Complement C4b-Binding Protein
"Complement C4b-Binding Protein" 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.
A serum protein that regulates the CLASSICAL COMPLEMENT ACTIVATION PATHWAY. It binds as a cofactor to COMPLEMENT FACTOR I which then hydrolyzes the COMPLEMENT C4B in the CLASSICAL PATHWAY C3 CONVERTASE (C4bC2a).
| Descriptor ID |
D050716
|
| MeSH Number(s) |
D12.776.124.486.274.920.662
|
| Concept/Terms |
Complement C4b-Binding Protein- Complement C4b-Binding Protein
- C4b-Binding Protein, Complement
- Complement C4b Binding Protein
- Protein, Complement C4b-Binding
- C4b-C3b Inactivator Cofactor
- C4b C3b Inactivator Cofactor
- Cofactor, C4b-C3b Inactivator
- C4bC3bINA-Cofactor
- C4bC3bINA Cofactor
- Complement C3b-C4b Inactivator Cofactor
- Complement C3b C4b Inactivator Cofactor
- Complement Component 4b-Binding Protein
- Complement Component 4b Binding Protein
- C4b-Binding Protein
- C4b Binding Protein
- Protein, C4b-Binding
- Complement 4b Binding Protein
|
Below are MeSH descriptors whose meaning is more general than "Complement C4b-Binding Protein".
Below are MeSH descriptors whose meaning is more specific than "Complement C4b-Binding Protein".
This graph shows the total number of publications written about "Complement C4b-Binding Protein" by people in this website by year, and whether "Complement C4b-Binding Protein" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 2017 | 0 | 1 | 1 |
To return to the timeline,
click here.
Below are the most recent publications written about "Complement C4b-Binding Protein" by people in Profiles.
-
Kumar J, Yadav VN, Phulera S, Kamble A, Gautam AK, Panwar HS, Sahu A. Species Specificity of Vaccinia Virus Complement Control Protein for the Bovine Classical Pathway Is Governed Primarily by Direct Interaction of Its Acidic Residues with Factor I. J Virol. 2017 10 01; 91(19).