Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36 (Q24338905)

15

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Peter Loppnau

9

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Michael Schwake

2

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Paul Saftig

13

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Sergio Grinstein

14

object named as

Sergio Grinstein

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author name string

Dante Neculai

1

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Mani Ravichandran

3

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Friederike Zunke

4

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Richard F Collins

5

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Judith Peters

6

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Mirela Neculai

7

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Jonathan Plumb

8

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Juan Carlos Pizarro

10

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Alma Seitova

11

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William S Trimble

Scavenger receptors in homeostasis and immunity

12

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language of work or name

English

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publication date

5 December 2013

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published in

Nature

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volume

504

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issue

7478

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page(s)

172-6

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cites work

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Exoplasmic cysteine Cys384 of the HDL receptor SR-BI is critical for its sensitivity to a small-molecule inhibitor and normal lipid transport activity

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Assignment of disulfide bridges in bovine CD36.

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LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase

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Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase

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A critical histidine residue within LIMP-2 mediates pH sensitive binding to its ligand β-glucocerebrosidase.

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Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands and acts as a co-receptor for TLR2.

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Identification on human CD36 of a domain (155-183) implicated in binding oxidized low-density lipoproteins (Ox-LDL).

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Novel ENU-induced point mutation in scavenger receptor class B, member 1, results in liver specific loss of SCARB1 protein

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Functional characterization of newly-discovered mutations in human SR-BI

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Mapping and characterization of the binding site for specific oxidized phospholipids and oxidized low density lipoprotein of scavenger receptor CD36.

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The role of the high-density lipoprotein receptor SR-BI in the lipid metabolism of endocrine and other tissues

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The efficient cellular uptake of high density lipoprotein lipids via scavenger receptor class B type I requires not only receptor-mediated surface binding but also receptor-specific lipid transfer mediated by its extracellular domain

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Highly purified scavenger receptor class B, type I reconstituted into phosphatidylcholine/cholesterol liposomes mediates high affinity high density lipoprotein binding and selective lipid uptake

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Discovery of chemical inhibitors of the selective transfer of lipids mediated by the HDL receptor SR-BI.

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Identification of the molecular target of small molecule inhibitors of HDL receptor SR-BI activity

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Contributions of a disulfide bond and a reduced cysteine side chain to the intrinsic activity of the high-density lipoprotein receptor SR-BI.

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Binding of anionic phospholipids to retinal pigment epithelium may be mediated by the scavenger receptor CD36

21 January 2018

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12 December 2020

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Scavenger receptor class B, type I-mediated [3H]cholesterol efflux to high and low density lipoproteins is dependent on lipoprotein binding to the receptor

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Scavenger receptor BI promotes high density lipoprotein-mediated cellular cholesterol efflux

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