibody. J Mol Recognit. 1999 Jan-Feb; 12(1):19-32.
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The influence of the hinge region length in binding of human IgG to human Fcgamma receptors. Hum Immunol. 1998 Nov; 59(11):720-7.