Evidence map›Paper›PMID 39924651›Full record

ReviewMass spectrometry reviews

Mass Spectrometry-Based Proteomics Technologies to Define Endogenous Protein-Protein Interactions and Their Applications to Cancer and Viral Infectious Diseases.

Clinton Yu, Rithika Adavikolanu, Robyn M Kaake, Lan Huang

Abstract readReview
In one paragraph

Review in Mass spectrometry reviews. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. 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

4 authors.

Clinton YuDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California, USA.ORCID http://orcid.org/0000-0002-2931-5474
Rithika AdavikolanuDepartment of Bioengineering, University of California, San Francisco, San Francisco, California, USA.ORCID http://orcid.org/0009-0007-6789-5194
Robyn M KaakeDepartment of Bioengineering, University of California, San Francisco, San Francisco, California, USA.ORCID http://orcid.org/0000-0002-8341-3067
Lan HuangDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California, USA.ORCID http://orcid.org/0000-0002-3140-4687

Funding

Supplement: Advancing Proteomics Technologies to Decipher the Ubiquitin-Proteasome SystemR35GM145249 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI Lan Huang · 2022 to 2026
$3.2M
NIGMS NIH HHS R35 GM145249This work was supported by National Institutes of Health grants R35GM145249 to L.H.
6 · The paper itself

Abstract

An intricate network of protein assemblies and protein-protein interactions (PPIs) underlies nearly every biological process in living systems. The organization of these cellular networks is highly dynamic and intimately tied to the genomic and proteomic landscapes of a cell. Disruptions in normal PPIs can impair cellular functions and contribute to the development of human diseases. In recent years, targeting PPIs has emerged as an attractive strategy for drug discovery. Consequently, the identification and characterization of endogenous PPIs-those occurring naturally under physiological conditions-has become crucial for unraveling the molecular mechanisms driving human pathology and for laying the groundwork for novel diagnostics and therapeutics. Owing to numerous technological advancements, mass spectrometry (MS)-based proteomics has transformed the study of PPIs at the systems-level. This review focuses on proteomics approaches that enable the characterization of physiologically relevant endogenous interactions, spanning complex-centric to structure-centric analyses. Additionally, their applications to define native PPIs in the contexts of cancer and viral infectious diseases is highlighted.

Indexed as

Mass SpectrometryNeoplasmsProtein Interaction MappingProteomicsVirus DiseasesAnimalsHumansProtein Interaction MapsAffinity Purification Mass Spectrometry (AP‐MS)CancerCo‐Fractionation Mass Spectrometry (CF‐MS)Cross‐Linking Mass Spectrometry (XL‐MS)genome taggingimmunoprecipitation (IP)protein footprintingprotein‐protein interactions (PPIs)Proximity Labeling Mass Spectrometry (PL‐MS)virology

Identifiers

PMID39924651
PMCPMC12334737

What OpenQuestion holds

Textmetadata
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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.