Results 211 to 220 of about 37,733 (224)
Some of the next articles are maybe not open access.
2004
Retinol-binding protein (RBP) is the retinol-specific transport protein present in plasma. The available crystal structures of different forms of RBP have provided details of the interactions of this binding protein with retinol, retinoids, and transthyretin (TTR, one of the plasma carriers of thyroid hormones).
ZANOTTI, GIUSEPPE, BERNI R.
openaire +4 more sources
Retinol-binding protein (RBP) is the retinol-specific transport protein present in plasma. The available crystal structures of different forms of RBP have provided details of the interactions of this binding protein with retinol, retinoids, and transthyretin (TTR, one of the plasma carriers of thyroid hormones).
ZANOTTI, GIUSEPPE, BERNI R.
openaire +4 more sources
Bakuchiol: A Retinol-Like Functional Compound, Modulating Multiple Retinol and Non-Retinol Targets
2015Bakuchiol (Figure 1.1; Phenol, 4-[1E, 3S]-3-ethenyl-3, 7-dimethyl-1, 6-octadienyl) was rst isolated by Mehta et al. from the Psoralea corylifolia seed in 1973.1 Absolute conguration of bakuchiol was established in the same year by Parakasarao et al.2 Bakuchiol has one asymmetric center and is shown to possess (S)-chirality.3 Mechanistically, both the
openaire +2 more sources
Biochemistry, 1992
The interactions within the molecular complex in which retinol circulates in blood were studied. To monitor binding between retinol-binding protein (RBP) and transthyretin (TTR), TTR was labeled with a long-lived fluorescence probe (pyrene). Changes in the rotational volume of TTR following its association with RBP were monitored by fluorescence ...
Suzanne Scarlata, Eric Slosberg, Noa Noy
openaire +3 more sources
The interactions within the molecular complex in which retinol circulates in blood were studied. To monitor binding between retinol-binding protein (RBP) and transthyretin (TTR), TTR was labeled with a long-lived fluorescence probe (pyrene). Changes in the rotational volume of TTR following its association with RBP were monitored by fluorescence ...
Suzanne Scarlata, Eric Slosberg, Noa Noy
openaire +3 more sources
Retinol transport proteins [PDF]
Biochemical Society Transactions, 1986 John Glover, Helmina O. James, Chen Wy
openaire +2 more sources
PLASMA RETINOL‐BINDING PROTEIN*
Annals of the New York Academy of Sciences, 1980Vitamin A is mobilized from liver stores and transported in plasma in the form of the lipid alcohol retinol, bound to a specific transport protein, retinol-binding protein (RBP). A great deal is known about the chemical structure, metabolism, and biological roles of RBP. RBP is a single polypeptide chain with molecular weight close to 20,000.
openaire +3 more sources
The Affinity of Retinol and its Analogues for Retinol-Binding Protein [PDF]
Biochemical Society Transactions, 1975 John Glover, H. Muhilal
openaire +2 more sources
PROTEIN-BOUND RETINOL OR A RETINOL METABOLITE IN URINE
Nutrition Reviews, 2009openaire +2 more sources