Evidence map›Paper›PMID 34046695›Full record

ReviewCellular and molecular life sciences : CMLS2021

Recent progress in mass spectrometry-based strategies for elucidating protein-protein interactions.

Teck Yew Low, Saiful Effendi Syafruddin, M Aiman Mohtar, Adaikkalam Vellaichamy, Nisa Syakila A Rahman, Yuh-Fen Pung, Chris Soon Heng Tan

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing 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

54 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Proteomic Technology.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Article
  8. Review
  9. Metabolic control of glycosylation forms for establishing glycan-dependent protein interaction networks.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. Simplicity within biological complexity.Bioinformatics advances · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Journal of proteome research · 2024
    Review
  20. 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

7 authors.

Teck Yew LowUKM Medical Molecular Biology Institute (UMBI), Universiti Kebangsaan Malaysia (UKM), Jalan Yaacob Latiff, Bandar Tun Razak, 56000, Kuala Lumpur, Malaysia. lowteckyew@ppukm.ukm.edu.my.ORCID http://orcid.org/0000-0001-7878-7534
Saiful Effendi Syafruddin *UKM Medical Molecular Biology Institute (UMBI), Universiti Kebangsaan Malaysia (UKM), Jalan Yaacob Latiff, Bandar Tun Razak, 56000, Kuala Lumpur, Malaysia.
M Aiman Mohtar *UKM Medical Molecular Biology Institute (UMBI), Universiti Kebangsaan Malaysia (UKM), Jalan Yaacob Latiff, Bandar Tun Razak, 56000, Kuala Lumpur, Malaysia.
Adaikkalam VellaichamyCentre for Biotechnology, Anna University, Chennai, 600025, India.
Nisa Syakila A RahmanUKM Medical Molecular Biology Institute (UMBI), Universiti Kebangsaan Malaysia (UKM), Jalan Yaacob Latiff, Bandar Tun Razak, 56000, Kuala Lumpur, Malaysia.
Yuh-Fen PungDivision of Biomedical Science, University of Nottingham Malaysia, 43500, Semenyih, Malaysia.
Chris Soon Heng TanDepartment of Chemistry, College of Science , Southern University of Science and Technology, Shenzhen, 518055, China. christan@sustech.edu.cn.

Funding

Ministry of Higher Education Malaysia FRGS/1/2019/SKK08/UNIM/02/2Universiti Kebangsaan Malaysia Geran Universiti Penyelidikan (GUP-2020-078)
6 · The paper itself

Abstract

Protein-protein interactions are fundamental to various aspects of cell biology with many protein complexes participating in numerous fundamental biological processes such as transcription, translation and cell cycle. MS-based proteomics techniques are routinely applied for characterising the interactome, such as affinity purification coupled to mass spectrometry that has been used to selectively enrich and identify interacting partners of a bait protein. In recent years, many orthogonal MS-based techniques and approaches have surfaced including proximity-dependent labelling of neighbouring proteins, chemical cross-linking of two interacting proteins, as well as inferring PPIs from the co-behaviour of proteins such as the co-fractionating profiles and the thermal solubility profiles of proteins. This review discusses the underlying principles, advantages, limitations and experimental considerations of these emerging techniques. In addition, a brief account on how MS-based techniques are used to investigate the structural and functional properties of protein complexes, including their topology, stoichiometry, copy number and dynamics, are discussed.

Indexed as

AnimalsChromatography, AffinityHumansMass SpectrometryProtein Interaction MappingProteinsProteomeProteinsProteomeAffinity purification coupled to mass spectrometry (AP-MS)Co-fractionation mass spectrometry (coFrac-MS)Cross-linking mass spectrometry (XL-MS)Proximity-dependent biotinylation coupled to MS (PDB-MS)Thermal proximity coaggregation (TPCA)

Identifiers

PMID34046695
PMCPMC8159249

What OpenQuestion holds

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Registered trials

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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.