ReviewMolecules (Basel, Switzerland)2020
Insight to Functional Conformation and Noncovalent Interactions of Protein-Protein Assembly Using MALDI Mass Spectrometry.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Dual-Laser Laser-Induced Liquid Bead Ion Desorption Mass Spectrometry: A New Approach for Adjustable Softness and Higher Sensitivity.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Machine Learning Methods for Protein-Protein Interaction Prediction Based on Noncovalent Interactions.ACS omega · 2026Article
- Stallion spermatozoa express LDH isoforms A, B, and C, with LDHC playing a crucial role in sustaining sperm viability.Reproduction (Cambridge, England) · 2025Article
- Visualization of Small Intact Proteins in Breast Cancer FFPE Tissue.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Applications of MALDI-MS/MS-Based Proteomics in Biomedical Research.Molecules (Basel, Switzerland) · 2022Review
- Cu and Zn Interactions with Peptides Revealed by High-Resolution Mass Spectrometry.Pharmaceuticals (Basel, Switzerland) · 2022Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Noncovalent interactions are the keys to the structural organization of biomolecule e.g., proteins, glycans, lipids in the process of molecular recognition processes e.g., enzyme-substrate, antigen-antibody. Protein interactions lead to conformational changes, which dictate the functionality of that protein-protein complex. Besides biophysics techniques, noncovalent interaction and conformational dynamics, can be studied via mass spectrometry (MS), which represents a powerful tool, due to its low sample consumption, high sensitivity, and label-free sample. In this review, the focus will be placed on Matrix-Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS) and its role in the analysis of protein-protein noncovalent assemblies exploring the relationship within noncovalent interaction, conformation, and biological function.
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Registered trials
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.