Evidence map›Paper›PMID 31632896›Full record

ArticleChemNanoMat : chemistry of nanomaterials for energy, biology and more2016

Biomimetic Crystallization of MnFe

Yoshiaki Maeda, Zengyan Wei, Yasuhiro Ikezoe, Edmund Tam, Hiroshi Matsui

Abstract read
In one paragraph

Article in ChemNanoMat : chemistry of nanomaterials for energy, biology and more, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Review
  2. Biomimetic Crystallization of MnFeChemNanoMat : chemistry of nanomaterials for energy, biology and more · 2016
    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.

Yoshiaki MaedaDepartment of Chemistry and Biochemistry, City University of New York-Hunter College, 695 Park Ave., New York, NY 10065 (USA), hmatsui@hunter.cuny.edu.
Zengyan WeiDepartment of Chemistry and Biochemistry, City University of New York-Hunter College, 695 Park Ave., New York, NY 10065 (USA), hmatsui@hunter.cuny.edu.
Yasuhiro IkezoeDepartment of Chemistry and Biochemistry, City University of New York-Hunter College, 695 Park Ave., New York, NY 10065 (USA), hmatsui@hunter.cuny.edu.
Edmund TamDepartment of Chemistry and Biochemistry, City University of New York-Hunter College, 695 Park Ave., New York, NY 10065 (USA), hmatsui@hunter.cuny.edu.
Hiroshi MatsuiDepartment of Chemistry and Biochemistry, City University of New York-Hunter College, 695 Park Ave., New York, NY 10065 (USA), hmatsui@hunter.cuny.edu.

Funding

Basic and Translational Research Center for Reducing Health DisparitiesG12MD007599 · NIMHD · HUNTER COLLEGE · PI ANGULO, JESUS A · 2012 to 2017
$14.6M
NIMHD NIH HHS G12 MD007599
6 · The paper itself

Abstract

Enzymes are some of the most efficient catalysts in nature. If small catalytic peptides mimic enzymes, there is potential for broad applications from catalysis for new material synthesis to drug development, due to the ease of molecular design. Recently a hydrogel-based combinatory phage display library was developed and protease-mimicking peptides were identified. Here we advanced the previous discovery to apply one of these catalytic peptides for the synthesis of bimetal oxide nanocrystals through the catalytic ester-elimination pathway. Conventional bimetal oxide crystallization usually requires high temperatures above several hundred °C; however, this catalytic peptide could grow superparamagnetic MnFe

Indexed as

biomineralizationcatalytic peptideester eliminationMnFe2O4superparamagnetism

Identifiers

PMID31632896
PMCPMC6801106

What OpenQuestion holds

Textmetadata
LicenceTDM
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.