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Electromagnetic-field effects on structure and dynamics of amyloidogenic peptides

1 of 40 checkable references need attention · checked 2026-07-22

At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.

1 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.

References needing attention

does not resolve to a known work10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H

The 39 checked references that resolve

resolves10.1109/TMTT.2013.2250298

Feasibility for Microwaves Energy to Affect Biological Systems Via Nonthermal Mechanisms: A Systematic Approach

resolves10.1021/jp052742q

Electric Field Effects on Insulin Chain-B Conformation

resolves10.1021/jp800350v

Comparative Study of Insulin Chain-B in Isolated and Monomeric Environments under External Stress

resolves10.1002/jcp.20327

Electromagnetic fields at mobile phone frequency induce apoptosis and inactivation of the multi‐chaperone complex in human epidermoid cancer cells

resolves10.1002/bem.20119

Mechanisms for interaction between RF fields and biological tissue

resolves10.1016/S0014-5793(03)00413-7

Microwave radiation can alter protein conformation without bulk heating

resolves10.1039/C5CP00629E

Perspectives on external electric fields in molecular simulation: progress, prospects and challenges

resolves10.1111/j.1469-185X.2009.00112.x

Biological monitoring of non‐thermal effects of mobile phone radiation: recent approaches and challenges

resolves10.1063/1.4813854

Proteins in the electric field near the surface of mica

resolves10.1289/ehp.6039

Nerve cell damage in mammalian brain after exposure to microwaves from GSM mobile phones.

resolves10.1002/jcb.20164

Non‐thermal effects of electromagnetic fields at mobile phone frequency on the refolding of an intracellular protein: Myoglobin

resolves10.1016/S0378-4274(01)00285-5

Health risks from the use of mobile phones

resolves10.1063/1.2515315

Denaturation of hen egg white lysozyme in electromagnetic fields: A molecular dynamics study

resolves10.1063/1.3184794

Nonequilibrium molecular dynamics study of electric and low-frequency microwave fields on hen egg white lysozyme

resolves10.1006/jtbi.2000.2123

Biological Effects of Electromagnetic Fields—Mechanisms for the Effects of Pulsed Microwave Radiation on Protein Conformation

resolves10.1016/j.apsusc.2014.11.078

Modulating protein behaviors on responsive surface by external electric fields: A molecular dynamics study

resolves10.1007/s11947-012-1040-1

Review: Pulsed Electric Fields Processing of Protein-Based Foods

resolves10.1021/ct1001335

Electric Field Effects on Short Fibrils of Aβ Amyloid Peptides

resolves10.1103/PhysRevE.61.4310

Microwave-enhanced folding and denaturation of globular proteins

resolves10.1016/j.sbi.2006.03.007

Recent atomic models of amyloid fibril structure

resolves10.1021/jp807896g

Effects of Electric Field Stress on a β-Amyloid Peptide

resolves10.3233/JAD-2010-1228

Electromagnetic Field Treatment Protects Against and Reverses Cognitive Impairment in Alzheimer's Disease Mice

resolves10.1021/jp067248g

Effect of Frequency on Insulin Response to Electric Field Stress

resolves10.1007/s00249-003-0359-y

Effect of external stresses on protein conformation: a computer modelling study

resolves10.1021/bi000002w

Human Apolipoprotein C-II Forms Twisted Amyloid Ribbons and Closed Loops

resolves10.1007/s13238-011-1013-6

Apolipoproteins and amyloid fibril formation in atherosclerosis

resolves10.1016/j.jmb.2006.12.040

A Structural Core Within Apolipoprotein C-II Amyloid Fibrils Identified Using Hydrogen Exchange and Proteolysis

resolves10.1016/j.jmb.2011.12.059

A Cyclic Peptide Inhibitor of ApoC-II Peptide Fibril Formation: Mechanistic Insight from NMR and Molecular Dynamics Analysis

resolves10.1039/c0cp00299b

Effects of mutation on the amyloidogenic propensity of apolipoprotein C-II <sub>60–70</sub> peptide

resolves10.1021/jp102142x

Lipid Concentration Effects on the Amyloidogenic apoC-II<sub>60−70</sub> Peptide: A Computational Study

resolves10.1371/journal.pcbi.1003360

Dimensionality of Carbon Nanomaterials Determines the Binding and Dynamics of Amyloidogenic Peptides: Multiscale Theoretical Simulations

resolves10.1371/journal.pone.0057437

"Janus" Cyclic Peptides: A New Approach to Amyloid Fibril Inhibition?

resolves10.1007/s00249-008-0363-3

Effects of oxidation, pH and lipids on amyloidogenic peptide structure: implications for fibril formation?

resolves10.1063/1.448118

Molecular dynamics with coupling to an external bath

resolves10.1063/1.1538595

Molecular dynamics simulations of microwave heating of water

resolves10.1063/1.1624363

Hydrogen bonding and molecular mobility in liquid water in external electromagnetic fields

resolves10.1021/ct700119m

Clustering Molecular Dynamics Trajectories: 1. Characterizing the Performance of Different Clustering Algorithms

resolves10.1016/0263-7855(96)00018-5

VMD: Visual molecular dynamics

resolves10.1002/jcc.22912

Effects of external electromagnetic fields on the conformational sampling of a short alanine peptide

The 1 reference without a DOI — listed, not checked

no DOI — not checkedSee supplementary material at http://dx.doi.org/10.1063/1.4941108E-JCPSA6-144-026606 for additional data from the clustering analysis, N-C terminal and radius of gyration calculations, and segmented free energy maps.

What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-07-22 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

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