Results 11 to 20 of about 4,223,808 (257)

Retinol‐induced secretion of human retinol‐binding protein in yeast [PDF]

open access: yesFEBS Letters, 1998
Retinol‐binding protein (RBP) functions as a transporter for retinol (vitamin A) in plasma in higher eukaryotes. We have successfully expressed human RBP in Saccharomyces cerevisiae, and its secretion was found to be induced by retinol also in this lower eukaryote. Reduced induction of secretion by retinol in a temperature‐sensitive sec18‐1 mutant that
Reppe, Sjur   +3 more
openaire   +4 more sources

High resolution crystal structure data of human plasma retinol-binding protein (RBP4) bound to retinol and fatty acids [PDF]

open access: yesData in Brief, 2018
Retinol is transported in vertebrate plasma bound to a protein called retinol-binding protein (RBP4) so far believed to be specific for the vitamin. When the protein is saturated with retinol it binds tightly to another plasma protein, transthyretin ...
Massimiliano Perduca   +4 more
doaj   +2 more sources

Serum amyloid A is a retinol binding protein that transports retinol during bacterial infection

open access: yeseLife, 2014
Retinol plays a vital role in the immune response to infection, yet proteins that mediate retinol transport during infection have not been identified.
Mehabaw G Derebe   +8 more
doaj   +2 more sources

Loss of Retinol-Binding Properties for Plasma Retinol-Binding Protein in Normal Human Epidermis [PDF]

open access: yesJournal of Investigative Dermatology, 1987
Terminal differentiation of the keratinocytes (cornification) has been linked to a restricted supply of retinol. Retinol is distributed to target cells by the retinol-binding protein (RBP), which circulates in the plasma in complex with transthyretin (TTR).
Siegenthaler, Georges   +1 more
openaire   +3 more sources

Mechanism of pH‐induced release of retinol from retinol‐binding protein [PDF]

open access: yesFEBS Letters, 1993
A hypothesis is proposed explaining the mechanism of pH‐induced release of retinol from retinol‐binding protein (RBP). A number of conservative positively charged side chains located on the retinol‐binding face of the RBP molecule are involved in salt bridges with conservative negatively charged groups.
PTYTSIN O. B.   +3 more
openaire   +3 more sources

Identification of Transthyretin Tetramer Kinetic Stabilizers That Are Capable of Inhibiting the Retinol-Dependent Retinol Binding Protein 4-Transthyretin Interaction [PDF]

open access: yes, 2021
Dissociation of transthyretin (TTR) tetramers may lead to misfolding and aggregation of pro-amyloidogenic monomers, which underlies TTR amyloidosis (ATTR) pathophysiology.
Arun, Raja   +7 more
core   +1 more source

Polyclonal aptamer libraries as binding entities on a graphene FET based biosensor for the discrimination of apo- and holo- retinol binding protein 4 [PDF]

open access: yes, 2021
Oligonucleotide DNA aptamers represent an emergently important class of binding entities towards as different analytes as small molecules or even whole cells.
Ann-Kathrin , Kissmann   +9 more
core   +2 more sources

Possible Interacting Proteins for Retinol Binding Protein and Cellular Retinol Binding Protein [PDF]

open access: yes, 2011
Retinol or vitamin A is crucial for many biological processes in the body such as proliferation, differentiation and reproduction. It is mainly stored in the liver and can be broken down to retinoic acid inside the cell. It travels in the circulatory system attached to Retinol Binding Protein (RBP) and its transport into the cell is mediated by the RBP
Cooney, David
core   +5 more sources

TNF receptor–related factor 3 inactivation promotes the development of intrahepatic cholangiocarcinoma through NF‐κB‐inducing kinase–mediated hepatocyte transdifferentiation

open access: yesHepatology, EarlyView., 2022
Abstract Background and Aims Intrahepatic cholangiocarcinoma (ICC) is a deadly but poorly understood disease, and its treatment options are very limited. The aim of this study was to identify the molecular drivers of ICC and search for therapeutic targets.
Yuto Shiode   +16 more
wiley   +1 more source

Genetic predisposition to porto‐sinusoidal vascular disorder: A functional genomic‐based, multigenerational family study

open access: yesHepatology, EarlyView., 2022
A deleterious variant of FCHSD1 results in mTOR pathway overactivation and may cause porto‐sinusoidal vascular disorder (PSVD). The pedigree of the family demonstrated an autosomal dominant disease with variable expressivity. Whole‐genome sequencing and Sanger sequencing both validated the existence of the FCHSD1 variant and the heterozygosity of c ...
Jingxuan Shan   +19 more
wiley   +1 more source

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