Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures (Q36884646)

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scientific article published on 21 February 2016

Language	Label	Description	Also known as
English	Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures	scientific article published on 21 February 2016

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Ligand Binding Induces Conformational Changes in Human Cellular Retinol-binding Protein 1 (CRBP1) Revealed by Atomic Resolution Crystal Structures (English)

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

crystal structure

1 reference

based on heuristic

inferred from title

1 reference

based on heuristic

inferred from title

author name string

Josie A Silvaroli

1

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Jason M Arne

2

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Sylwia Chelstowska

3

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Philip D Kiser

4

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Surajit Banerjee

5

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Marcin Golczak

6

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

language of work or name

0 references

publication date

21 February 2016

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Journal of Biological Chemistry

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Europe PubMed Central

PMC publication ID

16 August 2017

291

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

16

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

8528-8540

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

Expansion of first-in-class drug candidates that sequester toxic all-trans-retinal and prevent light-induced retinal degeneration

1 reference

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29 September 2017

Structures of holo wild-type human cellular retinol-binding protein II (hCRBPII) bound to retinol and retinal

1 reference

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LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3

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Intracellular transport of fat-soluble vitamins A and E

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Local dynamics of proteins and DNA evaluated from crystallographic B factors

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Functions, therapeutic applications, and synthesis of retinoids and carotenoids

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Retinol and retinyl esters: biochemistry and physiology

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Vitamin A and retinoid signaling: genomic and nongenomic effects

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Receptor-mediated cellular uptake mechanism that couples to intracellular storage

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Overview of the CCP4 suite and current developments

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Retinopathy in mice induced by disrupted all-trans-retinal clearance

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Crystal structure of human cellular retinol-binding protein II to 1.2 A resolution

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Effects of potent inhibitors of the retinoid cycle on visual function and photoreceptor protection from light damage in mice

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Mass spectrometry techniques for detection of ligand-dependent changes in the conformational flexibility of cellular retinol-binding protein type I localized by hydrogen/deuterium exchange

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Overview of retinoid metabolism and function

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Lecithin:retinol acyltransferase is responsible for amidation of retinylamine, a potent inhibitor of the retinoid cycle

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29 September 2017

Positively charged retinoids are potent and selective inhibitors of the trans-cis isomerization in the retinoid (visual) cycle

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The CCP4 suite: programs for protein crystallography

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UCSF Chimera--a visualization system for exploratory research and analysis

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Two homologous rat cellular retinol-binding proteins differ in local conformational flexibility

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Ligand binding and structural analysis of a human putative cellular retinol-binding protein

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Identification and structural analysis of a zebrafish apo and holo cellular retinol-binding protein

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Structure and backbone dynamics of Apo- and holo-cellular retinol-binding protein in solution

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Characterization of a new member of the fatty acid-binding protein family that binds all-trans-retinol

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Retinoid-binding proteins: mediators of retinoid action

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Cellular retinol-binding protein I is essential for vitamin A homeostasis.

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The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure

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Ligand binding alters the backbone mobility of intestinal fatty acid-binding protein as monitored by 15N NMR relaxation and 1H exchange

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Crystal structures of holo and apo-cellular retinol-binding protein II

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Cellular retinol-binding protein. Quantitation and distribution

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Cellular retinol-binding protein from rat liver. Purification and characterization

1 reference

https://pubmed.ncbi.nlm.nih.gov/26900151

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Storage, distribution and utilization of vitamins A in the eyes of adult amphibians and their tadpoles

1 reference

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Identifiers

10.1074/JBC.M116.714535

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 August 2017

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