Unique biochemical nature of carp retinol-binding protein. N-linked glycosylation and uncleavable NH2-terminal signal peptide (Q30661447)

26 June 2017

title

Unique biochemical nature of carp retinol-binding protein. N-linked glycosylation and uncleavable NH2-terminal signal peptide (English)

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26 June 2017

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Bellovino D

1

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26 June 2017

Morimoto T

2

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26 June 2017

Mengheri E

3

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26 June 2017

Perozzi G

4

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26 June 2017

Garaguso I

5

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26 June 2017

Nobili F

6

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26 June 2017

Gaetani S

7

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26 June 2017

language of work or name

English

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publication date

23 January 2001

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Journal of Biological Chemistry

26 June 2017

published in

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26 June 2017

volume

276

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26 June 2017

issue

17

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26 June 2017

page(s)

13949-13956

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Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells

26 June 2017

cites work

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The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP

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21 January 2018

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The primary structure of piscine (Oncorhynchus mykiss) retinol-binding protein and a comparison with the three-dimensional structure of mammalian retinol-binding protein

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Ligand-dependent regulation of intracellular protein transport: effect of vitamin a on the secretion of the retinol-binding protein

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21 January 2018

Identifiers

DOI

10.1074/JBC.M006779200

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