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1 ly most abundant substrate: retinol bound to cellular retinol-binding protein.
2 induced fit upon ligand binding by mammalian cellular retinol-binding proteins.
4 ptake, storage, and metabolism of retinoids, cellular retinol-binding protein 1 (CRBP1) is essential
6 sents a promising therapeutic strategy, with cellular retinol-binding protein 1 (RBP1) emerging as a
7 uscle actin, and desmin, and negatively with cellular retinol-binding protein 1 and matrix metallopro
8 and increased markers of dedifferentiation, cellular retinol-binding protein 1, and matrix metallopr
11 ssion of the fatty acid binding proteins and cellular retinol binding protein also are down-regulated
13 dehydrogenases (RoDH), which recognize holo-cellular retinol-binding protein as substrate, had been
14 RRD functions with both unbound and CRBP(I) (cellular retinol-binding protein)-bound retinal, but apo
15 , with a Km of approximately 0.7 microM, and cellular retinol-binding protein-bound retinal, with a K
17 activity toward retinoids in the presence of cellular retinol-binding protein (CRBP) type I or cellul
18 ratinocyte lipid-binding protein (KLBP), the cellular retinol-binding protein (CRBP), and the cellula
19 ar retinoic-acid-binding protein (CRABP) and cellular retinol-binding protein (CRBP), as well as thei
26 ding protein II (CRBP II) is a member of the cellular retinol-binding protein family, which is expres
28 enes encoding serum retinol binding protein, cellular retinol binding protein I and cellular retinol
30 etamidodecyl chloromethyl ketone (AcDCMK) or cellular retinol-binding protein I (CRBP) diminished the
34 side the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully e
35 etinoic acid increases the mRNA level of the cellular retinol binding protein II and the rate of reti
36 tein, cellular retinol binding protein I and cellular retinol binding protein II have been disrupted
37 ge of a rationally engineered protein (human cellular retinol binding protein II, hCRBPII) and differ
38 lular retinol-binding protein I (CRBP I) and cellular retinol-binding protein II (CRBP II) are closel
41 structure and backbone dynamics of rat holo cellular retinol-binding protein II (holo-CRBP II) in so
43 NK1/p38 cascade, suppressed CRBP-I/RARalpha (cellular retinol-binding protein/retinoic acid receptor
44 form, at least one retinoid binding protein (cellular retinol binding protein) serves as a retinoid c
45 oreceptor retinoid-binding protein (IRBP) or cellular retinol-binding protein, suggesting that perops
46 es transcriptionally up-regulated by RA, the cellular retinol binding protein type I (CRBPI) and the
47 tinol exists in a bound form, complexed with cellular retinol binding protein type I (holo-CRBP).
48 taken up by the enterocyte is complexed with cellular retinol-binding protein type 2 and the complex
50 rate of retinol oxidation in the presence of cellular retinol-binding protein type I (CRBPI) than hum
52 in the presence of a 10-fold molar excess of cellular retinol-binding protein type I, which is believ
53 ic acid (9cRA)-inducible enhancer of the rat cellular retinol-binding protein type II gene (CRBP II)