Evidence map›Paper›PMID 28599848›Full record

ReviewBiochimica et biophysica acta. General subjects2018

Dynamic membrane interactions of antibacterial and antifungal biomolecules, and amyloid peptides, revealed by solid-state NMR spectroscopy.

Akira Naito, Nobuaki Matsumori, Ayyalusamy Ramamoorthy

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta. General subjects, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

13 citing papers in PubMed, 46 citations in OpenAlex.

  1. β-Amyloid (Aβ) and Human Cathelicidin LL-37: Two Sides of the Same Coin?International journal of molecular sciences · 2026
    Review
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  3. Article
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  11. Helical Structure of Recombinant Melittin.The journal of physical chemistry. B · 2019
    Article
  12. Review
  13. 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

3 authors at 3 institutions in 2 countries.

Akira NaitoGraduate School of Engineering, Yokohama National University, Yokohama 240-8501, Japan. Electronic address: naito@ynu.ac.jp.
Nobuaki MatsumoriDepartment of Chemistry, Graduate School of Science, Kyushu University, Fukuoka 819-0395, Japan.
Ayyalusamy RamamoorthyBiophysics Program, University of Michigan, Ann Arbor, MI 48109-1055, USA; Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Kyushu University · JPUniversity of Michigan–Ann Arbor · USYokohama National University · JP

Funding

Supplement: Investigation of Membrane-Bound Cytochromes-P450-b5 InteractionsR01GM084018 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2009 to 2018
$3.8M
Membrane interaction and disruption by the Alzheimer's amyloid-beta peptideR01AG048934 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2016 to 2020
$2.0M
Structure and function of antimicrobial peptidesR01AI054515 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RAMAMOORTHY, AYYALUSAMY · 2004 to 2008
$1.3M
NIAID NIH HHS R01 AI054515NIA NIH HHS R01 AG048934NIGMS NIH HHS R01 GM084018
6 · The paper itself

Abstract

A variety of biomolecules acting on the cell membrane folds into a biologically active structure in the membrane environment. It is, therefore, important to determine the structures and dynamics of such biomolecules in a membrane environment. While several biophysical techniques are used to obtain low-resolution information, solid-state NMR spectroscopy is one of the most powerful means for determining the structure and dynamics of membrane bound biomolecules such as antibacterial biomolecules and amyloidogenic proteins; unlike X-ray crystallography and solution NMR spectroscopy, applications of solid-state NMR spectroscopy are not limited by non-crystalline, non-soluble nature or molecular size of membrane-associated biomolecules. This review article focuses on the applications of solid-state NMR techniques to study a few selected antibacterial and amyloid peptides. Solid-state NMR studies revealing the membrane inserted bent α-helical structure associated with the hemolytic activity of bee venom melittin and the chemical shift oscillation analysis used to determine the transmembrane structure (with α-helix and 3

Indexed as

Computational BiologyModels, BiologicalNuclear Magnetic Resonance, BiomolecularAmyloidogenic ProteinsAnimalsAnti-Bacterial AgentsAntifungal AgentsHumansKineticsLigandsMembrane LipidsMembrane MicrodomainsMembrane ProteinsMembranes, ArtificialMolecular Dynamics SimulationProtein BindingAmyloidogenic ProteinsAnti-Bacterial AgentsAntifungal AgentsLigandsMembrane LipidsMembrane ProteinsMembranes, ArtificialAmyloidogenic peptideAntibacterial peptideAntifungal natural productIAPPLipid raftMembrane environmentSolid-state NMR

Identifiers

PMID28599848
PMCPMC6384124
OpenAlexW2623336582

What OpenQuestion holds

Textmetadata
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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.