RBP cDNA ORF clone, Gallus gallus(chicken)

Protein-cofactor binding and ultrafast electron transfer in riboflavin binding protein under the spatial confinement of nanoscopic reverse micelles.
Saha R, Rakshit S, Verma PK, Mitra RK, Pal SK
Journal of molecular recognition : JMR26(2)59-66(2013 Feb)

Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.
Maehashi K, Matano M, Kondo A, Yamamoto Y, Udaka S
Chemical senses32(2)183-90(2007 Feb)

Estrogen regulation of chicken riboflavin carrier protein gene is mediated by ERE half sites without direct binding of estrogen receptor.
Bahadur U, Ganjam GK, Vasudevan N, Kondaiah P
Molecular and cellular endocrinology231(1-2)1-11(2005 Feb)

Evaluation of riboflavin binding protein domain interaction using differential scanning calorimetry.
Wasylewski M
Biochimica et biophysica acta1702(2)137-43(2004 Nov)

A comprehensive collection of chicken cDNAs.
Boardman PE, Sanz-Ezquerro J, Overton IM, Burt DW, Bosch E, Fong WT, Tickle C, Brown WR, Wilson SA, Hubbard SJ
Current biology : CB12(22)1965-9(2002 Nov)

Both the hydration and surface charge of the confining volume is expected to largely determine the biochemical reaction dynamics of the riboflavin-binding protein.
Title: Protein-cofactor binding and ultrafast electron transfer in riboflavin binding protein under the spatial confinement of nanoscopic reverse micelles.

The selectivity in the sweet suppression by RBP is consistent with the existence of multiple interaction sites within a single sweet taste receptor.
Title: Riboflavin-binding protein exhibits selective sweet suppression toward protein sweeteners.

Using moxestrol and riboflavin carrier protein promoter/reporter constructs in chicken hepatoma cells, an estrogen response unit (ERU) composed of two consensus ERE 1/2 sites and one non-consensus ERE 1/2 site was identified .
Title: Estrogen regulation of chicken riboflavin carrier protein gene is mediated by ERE half sites without direct binding of estrogen receptor.

Data estimate not only the thermostability of both N- and C-terminal domains of riboflavin-binding protein but also the strength of domain interactions.
Title: Evaluation of riboflavin binding protein domain interaction using differential scanning calorimetry.

Phosporylation of RBP occurs on serines in a single tryptic peptide and is necessary for uptake of riboflavin to developing oocytes. Egg white and egg yolk proteins have the same peptides but have minor difference in Phosporylation.
Title: Highly phosphorylated region of chicken riboflavin-binding protein: chemical characterization and 31P NMR studies.