Evidence map›Paper›PMID 20097206›Full record

ArticleJournal of molecular biology2010

Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR.

Yuan Zhang, Tim Doherty, Jing Li, Wuyuan Lu, Cyril Barinka, Jacek Lubkowski, Mei Hong

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.8field-weighted citation impact, top 8% 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

23 citing papers in PubMed, 46 citations in OpenAlex.

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  12. The Antimicrobial and Antiviral Applications of Cell-Penetrating Peptides.Methods in molecular biology (Clifton, N.J.) · 2015
    Review
  13. Article
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  19. Simultaneous acquisition of PAR and PAIN spectra.Journal of biomolecular NMR · 2012
    Article
  20. 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

7 authors at 3 institutions in 1 country.

Yuan ZhangDepartment of Chemistry, Iowa State University, Ames, IA 50011, USA.
Tim Doherty
Jing Li
Wuyuan Lu
Cyril Barinka
Jacek Lubkowski
Mei Hong
Iowa State University · USNational Cancer Institute · USUniversity of Maryland, Baltimore · US

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Structures and lipid interactions of curvature-inducing membrane peptides by NMRR01GM066976 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI HONG, MEI · 2003 to 2021
$4.8M
Inhibition of Anthrax Lethal Factor by alpha-defensinsR01AI072732 · NIAID · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI LU, WUYUAN · 2007 to 2011
$2.4M
NIAID NIH HHS R01 AI072732NIBIB NIH HHS P41 EB002026NIBIB NIH HHS P41-EB-002026NIGMS NIH HHS GM66976NIGMS NIH HHS R01 GM066976
6 · The paper itself

Abstract

Human alpha-defensins [human neutrophil peptides (HNPs)] are immune defense mini-proteins that act by disrupting microbial cell membranes. Elucidating the three-dimensional (3D) structures of HNPs in lipid membranes is important for understanding their mechanisms of action. Using solid-state NMR (SSNMR), we have determined the 3D structure of HNP-1 in a microcrystalline state outside the lipid membrane, which provides benchmarks for structure determination and comparison with the membrane-bound state. From a suite of two-dimensional and 3D magic-angle spinning experiments, (13)C and (15)N chemical shifts that yielded torsion angle constraints were obtained, while inter-residue distances were obtained to restrain the 3D fold. Together, these constraints led to the first high-resolution SSNMR structure of a human defensin. The SSNMR structure has close similarity to the crystal structures of the HNP family, with the exception of the loop region between the first and second beta-strands. The difference, which is partially validated by direct torsion angle measurements of selected loop residues, suggests possible conformational variation and flexibility of this segment of the protein, which may regulate HNP interaction with the phospholipid membrane of microbial cells.

Indexed as

alpha-DefensinsHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein Structure, Tertiaryalpha-Defensinshuman neutrophil peptide 1

Identifiers

PMID20097206
PMCPMC2873975
OpenAlexW1970345909

What OpenQuestion holds

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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.