Evidence map›Paper›PMID 16443648›Full record

ArticleBiophysical journal2006

Molecular dynamics of surfactant protein C: from single molecule to heptameric aggregates.

Eunice Ramírez, Alberto Santana, Anthony Cruz, Inés Plasencia, Gustavo E López

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 92% 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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Article
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

5 authors at 1 institution in 1 country.

Eunice RamírezDepartment of Chemistry, University of Puerto Rico, Mayagüez, Puerto Rico 00681.
Alberto Santana
Anthony Cruz
Inés Plasencia
Gustavo E López
University of Puerto Rico-Mayaguez · PR

Funding

Unraveling the Reaction between Heme (FeIV=O) Moiety and H2SS06GM008103 · NIGMS · UNIVERSITY OF PUERTO RICO MAYAGUEZ · PI MELENDEZ, ENRIQUE · 1989 to 2010
$10.6M
UPR COBRE: PROTEIN STRUCTURE FUNCTION &DYNAMICS: ADMINISTRATIVE COREP20RR016439 · NCRR · UNIVERSITY OF PUERTO RICO MAYAGUEZ · PI LOPEZ-QUINONES, GUSTAVO E · 2001 to 2005
$7.3M
NCRR NIH HHS P20 RR016439NCRR NIH HHS P20RR16439-01NIGMS NIH HHS GM008103-03NIGMS NIH HHS S06 GM008103
6 · The paper itself

Abstract

Surfactant protein C (SP-C) is a membrane-associated protein essential for normal respiration. It has been found that the alpha-helix form of SP-C can undergo, under certain conditions, a transformation from an alpha-helix to a beta-strand conformation that closely resembles amyloid fibrils, which are possible contributors to the pathogenesis of pulmonary alveolar proteinosis. Molecular dynamics simulations using the NAMD2 package were performed for systems containing from one to seven SP-C molecules to study their behavior in water. The results of our simulations show that unfolding of the protein occurs at the amino terminal, and despite this unfolding, no transition from alpha-helix to beta-strand was observed.

Indexed as

Models, MolecularComputer SimulationProtein ConformationPulmonary Surfactant-Associated Protein CPulmonary SurfactantsWaterPulmonary Surfactant-Associated Protein CPulmonary SurfactantsWater

Identifiers

PMID16443648
PMCPMC1414559
OpenAlexW1993132228

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.