Evidence map›Paper›PMID 22081141›Full record

ArticleEMBO reports2011

Mechanistic implications for LDL receptor degradation from the PCSK9/LDLR structure at neutral pH.

Paola Lo Surdo, Matthew J Bottomley, Alessandra Calzetta, Ethan C Settembre, Agostino Cirillo, Shilpa Pandit, Yan G Ni, Brian Hubbard, Ayesha Sitlani, Andrea Carfí

Abstract read
In one paragraph

Article in EMBO reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

112 citing papers in PubMed, 2 syntheses or guidelines pooled it.

  1. Lipid homeostasis in diabetic kidney disease.International journal of biological sciences · 2024
    Pooled it
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  10. PCSK9 in critical illness - It's not all about lipids.Annals of clinical biochemistry · 2026
    Review
  11. Article
  12. Mitigating atherosclerosis: Integrating vaccines with gene targets.American heart journal plus : cardiology research and practice · 2025
    Review
  13. Article
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  15. Article
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  17. Article
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  20. Article

52 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

10 authors.

Paola Lo SurdoDepartment of Biochemistry and Molecular Biology, IRBM P. Angeletti, Via Pontina Km 30.600, Pomezia, Rome I-00040, Italy.
Matthew J Bottomley
Alessandra Calzetta
Ethan C Settembre
Agostino Cirillo
Shilpa Pandit
Yan G Ni
Brian Hubbard
Ayesha Sitlani
Andrea Carfí

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein PCSK9 (proprotein convertase subtilisin/kexin type 9) is a key regulator of low-density lipoprotein receptor (LDLR) levels and cardiovascular health. We have determined the crystal structure of LDLR bound to PCSK9 at neutral pH. The structure shows LDLR in a new extended conformation. The PCSK9 C-terminal domain is solvent exposed, enabling cofactor binding, whereas the catalytic domain and prodomain interact with LDLR epidermal growth factor(A) and β-propeller domains, respectively. Thus, PCSK9 seems to hold LDLR in an extended conformation and to interfere with conformational rearrangements required for LDLR recycling.

Indexed as

Down-RegulationHumansHydrogen-Ion ConcentrationModels, MolecularProprotein Convertase 9Proprotein ConvertasesProtein BindingProtein Structure, TertiaryProteolysisReceptors, LDLSerine EndopeptidasesSurface Plasmon ResonancePCSK9 protein, humanProprotein Convertase 9Proprotein ConvertasesReceptors, LDLSerine Endopeptidases

Identifiers

PMID22081141
PMCPMC3245695

What OpenQuestion holds

Textmetadata
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.