Evidence map›Paper›PMID 37175379›Full record

ReviewMolecules (Basel, Switzerland)2023

Non-Native Structures of Apomyoglobin and Apoleghemoglobin in Folding Intermediates Related to the Protein Misfolding.

Chiaki Nishimura, Takeshi Kikuchi

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Review
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

2 authors at 2 institutions in 1 country.

Chiaki NishimuraFaculty of Pharmaceutical Sciences, Teikyo Heisei University, Tokyo 164-8530, Japan.ORCID 0000-0001-8417-3328
Takeshi KikuchiDepartment of Bioinformatics, College of Life Sciences, Ritsumeikan University, Kusatsu 528-8577, Japan.ORCID 0000-0002-0578-5965
Ritsumeikan University · JPTeikyo Heisei University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein folding is essential for a polypeptide chain to acquire its proper structure and function. Globins are a superfamily of ubiquitous heme-binding α-helical proteins whose function is principally to regulate oxygen homoeostasis. In this review, we explore the hierarchical helical formation in the globin proteins apomyoglobin and leghemoglobin, and we discuss the existence of non-native and misfolded structures occurring during the course of folding to its native state. This review summarizes the research aimed at characterizing and comparing the equilibrium and kinetic intermediates, as well as delineating the complete folding pathway at a molecular level, in order to answer the following questions: "What is the mechanism of misfolding via a folding intermediate? Does the non-native structure stabilize the contemporary intermediate structure? Does the non-native structure induce slower folding?" The role of the non-native structures in the folding intermediate related to misfolding is also discussed.

Indexed as

ApoproteinsMyoglobinKineticsLeghemoglobinProtein FoldingapomyoglobinApoproteinsLeghemoglobinMyoglobinapoleghemoglobinapomyoglobinfolding intermediatehydrophobic buried surface areaprotein foldingquench flow

Identifiers

PMID37175379
PMCPMC10179781
OpenAlexW4376630969

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.