Evidence map›Paper›PMID 16452169›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases.

A Abdul Ajees, G M Anantharamaiah, Vinod K Mishra, M Mahmood Hussain, H M Krishna Murthy

RetractedAbstract readRetracted Publication
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
17.1field-weighted citation impact, top 1% 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

75 citing papers in PubMed, 204 citations in OpenAlex.

  1. Case-Control Study to Investigate the Association Between Serum Apolipoprotein B/A1 Ratio and Atrial Fibrillation by Sex in 920 Patients from China.Medical science monitor : international medical journal of experimental and clinical research · 2022
    Article
  2. Large nanodiscs going viral.Current opinion in structural biology · 2020
    Review
  3. Article
  4. Review
  5. Covalently circularized nanodiscs; challenges and applications.Current opinion in structural biology · 2018
    Review
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  10. Review
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  20. Article

15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

A Abdul AjeesCenter for Biophysical Sciences and Engineering and Atherosclerosis Research Unit and Department of Medicine, University of Alabama, 1530 3rd Avenue South, Birmingham, AL 35294, USA.
G M Anantharamaiah
Vinod K Mishra
M Mahmood Hussain
H M Krishna Murthy
University of Alabama · USState University of New York · US

Funding

SYNTHETIC PEPTIDE STUDIES OF THE AMPHIPATHIC HELIXP01HL034343 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SEGREST, JERE P · 1985 to 2012
$18.8M
MOLECULAR MECHANISMS OF CHYLOMICRON ASSEMBLYR01DK046900 · NIDDK · SUNY DOWNSTATE MEDICAL CENTER · PI HUSSAIN, M MAHMOOD · 2001 to 2011
$3.0M
BINDING OF MTP TO APOB DURING LIPOPROTEIN ASSEMBLYR01HL064272 · NHLBI · SUNY DOWNSTATE MEDICAL CENTER · PI HUSSAIN, M MAHMOOD · 1999 to 2006
$1.8M
STRUCTURE BASED ANALYSIS OF DENGUE VIRUS SERINE PROTEASER01AI045623 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MURTHY, KRISHNA H · 2000 to 2004
$1.5M
Study of Interactions of VCP with Complement ComponentsR01AI051615 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MURTHY, KRISHNA H · 2003 to 2007
$1.5M
Molecular mechanisms of chylomicron assemblyR56DK046900 · NIDDK · SUNY DOWNSTATE MEDICAL CENTER · PI HUSSAIN, M MAHMOOD · 2015 to 2015
$140k
ASSEMBLY OF APOB48 CONTAINING LIPOPROTEINSR29DK046900 · NIDDK · MCP HAHNEMANN UNIVERSITY · PI HUSSAIN, M MAHMOOD · 1995 to 1999
–
NHLBI NIH HHS P01 HL034343NHLBI NIH HHS R01 HL064272NIAID NIH HHS R01 AI045623NIAID NIH HHS R01 AI051615NIDDK NIH HHS R01 DK046900NIDDK NIH HHS R29 DK046900NIDDK NIH HHS R56 DK046900
6 · The paper itself

Abstract

Despite three decades of extensive studies on human apolipoprotein A-I (apoA-I), the major protein component in high-density lipoproteins, the molecular basis for its antiatherogenic function is elusive, in part because of lack of a structure of the full-length protein. We describe here the crystal structure of lipid-free apoA-I at 2.4 A. The structure shows that apoA-I is comprised of an N-terminal four-helix bundle and two C-terminal helices. The N-terminal domain plays a prominent role in maintaining its lipid-free conformation, indicating that mutants with truncations in this region form inadequate models for explaining functional properties of apoA-I. A model for transformation of the lipid-free conformation to the high-density lipoprotein-bound form follows from an analysis of solvent-accessible hydrophobic patches on the surface of the structure and their proximity to the hydrophobic core of the four-helix bundle. The crystal structure of human apoA-I displays a hitherto-unobserved array of positively and negatively charged areas on the surface. Positioning of the charged surface patches relative to hydrophobic regions near the C terminus of the protein offers insights into its interaction with cell-surface components of the reverse cholesterol transport pathway and antiatherogenic properties of this protein. This structure provides a much-needed structural template for exploration of molecular mechanisms by which human apoA-I ameliorates atherosclerosis and inflammatory diseases.

Indexed as

Apolipoprotein A-ICardiotonic AgentsCardiovascular DiseasesCrystallographyHumansHydrophobic and Hydrophilic InteractionsLipidsProtein Structure, SecondaryApolipoprotein A-ICardiotonic AgentsLipids

Identifiers

PMID16452169
PMCPMC1413691
OpenAlexW2037031239

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.