Evidence map›Paper›PMID 30280012›Full record

ArticlePeerJ2018

Crystal structure and functional analysis of human C1ORF123.

Siti Nurulnabila A Rahaman, Jastina Mat Yusop, Zeti-Azura Mohamed-Hussein, Wan Mohd Aizat, Kok Lian Ho, Aik-Hong Teh, Jitka Waterman, Boon Keat Tan, Hwei Ling Tan, Adelicia Yongling Li and 2 more

Open access · goldAbstract read
In one paragraph

Article in PeerJ, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. 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

12 authors at 6 institutions in 3 countries.

Siti Nurulnabila A RahamanInstitute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Selangor, Malaysia.
Jastina Mat YusopInstitute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Selangor, Malaysia.
Zeti-Azura Mohamed-HusseinInstitute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Selangor, Malaysia.
Wan Mohd AizatInstitute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Selangor, Malaysia.
Kok Lian HoDepartment of Pathology, Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Serdang, Selangor, Malaysia.
Aik-Hong TehCentre for Chemical Biology, Universiti Sains Malaysia, Bayan Lepas, Penang, Malaysia.
Jitka WatermanDiamond Light Source, Harwell Science and Innovation Campus, Didcot, England, United Kingdom.
Boon Keat TanDivision of Human Biology, School of Medicine, International Medical University, Bukit Jalil, Kuala Lumpur, Malaysia.
Hwei Ling TanDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore.
Adelicia Yongling LiDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore.
Ee Sin ChenDepartment of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore.
Chyan Leong NgInstitute of Systems Biology, Universiti Kebangsaan Malaysia, Bangi, Selangor, Malaysia.
National University of Malaysia · MYNational University of Singapore · SGDiamond Light Source · GBInternational Medical University · MYUniversiti Putra Malaysia · MYUniversiti Sains Malaysia · MY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins of the DUF866 superfamily are exclusively found in eukaryotic cells. A member of the DUF866 superfamily, C1ORF123, is a human protein found in the open reading frame 123 of chromosome 1. The physiological role of C1ORF123 is yet to be determined. The only available protein structure of the DUF866 family shares just 26% sequence similarity and does not contain a zinc binding motif. Here, we present the crystal structure of the recombinant human C1ORF123 protein (rC1ORF123). The structure has a 2-fold internal symmetry dividing the monomeric protein into two mirrored halves that comprise of distinct electrostatic potential. The N-terminal half of rC1ORF123 includes a zinc-binding domain interacting with a zinc ion near to a potential ligand binding cavity. Functional studies of human C1ORF123 and its homologue in the fission yeast

Indexed as

C1ORF123Crystal structureCXXC motifDUF866Internal symmetryMitochondrial oxidative phosphorylationZinc-binding domain

Identifiers

PMID30280012
PMCPMC6166629
OpenAlexW2894207945

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.