Comparer des méthodes

	Reconstruction par cryo-ME	Topologie de réseau d'interactions protéine-protéine
Domaine	Bio-informatique	Bio-informatique
Famille	Process / pipeline	Process / pipeline
Année d'origine	1975	2000
Auteur d'origine	Joachim Frank	Peter Uetz
Type	Image reconstruction pipeline	Network analysis pipeline
Source fondatrice	Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319.	Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., ... & Lomax, J. (2000). A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature, 403(6770), 623-627.
Alias	cryo-electron microscopy, cryo-EM, single-particle cryo-EM	protein interaction networks, interactome analysis, network topology
Apparentées	3	3
Résumé	Cryo-electron microscopy (cryo-EM) determines three-dimensional macromolecular structures at atomic or near-atomic resolution by imaging proteins frozen in vitreous ice. Pioneered by Frank, Henderson, and others, this technique has revolutionized structural biology by enabling visualization of large, non-crystallizable complexes and capturing functional conformational states.	Protein-protein interaction network analysis identifies and characterizes the structural properties of cellular interaction networks. Pioneered by Uetz and colleagues through large-scale yeast two-hybrid screening, this approach reveals topological features like hubs, modules, and motifs that encode functional organization and disease associations.