Evidence map›Paper›PMID 36140407›Full record

ReviewBiomedicines2022

A Comprehensive Review on Collagen Type I Development of Biomaterials for Tissue Engineering: From Biosynthesis to Bioscaffold.

Ibrahim N Amirrah, Yogeswaran Lokanathan, Izzat Zulkiflee, M F Mohd Razip Wee, Antonella Motta, Mh Busra Fauzi

Open access · goldAbstract readReview
In one paragraph

Review in Biomedicines, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 173 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
173citing papers in PubMed, 1 pooled it
23.3field-weighted citation impact, top 1% 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

173 citing papers in PubMed, 1 synthesis or guideline pooled it, 335 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. High-Density Type I Collagen Promotes IFN-γAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
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  18. Article
  19. Assessment of Bovine Collagen Manufactured via Cellular Agriculture.ACS biomaterials science & engineering · 2026
    Article
  20. Review

113 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

Ibrahim N AmirrahCentre for Tissue Engineering and Regenerative Medicine, Faculty of Medicine, Universiti Kebangsaan Malaysia, Jalan Yaacob Latiff, Bandar Tun Razak, Cheras, Kuala Lumpur 56000, Malaysia.ORCID 0000-0002-4256-0626
Yogeswaran LokanathanCentre for Tissue Engineering and Regenerative Medicine, Faculty of Medicine, Universiti Kebangsaan Malaysia, Jalan Yaacob Latiff, Bandar Tun Razak, Cheras, Kuala Lumpur 56000, Malaysia.ORCID 0000-0002-9548-6490
Izzat ZulkifleeCentre for Tissue Engineering and Regenerative Medicine, Faculty of Medicine, Universiti Kebangsaan Malaysia, Jalan Yaacob Latiff, Bandar Tun Razak, Cheras, Kuala Lumpur 56000, Malaysia.ORCID 0000-0001-5493-7876
M F Mohd Razip WeeInstitute of Microengineering and Nanoelectronics (IMEN), Universiti Kebangsaan Malaysia, Bangi 43600, Malaysia.ORCID 0000-0001-5543-2300
Antonella MottaDepartment of Industrial Engineering, University of Trento, Via Sommarive 9, 38122 Trento, Italy.
Mh Busra FauziCentre for Tissue Engineering and Regenerative Medicine, Faculty of Medicine, Universiti Kebangsaan Malaysia, Jalan Yaacob Latiff, Bandar Tun Razak, Cheras, Kuala Lumpur 56000, Malaysia.ORCID 0000-0001-6449-639X
National University of Malaysia · MYUniversity of Trento · IT

Funding

Ministry of Science, Technology and Innovation (MOSTI; Malaysia) under International Collaboration Fund Grant code: IF0419Q1081The European Union's Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant agreement No:101008041 Grant agreement No:101008041
6 · The paper itself

Abstract

Collagen is the most abundant structural protein found in humans and mammals, particularly in the extracellular matrix (ECM). Its primary function is to hold the body together. The collagen superfamily of proteins includes over 20 types that have been identified. Yet, collagen type I is the major component in many tissues and can be extracted as a natural biomaterial for various medical and biological purposes. Collagen has multiple advantageous characteristics, including varied sources, biocompatibility, sustainability, low immunogenicity, porosity, and biodegradability. As such, collagen-type-I-based bioscaffolds have been widely used in tissue engineering. Biomaterials based on collagen type I can also be modified to improve their functions, such as by crosslinking to strengthen the mechanical property or adding biochemical factors to enhance their biological activity. This review discusses the complexities of collagen type I structure, biosynthesis, sources for collagen derivatives, methods of isolation and purification, physicochemical characteristics, and the current development of collagen-type-I-based scaffolds in tissue engineering applications. The advancement of additional novel tissue engineered bioproducts with refined techniques and continuous biomaterial augmentation is facilitated by understanding the conventional design and application of biomaterials based on collagen type I.

Indexed as

biomaterialcollagenfabricationpurificationscaffoldtissue engineering

Identifiers

PMID36140407
PMCPMC9496548
OpenAlexW4296251990

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.