Σύγκριση μεθόδων

	Τοπολογία Δικτύου Αλληλεπιδράσεων Πρωτεϊνών-Πρωτεϊνών	Ανασύσταση με Κρυο-Ηλεκτρονική Μικροσκοπία
Πεδίο	Βιοπληροφορική	Βιοπληροφορική
Οικογένεια	Process / pipeline	Process / pipeline
Έτος προέλευσης	2000	1975
Δημιουργός	Peter Uetz	Joachim Frank
Τύπος	Network analysis pipeline	Image reconstruction pipeline
Θεμελιώδης πηγή	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.	Frank, J. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy. Annual Review of Biophysics and Biomolecular Structure, 31, 303-319.
Εναλλακτικές ονομασίες	protein interaction networks, interactome analysis, network topology	cryo-electron microscopy, cryo-EM, single-particle cryo-EM
Συναφείς	3	3
Σύνοψη	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.	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.