Evidence map›Paper›PMID 40290146›Full record

ArticleACS central science2025

Amino Acid Sequence Controls Enhanced Electron Transport in Heme-Binding Peptide Monolayers.

Hao Yang, Xiaolin Liu, Moeen Meigooni, Li Zhang, Jitong Ren, Qian Chen, Mark Losego, Emad Tajkhorshid, Jeffrey S Moore, Charles M Schroeder

Abstract read
In one paragraph

Article in ACS central science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Single-Molecule Electron Transport in Peptoids.The journal of physical chemistry. B · 2026
    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

10 authors.

Hao YangBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Xiaolin LiuBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID https://orcid.org/0000-0002-6909-117X
Moeen MeigooniBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Li ZhangSchool of Materials Science and Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.ORCID https://orcid.org/0000-0001-9110-6481
Jitong RenBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.
Qian ChenBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID https://orcid.org/0000-0002-1968-441X
Mark LosegoSchool of Materials Science and Engineering, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.ORCID https://orcid.org/0000-0002-9810-9834
Emad TajkhorshidBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID https://orcid.org/0000-0001-8434-1010
Jeffrey S MooreBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID https://orcid.org/0000-0001-5841-6269
Charles M SchroederBeckman Institute for Advanced Science and Technology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, United States.ORCID https://orcid.org/0000-0001-6023-2274

Funding

Resource for Macromolecular Modeling and VisualizationR24GM145965 · NIGMS · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI Emad Tajkhorshid · 2022 to 2026
$6.2M
NIGMS NIH HHS R24 GM145965
6 · The paper itself

Abstract

Metal-binding proteins have the exceptional ability to facilitate long-range electron transport in nature. Despite recent progress, the sequence-structure-function relationships governing electron transport in heme-binding peptides and protein assemblies are not yet fully understood. In this work, the electronic properties of a series of heme-binding peptides inspired by cytochrome

Identifiers

PMID40290146
PMCPMC12022913

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.