Evidence map›Paper›PMID 20920479›Full record

ArticleBiochemical pharmacology2011

Signaling through LRP1: Protection from atherosclerosis and beyond.

Philippe Boucher, Joachim Herz

Open access · greenAbstract read
In one paragraph

Article in Biochemical pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed, 1 pooled it
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

70 citing papers in PubMed, 1 synthesis or guideline pooled it, 118 citations in OpenAlex.

  1. Pooled it
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  7. Review
  8. Mitigating atherosclerosis: Integrating vaccines with gene targets.American heart journal plus : cardiology research and practice · 2025
    Review
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10 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Philippe BoucherCNRS, UMR7175, Université de Strasbourg, 74, route du Rhin, Illkirch F-67401, France. philippe.boucher@pharma.u-strasbg.fr
Joachim Herz
The University of Texas Southwestern Medical Center · USUniversité de Strasbourg · FR

Funding

TRANSCRIPTIONAL REGULATION OF LDL RECEPTOR PROMOTERP01HL020948 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI GOLDSTEIN, JOSEPH L · 1985 to 2021
$103.1M
Metabolism of the VLDL receptor and ApoE receptor 2R37HL063762 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI HERZ, JOACHIM J · 2010 to 2019
$4.0M
METABOLISM OF THE VLDL RECEPTOR AND APOE RECEPTOR 2R01HL063762 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI HERZ, JOACHIM J · 2000 to 2009
$3.1M
APO E Receptors and Modulation of Fast Axonal TransportR01NS043408 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI HERZ, JOACHIM J · 2002 to 2006
$1.8M
Enhancing Progranulin Expression - a Therapy for Frontotemporal DementiaRC1NS068697 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI FARESE, ROBERT V, HERZ, JOACHIM J · 2009 to 2010
$1000k
NHLBI NIH HHS P01 HL020948NHLBI NIH HHS R01 HL063762NHLBI NIH HHS R37 HL063762NINDS NIH HHS R01 NS043408NINDS NIH HHS RC1 NS068697
6 · The paper itself

Abstract

The low-density lipoprotein receptor-related protein (LRP1) is a multifunctional cell surface receptor that belongs to the LDL receptor (LDLR) gene family and that is widely expressed in several tissues. LRP1 consists of an 85-kDa membrane-bound carboxyl fragment (β chain) and a non-covalently attached 515-kDa (α chain) amino-terminal fragment. Through its extracellular domain, LRP1 binds at least 40 different ligands ranging from lipoprotein and protease inhibitor complex to growth factors and extracellular matrix proteins. LRP-1 has also been shown to interact with scaffolding and signaling proteins via its intracellular domain in a phosphorylation-dependent manner and to function as a co-receptor partnering with other cell surface or integral membrane proteins. LRP-1 is thus implicated in two major physiological processes: endocytosis and regulation of signaling pathways, which are both involved in diverse biological roles including lipid metabolism, cell growth/differentiation processes, degradation of proteases, and tissue invasion. The embryonic lethal phenotype obtained after target disruption of the LRP-1 gene in the mouse highlights the biological importance of this receptor and revealed a critical, but yet undefined role in development. Tissue-specific gene deletion studies also reveal an important contribution of LRP1 in vascular remodeling, foam cell biology, the central nervous system, and in the molecular mechanisms of atherosclerosis.

Indexed as

AnimalsAtherosclerosisCell DifferentiationEndocytosisGene Expression RegulationLow Density Lipoprotein Receptor-Related Protein-1MacrophagesMiceMice, KnockoutProtein BindingReceptors, LDLSignal TransductionTumor Suppressor ProteinsLow Density Lipoprotein Receptor-Related Protein-1Lrp1 protein, mouseReceptors, LDLTumor Suppressor Proteins

Identifiers

PMID20920479
PMCPMC2991482
OpenAlexW1968238953

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.