Pub. Date : 2022 Apr 24
PMID : 35565751
6 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. | Tretinoin | cellular retinoic acid binding protein 1 | Homo sapiens |
2 | Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. | Tretinoin | cellular retinoic acid binding protein 1 | Homo sapiens |
3 | Cellular retinoic acid binding proteins (CRABP1 and CRABP2) bind all-trans-retinoic acid (atRA), the active metabolite of vitamin A, with high affinity. | Tretinoin | cellular retinoic acid binding protein 1 | Homo sapiens |
4 | CRABP1 and CRABP2 have been shown to interact with the atRA-clearing cytochrome P450 enzymes CYP26B1 and CYP26C1 and with nuclear retinoic acid receptors (RARs). | Tretinoin | cellular retinoic acid binding protein 1 | Homo sapiens |
5 | We hypothesized that CRABP1 and CRABP2 also alter atRA metabolism and clearance by CYP26A1, the third key atRA-metabolizing enzyme in the CYP26 family. | Tretinoin | cellular retinoic acid binding protein 1 | Homo sapiens |
6 | In comparison, the apparent kcat value was about 30% lower (0.71 +- 0.07 min-1 for holo-CRABP1 and 0.75 +- 0.09 min-1 for holo-CRABP2) in the presence of CRABPs than with free atRA (1.07 +- 0.08 min-1). | Tretinoin | cellular retinoic acid binding protein 1 | Homo sapiens |