Tacrolimus Binding Proteins
"Tacrolimus Binding Proteins" 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 family of immunophilin proteins that bind to the immunosuppressive drugs TACROLIMUS (also known as FK506) and SIROLIMUS. EC 5.2.1.-
| Descriptor ID |
D022021
|
| MeSH Number(s) |
D08.811.399.325.500.400.700 D12.776.543.750.705.400.700 D12.776.827.275.700
|
| Concept/Terms |
Tacrolimus Binding Proteins- Tacrolimus Binding Proteins
- FK506 Binding Protein
- FK506-Binding Protein
- Protein, FK506-Binding
- FKBP Rotamase
- Rotamase, FKBP
- FK506 Binding Proteins
- FK-506-Binding Protein
- FK 506 Binding Protein
- Protein, FK-506-Binding
- FKBP
Rapamycin Binding Proteins- Rapamycin Binding Proteins
- Binding Proteins, Rapamycin
- Rapamycin-Binding Proteins
- Proteins, Rapamycin-Binding
|
Below are MeSH descriptors whose meaning is more general than "Tacrolimus Binding Proteins".
Below are MeSH descriptors whose meaning is more specific than "Tacrolimus Binding Proteins".
This graph shows the total number of publications written about "Tacrolimus Binding Proteins" by people in this website by year, and whether "Tacrolimus Binding Proteins" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2004 | 0 | 1 | 1 |
| 2015 | 1 | 0 | 1 |
| 2019 | 1 | 0 | 1 |
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Below are the most recent publications written about "Tacrolimus Binding Proteins" by people in Profiles.
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Working memory reflects vulnerability to early life adversity as a risk factor for substance use disorder in the FKBP5 cortisol cochaperone polymorphism, rs9296158. PLoS One. 2019; 14(6):e0218212.
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Early-Life Adversity Interacts with FKBP5 Genotypes: Altered Working Memory and Cardiac Stress Reactivity in the Oklahoma Family Health Patterns Project. Neuropsychopharmacology. 2016 06; 41(7):1724-32.
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Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions. Biochemistry. 2004 Jun 29; 43(25):8217-29.