Evidence map›Paper›PMID 30168208›Full record

ArticleProtein science : a publication of the Protein Society2018

Structural enzymology binding studies of the peptide-substrate-binding domain of human collagen prolyl 4-hydroxylase (type-II): High affinity peptides have a PxGP sequence motif.

Abhinandan V Murthy, Ramita Sulu, M Kristian Koski, Hongmin Tu, Jothi Anantharajan, Shiv K Sah-Teli, Johanna Myllyharju, Rik K Wierenga

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Collagen IV biosynthesis: Intracellular choreography of post-translational modifications.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. 3D-Printed Protein Models as an Educational Tool in Biochemistry Outreach.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology
    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

8 authors at 1 institution in 1 country.

Abhinandan V MurthyBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Ramita SuluBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
M Kristian KoskiBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Hongmin TuOulu Center for Cell-Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Jothi AnantharajanBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Shiv K Sah-TeliBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Johanna MyllyharjuOulu Center for Cell-Matrix Research, Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Rik K WierengaBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
University of Oulu · FI

Funding

Academy of Finland, Center of Excellence 2012-2017 251314Academy of Finland, Research council for Biosciences and Environment 296498Jane and Aatos Erkko FoundationSigrid Jusélius Foundation
6 · The paper itself

Abstract

The peptide-substrate-binding (PSB) domain of collagen prolyl 4-hydroxylase (C-P4H, an α

Indexed as

HumansPeptidesProlyl HydroxylasesProtein BindingProtein ConformationP4HA2 protein, humanPeptidesProlyl Hydroxylasescalorimetrycollagenextracellular matrix proteinproline-rich peptideprolyl 4-hydroxylaseprotein-peptide interactionsX-ray crystallography

Identifiers

PMID30168208
PMCPMC6194285
OpenAlexW2889823936

What OpenQuestion holds

Textmetadata
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.